HEADER AGGLUTININ 28-JAN-97 1NLS TITLE CONCANAVALIN A AND ITS BOUND SOLVENT AT 0.94A RESOLUTION COMPND MOL_ID: 1; COMPND 2 MOLECULE: CONCANAVALIN A; COMPND 3 CHAIN: A SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CANAVALIA ENSIFORMIS; SOURCE 3 ORGANISM_COMMON: JACK BEAN; SOURCE 4 ORGANISM_TAXID: 3823 KEYWDS CONCANAVALIN A, LECTIN, AGGLUTININ EXPDTA X-RAY DIFFRACTION AUTHOR A.M.DEACON,T.GLEICHMANN,J.R.HELLIWELL,A.J.KALB(GILBOA) REVDAT 2 24-FEB-09 1NLS 1 VERSN REVDAT 1 26-NOV-97 1NLS 0 JRNL AUTH A.DEACON,T.GLEICHMANN,A.J.KALB(GILBOA),H.PRICE, JRNL AUTH 2 J.RAFTERY,G.BRADBROOK,J.YARIV,J.R.HELLIWELL JRNL TITL THE STRUCTURE OF CONCANAVALIN A AND ITS BOUND JRNL TITL 2 SOLVENT DETERMINED WITH SMALL-MOLECULE ACCURACY AT JRNL TITL 3 0.94 A RESOLUTION JRNL REF J.CHEM.SOC.,FARADAY TRANS. V. 93 4305 1997 JRNL REFN ISSN 0956-5000 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.HABASH,J.RAFTERY,S.WEISGERBER,A.CASSETTA, REMARK 1 AUTH 2 M.S.LEHMANN,P.HOGHOJ,C.WILKINSON,J.W.CAMPBELL, REMARK 1 AUTH 3 J.R.HELLIWELL REMARK 1 TITL NEUTRON LAUE DIFFRACTION STUDY OF CONCANAVALIN A. REMARK 1 TITL 2 THE PROTON OF ASP28 REMARK 1 REF J.CHEM.SOC.,FARADAY TRANS. V. 93 4313 1997 REMARK 1 REFN ISSN 0956-5000 REMARK 1 REFERENCE 2 REMARK 1 AUTH C.EMMERICH,J.R.HELLIWELL,M.REDSHAW,J.H.NAISMITH, REMARK 1 AUTH 2 S.J.HARROP,J.RAFTERY,A.J.KALB(GILBOA),J.YARIV, REMARK 1 AUTH 3 Z.DAUTER,K.S.WILSON REMARK 1 TITL HIGH-RESOLUTION STRUCTURES OF REMARK 1 TITL 2 SINGLE-METAL-SUBSTITUTED CONCANAVALIN A: THE REMARK 1 TITL 3 CO,CA-PROTEIN AT 1.6 A AND THE NI,CA-PROTEIN AT REMARK 1 TITL 4 2.0 A REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 50 749 1994 REMARK 1 REFN ISSN 0907-4449 REMARK 1 REFERENCE 3 REMARK 1 AUTH S.WEISGERBER,J.R.HELLIWELL REMARK 1 TITL HIGH RESOLUTION CRYSTALLOGRAPHIC STUDIES OF NATIVE REMARK 1 TITL 2 CONCANAVALIN A USING RAPID LAUE DATA COLLECTION REMARK 1 TITL 3 METHODS AND THE INTRODUCTION OF A MONOCHROMATIC REMARK 1 TITL 4 LARGE-ANGLE OSCILLATION TECHNIQUE (LOT) REMARK 1 REF J.CHEM.SOC.,FARADAY TRANS. V. 89 2667 1993 REMARK 1 REFN ISSN 0956-5000 REMARK 2 REMARK 2 RESOLUTION. 0.94 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : SHELXL-97 REMARK 3 AUTHORS : G.M.SHELDRICK REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 0.94 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 75.0 REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF). REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.127 REMARK 3 FREE R VALUE (NO CUTOFF) : 0.154 REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 1.000 REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 1167 REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 116712 REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F). REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.122 REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.148 REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1809 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 2 REMARK 3 SOLVENT ATOMS : 323 REMARK 3 REMARK 3 MODEL REFINEMENT. REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 19158 REMARK 3 NUMBER OF RESTRAINTS : 23649 REMARK 3 REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES. REMARK 3 BOND LENGTHS (A) : NULL REMARK 3 ANGLE DISTANCES (A) : NULL REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : NULL REMARK 3 ZERO CHIRAL VOLUMES (A**3) : NULL REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : NULL REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : NULL REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED: SHELXL SWAT REMARK 3 REMARK 3 STEREOCHEMISTRY TARGET VALUES : 0.02A BOND LENGTH ESDS REMARK 3 RESTRAINT REMARK 3 SPECIAL CASE: NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: RESIDUE THR 120 IS POORLY DEFINED IN REMARK 3 ELECTRON DENSITY. THE FOLLOWING RESIDUES HAVE SIDE CHAINS REMARK 3 MODELLED WITH TWO CONFORMATIONS AND WERE REFINED WITH REMARK 3 COMPLEMENTARY OCCUPANCIES: LEU 9, SER 21, ILE 25, ILE 27, LYS REMARK 3 39, MET 42, LYS 59, ARG 60, VAL 65, SER 72, ASP 78, LEU 107, REMARK 3 SER 110, SER 113, ASN 124, SER 164, SER 185, VAL 188, GLU 192, REMARK 3 THR 196, SER 204, SER 215, ASP 218, SER 220, SER 223. CIS REMARK 3 PEPTIDES 1 AND 2 ARE DUE TO POORLY DEFINED ELECTRON DENSITY. REMARK 4 REMARK 4 1NLS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 1994 REMARK 200 TEMPERATURE (KELVIN) : 110 REMARK 200 PH : 6.8 REMARK 200 NUMBER OF CRYSTALS USED : 4 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : CHESS REMARK 200 BEAMLINE : A1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.92 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : MIRROR + MONO POINT FOCUSSING REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 116923 REMARK 200 RESOLUTION RANGE HIGH (A) : NULL REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 75.4 REMARK 200 DATA REDUNDANCY : 4.300 REMARK 200 R MERGE (I) : 0.09300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.94 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.01 REMARK 200 COMPLETENESS FOR SHELL (%) : 30.4 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.15000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: SHELXL-97 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 49.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.8 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X,Y,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 44.77500 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 43.23000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 31.05500 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 44.77500 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 43.23000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 31.05500 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 44.77500 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 43.23000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 31.05500 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 44.77500 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 43.23000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 31.05500 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 300 REMARK: REMARK 300 CONCANAVALIN A EXISTS AS A TETRAMER, ALTHOUGH THE REMARK 300 ASYMMETRIC UNIT CONTAINS A MONOMER. THE TETRAMER CAN BE REMARK 300 GENERATED BY SYMMETRY OPERATORS. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 89.55000 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 89.55000 REMARK 350 BIOMT2 3 0.000000 -1.000000 0.000000 86.46000 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 86.46000 REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH A 534 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 544 LIES ON A SPECIAL POSITION. REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 GLU A 102 CD GLU A 102 OE2 0.093 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 LEU A 9 CB - CG - CD1 ANGL. DEV. = 10.8 DEGREES REMARK 500 ILE A 25 N - CA - CB ANGL. DEV. = 19.0 DEGREES REMARK 500 ILE A 25 CA - CB - CG1 ANGL. DEV. = 14.9 DEGREES REMARK 500 ILE A 27 CA - CB - CG1 ANGL. DEV. = 12.8 DEGREES REMARK 500 MET A 42 CG - SD - CE ANGL. DEV. = -11.9 DEGREES REMARK 500 ARG A 60 CD - NE - CZ ANGL. DEV. = 32.1 DEGREES REMARK 500 VAL A 65 CG1 - CB - CG2 ANGL. DEV. = 10.8 DEGREES REMARK 500 VAL A 65 CA - CB - CG2 ANGL. DEV. = 12.6 DEGREES REMARK 500 ASP A 78 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES REMARK 500 HIS A 121 C - N - CA ANGL. DEV. = 34.5 DEGREES REMARK 500 LYS A 135 CB - CG - CD ANGL. DEV. = 26.9 DEGREES REMARK 500 ASP A 151 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES REMARK 500 ARG A 158 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES REMARK 500 ARG A 158 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES REMARK 500 ARG A 172 NH1 - CZ - NH2 ANGL. DEV. = 6.6 DEGREES REMARK 500 ARG A 172 NE - CZ - NH2 ANGL. DEV. = -6.1 DEGREES REMARK 500 VAL A 188 CB - CA - C ANGL. DEV. = 11.7 DEGREES REMARK 500 THR A 196 N - CA - CB ANGL. DEV. = 17.3 DEGREES REMARK 500 ASP A 218 OD1 - CG - OD2 ANGL. DEV. = -12.4 DEGREES REMARK 500 ASP A 218 CB - CG - OD2 ANGL. DEV. = 10.8 DEGREES REMARK 500 ASP A 218 CB - CG - OD2 ANGL. DEV. = -7.9 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER A 21 38.24 -82.19 REMARK 500 THR A 120 100.63 -46.59 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 323 DISTANCE = 6.75 ANGSTROMS REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MN A 239 MN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 8 OE2 REMARK 620 2 ASP A 10 OD2 94.8 REMARK 620 3 ASP A 19 OD1 169.5 95.2 REMARK 620 4 HIS A 24 NE2 93.0 85.9 91.1 REMARK 620 5 HOH A 412 O 85.3 89.5 91.4 174.9 REMARK 620 6 HOH A 413 O 88.5 175.6 81.8 91.0 93.8 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 240 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 TYR A 12 O REMARK 620 2 ASN A 14 OD1 84.3 REMARK 620 3 HOH A 411 O 172.9 88.7 REMARK 620 4 ASP A 19 OD2 80.8 87.4 97.9 REMARK 620 5 ASP A 10 OD1 76.4 151.5 110.5 109.6 REMARK 620 6 HOH A 410 O 90.8 86.7 89.8 170.1 73.0 REMARK 620 7 ASP A 10 OD2 112.0 155.9 74.4 78.2 52.7 109.9 REMARK 620 N 1 2 3 4 5 6 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 239 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 240 DBREF 1NLS A 119 237 UNP P02866 CONA_CANEN 30 148 SEQADV 1NLS ASP A 151 UNP P02866 GLU 62 CONFLICT SEQADV 1NLS GLU A 155 UNP P02866 ARG 66 CONFLICT SEQRES 1 A 237 ALA ASP THR ILE VAL ALA VAL GLU LEU ASP THR TYR PRO SEQRES 2 A 237 ASN THR ASP ILE GLY ASP PRO SER TYR PRO HIS ILE GLY SEQRES 3 A 237 ILE ASP ILE LYS SER VAL ARG SER LYS LYS THR ALA LYS SEQRES 4 A 237 TRP ASN MET GLN ASN GLY LYS VAL GLY THR ALA HIS ILE SEQRES 5 A 237 ILE TYR ASN SER VAL ASP LYS ARG LEU SER ALA VAL VAL SEQRES 6 A 237 SER TYR PRO ASN ALA ASP SER ALA THR VAL SER TYR ASP SEQRES 7 A 237 VAL ASP LEU ASP ASN VAL LEU PRO GLU TRP VAL ARG VAL SEQRES 8 A 237 GLY LEU SER ALA SER THR GLY LEU TYR LYS GLU THR ASN SEQRES 9 A 237 THR ILE LEU SER TRP SER PHE THR SER LYS LEU LYS SER SEQRES 10 A 237 ASN SER THR HIS GLU THR ASN ALA LEU HIS PHE MET PHE SEQRES 11 A 237 ASN GLN PHE SER LYS ASP GLN LYS ASP LEU ILE LEU GLN SEQRES 12 A 237 GLY ASP ALA THR THR GLY THR ASP GLY ASN LEU GLU LEU SEQRES 13 A 237 THR ARG VAL SER SER ASN GLY SER PRO GLN GLY SER SER SEQRES 14 A 237 VAL GLY ARG ALA LEU PHE TYR ALA PRO VAL HIS ILE TRP SEQRES 15 A 237 GLU SER SER ALA VAL VAL ALA SER PHE GLU ALA THR PHE SEQRES 16 A 237 THR PHE LEU ILE LYS SER PRO ASP SER HIS PRO ALA ASP SEQRES 17 A 237 GLY ILE ALA PHE PHE ILE SER ASN ILE ASP SER SER ILE SEQRES 18 A 237 PRO SER GLY SER THR GLY ARG LEU LEU GLY LEU PHE PRO SEQRES 19 A 237 ASP ALA ASN HET MN A 239 1 HET CA A 240 1 HETNAM MN MANGANESE (II) ION HETNAM CA CALCIUM ION FORMUL 2 MN MN 2+ FORMUL 3 CA CA 2+ FORMUL 4 HOH *319(H2 O) HELIX 1 1 ASN A 14 GLY A 18 5 5 HELIX 2 2 ASP A 80 VAL A 84 5 5 HELIX 3 3 THR A 150 GLY A 152 5 3 HELIX 4 4 THR A 226 LEU A 230 5 5 SHEET 1 A 7 LYS A 36 LYS A 39 0 SHEET 2 A 7 HIS A 24 ILE A 29 -1 N ILE A 27 O LYS A 36 SHEET 3 A 7 ILE A 4 ASP A 10 -1 N ASP A 10 O HIS A 24 SHEET 4 A 7 GLY A 209 SER A 215 -1 N ILE A 214 O VAL A 5 SHEET 5 A 7 ARG A 90 SER A 96 -1 N SER A 96 O GLY A 209 SHEET 6 A 7 VAL A 170 PHE A 175 -1 N ALA A 173 O LEU A 93 SHEET 7 A 7 LEU A 140 GLY A 144 -1 N GLN A 143 O ARG A 172 SHEET 1 B 6 ALA A 73 ASP A 78 0 SHEET 2 B 6 ARG A 60 TYR A 67 -1 N VAL A 65 O ALA A 73 SHEET 3 B 6 VAL A 47 ASN A 55 -1 N ILE A 53 O SER A 62 SHEET 4 B 6 VAL A 188 LEU A 198 -1 N PHE A 197 O GLY A 48 SHEET 5 B 6 THR A 105 LYS A 116 -1 N LYS A 116 O VAL A 188 SHEET 6 B 6 THR A 123 PHE A 130 -1 N PHE A 130 O TRP A 109 SHEET 1 C 2 THR A 147 THR A 150 0 SHEET 2 C 2 ASN A 153 GLU A 155 -1 N GLU A 155 O THR A 147 LINK MN MN A 239 OE2 GLU A 8 1555 1555 2.17 LINK MN MN A 239 OD2 ASP A 10 1555 1555 2.15 LINK MN MN A 239 OD1 ASP A 19 1555 1555 2.19 LINK MN MN A 239 NE2 HIS A 24 1555 1555 2.23 LINK CA CA A 240 O TYR A 12 1555 1555 2.38 LINK CA CA A 240 OD1 ASN A 14 1555 1555 2.35 LINK MN MN A 239 O HOH A 412 1555 1555 2.26 LINK MN MN A 239 O HOH A 413 1555 1555 2.18 LINK CA CA A 240 O HOH A 411 1555 1555 2.43 LINK CA CA A 240 OD2 ASP A 19 1555 1555 2.41 LINK CA CA A 240 OD1 ASP A 10 1555 1555 2.47 LINK CA CA A 240 O HOH A 410 1555 1555 2.36 LINK CA CA A 240 OD2 ASP A 10 1555 1555 2.51 CISPEP 1 THR A 120 HIS A 121 0 -6.53 CISPEP 2 HIS A 121 GLU A 122 0 8.22 CISPEP 3 ALA A 207 ASP A 208 0 0.90 SITE 1 AC1 6 GLU A 8 ASP A 10 ASP A 19 HIS A 24 SITE 2 AC1 6 HOH A 412 HOH A 413 SITE 1 AC2 6 ASP A 10 TYR A 12 ASN A 14 ASP A 19 SITE 2 AC2 6 HOH A 410 HOH A 411 CRYST1 89.550 86.460 62.110 90.00 90.00 90.00 I 2 2 2 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.011167 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011566 0.000000 0.00000 SCALE3 0.000000 0.000000 0.016100 0.00000 ATOM 1 N ALA A 1 47.699 22.521 30.384 1.00 37.82 N ANISOU 1 N ALA A 1 4790 4790 4790 0 0 0 N ATOM 2 CA ALA A 1 48.661 22.866 29.347 1.00 27.31 C ANISOU 2 CA ALA A 1 3459 3459 3459 0 0 0 C ATOM 3 C ALA A 1 48.041 23.492 28.087 1.00 17.36 C ANISOU 3 C ALA A 1 2199 2199 2199 0 0 0 C ATOM 4 O ALA A 1 46.799 23.304 27.872 1.00 20.88 O ANISOU 4 O ALA A 1 2644 2644 2644 0 0 0 O ATOM 5 CB ALA A 1 49.485 21.642 28.972 1.00 37.46 C ANISOU 5 CB ALA A 1 4744 4744 4744 0 0 0 C ATOM 6 N ASP A 2 48.807 24.328 27.430 1.00 14.37 N ANISOU 6 N ASP A 2 1531 2486 1308 -181 76 711 N ATOM 7 CA ASP A 2 48.339 24.986 26.199 1.00 11.73 C ANISOU 7 CA ASP A 2 1221 1853 1272 110 96 592 C ATOM 8 C ASP A 2 48.019 23.911 25.143 1.00 11.22 C ANISOU 8 C ASP A 2 1116 1714 1327 -46 145 666 C ATOM 9 O ASP A 2 48.472 22.767 25.288 1.00 14.34 O ANISOU 9 O ASP A 2 1578 1813 1921 244 -368 502 O ATOM 10 CB ASP A 2 49.459 25.935 25.739 1.00 11.73 C ANISOU 10 CB ASP A 2 1135 1771 1440 104 153 519 C ATOM 11 CG ASP A 2 49.689 27.098 26.628 1.00 11.84 C ANISOU 11 CG ASP A 2 1110 1846 1432 185 101 440 C ATOM 12 OD1 ASP A 2 48.780 27.470 27.431 1.00 13.27 O ANISOU 12 OD1 ASP A 2 1210 2307 1399 -46 110 309 O ATOM 13 OD2 ASP A 2 50.781 27.745 26.499 1.00 13.42 O ANISOU 13 OD2 ASP A 2 1009 2193 1771 159 -106 295 O ATOM 14 N THR A 3 47.341 24.394 24.096 1.00 10.42 N ANISOU 14 N THR A 3 1035 1552 1275 243 253 382 N ATOM 15 CA THR A 3 47.152 23.618 22.861 1.00 10.52 C ANISOU 15 CA THR A 3 993 1578 1327 -12 159 360 C ATOM 16 C THR A 3 47.984 24.298 21.775 1.00 9.81 C ANISOU 16 C THR A 3 1047 1453 1136 119 93 330 C ATOM 17 O THR A 3 47.730 25.469 21.509 1.00 12.38 O ANISOU 17 O THR A 3 1432 1460 1696 170 438 500 O ATOM 18 CB THR A 3 45.680 23.535 22.464 1.00 12.74 C ANISOU 18 CB THR A 3 1101 1869 1751 -8 86 433 C ATOM 19 OG1 THR A 3 44.921 23.005 23.547 1.00 17.15 O ANISOU 19 OG1 THR A 3 1265 2791 2298 -447 157 776 O ATOM 20 CG2 THR A 3 45.523 22.754 21.215 1.00 15.70 C ANISOU 20 CG2 THR A 3 1619 2001 2199 -492 -413 230 C ATOM 21 N ILE A 4 48.877 23.541 21.145 1.00 9.08 N ANISOU 21 N ILE A 4 995 1178 1192 -19 109 289 N ATOM 22 CA ILE A 4 49.788 24.096 20.140 1.00 8.61 C ANISOU 22 CA ILE A 4 786 1291 1113 -50 31 415 C ATOM 23 C ILE A 4 49.718 23.366 18.824 1.00 7.82 C ANISOU 23 C ILE A 4 610 1088 1200 19 -47 298 C ATOM 24 O ILE A 4 49.820 22.117 18.783 1.00 9.22 O ANISOU 24 O ILE A 4 906 1175 1335 140 170 422 O ATOM 25 CB ILE A 4 51.275 24.014 20.650 1.00 10.85 C ANISOU 25 CB ILE A 4 825 1939 1255 -51 -152 410 C ATOM 26 CG1 ILE A 4 51.454 24.825 21.950 1.00 12.62 C ANISOU 26 CG1 ILE A 4 1158 2047 1472 -113 -349 371 C ATOM 27 CG2 ILE A 4 52.273 24.428 19.584 1.00 11.90 C ANISOU 27 CG2 ILE A 4 690 2145 1575 -231 -158 658 C ATOM 28 CD1 ILE A 4 51.386 26.327 21.723 1.00 18.81 C ANISOU 28 CD1 ILE A 4 2400 1928 2643 -473 -1075 182 C ATOM 29 N VAL A 5 49.616 24.128 17.736 1.00 6.90 N ANISOU 29 N VAL A 5 567 895 1096 80 51 171 N ATOM 30 CA VAL A 5 49.878 23.685 16.375 1.00 6.84 C ANISOU 30 CA VAL A 5 615 783 1136 97 98 58 C ATOM 31 C VAL A 5 51.049 24.523 15.847 1.00 6.43 C ANISOU 31 C VAL A 5 551 751 1080 68 53 -1 C ATOM 32 O VAL A 5 51.032 25.748 16.034 1.00 7.78 O ANISOU 32 O VAL A 5 652 811 1419 87 244 35 O ATOM 33 CB VAL A 5 48.622 23.886 15.483 1.00 7.72 C ANISOU 33 CB VAL A 5 643 1024 1193 -38 27 191 C ATOM 34 CG1 VAL A 5 48.941 23.747 14.008 1.00 8.83 C ANISOU 34 CG1 VAL A 5 836 1251 1185 -107 16 166 C ATOM 35 CG2 VAL A 5 47.538 22.907 15.946 1.00 9.24 C ANISOU 35 CG2 VAL A 5 811 1259 1355 -239 49 78 C ATOM 36 N ALA A 6 52.074 23.896 15.280 1.00 6.79 N ANISOU 36 N ALA A 6 597 777 1144 82 86 50 N ATOM 37 CA ALA A 6 53.224 24.682 14.851 1.00 6.34 C ANISOU 37 CA ALA A 6 566 666 1118 55 52 90 C ATOM 38 C ALA A 6 53.866 24.102 13.585 1.00 6.05 C ANISOU 38 C ALA A 6 490 789 963 123 -30 69 C ATOM 39 O ALA A 6 53.777 22.881 13.329 1.00 7.28 O ANISOU 39 O ALA A 6 697 786 1216 91 206 29 O ATOM 40 CB ALA A 6 54.291 24.716 15.959 1.00 7.16 C ANISOU 40 CB ALA A 6 654 958 1041 -52 26 70 C ATOM 41 N VAL A 7 54.559 24.982 12.870 1.00 6.11 N ANISOU 41 N VAL A 7 480 722 1064 79 45 90 N ATOM 42 CA VAL A 7 55.508 24.605 11.813 1.00 5.87 C ANISOU 42 CA VAL A 7 520 783 873 66 -17 -66 C ATOM 43 C VAL A 7 56.902 24.932 12.387 1.00 5.93 C ANISOU 43 C VAL A 7 436 792 969 11 3 49 C ATOM 44 O VAL A 7 57.175 26.100 12.699 1.00 6.21 O ANISOU 44 O VAL A 7 545 727 1028 83 -68 -62 O ATOM 45 CB VAL A 7 55.254 25.324 10.513 1.00 6.44 C ANISOU 45 CB VAL A 7 588 837 962 -36 -81 -48 C ATOM 46 CG1 VAL A 7 56.364 25.047 9.484 1.00 8.16 C ANISOU 46 CG1 VAL A 7 724 1400 901 151 37 28 C ATOM 47 CG2 VAL A 7 53.872 24.922 9.934 1.00 8.29 C ANISOU 47 CG2 VAL A 7 684 1195 1192 -31 -222 -75 C ATOM 48 N GLU A 8 57.733 23.897 12.551 1.00 5.80 N ANISOU 48 N GLU A 8 444 677 1030 87 -43 21 N ATOM 49 CA GLU A 8 59.089 24.088 13.099 1.00 6.06 C ANISOU 49 CA GLU A 8 472 821 954 109 -108 -114 C ATOM 50 C GLU A 8 60.135 24.096 11.995 1.00 5.39 C ANISOU 50 C GLU A 8 523 628 847 106 -19 78 C ATOM 51 O GLU A 8 60.108 23.277 11.072 1.00 6.36 O ANISOU 51 O GLU A 8 601 786 968 46 52 -46 O ATOM 52 CB GLU A 8 59.424 23.001 14.149 1.00 6.41 C ANISOU 52 CB GLU A 8 564 848 965 78 -29 121 C ATOM 53 CG GLU A 8 59.338 21.549 13.649 1.00 6.91 C ANISOU 53 CG GLU A 8 636 883 1041 124 -124 38 C ATOM 54 CD GLU A 8 59.921 20.541 14.621 1.00 6.73 C ANISOU 54 CD GLU A 8 570 918 1005 41 -52 113 C ATOM 55 OE1 GLU A 8 59.449 20.470 15.799 1.00 7.37 O ANISOU 55 OE1 GLU A 8 652 998 1080 166 -35 122 O ATOM 56 OE2 GLU A 8 60.853 19.785 14.225 1.00 6.81 O ANISOU 56 OE2 GLU A 8 578 845 1101 148 -46 40 O ATOM 57 N LEU A 9 61.094 25.003 12.154 1.00 5.89 N ANISOU 57 N LEU A 9 498 783 903 127 -14 -35 N ATOM 58 CA LEU A 9 62.379 25.046 11.403 1.00 6.02 C ANISOU 58 CA LEU A 9 469 795 966 105 24 -12 C ATOM 59 C LEU A 9 63.408 24.592 12.458 1.00 5.69 C ANISOU 59 C LEU A 9 474 805 831 121 -41 7 C ATOM 60 O LEU A 9 63.890 25.375 13.252 1.00 6.33 O ANISOU 60 O LEU A 9 610 741 995 133 -115 -132 O ATOM 61 CB LEU A 9 62.681 26.439 10.863 1.00 6.91 C ANISOU 61 CB LEU A 9 604 840 1117 128 -4 170 C ATOM 62 CG ALEU A 9 61.772 26.928 9.734 0.69 6.80 C ANISOU 62 CG ALEU A 9 404 1076 1041 -23 -39 243 C ATOM 63 CG BLEU A 9 62.529 26.872 9.469 0.69 23.38 C ANISOU 63 CG BLEU A 9 5496 1142 2026 -805 -1981 684 C ATOM 64 CD1ALEU A 9 60.305 26.660 9.734 0.31 7.31 C ANISOU 64 CD1ALEU A 9 514 1134 1062 232 2 276 C ATOM 65 CD1BLEU A 9 61.538 26.133 8.627 0.69 13.39 C ANISOU 65 CD1BLEU A 9 2017 1411 1533 -279 -726 792 C ATOM 66 CD2 LEU A 9 62.209 28.342 9.363 1.00 9.76 C ANISOU 66 CD2 LEU A 9 920 1340 1358 -68 -139 582 C ATOM 67 N ASP A 10 63.657 23.273 12.488 1.00 5.90 N ANISOU 67 N ASP A 10 564 747 874 138 -109 -17 N ATOM 68 CA ASP A 10 64.398 22.614 13.554 1.00 6.24 C ANISOU 68 CA ASP A 10 533 869 908 83 -24 117 C ATOM 69 C ASP A 10 65.857 22.421 13.111 1.00 6.09 C ANISOU 69 C ASP A 10 484 796 977 89 -39 29 C ATOM 70 O ASP A 10 66.151 21.677 12.167 1.00 6.75 O ANISOU 70 O ASP A 10 587 866 1047 102 -49 -77 O ATOM 71 CB ASP A 10 63.738 21.270 13.877 1.00 6.09 C ANISOU 71 CB ASP A 10 517 806 933 110 -80 54 C ATOM 72 CG ASP A 10 64.342 20.580 15.092 1.00 6.18 C ANISOU 72 CG ASP A 10 650 645 995 171 -39 85 C ATOM 73 OD1 ASP A 10 65.474 20.936 15.495 1.00 7.10 O ANISOU 73 OD1 ASP A 10 564 976 1092 70 -102 68 O ATOM 74 OD2 ASP A 10 63.678 19.660 15.674 1.00 6.50 O ANISOU 74 OD2 ASP A 10 643 750 1015 63 -51 148 O ATOM 75 N THR A 11 66.747 23.217 13.756 1.00 6.15 N ANISOU 75 N THR A 11 547 768 964 147 -33 -63 N ATOM 76 CA THR A 11 68.158 23.256 13.324 1.00 6.36 C ANISOU 76 CA THR A 11 493 880 986 1 -5 126 C ATOM 77 C THR A 11 69.026 22.161 13.940 1.00 6.43 C ANISOU 77 C THR A 11 605 795 984 101 -42 -32 C ATOM 78 O THR A 11 70.160 21.977 13.423 1.00 8.01 O ANISOU 78 O THR A 11 609 1113 1247 233 103 217 O ATOM 79 CB THR A 11 68.751 24.632 13.605 1.00 6.72 C ANISOU 79 CB THR A 11 600 905 983 -1 -13 5 C ATOM 80 OG1 THR A 11 68.618 24.849 15.004 1.00 7.08 O ANISOU 80 OG1 THR A 11 748 853 1021 108 -55 65 O ATOM 81 CG2 THR A 11 68.087 25.730 12.815 1.00 8.17 C ANISOU 81 CG2 THR A 11 839 928 1260 76 -104 188 C ATOM 82 N TYR A 12 68.562 21.439 14.959 1.00 6.76 N ANISOU 82 N TYR A 12 561 788 1156 208 27 107 N ATOM 83 CA TYR A 12 69.434 20.494 15.676 1.00 6.73 C ANISOU 83 CA TYR A 12 600 790 1105 122 8 74 C ATOM 84 C TYR A 12 68.738 19.147 15.764 1.00 7.01 C ANISOU 84 C TYR A 12 522 874 1204 184 -27 27 C ATOM 85 O TYR A 12 67.629 19.037 16.365 1.00 7.85 O ANISOU 85 O TYR A 12 702 814 1392 136 123 224 O ATOM 86 CB TYR A 12 69.793 21.032 17.076 1.00 7.17 C ANISOU 86 CB TYR A 12 700 870 1086 199 -15 30 C ATOM 87 CG TYR A 12 70.847 20.188 17.744 1.00 7.49 C ANISOU 87 CG TYR A 12 766 877 1131 141 -75 -13 C ATOM 88 CD1 TYR A 12 70.545 18.967 18.350 1.00 7.89 C ANISOU 88 CD1 TYR A 12 889 1062 973 135 -3 143 C ATOM 89 CD2 TYR A 12 72.206 20.579 17.742 1.00 7.86 C ANISOU 89 CD2 TYR A 12 749 1037 1128 153 0 68 C ATOM 90 CE1 TYR A 12 71.488 18.144 18.904 1.00 8.04 C ANISOU 90 CE1 TYR A 12 950 1015 1016 109 -55 175 C ATOM 91 CE2 TYR A 12 73.184 19.766 18.349 1.00 8.29 C ANISOU 91 CE2 TYR A 12 744 1095 1234 243 142 192 C ATOM 92 CZ TYR A 12 72.836 18.560 18.899 1.00 8.29 C ANISOU 92 CZ TYR A 12 867 964 1239 193 -75 81 C ATOM 93 OH TYR A 12 73.833 17.801 19.470 1.00 9.34 O ANISOU 93 OH TYR A 12 1092 1066 1303 336 -159 255 O ATOM 94 N PRO A 13 69.373 18.066 15.328 1.00 7.58 N ANISOU 94 N PRO A 13 690 903 1217 99 22 -54 N ATOM 95 CA PRO A 13 68.740 16.752 15.360 1.00 8.41 C ANISOU 95 CA PRO A 13 706 966 1444 57 -107 -64 C ATOM 96 C PRO A 13 68.803 16.086 16.737 1.00 8.73 C ANISOU 96 C PRO A 13 625 891 1720 166 -79 130 C ATOM 97 O PRO A 13 69.871 15.694 17.219 1.00 11.03 O ANISOU 97 O PRO A 13 748 1426 1911 235 -10 563 O ATOM 98 CB PRO A 13 69.559 15.960 14.316 1.00 11.07 C ANISOU 98 CB PRO A 13 1336 967 1799 254 1 -370 C ATOM 99 CG PRO A 13 70.917 16.565 14.406 1.00 11.74 C ANISOU 99 CG PRO A 13 1275 1186 1890 174 403 -336 C ATOM 100 CD PRO A 13 70.692 18.042 14.649 1.00 9.25 C ANISOU 100 CD PRO A 13 809 1048 1569 248 305 59 C ATOM 101 N ASN A 14 67.631 15.945 17.362 1.00 8.07 N ANISOU 101 N ASN A 14 684 748 1557 120 -136 71 N ATOM 102 CA ASN A 14 67.472 15.226 18.641 1.00 8.61 C ANISOU 102 CA ASN A 14 718 864 1610 96 -244 199 C ATOM 103 C ASN A 14 66.815 13.865 18.328 1.00 8.78 C ANISOU 103 C ASN A 14 814 931 1509 117 -160 189 C ATOM 104 O ASN A 14 65.592 13.714 18.262 1.00 8.99 O ANISOU 104 O ASN A 14 871 1060 1400 -66 -294 264 O ATOM 105 CB ASN A 14 66.599 16.016 19.611 1.00 8.78 C ANISOU 105 CB ASN A 14 746 1056 1451 29 -249 184 C ATOM 106 CG ASN A 14 67.071 17.442 19.813 1.00 7.58 C ANISOU 106 CG ASN A 14 677 980 1151 126 -187 257 C ATOM 107 OD1 ASN A 14 66.520 18.395 19.272 1.00 7.89 O ANISOU 107 OD1 ASN A 14 759 924 1242 185 -191 123 O ATOM 108 ND2 ASN A 14 68.122 17.603 20.619 1.00 7.42 N ANISOU 108 ND2 ASN A 14 794 840 1114 143 -155 116 N ATOM 109 N THR A 15 67.626 12.840 18.066 1.00 11.47 N ANISOU 109 N THR A 15 1009 793 2447 101 -215 110 N ATOM 110 CA THR A 15 67.102 11.626 17.465 1.00 11.62 C ANISOU 110 CA THR A 15 1287 893 2127 59 -155 97 C ATOM 111 C THR A 15 66.220 10.850 18.449 1.00 11.94 C ANISOU 111 C THR A 15 1455 1080 1889 -206 -454 305 C ATOM 112 O THR A 15 65.348 10.111 17.998 1.00 14.60 O ANISOU 112 O THR A 15 2292 1397 1721 -655 -675 327 O ATOM 113 CB THR A 15 68.199 10.791 16.766 1.00 16.59 C ANISOU 113 CB THR A 15 1597 1218 3334 75 172 -356 C ATOM 114 OG1 THR A 15 69.150 10.480 17.761 1.00 23.48 O ANISOU 114 OG1 THR A 15 2118 1494 5087 828 -867 -296 O ATOM 115 CG2 THR A 15 68.844 11.542 15.621 1.00 19.69 C ANISOU 115 CG2 THR A 15 1764 1415 4117 -81 1122 -666 C ATOM 116 N ASP A 16 66.429 10.976 19.778 1.00 12.22 N ANISOU 116 N ASP A 16 1435 1211 1882 -129 -331 -32 N ATOM 117 CA ASP A 16 65.542 10.311 20.759 1.00 12.98 C ANISOU 117 CA ASP A 16 1707 1336 1768 -97 -409 292 C ATOM 118 C ASP A 16 64.134 10.866 20.925 1.00 14.16 C ANISOU 118 C ASP A 16 1393 2112 1744 -318 -363 612 C ATOM 119 O ASP A 16 63.334 10.147 21.522 1.00 22.44 O ANISOU 119 O ASP A 16 2111 2916 3288 -551 73 1654 O ATOM 120 CB ASP A 16 66.217 10.162 22.145 1.00 15.02 C ANISOU 120 CB ASP A 16 2104 1575 1885 505 -642 73 C ATOM 121 CG ASP A 16 66.527 11.446 22.865 1.00 21.59 C ANISOU 121 CG ASP A 16 2595 2142 3262 1147 -1817 -865 C ATOM 122 OD1 ASP A 16 66.296 12.518 22.229 1.00 29.40 O ANISOU 122 OD1 ASP A 16 4933 1632 4328 1021 -3137 -1131 O ATOM 123 OD2 ASP A 16 66.978 11.439 24.058 1.00 19.44 O ANISOU 123 OD2 ASP A 16 1620 3349 2235 139 -318 -727 O ATOM 124 N ILE A 17 63.801 11.984 20.315 1.00 11.87 N ANISOU 124 N ILE A 17 1429 1553 1417 -149 -60 270 N ATOM 125 CA ILE A 17 62.449 12.474 20.238 1.00 11.95 C ANISOU 125 CA ILE A 17 1158 1874 1397 -347 -15 187 C ATOM 126 C ILE A 17 61.908 12.483 18.798 1.00 10.47 C ANISOU 126 C ILE A 17 1220 1417 1242 -389 -2 105 C ATOM 127 O ILE A 17 60.982 13.197 18.483 1.00 13.62 O ANISOU 127 O ILE A 17 1137 2316 1594 -89 -99 -5 O ATOM 128 CB ILE A 17 62.331 13.806 20.962 1.00 12.04 C ANISOU 128 CB ILE A 17 1096 2055 1310 -297 -31 -75 C ATOM 129 CG1 ILE A 17 63.143 14.910 20.335 1.00 11.54 C ANISOU 129 CG1 ILE A 17 882 1868 1528 -113 14 41 C ATOM 130 CG2 ILE A 17 62.659 13.637 22.472 1.00 15.02 C ANISOU 130 CG2 ILE A 17 1872 2353 1341 -688 39 10 C ATOM 131 CD1 ILE A 17 62.600 16.308 20.644 1.00 13.09 C ANISOU 131 CD1 ILE A 17 998 1934 1921 131 -276 -70 C ATOM 132 N GLY A 18 62.573 11.645 17.972 1.00 11.35 N ANISOU 132 N GLY A 18 1375 1362 1470 -417 -45 115 N ATOM 133 CA GLY A 18 62.042 11.352 16.622 1.00 11.92 C ANISOU 133 CA GLY A 18 1335 1558 1524 -484 -19 -141 C ATOM 134 C GLY A 18 62.562 12.288 15.577 1.00 10.09 C ANISOU 134 C GLY A 18 1201 1237 1300 -203 -181 -121 C ATOM 135 O GLY A 18 62.144 12.132 14.397 1.00 11.03 O ANISOU 135 O GLY A 18 1289 1336 1464 -157 -395 -94 O ATOM 136 N ASP A 19 63.452 13.227 15.882 1.00 8.47 N ANISOU 136 N ASP A 19 927 979 1232 -42 -128 -41 N ATOM 137 CA ASP A 19 63.987 14.045 14.809 1.00 8.19 C ANISOU 137 CA ASP A 19 1020 887 1127 146 -215 19 C ATOM 138 C ASP A 19 64.750 13.147 13.827 1.00 8.42 C ANISOU 138 C ASP A 19 997 872 1252 101 -116 -8 C ATOM 139 O ASP A 19 65.482 12.223 14.246 1.00 9.89 O ANISOU 139 O ASP A 19 1278 1088 1298 330 -54 148 O ATOM 140 CB ASP A 19 64.969 15.105 15.291 1.00 7.32 C ANISOU 140 CB ASP A 19 733 822 1157 182 -135 165 C ATOM 141 CG ASP A 19 64.387 16.311 16.004 1.00 7.06 C ANISOU 141 CG ASP A 19 699 823 1094 107 -170 166 C ATOM 142 OD1 ASP A 19 63.128 16.511 15.937 1.00 7.33 O ANISOU 142 OD1 ASP A 19 718 852 1145 131 -29 186 O ATOM 143 OD2 ASP A 19 65.208 17.105 16.548 1.00 7.28 O ANISOU 143 OD2 ASP A 19 619 850 1230 134 -117 68 O ATOM 144 N PRO A 20 64.713 13.448 12.544 1.00 9.29 N ANISOU 144 N PRO A 20 1238 996 1210 218 -224 21 N ATOM 145 CA PRO A 20 65.680 12.847 11.599 1.00 10.07 C ANISOU 145 CA PRO A 20 1365 1111 1255 112 47 16 C ATOM 146 C PRO A 20 67.069 13.355 11.931 1.00 9.45 C ANISOU 146 C PRO A 20 1308 1072 1123 255 60 61 C ATOM 147 O PRO A 20 67.248 14.328 12.654 1.00 10.21 O ANISOU 147 O PRO A 20 1149 1126 1507 229 104 -122 O ATOM 148 CB PRO A 20 65.140 13.258 10.228 1.00 12.02 C ANISOU 148 CB PRO A 20 1771 1442 1241 286 -173 -153 C ATOM 149 CG PRO A 20 64.562 14.614 10.527 1.00 12.48 C ANISOU 149 CG PRO A 20 2022 1478 1125 585 -182 65 C ATOM 150 CD PRO A 20 63.893 14.490 11.865 1.00 9.50 C ANISOU 150 CD PRO A 20 1398 884 1238 180 -354 -128 C ATOM 151 N SER A 21 68.089 12.692 11.335 1.00 11.45 N ANISOU 151 N SER A 21 1478 1273 1493 519 -83 -64 N ATOM 152 CA SER A 21 69.499 13.023 11.626 1.00 12.47 C ANISOU 152 CA SER A 21 1266 1297 2060 575 36 3 C ATOM 153 C SER A 21 70.050 14.225 10.840 1.00 12.50 C ANISOU 153 C SER A 21 1402 1571 1659 778 385 106 C ATOM 154 O SER A 21 71.191 14.181 10.391 1.00 20.26 O ANISOU 154 O SER A 21 1447 2639 3421 1163 760 1022 O ATOM 155 CB ASER A 21 70.358 11.774 11.410 0.39 15.12 C ANISOU 155 CB ASER A 21 2064 1820 1719 1230 -87 196 C ATOM 156 CB BSER A 21 70.334 11.764 11.310 0.61 17.39 C ANISOU 156 CB BSER A 21 2167 1885 2393 1314 474 466 C ATOM 157 OG ASER A 21 70.021 10.933 12.502 0.39 17.76 O ANISOU 157 OG ASER A 21 2482 1749 2353 1243 192 460 O ATOM 158 OG BSER A 21 70.309 11.454 9.930 0.61 24.30 O ANISOU 158 OG BSER A 21 3274 2616 3114 1482 -235 -1192 O ATOM 159 N TYR A 22 69.264 15.252 10.634 1.00 10.64 N ANISOU 159 N TYR A 22 1043 1268 1630 475 161 -16 N ATOM 160 CA TYR A 22 69.632 16.417 9.881 1.00 10.70 C ANISOU 160 CA TYR A 22 1064 1429 1472 504 384 119 C ATOM 161 C TYR A 22 68.665 17.567 10.238 1.00 8.94 C ANISOU 161 C TYR A 22 788 1266 1258 381 23 44 C ATOM 162 O TYR A 22 67.536 17.277 10.727 1.00 9.12 O ANISOU 162 O TYR A 22 810 1210 1360 352 74 38 O ATOM 163 CB TYR A 22 69.556 16.136 8.340 1.00 13.77 C ANISOU 163 CB TYR A 22 1746 1739 1616 794 501 -39 C ATOM 164 CG TYR A 22 68.377 15.284 7.885 1.00 13.57 C ANISOU 164 CG TYR A 22 2153 1624 1252 580 417 -105 C ATOM 165 CD1 TYR A 22 67.089 15.824 7.772 1.00 13.88 C ANISOU 165 CD1 TYR A 22 2097 1633 1415 417 -46 -36 C ATOM 166 CD2 TYR A 22 68.524 13.943 7.491 1.00 17.52 C ANISOU 166 CD2 TYR A 22 2753 1647 2093 528 716 -95 C ATOM 167 CE1 TYR A 22 66.009 15.052 7.338 1.00 14.05 C ANISOU 167 CE1 TYR A 22 2501 1311 1395 406 -194 -4 C ATOM 168 CE2 TYR A 22 67.400 13.205 7.089 1.00 17.16 C ANISOU 168 CE2 TYR A 22 2942 1338 2078 544 873 -368 C ATOM 169 CZ TYR A 22 66.125 13.759 6.995 1.00 16.56 C ANISOU 169 CZ TYR A 22 3031 1603 1504 581 -65 -490 C ATOM 170 OH TYR A 22 65.113 12.927 6.595 1.00 19.54 O ANISOU 170 OH TYR A 22 3703 1526 2012 287 -635 -372 O ATOM 171 N PRO A 23 69.033 18.809 9.986 1.00 8.68 N ANISOU 171 N PRO A 23 716 1289 1211 260 3 64 N ATOM 172 CA PRO A 23 68.054 19.932 10.103 1.00 7.81 C ANISOU 172 CA PRO A 23 728 1176 992 144 79 -140 C ATOM 173 C PRO A 23 66.838 19.612 9.216 1.00 6.92 C ANISOU 173 C PRO A 23 671 942 951 149 18 45 C ATOM 174 O PRO A 23 66.955 19.026 8.154 1.00 7.60 O ANISOU 174 O PRO A 23 770 1065 981 224 -1 -12 O ATOM 175 CB PRO A 23 68.842 21.151 9.612 1.00 8.51 C ANISOU 175 CB PRO A 23 791 1262 1102 3 34 -73 C ATOM 176 CG PRO A 23 70.287 20.784 9.964 1.00 10.48 C ANISOU 176 CG PRO A 23 811 1811 1261 11 121 224 C ATOM 177 CD PRO A 23 70.366 19.300 9.600 1.00 10.81 C ANISOU 177 CD PRO A 23 749 1794 1465 202 120 68 C ATOM 178 N HIS A 24 65.661 20.075 9.685 1.00 6.57 N ANISOU 178 N HIS A 24 636 859 941 111 41 -19 N ATOM 179 CA HIS A 24 64.415 19.632 9.035 1.00 6.76 C ANISOU 179 CA HIS A 24 657 880 968 74 53 21 C ATOM 180 C HIS A 24 63.309 20.663 9.325 1.00 6.14 C ANISOU 180 C HIS A 24 713 687 875 65 32 32 C ATOM 181 O HIS A 24 63.378 21.424 10.283 1.00 7.28 O ANISOU 181 O HIS A 24 751 961 988 106 -49 -62 O ATOM 182 CB HIS A 24 63.987 18.247 9.512 1.00 7.02 C ANISOU 182 CB HIS A 24 809 808 986 89 -1 -20 C ATOM 183 CG HIS A 24 63.909 18.105 10.988 1.00 6.65 C ANISOU 183 CG HIS A 24 729 721 1013 209 -72 26 C ATOM 184 ND1 HIS A 24 65.034 17.959 11.790 1.00 7.04 N ANISOU 184 ND1 HIS A 24 666 876 1067 168 -24 15 N ATOM 185 CD2 HIS A 24 62.876 18.142 11.883 1.00 7.12 C ANISOU 185 CD2 HIS A 24 742 871 1026 -2 -33 86 C ATOM 186 CE1 HIS A 24 64.644 17.940 13.073 1.00 7.22 C ANISOU 186 CE1 HIS A 24 688 823 1163 207 -61 171 C ATOM 187 NE2 HIS A 24 63.318 18.047 13.185 1.00 6.72 N ANISOU 187 NE2 HIS A 24 666 739 1087 116 -51 78 N ATOM 188 N ILE A 25 62.307 20.625 8.430 1.00 6.97 N ANISOU 188 N ILE A 25 562 1031 991 81 22 -46 N ATOM 189 CA ILE A 25 61.035 21.357 8.661 1.00 7.04 C ANISOU 189 CA ILE A 25 593 887 1129 107 16 -205 C ATOM 190 C ILE A 25 60.004 20.349 9.079 1.00 7.09 C ANISOU 190 C ILE A 25 623 990 1014 91 14 -201 C ATOM 191 O ILE A 25 60.009 19.175 8.607 1.00 9.69 O ANISOU 191 O ILE A 25 983 1014 1593 -123 379 -308 O ATOM 192 CB AILE A 25 60.636 22.167 7.441 0.67 6.01 C ANISOU 192 CB AILE A 25 388 733 1105 221 -1 -293 C ATOM 193 CB BILE A 25 60.625 22.704 8.214 0.33 16.98 C ANISOU 193 CB BILE A 25 964 1995 3332 398 -217 1770 C ATOM 194 CG1AILE A 25 60.475 21.372 6.166 0.67 5.90 C ANISOU 194 CG1AILE A 25 431 639 1116 70 50 31 C ATOM 195 CG1BILE A 25 59.319 23.057 7.567 0.33 3.86 C ANISOU 195 CG1BILE A 25 549 381 501 167 160 -227 C ATOM 196 CG2 ILE A 25 61.679 23.191 7.299 1.00 13.33 C ANISOU 196 CG2 ILE A 25 1265 1319 2357 -323 -60 149 C ATOM 197 CD1AILE A 25 59.811 22.221 5.166 0.67 12.76 C ANISOU 197 CD1AILE A 25 1631 1917 1179 305 -101 390 C ATOM 198 CD1BILE A 25 59.039 24.029 6.445 0.33 4.15 C ANISOU 198 CD1BILE A 25 266 365 907 81 127 -25 C ATOM 199 N GLY A 26 59.126 20.681 10.020 1.00 6.51 N ANISOU 199 N GLY A 26 537 803 1074 85 -13 -1 N ATOM 200 CA GLY A 26 58.174 19.696 10.559 1.00 7.44 C ANISOU 200 CA GLY A 26 662 666 1429 46 121 -51 C ATOM 201 C GLY A 26 56.834 20.372 10.868 1.00 6.44 C ANISOU 201 C GLY A 26 583 783 1019 40 22 -73 C ATOM 202 O GLY A 26 56.747 21.567 11.175 1.00 7.00 O ANISOU 202 O GLY A 26 591 806 1199 53 38 -87 O ATOM 203 N ILE A 27 55.795 19.519 10.900 1.00 7.13 N ANISOU 203 N ILE A 27 614 711 1319 63 51 14 N ATOM 204 CA ILE A 27 54.445 19.903 11.368 1.00 6.99 C ANISOU 204 CA ILE A 27 593 762 1238 50 92 71 C ATOM 205 C ILE A 27 54.189 19.262 12.706 1.00 7.04 C ANISOU 205 C ILE A 27 586 821 1201 8 -35 4 C ATOM 206 O ILE A 27 54.243 18.006 12.811 1.00 7.72 O ANISOU 206 O ILE A 27 802 732 1328 53 29 40 O ATOM 207 CB ILE A 27 53.373 19.521 10.317 1.00 8.37 C ANISOU 207 CB ILE A 27 681 1278 1143 102 20 91 C ATOM 208 CG1AILE A 27 53.587 20.513 9.141 0.57 8.46 C ANISOU 208 CG1AILE A 27 845 1134 1156 13 31 -6 C ATOM 209 CG1BILE A 27 53.485 19.844 8.855 0.43 8.48 C ANISOU 209 CG1BILE A 27 732 1155 1256 166 -30 249 C ATOM 210 CG2 ILE A 27 51.983 19.734 10.922 1.00 8.10 C ANISOU 210 CG2 ILE A 27 572 1097 1332 -71 -54 3 C ATOM 211 CD1AILE A 27 52.864 20.156 7.902 0.57 8.75 C ANISOU 211 CD1AILE A 27 806 1156 1282 -132 -137 189 C ATOM 212 CD1BILE A 27 53.494 21.351 8.712 0.43 9.23 C ANISOU 212 CD1BILE A 27 700 1129 1592 68 -186 174 C ATOM 213 N ASP A 28 53.923 20.091 13.708 1.00 6.68 N ANISOU 213 N ASP A 28 596 732 1148 25 21 93 N ATOM 214 CA ASP A 28 53.758 19.671 15.104 1.00 6.58 C ANISOU 214 CA ASP A 28 534 713 1192 29 12 98 C ATOM 215 C ASP A 28 52.302 19.881 15.530 1.00 7.06 C ANISOU 215 C ASP A 28 641 890 1087 4 26 93 C ATOM 216 O ASP A 28 51.810 21.026 15.530 1.00 7.81 O ANISOU 216 O ASP A 28 662 821 1411 63 179 81 O ATOM 217 CB ASP A 28 54.685 20.456 16.035 1.00 7.06 C ANISOU 217 CB ASP A 28 649 836 1133 17 15 135 C ATOM 218 CG ASP A 28 56.170 20.229 15.714 1.00 6.95 C ANISOU 218 CG ASP A 28 625 624 1327 68 -32 54 C ATOM 219 OD1 ASP A 28 56.508 19.362 14.946 1.00 8.67 O ANISOU 219 OD1 ASP A 28 669 984 1562 108 -65 -107 O ATOM 220 OD2 ASP A 28 56.982 21.023 16.337 1.00 7.79 O ANISOU 220 OD2 ASP A 28 626 1026 1234 13 -2 -7 O ATOM 221 N ILE A 29 51.617 18.806 15.877 1.00 7.37 N ANISOU 221 N ILE A 29 563 818 1349 40 0 113 N ATOM 222 CA ILE A 29 50.189 18.865 16.289 1.00 8.01 C ANISOU 222 CA ILE A 29 577 1061 1330 25 98 186 C ATOM 223 C ILE A 29 50.172 18.349 17.736 1.00 8.41 C ANISOU 223 C ILE A 29 650 995 1470 -19 104 274 C ATOM 224 O ILE A 29 50.188 17.135 17.995 1.00 9.43 O ANISOU 224 O ILE A 29 864 989 1641 6 79 391 O ATOM 225 CB ILE A 29 49.267 18.053 15.391 1.00 8.89 C ANISOU 225 CB ILE A 29 630 1047 1616 -20 23 138 C ATOM 226 CG1 ILE A 29 49.394 18.399 13.901 1.00 9.37 C ANISOU 226 CG1 ILE A 29 762 1203 1507 -26 -221 113 C ATOM 227 CG2 ILE A 29 47.806 18.231 15.899 1.00 9.66 C ANISOU 227 CG2 ILE A 29 611 1164 1805 -68 50 117 C ATOM 228 CD1 ILE A 29 49.098 19.825 13.539 1.00 9.81 C ANISOU 228 CD1 ILE A 29 980 1172 1482 84 -213 12 C ATOM 229 N LYS A 30 50.203 19.285 18.708 1.00 8.68 N ANISOU 229 N LYS A 30 721 1132 1362 -26 92 246 N ATOM 230 CA LYS A 30 50.100 18.984 20.117 1.00 9.49 C ANISOU 230 CA LYS A 30 775 1316 1428 113 103 156 C ATOM 231 C LYS A 30 51.280 18.180 20.701 1.00 10.50 C ANISOU 231 C LYS A 30 994 1608 1288 250 142 302 C ATOM 232 O LYS A 30 51.191 17.622 21.804 1.00 12.42 O ANISOU 232 O LYS A 30 1093 1921 1588 365 258 658 O ATOM 233 CB LYS A 30 48.770 18.321 20.517 1.00 11.63 C ANISOU 233 CB LYS A 30 900 1757 1653 -19 230 613 C ATOM 234 CG LYS A 30 47.581 19.246 20.176 1.00 14.64 C ANISOU 234 CG LYS A 30 867 2672 1886 267 144 449 C ATOM 235 CD LYS A 30 46.247 18.746 20.574 1.00 20.54 C ANISOU 235 CD LYS A 30 948 3583 3082 335 427 1488 C ATOM 236 CE LYS A 30 45.797 17.383 20.147 1.00 37.13 C ANISOU 236 CE LYS A 30 1894 3615 8250 -733 1281 1442 C ATOM 237 NZ LYS A 30 44.516 17.099 20.914 1.00 37.88 N ANISOU 237 NZ LYS A 30 4798 4798 4798 0 0 0 N ATOM 238 N SER A 31 52.402 18.112 19.958 1.00 9.70 N ANISOU 238 N SER A 31 787 1340 1469 68 39 482 N ATOM 239 CA SER A 31 53.585 17.372 20.423 1.00 9.55 C ANISOU 239 CA SER A 31 798 1297 1445 93 -2 331 C ATOM 240 C SER A 31 54.789 17.908 19.649 1.00 8.32 C ANISOU 240 C SER A 31 829 963 1292 48 2 268 C ATOM 241 O SER A 31 54.686 18.195 18.442 1.00 8.61 O ANISOU 241 O SER A 31 877 995 1317 67 -39 234 O ATOM 242 CB SER A 31 53.445 15.907 20.125 1.00 10.72 C ANISOU 242 CB SER A 31 835 1296 1843 8 37 371 C ATOM 243 OG SER A 31 54.579 15.121 20.394 1.00 11.96 O ANISOU 243 OG SER A 31 934 1123 2374 -31 -35 492 O ATOM 244 N VAL A 32 55.951 17.924 20.320 1.00 8.39 N ANISOU 244 N VAL A 32 838 960 1310 -13 51 248 N ATOM 245 CA VAL A 32 57.232 18.228 19.671 1.00 8.79 C ANISOU 245 CA VAL A 32 752 1119 1388 16 20 149 C ATOM 246 C VAL A 32 57.689 17.139 18.712 1.00 8.87 C ANISOU 246 C VAL A 32 843 1018 1424 -143 -40 78 C ATOM 247 O VAL A 32 58.584 17.335 17.888 1.00 10.24 O ANISOU 247 O VAL A 32 942 1216 1638 -194 110 -19 O ATOM 248 CB VAL A 32 58.309 18.517 20.750 1.00 9.26 C ANISOU 248 CB VAL A 32 924 1189 1317 -62 20 17 C ATOM 249 CG1 VAL A 32 58.868 17.194 21.370 1.00 11.44 C ANISOU 249 CG1 VAL A 32 1011 1447 1780 188 -254 58 C ATOM 250 CG2 VAL A 32 59.481 19.382 20.250 1.00 12.67 C ANISOU 250 CG2 VAL A 32 1223 2010 1464 -638 330 -217 C ATOM 251 N ARG A 33 57.145 15.941 18.802 1.00 9.34 N ANISOU 251 N ARG A 33 800 1099 1563 -8 -30 121 N ATOM 252 CA ARG A 33 57.397 14.797 17.943 1.00 9.37 C ANISOU 252 CA ARG A 33 900 980 1592 106 -41 114 C ATOM 253 C ARG A 33 56.557 14.978 16.709 1.00 9.36 C ANISOU 253 C ARG A 33 752 1033 1685 9 -78 54 C ATOM 254 O ARG A 33 55.359 14.632 16.659 1.00 10.02 O ANISOU 254 O ARG A 33 815 984 1916 41 -146 107 O ATOM 255 CB ARG A 33 57.125 13.473 18.644 1.00 11.76 C ANISOU 255 CB ARG A 33 1122 1110 2124 -37 -361 386 C ATOM 256 CG ARG A 33 57.965 13.277 19.937 1.00 12.16 C ANISOU 256 CG ARG A 33 1200 1278 2027 53 -376 344 C ATOM 257 CD ARG A 33 57.643 11.971 20.621 1.00 19.20 C ANISOU 257 CD ARG A 33 2559 1437 3118 -124 -1302 928 C ATOM 258 NE ARG A 33 58.499 11.699 21.761 1.00 15.67 N ANISOU 258 NE ARG A 33 1922 1344 2539 189 -742 486 N ATOM 259 CZ ARG A 33 59.449 10.799 21.903 1.00 21.47 C ANISOU 259 CZ ARG A 33 1533 1362 5060 -111 -928 1222 C ATOM 260 NH1 ARG A 33 59.767 9.943 20.955 1.00 33.93 N ANISOU 260 NH1 ARG A 33 1893 1622 9060 531 -1246 -1057 N ATOM 261 NH2 ARG A 33 60.096 10.719 23.065 1.00 32.03 N ANISOU 261 NH2 ARG A 33 2328 2998 6543 -761 -2300 2724 N ATOM 262 N SER A 34 57.152 15.584 15.685 1.00 9.04 N ANISOU 262 N SER A 34 735 977 1637 58 -142 5 N ATOM 263 CA SER A 34 56.417 16.032 14.500 1.00 8.25 C ANISOU 263 CA SER A 34 690 749 1620 10 -109 8 C ATOM 264 C SER A 34 55.632 14.888 13.900 1.00 8.52 C ANISOU 264 C SER A 34 721 842 1595 60 -103 65 C ATOM 265 O SER A 34 56.108 13.764 13.808 1.00 10.25 O ANISOU 265 O SER A 34 907 837 2054 144 -301 -118 O ATOM 266 CB SER A 34 57.380 16.578 13.441 1.00 8.86 C ANISOU 266 CB SER A 34 656 939 1687 -1 -44 -35 C ATOM 267 OG SER A 34 58.241 17.591 13.922 1.00 9.03 O ANISOU 267 OG SER A 34 668 897 1782 -40 -15 -181 O ATOM 268 N LYS A 35 54.457 15.239 13.372 1.00 8.51 N ANISOU 268 N LYS A 35 683 801 1669 -36 -149 35 N ATOM 269 CA LYS A 35 53.640 14.305 12.587 1.00 8.85 C ANISOU 269 CA LYS A 35 776 788 1717 -62 -108 35 C ATOM 270 C LYS A 35 54.219 14.049 11.202 1.00 9.26 C ANISOU 270 C LYS A 35 770 956 1705 -100 -116 -8 C ATOM 271 O LYS A 35 53.949 12.957 10.618 1.00 10.92 O ANISOU 271 O LYS A 35 1164 1231 1651 -286 29 -164 O ATOM 272 CB LYS A 35 52.200 14.800 12.470 1.00 9.39 C ANISOU 272 CB LYS A 35 751 1213 1516 -77 -126 117 C ATOM 273 CG LYS A 35 51.536 15.041 13.815 1.00 9.30 C ANISOU 273 CG LYS A 35 858 1015 1575 18 -46 95 C ATOM 274 CD LYS A 35 51.589 13.914 14.834 1.00 10.55 C ANISOU 274 CD LYS A 35 966 1230 1712 -68 -141 233 C ATOM 275 CE LYS A 35 50.820 14.267 16.109 1.00 11.95 C ANISOU 275 CE LYS A 35 1035 1625 1768 -220 66 365 C ATOM 276 NZ LYS A 35 50.868 13.185 17.097 1.00 13.83 N ANISOU 276 NZ LYS A 35 1241 1760 2124 -342 63 471 N ATOM 277 N LYS A 36 54.955 14.974 10.636 1.00 9.15 N ANISOU 277 N LYS A 36 739 954 1698 -2 -16 -132 N ATOM 278 CA LYS A 36 55.556 14.883 9.305 1.00 10.04 C ANISOU 278 CA LYS A 36 925 1040 1754 -20 23 -51 C ATOM 279 C LYS A 36 56.779 15.799 9.289 1.00 8.66 C ANISOU 279 C LYS A 36 856 811 1540 83 44 -87 C ATOM 280 O LYS A 36 56.728 16.883 9.873 1.00 8.51 O ANISOU 280 O LYS A 36 757 923 1473 99 45 -60 O ATOM 281 CB LYS A 36 54.599 15.320 8.212 1.00 11.42 C ANISOU 281 CB LYS A 36 988 1444 1799 -270 -140 -39 C ATOM 282 CG LYS A 36 54.945 15.004 6.787 1.00 15.61 C ANISOU 282 CG LYS A 36 1625 2319 1840 -95 -196 24 C ATOM 283 CD LYS A 36 54.753 13.577 6.327 1.00 32.81 C ANISOU 283 CD LYS A 36 4328 3850 3979 -1240 1017 -2409 C ATOM 284 CE LYS A 36 54.566 13.364 4.828 1.00 36.77 C ANISOU 284 CE LYS A 36 6515 2907 4204 236 -1144 -1536 C ATOM 285 NZ LYS A 36 53.357 14.121 4.299 1.00 30.50 N ANISOU 285 NZ LYS A 36 3440 2666 5198 -707 1008 -1547 N ATOM 286 N THR A 37 57.869 15.339 8.656 1.00 9.21 N ANISOU 286 N THR A 37 905 775 1735 29 156 -138 N ATOM 287 CA THR A 37 59.094 16.121 8.495 1.00 8.71 C ANISOU 287 CA THR A 37 763 936 1527 36 64 -100 C ATOM 288 C THR A 37 59.583 16.074 7.043 1.00 8.86 C ANISOU 288 C THR A 37 777 991 1515 72 -23 -170 C ATOM 289 O THR A 37 59.232 15.120 6.315 1.00 10.08 O ANISOU 289 O THR A 37 957 1138 1641 -110 41 -359 O ATOM 290 CB THR A 37 60.213 15.718 9.449 1.00 10.60 C ANISOU 290 CB THR A 37 878 1360 1690 253 77 84 C ATOM 291 OG1 THR A 37 60.747 14.431 9.176 1.00 15.68 O ANISOU 291 OG1 THR A 37 1625 1706 2481 775 6 -116 O ATOM 292 CG2 THR A 37 59.821 15.779 10.887 1.00 12.76 C ANISOU 292 CG2 THR A 37 1054 2030 1643 478 -25 212 C ATOM 293 N ALA A 38 60.440 17.008 6.680 1.00 8.29 N ANISOU 293 N ALA A 38 881 805 1385 44 19 -239 N ATOM 294 CA ALA A 38 61.207 16.982 5.439 1.00 8.50 C ANISOU 294 CA ALA A 38 935 1004 1213 53 -27 -293 C ATOM 295 C ALA A 38 62.611 17.560 5.707 1.00 7.19 C ANISOU 295 C ALA A 38 890 716 1057 130 -14 -99 C ATOM 296 O ALA A 38 62.787 18.432 6.542 1.00 7.74 O ANISOU 296 O ALA A 38 774 993 1101 141 12 -218 O ATOM 297 CB ALA A 38 60.522 17.811 4.341 1.00 10.06 C ANISOU 297 CB ALA A 38 969 1399 1360 59 -198 -180 C ATOM 298 N LYS A 39 63.591 17.020 4.974 1.00 8.53 N ANISOU 298 N LYS A 39 913 921 1328 102 68 -285 N ATOM 299 CA LYS A 39 64.954 17.526 5.084 1.00 7.91 C ANISOU 299 CA LYS A 39 798 982 1152 153 -22 -215 C ATOM 300 C LYS A 39 65.029 19.020 4.691 1.00 7.41 C ANISOU 300 C LYS A 39 719 1040 987 106 88 -90 C ATOM 301 O LYS A 39 64.428 19.466 3.705 1.00 8.72 O ANISOU 301 O LYS A 39 1041 1068 1123 89 -150 -74 O ATOM 302 CB LYS A 39 65.874 16.720 4.179 1.00 9.41 C ANISOU 302 CB LYS A 39 949 1179 1360 316 29 -399 C ATOM 303 CG LYS A 39 67.354 17.095 4.286 1.00 10.06 C ANISOU 303 CG LYS A 39 933 1424 1372 222 120 -349 C ATOM 304 CD LYS A 39 68.216 15.999 3.617 1.00 16.14 C ANISOU 304 CD LYS A 39 1292 2731 1959 732 306 -913 C ATOM 305 CE ALYS A 39 69.634 15.901 4.150 0.56 15.35 C ANISOU 305 CE ALYS A 39 1484 1997 2208 859 96 -454 C ATOM 306 CE BLYS A 39 69.658 16.469 3.493 0.44 15.16 C ANISOU 306 CE BLYS A 39 1223 2183 2210 770 -56 -1154 C ATOM 307 NZ ALYS A 39 70.395 17.161 3.878 0.56 21.41 N ANISOU 307 NZ ALYS A 39 2291 2000 3644 239 -752 -721 N ATOM 308 NZ BLYS A 39 70.331 16.421 4.826 0.44 16.66 N ANISOU 308 NZ BLYS A 39 1591 2665 1919 368 163 -757 N ATOM 309 N TRP A 40 65.799 19.772 5.471 1.00 7.54 N ANISOU 309 N TRP A 40 700 1025 1068 63 87 -67 N ATOM 310 CA TRP A 40 65.963 21.216 5.273 1.00 7.58 C ANISOU 310 CA TRP A 40 705 1090 1015 62 41 -22 C ATOM 311 C TRP A 40 67.493 21.517 5.224 1.00 7.83 C ANISOU 311 C TRP A 40 700 1200 1003 -1 6 27 C ATOM 312 O TRP A 40 68.196 21.323 6.226 1.00 8.99 O ANISOU 312 O TRP A 40 870 1463 998 37 -31 82 O ATOM 313 CB TRP A 40 65.269 21.969 6.394 1.00 8.09 C ANISOU 313 CB TRP A 40 922 994 1083 66 150 14 C ATOM 314 CG TRP A 40 65.497 23.463 6.369 1.00 7.96 C ANISOU 314 CG TRP A 40 845 958 1148 168 160 4 C ATOM 315 CD1 TRP A 40 65.526 24.267 5.281 1.00 8.79 C ANISOU 315 CD1 TRP A 40 986 1048 1224 227 182 78 C ATOM 316 CD2 TRP A 40 65.683 24.312 7.523 1.00 7.77 C ANISOU 316 CD2 TRP A 40 642 1013 1224 95 142 -45 C ATOM 317 NE1 TRP A 40 65.786 25.575 5.641 1.00 10.20 N ANISOU 317 NE1 TRP A 40 1247 996 1538 130 439 101 N ATOM 318 CE2 TRP A 40 65.864 25.628 7.007 1.00 8.92 C ANISOU 318 CE2 TRP A 40 945 890 1470 163 401 44 C ATOM 319 CE3 TRP A 40 65.717 24.083 8.902 1.00 7.53 C ANISOU 319 CE3 TRP A 40 673 921 1196 122 54 -80 C ATOM 320 CZ2 TRP A 40 66.102 26.680 7.890 1.00 11.10 C ANISOU 320 CZ2 TRP A 40 1101 1116 1895 97 549 -235 C ATOM 321 CZ3 TRP A 40 65.960 25.143 9.761 1.00 9.34 C ANISOU 321 CZ3 TRP A 40 768 1266 1425 -65 165 -416 C ATOM 322 CH2 TRP A 40 66.144 26.439 9.228 1.00 10.69 C ANISOU 322 CH2 TRP A 40 1020 1093 1847 -145 384 -597 C ATOM 323 N ASN A 41 67.951 22.002 4.071 1.00 7.55 N ANISOU 323 N ASN A 41 663 1183 952 54 8 1 N ATOM 324 CA ASN A 41 69.360 22.384 3.903 1.00 8.46 C ANISOU 324 CA ASN A 41 674 1347 1115 61 15 40 C ATOM 325 C ASN A 41 69.570 23.783 4.432 1.00 8.85 C ANISOU 325 C ASN A 41 768 1488 1021 -107 -7 44 C ATOM 326 O ASN A 41 69.755 24.785 3.723 1.00 9.80 O ANISOU 326 O ASN A 41 1058 1455 1118 -204 -13 64 O ATOM 327 CB ASN A 41 69.764 22.164 2.450 1.00 9.30 C ANISOU 327 CB ASN A 41 797 1468 1180 8 160 -24 C ATOM 328 CG ASN A 41 69.813 20.684 2.110 1.00 9.22 C ANISOU 328 CG ASN A 41 798 1444 1175 208 157 -83 C ATOM 329 OD1 ASN A 41 70.412 19.865 2.820 1.00 13.47 O ANISOU 329 OD1 ASN A 41 1468 1707 1816 454 -118 -6 O ATOM 330 ND2 ASN A 41 69.175 20.294 1.013 1.00 11.17 N ANISOU 330 ND2 ASN A 41 1132 1709 1299 179 203 -314 N ATOM 331 N MET A 42 69.573 23.891 5.773 1.00 9.30 N ANISOU 331 N MET A 42 1029 1401 1017 -131 -137 154 N ATOM 332 CA MET A 42 69.699 25.158 6.460 1.00 9.66 C ANISOU 332 CA MET A 42 905 1607 1068 -194 -44 -3 C ATOM 333 C MET A 42 71.070 25.782 6.148 1.00 9.64 C ANISOU 333 C MET A 42 868 1557 1145 -125 -33 -20 C ATOM 334 O MET A 42 72.088 25.079 6.101 1.00 12.03 O ANISOU 334 O MET A 42 931 1762 1766 -88 137 -167 O ATOM 335 CB MET A 42 69.493 24.949 7.952 1.00 11.14 C ANISOU 335 CB MET A 42 793 2270 1065 -59 -44 -2 C ATOM 336 CG MET A 42 69.658 26.068 8.892 1.00 15.45 C ANISOU 336 CG MET A 42 1285 3076 1365 -84 64 -554 C ATOM 337 SD AMET A 42 71.423 26.172 9.445 0.46 9.38 S ANISOU 337 SD AMET A 42 991 1453 1033 317 -91 49 S ATOM 338 SD BMET A 42 71.294 26.556 9.405 0.55 29.48 S ANISOU 338 SD BMET A 42 2577 3964 4384 -1625 -525 -934 S ATOM 339 CE AMET A 42 71.276 27.582 10.490 0.46 17.19 C ANISOU 339 CE AMET A 42 2346 3065 960 825 -807 -1018 C ATOM 340 CE BMET A 42 70.729 28.258 9.407 0.55 26.59 C ANISOU 340 CE BMET A 42 1545 4034 4273 -1540 555 170 C ATOM 341 N GLN A 43 71.102 27.072 5.951 1.00 10.04 N ANISOU 341 N GLN A 43 717 1675 1330 -138 31 30 N ATOM 342 CA GLN A 43 72.320 27.876 5.620 1.00 10.21 C ANISOU 342 CA GLN A 43 787 1520 1476 -233 26 -188 C ATOM 343 C GLN A 43 72.587 28.886 6.716 1.00 10.38 C ANISOU 343 C GLN A 43 793 1730 1323 -85 -49 -180 C ATOM 344 O GLN A 43 71.919 29.906 6.862 1.00 12.88 O ANISOU 344 O GLN A 43 808 2043 1921 92 -208 -535 O ATOM 345 CB GLN A 43 72.139 28.573 4.294 1.00 11.43 C ANISOU 345 CB GLN A 43 1031 1898 1306 -433 111 -166 C ATOM 346 CG GLN A 43 72.019 27.609 3.112 1.00 13.40 C ANISOU 346 CG GLN A 43 1632 1925 1410 -536 190 -156 C ATOM 347 CD GLN A 43 72.107 28.263 1.731 1.00 15.82 C ANISOU 347 CD GLN A 43 1600 3025 1235 -950 325 -193 C ATOM 348 OE1 GLN A 43 71.296 27.983 0.786 1.00 13.73 O ANISOU 348 OE1 GLN A 43 1255 2303 1530 -177 45 -144 O ATOM 349 NE2 GLN A 43 73.144 28.996 1.553 1.00 18.78 N ANISOU 349 NE2 GLN A 43 2042 3477 1442 -1577 46 183 N ATOM 350 N ASN A 44 73.658 28.622 7.473 1.00 11.80 N ANISOU 350 N ASN A 44 867 1908 1597 16 -176 -254 N ATOM 351 CA ASN A 44 74.093 29.472 8.579 1.00 10.91 C ANISOU 351 CA ASN A 44 855 1775 1414 36 -97 -205 C ATOM 352 C ASN A 44 74.440 30.827 8.030 1.00 10.98 C ANISOU 352 C ASN A 44 689 1872 1508 -20 130 -291 C ATOM 353 O ASN A 44 75.304 30.993 7.158 1.00 14.51 O ANISOU 353 O ASN A 44 1077 2045 2254 -217 693 -402 O ATOM 354 CB ASN A 44 75.291 28.774 9.232 1.00 14.40 C ANISOU 354 CB ASN A 44 1063 2201 2072 425 -455 -363 C ATOM 355 CG ASN A 44 75.792 29.460 10.489 1.00 14.18 C ANISOU 355 CG ASN A 44 956 2577 1722 722 -193 -539 C ATOM 356 OD1 ASN A 44 75.526 30.631 10.772 1.00 14.32 O ANISOU 356 OD1 ASN A 44 1116 2524 1667 472 -173 -370 O ATOM 357 ND2 ASN A 44 76.604 28.795 11.288 1.00 16.53 N ANISOU 357 ND2 ASN A 44 1357 2744 2025 729 -413 -542 N ATOM 358 N GLY A 45 73.788 31.874 8.536 1.00 10.18 N ANISOU 358 N GLY A 45 635 1802 1335 -27 36 -224 N ATOM 359 CA GLY A 45 74.134 33.258 8.199 1.00 11.79 C ANISOU 359 CA GLY A 45 776 1797 1794 -82 -75 -241 C ATOM 360 C GLY A 45 73.425 33.859 6.995 1.00 10.88 C ANISOU 360 C GLY A 45 773 1614 1645 -141 38 -208 C ATOM 361 O GLY A 45 73.689 35.040 6.664 1.00 14.46 O ANISOU 361 O GLY A 45 1242 1708 2408 -302 -237 34 O ATOM 362 N LYS A 46 72.510 33.108 6.376 1.00 9.86 N ANISOU 362 N LYS A 46 705 1503 1444 -26 -13 -41 N ATOM 363 CA LYS A 46 71.783 33.618 5.222 1.00 10.20 C ANISOU 363 CA LYS A 46 734 1657 1388 5 97 129 C ATOM 364 C LYS A 46 70.315 33.887 5.594 1.00 8.52 C ANISOU 364 C LYS A 46 655 1151 1352 -209 114 49 C ATOM 365 O LYS A 46 69.763 33.226 6.453 1.00 12.24 O ANISOU 365 O LYS A 46 736 1861 1936 -3 101 726 O ATOM 366 CB LYS A 46 71.815 32.621 4.084 1.00 11.83 C ANISOU 366 CB LYS A 46 977 1957 1449 100 5 -201 C ATOM 367 CG LYS A 46 73.151 32.430 3.441 1.00 20.63 C ANISOU 367 CG LYS A 46 1436 3696 2511 606 581 -395 C ATOM 368 CD LYS A 46 74.022 33.600 3.095 1.00 33.77 C ANISOU 368 CD LYS A 46 2413 5934 4167 -381 1931 1008 C ATOM 369 CE LYS A 46 75.379 33.109 2.549 1.00 38.13 C ANISOU 369 CE LYS A 46 4829 4829 4829 0 0 0 C ATOM 370 NZ LYS A 46 76.526 33.679 3.325 1.00 81.50 N ANISOU 370 NZ LYS A 46 10322 10322 10322 0 0 0 N ATOM 371 N VAL A 47 69.702 34.880 4.979 1.00 10.22 N ANISOU 371 N VAL A 47 842 1319 1625 -13 390 240 N ATOM 372 CA VAL A 47 68.285 35.195 5.209 1.00 9.01 C ANISOU 372 CA VAL A 47 770 1192 1379 -62 148 67 C ATOM 373 C VAL A 47 67.402 34.221 4.412 1.00 8.60 C ANISOU 373 C VAL A 47 1004 1092 1093 156 143 -28 C ATOM 374 O VAL A 47 67.543 34.129 3.186 1.00 12.70 O ANISOU 374 O VAL A 47 2291 1383 1031 -54 321 38 O ATOM 375 CB VAL A 47 68.003 36.655 4.841 1.00 11.09 C ANISOU 375 CB VAL A 47 1179 1145 1785 37 91 134 C ATOM 376 CG1 VAL A 47 66.507 36.965 4.956 1.00 11.70 C ANISOU 376 CG1 VAL A 47 1258 1178 1899 230 -43 -312 C ATOM 377 CG2 VAL A 47 68.825 37.640 5.734 1.00 13.24 C ANISOU 377 CG2 VAL A 47 1092 1338 2476 -140 208 -177 C ATOM 378 N GLY A 48 66.509 33.530 5.122 1.00 7.53 N ANISOU 378 N GLY A 48 477 1132 1181 107 39 -116 N ATOM 379 CA GLY A 48 65.550 32.638 4.484 1.00 9.29 C ANISOU 379 CA GLY A 48 561 1406 1476 167 -33 -514 C ATOM 380 C GLY A 48 64.107 33.114 4.689 1.00 6.39 C ANISOU 380 C GLY A 48 592 738 1038 17 45 -92 C ATOM 381 O GLY A 48 63.851 34.011 5.481 1.00 7.18 O ANISOU 381 O GLY A 48 573 950 1136 89 28 -201 O ATOM 382 N THR A 49 63.191 32.448 3.975 1.00 6.64 N ANISOU 382 N THR A 49 522 905 1033 16 97 -156 N ATOM 383 CA THR A 49 61.765 32.751 4.028 1.00 6.86 C ANISOU 383 CA THR A 49 512 754 1278 57 93 -62 C ATOM 384 C THR A 49 60.953 31.482 4.192 1.00 6.52 C ANISOU 384 C THR A 49 496 866 1056 102 23 -132 C ATOM 385 O THR A 49 61.178 30.533 3.424 1.00 8.19 O ANISOU 385 O THR A 49 696 936 1401 -1 310 -277 O ATOM 386 CB THR A 49 61.316 33.495 2.783 1.00 9.64 C ANISOU 386 CB THR A 49 734 1250 1587 50 -47 330 C ATOM 387 OG1 THR A 49 62.064 34.720 2.706 1.00 17.13 O ANISOU 387 OG1 THR A 49 1014 1663 3669 -336 -596 1395 O ATOM 388 CG2 THR A 49 59.812 33.834 2.840 1.00 12.98 C ANISOU 388 CG2 THR A 49 797 1438 2576 52 -426 310 C ATOM 389 N ALA A 50 59.987 31.507 5.099 1.00 6.70 N ANISOU 389 N ALA A 50 485 836 1162 14 32 -276 N ATOM 390 CA ALA A 50 59.044 30.430 5.305 1.00 6.53 C ANISOU 390 CA ALA A 50 533 759 1128 107 86 -41 C ATOM 391 C ALA A 50 57.610 30.921 4.986 1.00 6.68 C ANISOU 391 C ALA A 50 508 832 1137 58 81 -75 C ATOM 392 O ALA A 50 57.246 32.028 5.372 1.00 8.08 O ANISOU 392 O ALA A 50 516 911 1568 140 40 -293 O ATOM 393 CB ALA A 50 59.082 29.940 6.731 1.00 9.84 C ANISOU 393 CB ALA A 50 698 1619 1329 69 9 322 C ATOM 394 N HIS A 51 56.830 30.022 4.411 1.00 6.75 N ANISOU 394 N HIS A 51 479 770 1252 94 85 -141 N ATOM 395 CA HIS A 51 55.409 30.232 4.086 1.00 7.08 C ANISOU 395 CA HIS A 51 502 833 1289 107 14 -287 C ATOM 396 C HIS A 51 54.593 29.078 4.688 1.00 7.36 C ANISOU 396 C HIS A 51 491 869 1366 59 81 -348 C ATOM 397 O HIS A 51 54.995 27.921 4.564 1.00 9.56 O ANISOU 397 O HIS A 51 591 802 2149 5 316 -348 O ATOM 398 CB HIS A 51 55.170 30.277 2.583 1.00 9.75 C ANISOU 398 CB HIS A 51 884 1345 1385 -69 -197 -106 C ATOM 399 CG HIS A 51 55.896 31.314 1.847 1.00 10.67 C ANISOU 399 CG HIS A 51 963 1704 1289 -101 -54 -92 C ATOM 400 ND1 HIS A 51 55.636 32.663 1.951 1.00 13.94 N ANISOU 400 ND1 HIS A 51 1529 1696 1940 286 301 607 N ATOM 401 CD2 HIS A 51 57.014 31.181 1.060 1.00 12.90 C ANISOU 401 CD2 HIS A 51 1283 2116 1381 -263 166 -291 C ATOM 402 CE1 HIS A 51 56.528 33.307 1.210 1.00 15.44 C ANISOU 402 CE1 HIS A 51 1741 2064 1917 -170 267 503 C ATOM 403 NE2 HIS A 51 57.319 32.452 0.634 1.00 14.34 N ANISOU 403 NE2 HIS A 51 1630 2474 1210 -561 103 -18 N ATOM 404 N ILE A 52 53.448 29.414 5.300 1.00 6.95 N ANISOU 404 N ILE A 52 464 759 1353 62 -1 -204 N ATOM 405 CA ILE A 52 52.551 28.436 5.920 1.00 7.31 C ANISOU 405 CA ILE A 52 449 845 1415 91 11 -158 C ATOM 406 C ILE A 52 51.119 28.734 5.387 1.00 7.32 C ANISOU 406 C ILE A 52 434 700 1580 100 -22 -95 C ATOM 407 O ILE A 52 50.712 29.880 5.353 1.00 9.09 O ANISOU 407 O ILE A 52 480 750 2138 108 -171 -276 O ATOM 408 CB ILE A 52 52.582 28.552 7.454 1.00 7.92 C ANISOU 408 CB ILE A 52 564 952 1420 24 -51 -155 C ATOM 409 CG1 ILE A 52 54.025 28.363 8.004 1.00 9.20 C ANISOU 409 CG1 ILE A 52 680 1093 1635 16 -87 -15 C ATOM 410 CG2 ILE A 52 51.627 27.526 8.072 1.00 8.93 C ANISOU 410 CG2 ILE A 52 659 1277 1374 -24 28 -43 C ATOM 411 CD1 ILE A 52 54.806 29.635 8.302 1.00 10.58 C ANISOU 411 CD1 ILE A 52 811 1607 1503 -154 -126 -473 C ATOM 412 N ILE A 53 50.402 27.687 4.979 1.00 6.51 N ANISOU 412 N ILE A 53 450 706 1258 93 25 -163 N ATOM 413 CA ILE A 53 49.066 27.831 4.382 1.00 6.92 C ANISOU 413 CA ILE A 53 461 871 1233 -22 -67 -171 C ATOM 414 C ILE A 53 48.147 26.722 4.921 1.00 6.88 C ANISOU 414 C ILE A 53 500 884 1167 49 -18 -252 C ATOM 415 O ILE A 53 48.548 25.575 5.194 1.00 7.84 O ANISOU 415 O ILE A 53 519 813 1574 83 -8 -79 O ATOM 416 CB ILE A 53 49.109 27.851 2.871 1.00 8.51 C ANISOU 416 CB ILE A 53 669 1258 1228 -101 -37 -165 C ATOM 417 CG1 ILE A 53 49.784 26.608 2.297 1.00 10.76 C ANISOU 417 CG1 ILE A 53 1163 1459 1366 116 -21 -330 C ATOM 418 CG2 ILE A 53 49.740 29.129 2.333 1.00 12.17 C ANISOU 418 CG2 ILE A 53 1445 1485 1579 -172 12 237 C ATOM 419 CD1 ILE A 53 49.762 26.549 0.775 1.00 15.39 C ANISOU 419 CD1 ILE A 53 1999 2367 1336 407 -19 -473 C ATOM 420 N TYR A 54 46.835 27.078 5.025 1.00 7.10 N ANISOU 420 N TYR A 54 495 742 1394 58 -15 -12 N ATOM 421 CA TYR A 54 45.815 26.146 5.466 1.00 7.11 C ANISOU 421 CA TYR A 54 447 848 1340 47 -101 -42 C ATOM 422 C TYR A 54 44.430 26.663 5.023 1.00 7.04 C ANISOU 422 C TYR A 54 514 795 1298 140 -46 -108 C ATOM 423 O TYR A 54 44.184 27.863 5.120 1.00 7.44 O ANISOU 423 O TYR A 54 485 761 1512 44 -32 -89 O ATOM 424 CB TYR A 54 45.808 26.041 7.003 1.00 8.10 C ANISOU 424 CB TYR A 54 581 1028 1391 -48 -13 -17 C ATOM 425 CG TYR A 54 44.724 25.128 7.558 1.00 8.20 C ANISOU 425 CG TYR A 54 621 1117 1302 59 -87 45 C ATOM 426 CD1 TYR A 54 44.901 23.758 7.652 1.00 7.87 C ANISOU 426 CD1 TYR A 54 658 1125 1136 -24 -39 35 C ATOM 427 CD2 TYR A 54 43.496 25.670 7.976 1.00 8.72 C ANISOU 427 CD2 TYR A 54 611 1313 1309 9 14 -92 C ATOM 428 CE1 TYR A 54 43.890 22.929 8.123 1.00 8.57 C ANISOU 428 CE1 TYR A 54 860 1133 1182 -126 -58 -72 C ATOM 429 CE2 TYR A 54 42.465 24.843 8.434 1.00 9.26 C ANISOU 429 CE2 TYR A 54 641 1529 1262 12 -59 -70 C ATOM 430 CZ TYR A 54 42.671 23.508 8.509 1.00 8.78 C ANISOU 430 CZ TYR A 54 764 1476 1013 -185 -48 135 C ATOM 431 OH TYR A 54 41.706 22.621 8.985 1.00 10.84 O ANISOU 431 OH TYR A 54 806 1816 1395 -338 16 130 O ATOM 432 N ASN A 55 43.507 25.738 4.727 1.00 6.92 N ANISOU 432 N ASN A 55 445 763 1356 14 9 -120 N ATOM 433 CA ASN A 55 42.095 26.146 4.624 1.00 7.36 C ANISOU 433 CA ASN A 55 556 900 1272 -2 -16 32 C ATOM 434 C ASN A 55 41.225 24.988 5.146 1.00 7.21 C ANISOU 434 C ASN A 55 561 834 1275 46 -27 -53 C ATOM 435 O ASN A 55 41.600 23.828 5.148 1.00 7.53 O ANISOU 435 O ASN A 55 628 947 1217 -48 -40 56 O ATOM 436 CB ASN A 55 41.699 26.634 3.224 1.00 8.25 C ANISOU 436 CB ASN A 55 589 958 1510 15 -115 180 C ATOM 437 CG ASN A 55 41.574 25.523 2.247 1.00 8.52 C ANISOU 437 CG ASN A 55 763 1219 1174 -30 -50 144 C ATOM 438 OD1 ASN A 55 40.582 24.755 2.296 1.00 9.20 O ANISOU 438 OD1 ASN A 55 870 1239 1299 -158 -179 144 O ATOM 439 ND2 ASN A 55 42.547 25.329 1.379 1.00 12.19 N ANISOU 439 ND2 ASN A 55 999 1934 1584 -262 242 -306 N ATOM 440 N SER A 56 39.992 25.389 5.561 1.00 7.75 N ANISOU 440 N SER A 56 582 1054 1234 -55 -18 -23 N ATOM 441 CA SER A 56 39.075 24.431 6.195 1.00 7.97 C ANISOU 441 CA SER A 56 666 1051 1237 -60 -11 115 C ATOM 442 C SER A 56 38.357 23.504 5.219 1.00 8.04 C ANISOU 442 C SER A 56 651 1009 1320 -46 64 130 C ATOM 443 O SER A 56 37.705 22.540 5.691 1.00 9.80 O ANISOU 443 O SER A 56 846 1153 1635 -228 116 73 O ATOM 444 CB SER A 56 38.051 25.199 7.040 1.00 9.22 C ANISOU 444 CB SER A 56 724 1426 1268 -52 89 31 C ATOM 445 OG SER A 56 37.251 25.978 6.170 1.00 9.70 O ANISOU 445 OG SER A 56 724 1178 1692 -6 146 26 O ATOM 446 N VAL A 57 38.404 23.790 3.924 1.00 8.18 N ANISOU 446 N VAL A 57 760 990 1282 -201 -163 130 N ATOM 447 CA VAL A 57 37.827 22.871 2.928 1.00 9.05 C ANISOU 447 CA VAL A 57 709 1237 1407 -151 -135 -2 C ATOM 448 C VAL A 57 38.724 21.660 2.781 1.00 9.33 C ANISOU 448 C VAL A 57 891 1263 1304 -91 -75 -7 C ATOM 449 O VAL A 57 38.299 20.501 2.775 1.00 12.89 O ANISOU 449 O VAL A 57 1051 1242 2482 -251 -142 -184 O ATOM 450 CB VAL A 57 37.535 23.581 1.600 1.00 9.65 C ANISOU 450 CB VAL A 57 882 1353 1343 -114 -127 45 C ATOM 451 CG1 VAL A 57 36.947 22.628 0.565 1.00 12.62 C ANISOU 451 CG1 VAL A 57 1057 2178 1441 -258 -215 -241 C ATOM 452 CG2 VAL A 57 36.519 24.697 1.856 1.00 13.59 C ANISOU 452 CG2 VAL A 57 1300 1820 1914 367 -524 -26 C ATOM 453 N ASP A 58 40.022 21.943 2.517 1.00 9.16 N ANISOU 453 N ASP A 58 817 1247 1330 -74 -195 -49 N ATOM 454 CA ASP A 58 40.992 20.865 2.263 1.00 9.44 C ANISOU 454 CA ASP A 58 1023 1322 1154 76 -111 -98 C ATOM 455 C ASP A 58 41.576 20.242 3.497 1.00 8.67 C ANISOU 455 C ASP A 58 953 1005 1254 -55 -143 -50 C ATOM 456 O ASP A 58 42.020 19.070 3.461 1.00 10.90 O ANISOU 456 O ASP A 58 1267 1149 1623 100 -305 -159 O ATOM 457 CB ASP A 58 42.098 21.422 1.380 1.00 10.23 C ANISOU 457 CB ASP A 58 926 1517 1348 205 -184 118 C ATOM 458 CG ASP A 58 41.608 21.893 0.022 1.00 11.26 C ANISOU 458 CG ASP A 58 1062 1822 1288 129 -105 131 C ATOM 459 OD1 ASP A 58 40.580 21.363 -0.460 1.00 13.46 O ANISOU 459 OD1 ASP A 58 1438 2064 1486 -126 -482 139 O ATOM 460 OD2 ASP A 58 42.321 22.761 -0.502 1.00 14.53 O ANISOU 460 OD2 ASP A 58 1270 2613 1500 -134 -41 504 O ATOM 461 N LYS A 59 41.646 20.965 4.599 1.00 8.38 N ANISOU 461 N LYS A 59 931 984 1189 -4 -202 -14 N ATOM 462 CA LYS A 59 42.109 20.424 5.885 1.00 8.33 C ANISOU 462 CA LYS A 59 810 1021 1257 48 -146 138 C ATOM 463 C LYS A 59 43.525 19.826 5.720 1.00 8.26 C ANISOU 463 C LYS A 59 774 1052 1235 -24 -85 -33 C ATOM 464 O LYS A 59 43.819 18.703 6.169 1.00 9.86 O ANISOU 464 O LYS A 59 835 1128 1692 -19 -57 263 O ATOM 465 CB LYS A 59 41.094 19.415 6.480 1.00 10.39 C ANISOU 465 CB LYS A 59 850 1471 1530 -52 12 270 C ATOM 466 CG LYS A 59 39.704 20.061 6.620 1.00 12.64 C ANISOU 466 CG LYS A 59 779 1889 2018 -44 -47 250 C ATOM 467 CD LYS A 59 38.681 19.076 7.142 1.00 18.59 C ANISOU 467 CD LYS A 59 1024 2631 3235 194 373 1655 C ATOM 468 CE ALYS A 59 37.252 19.639 7.202 0.66 20.72 C ANISOU 468 CE ALYS A 59 673 3780 3225 34 -119 1492 C ATOM 469 CE BLYS A 59 37.442 19.785 7.672 0.34 14.45 C ANISOU 469 CE BLYS A 59 1150 2678 1528 -454 102 -90 C ATOM 470 NZ ALYS A 59 37.229 20.945 7.941 0.66 24.41 N ANISOU 470 NZ ALYS A 59 2041 4042 2962 998 1120 1423 N ATOM 471 NZ BLYS A 59 36.614 20.240 6.515 0.34 17.15 N ANISOU 471 NZ BLYS A 59 933 1997 3426 -403 -103 1674 N ATOM 472 N ARG A 60 44.416 20.646 5.176 1.00 8.86 N ANISOU 472 N ARG A 60 773 903 1607 -25 -123 127 N ATOM 473 CA ARG A 60 45.816 20.264 4.964 1.00 9.16 C ANISOU 473 CA ARG A 60 786 1019 1589 -44 -41 -46 C ATOM 474 C ARG A 60 46.701 21.450 5.353 1.00 8.23 C ANISOU 474 C ARG A 60 781 974 1296 -30 2 32 C ATOM 475 O ARG A 60 46.649 22.527 4.763 1.00 9.58 O ANISOU 475 O ARG A 60 1165 1038 1345 -174 -255 112 O ATOM 476 CB ARG A 60 46.070 19.827 3.538 1.00 11.59 C ANISOU 476 CB ARG A 60 1171 1397 1727 -109 89 -359 C ATOM 477 CG ARG A 60 47.448 19.241 3.324 1.00 12.43 C ANISOU 477 CG ARG A 60 1307 1361 1939 61 138 -302 C ATOM 478 CD AARG A 60 47.545 18.783 1.860 0.55 21.39 C ANISOU 478 CD AARG A 60 3336 2360 2231 -324 1549 -572 C ATOM 479 CD BARG A 60 47.863 18.768 1.983 0.45 12.94 C ANISOU 479 CD BARG A 60 1462 1146 2189 -19 341 -429 C ATOM 480 NE AARG A 60 48.465 17.755 1.604 0.55 29.06 N ANISOU 480 NE AARG A 60 2295 4034 4440 -180 1462 -2061 N ATOM 481 NE BARG A 60 47.003 17.621 1.667 0.45 10.99 N ANISOU 481 NE BARG A 60 1705 1036 1332 -118 304 8 N ATOM 482 CZ AARG A 60 48.977 16.786 0.945 0.55 28.14 C ANISOU 482 CZ AARG A 60 2269 3141 5018 -186 -180 -2451 C ATOM 483 CZ BARG A 60 46.844 17.167 0.437 0.45 18.13 C ANISOU 483 CZ BARG A 60 2005 3089 1625 -1045 343 -639 C ATOM 484 NH1AARG A 60 50.026 16.082 1.374 0.55 39.08 N ANISOU 484 NH1AARG A 60 3190 4413 6879 716 -1634 -3559 N ATOM 485 NH1BARG A 60 47.413 17.767 -0.602 0.45 21.41 N ANISOU 485 NH1BARG A 60 1883 4732 1320 904 86 861 N ATOM 486 NH2AARG A 60 48.479 16.493 -0.259 0.55 31.71 N ANISOU 486 NH2AARG A 60 2400 4636 4713 -300 -46 -2354 N ATOM 487 NH2BARG A 60 46.095 16.102 0.257 0.45 34.27 N ANISOU 487 NH2BARG A 60 4340 4340 4340 0 0 0 N ATOM 488 N LEU A 61 47.539 21.245 6.366 1.00 7.80 N ANISOU 488 N LEU A 61 706 873 1311 19 146 5 N ATOM 489 CA LEU A 61 48.498 22.277 6.809 1.00 7.23 C ANISOU 489 CA LEU A 61 664 724 1292 -25 177 -130 C ATOM 490 C LEU A 61 49.798 22.047 6.021 1.00 7.39 C ANISOU 490 C LEU A 61 596 855 1286 22 121 -49 C ATOM 491 O LEU A 61 50.369 20.954 6.094 1.00 9.27 O ANISOU 491 O LEU A 61 817 828 1790 113 374 119 O ATOM 492 CB LEU A 61 48.720 22.118 8.305 1.00 7.84 C ANISOU 492 CB LEU A 61 668 971 1266 35 142 42 C ATOM 493 CG LEU A 61 49.674 23.163 8.938 1.00 8.14 C ANISOU 493 CG LEU A 61 709 1091 1215 110 81 -82 C ATOM 494 CD1 LEU A 61 49.267 24.590 8.655 1.00 8.70 C ANISOU 494 CD1 LEU A 61 921 963 1340 -56 -28 -100 C ATOM 495 CD2 LEU A 61 49.817 22.878 10.414 1.00 10.48 C ANISOU 495 CD2 LEU A 61 1115 1439 1329 151 -115 94 C ATOM 496 N SER A 62 50.244 23.078 5.286 1.00 6.85 N ANISOU 496 N SER A 62 560 729 1249 18 162 -106 N ATOM 497 CA SER A 62 51.428 22.966 4.401 1.00 7.28 C ANISOU 497 CA SER A 62 562 805 1331 -7 137 -91 C ATOM 498 C SER A 62 52.380 24.115 4.681 1.00 7.03 C ANISOU 498 C SER A 62 608 754 1243 84 112 -46 C ATOM 499 O SER A 62 51.980 25.213 5.051 1.00 7.76 O ANISOU 499 O SER A 62 526 775 1574 81 106 -166 O ATOM 500 CB SER A 62 51.009 22.939 2.938 1.00 8.94 C ANISOU 500 CB SER A 62 933 1107 1272 -115 86 -10 C ATOM 501 OG SER A 62 50.313 21.709 2.695 1.00 9.33 O ANISOU 501 OG SER A 62 875 1176 1407 -48 -63 -129 O ATOM 502 N ALA A 63 53.682 23.833 4.443 1.00 6.78 N ANISOU 502 N ALA A 63 557 740 1217 116 164 -100 N ATOM 503 CA ALA A 63 54.699 24.843 4.616 1.00 6.53 C ANISOU 503 CA ALA A 63 535 750 1133 11 156 -101 C ATOM 504 C ALA A 63 55.804 24.656 3.571 1.00 6.32 C ANISOU 504 C ALA A 63 518 709 1115 83 127 -102 C ATOM 505 O ALA A 63 56.067 23.515 3.112 1.00 7.35 O ANISOU 505 O ALA A 63 705 713 1304 51 240 -124 O ATOM 506 CB ALA A 63 55.321 24.779 6.021 1.00 8.50 C ANISOU 506 CB ALA A 63 834 1180 1136 12 59 -77 C ATOM 507 N VAL A 64 56.455 25.759 3.212 1.00 6.63 N ANISOU 507 N VAL A 64 529 716 1215 51 169 -238 N ATOM 508 CA VAL A 64 57.577 25.793 2.276 1.00 6.84 C ANISOU 508 CA VAL A 64 568 786 1180 59 207 -152 C ATOM 509 C VAL A 64 58.640 26.749 2.859 1.00 7.43 C ANISOU 509 C VAL A 64 615 944 1194 42 252 -146 C ATOM 510 O VAL A 64 58.293 27.789 3.412 1.00 9.51 O ANISOU 510 O VAL A 64 561 996 1967 6 301 -494 O ATOM 511 CB VAL A 64 57.141 26.288 0.893 1.00 9.14 C ANISOU 511 CB VAL A 64 807 1336 1244 146 162 109 C ATOM 512 CG1 VAL A 64 58.327 26.280 -0.095 1.00 13.70 C ANISOU 512 CG1 VAL A 64 1040 2774 1264 36 270 106 C ATOM 513 CG2 VAL A 64 56.082 25.419 0.291 1.00 11.66 C ANISOU 513 CG2 VAL A 64 1296 1685 1339 -163 -126 18 C ATOM 514 N VAL A 65 59.925 26.364 2.770 1.00 7.16 N ANISOU 514 N VAL A 65 507 863 1282 -12 197 -98 N ATOM 515 CA VAL A 65 61.012 27.206 3.237 1.00 6.81 C ANISOU 515 CA VAL A 65 587 761 1176 -30 150 -157 C ATOM 516 C VAL A 65 62.065 27.237 2.082 1.00 6.97 C ANISOU 516 C VAL A 65 529 918 1137 82 221 -97 C ATOM 517 O VAL A 65 62.339 26.230 1.441 1.00 8.73 O ANISOU 517 O VAL A 65 741 924 1570 60 475 -202 O ATOM 518 CB AVAL A 65 61.520 26.689 4.573 0.50 5.99 C ANISOU 518 CB AVAL A 65 339 664 1218 38 345 -4 C ATOM 519 CB BVAL A 65 61.847 26.853 4.429 0.50 8.35 C ANISOU 519 CB BVAL A 65 879 1167 1048 149 142 -344 C ATOM 520 CG1AVAL A 65 62.704 27.572 4.976 0.50 7.01 C ANISOU 520 CG1AVAL A 65 783 1093 721 100 305 -780 C ATOM 521 CG1BVAL A 65 62.217 25.354 4.508 0.50 7.11 C ANISOU 521 CG1BVAL A 65 491 1006 1140 -28 94 -84 C ATOM 522 CG2AVAL A 65 60.471 26.620 5.635 0.50 10.84 C ANISOU 522 CG2AVAL A 65 1196 1430 1391 280 503 299 C ATOM 523 CG2BVAL A 65 62.518 27.898 5.333 0.50 9.28 C ANISOU 523 CG2BVAL A 65 849 1423 1168 22 333 -713 C ATOM 524 N SER A 66 62.681 28.398 1.907 1.00 7.22 N ANISOU 524 N SER A 66 600 874 1200 -39 79 -125 N ATOM 525 CA SER A 66 63.707 28.577 0.855 1.00 8.41 C ANISOU 525 CA SER A 66 763 1269 1084 -156 217 -102 C ATOM 526 C SER A 66 64.712 29.645 1.265 1.00 6.53 C ANISOU 526 C SER A 66 685 743 993 97 156 139 C ATOM 527 O SER A 66 64.500 30.430 2.178 1.00 8.25 O ANISOU 527 O SER A 66 703 1176 1179 -71 278 -208 O ATOM 528 CB SER A 66 63.105 28.917 -0.514 1.00 10.58 C ANISOU 528 CB SER A 66 963 1650 1306 -265 -26 68 C ATOM 529 OG SER A 66 62.618 30.202 -0.553 1.00 13.97 O ANISOU 529 OG SER A 66 1226 1874 2079 -232 -259 334 O ATOM 530 N TYR A 67 65.834 29.648 0.517 1.00 7.48 N ANISOU 530 N TYR A 67 666 928 1177 12 171 -167 N ATOM 531 CA TYR A 67 66.791 30.736 0.471 1.00 7.48 C ANISOU 531 CA TYR A 67 651 985 1137 -51 197 -171 C ATOM 532 C TYR A 67 66.943 31.223 -0.965 1.00 7.86 C ANISOU 532 C TYR A 67 730 993 1189 55 130 -103 C ATOM 533 O TYR A 67 66.764 30.419 -1.906 1.00 8.44 O ANISOU 533 O TYR A 67 908 1047 1172 -7 205 -72 O ATOM 534 CB TYR A 67 68.171 30.301 0.994 1.00 8.98 C ANISOU 534 CB TYR A 67 624 1555 1149 30 72 -364 C ATOM 535 CG TYR A 67 68.238 29.881 2.437 1.00 8.30 C ANISOU 535 CG TYR A 67 512 1145 1418 25 -20 -118 C ATOM 536 CD1 TYR A 67 68.375 30.794 3.447 1.00 8.06 C ANISOU 536 CD1 TYR A 67 740 1141 1108 104 181 53 C ATOM 537 CD2 TYR A 67 68.203 28.540 2.824 1.00 14.82 C ANISOU 537 CD2 TYR A 67 1671 1156 2664 43 -924 128 C ATOM 538 CE1 TYR A 67 68.452 30.435 4.772 1.00 9.94 C ANISOU 538 CE1 TYR A 67 642 1894 1149 346 90 71 C ATOM 539 CE2 TYR A 67 68.275 28.145 4.138 1.00 17.55 C ANISOU 539 CE2 TYR A 67 1824 1442 3237 -358 -1100 960 C ATOM 540 CZ TYR A 67 68.401 29.119 5.110 1.00 13.66 C ANISOU 540 CZ TYR A 67 765 2338 1959 76 -145 1010 C ATOM 541 OH TYR A 67 68.549 28.663 6.402 1.00 21.38 O ANISOU 541 OH TYR A 67 1094 4434 2396 -88 -178 2029 O ATOM 542 N PRO A 68 67.402 32.455 -1.173 1.00 9.40 N ANISOU 542 N PRO A 68 1129 1043 1311 -189 348 -82 N ATOM 543 CA PRO A 68 67.805 32.874 -2.524 1.00 10.83 C ANISOU 543 CA PRO A 68 1615 1043 1356 -161 439 -117 C ATOM 544 C PRO A 68 68.869 31.883 -3.083 1.00 8.83 C ANISOU 544 C PRO A 68 1082 1043 1146 -209 194 -23 C ATOM 545 O PRO A 68 69.742 31.418 -2.379 1.00 10.04 O ANISOU 545 O PRO A 68 1084 1530 1107 -222 243 -184 O ATOM 546 CB PRO A 68 68.343 34.304 -2.337 1.00 14.32 C ANISOU 546 CB PRO A 68 2282 1157 1868 -435 930 -110 C ATOM 547 CG PRO A 68 67.631 34.737 -1.086 1.00 15.68 C ANISOU 547 CG PRO A 68 2863 993 1954 -501 945 -339 C ATOM 548 CD PRO A 68 67.612 33.533 -0.178 1.00 11.10 C ANISOU 548 CD PRO A 68 1448 1190 1474 -259 528 -329 C ATOM 549 N ASN A 69 68.801 31.629 -4.387 1.00 10.10 N ANISOU 549 N ASN A 69 1242 1316 1186 -95 145 -116 N ATOM 550 CA ASN A 69 69.761 30.788 -5.110 1.00 10.07 C ANISOU 550 CA ASN A 69 1342 1316 1073 -256 267 -168 C ATOM 551 C ASN A 69 69.673 29.330 -4.751 1.00 9.49 C ANISOU 551 C ASN A 69 1207 1225 1083 -239 294 -225 C ATOM 552 O ASN A 69 70.498 28.541 -5.251 1.00 11.52 O ANISOU 552 O ASN A 69 1463 1429 1377 -145 601 -165 O ATOM 553 CB ASN A 69 71.199 31.305 -5.019 1.00 12.80 C ANISOU 553 CB ASN A 69 1414 1617 1712 -428 673 -217 C ATOM 554 CG ASN A 69 71.327 32.767 -5.341 1.00 13.70 C ANISOU 554 CG ASN A 69 1443 1579 2054 -465 522 -90 C ATOM 555 OD1 ASN A 69 71.616 33.625 -4.495 1.00 29.87 O ANISOU 555 OD1 ASN A 69 6160 2152 2757 -2121 -1289 190 O ATOM 556 ND2 ASN A 69 71.014 33.200 -6.497 1.00 17.06 N ANISOU 556 ND2 ASN A 69 2869 1511 1942 -69 335 -217 N ATOM 557 N ALA A 70 68.664 28.910 -3.963 1.00 8.89 N ANISOU 557 N ALA A 70 895 1304 1096 -88 169 -9 N ATOM 558 CA ALA A 70 68.573 27.519 -3.501 1.00 7.84 C ANISOU 558 CA ALA A 70 703 1122 1080 -74 181 -214 C ATOM 559 C ALA A 70 67.169 26.934 -3.768 1.00 7.58 C ANISOU 559 C ALA A 70 763 1088 959 19 129 -134 C ATOM 560 O ALA A 70 66.186 27.673 -3.852 1.00 8.47 O ANISOU 560 O ALA A 70 783 1093 1260 87 115 -13 O ATOM 561 CB ALA A 70 68.902 27.408 -2.032 1.00 9.40 C ANISOU 561 CB ALA A 70 977 1260 1246 -147 -90 -53 C ATOM 562 N ASP A 71 67.132 25.627 -3.868 1.00 7.37 N ANISOU 562 N ASP A 71 674 1068 988 -2 163 -146 N ATOM 563 CA ASP A 71 65.869 24.880 -3.894 1.00 7.38 C ANISOU 563 CA ASP A 71 709 1070 956 65 128 -107 C ATOM 564 C ASP A 71 65.145 25.031 -2.558 1.00 7.28 C ANISOU 564 C ASP A 71 637 1088 972 87 107 -25 C ATOM 565 O ASP A 71 65.688 25.339 -1.533 1.00 10.28 O ANISOU 565 O ASP A 71 856 2000 955 -182 57 -214 O ATOM 566 CB ASP A 71 66.159 23.396 -4.173 1.00 7.93 C ANISOU 566 CB ASP A 71 769 1048 1122 42 190 -21 C ATOM 567 CG ASP A 71 66.725 23.107 -5.564 1.00 8.35 C ANISOU 567 CG ASP A 71 755 1273 1067 120 253 -128 C ATOM 568 OD1 ASP A 71 66.387 23.811 -6.563 1.00 9.33 O ANISOU 568 OD1 ASP A 71 1058 1300 1101 230 133 -148 O ATOM 569 OD2 ASP A 71 67.534 22.131 -5.615 1.00 9.66 O ANISOU 569 OD2 ASP A 71 1037 1318 1227 201 228 -204 O ATOM 570 N SER A 72 63.842 24.763 -2.615 1.00 7.68 N ANISOU 570 N SER A 72 714 1125 1006 -42 197 -171 N ATOM 571 CA SER A 72 62.972 24.804 -1.441 1.00 7.62 C ANISOU 571 CA SER A 72 790 997 1036 81 326 -121 C ATOM 572 C SER A 72 62.872 23.433 -0.769 1.00 7.21 C ANISOU 572 C SER A 72 608 973 1090 79 238 -127 C ATOM 573 O SER A 72 63.210 22.381 -1.352 1.00 7.90 O ANISOU 573 O SER A 72 790 997 1139 107 173 -181 O ATOM 574 CB ASER A 72 61.630 25.465 -1.678 0.29 9.39 C ANISOU 574 CB ASER A 72 1163 1200 1116 481 236 -143 C ATOM 575 CB BSER A 72 61.539 25.113 -1.937 0.71 10.04 C ANISOU 575 CB BSER A 72 935 1456 1330 533 478 259 C ATOM 576 OG ASER A 72 60.904 24.723 -2.637 0.29 11.41 O ANISOU 576 OG ASER A 72 1289 1631 1308 327 -114 -41 O ATOM 577 OG BSER A 72 61.492 26.281 -2.683 0.71 11.19 O ANISOU 577 OG BSER A 72 932 1342 1871 409 414 265 O ATOM 578 N ALA A 73 62.338 23.449 0.471 1.00 7.37 N ANISOU 578 N ALA A 73 696 764 1271 33 264 -165 N ATOM 579 CA ALA A 73 61.887 22.270 1.201 1.00 7.47 C ANISOU 579 CA ALA A 73 589 927 1254 92 186 -25 C ATOM 580 C ALA A 73 60.406 22.479 1.510 1.00 6.80 C ANISOU 580 C ALA A 73 620 888 1013 96 152 21 C ATOM 581 O ALA A 73 59.977 23.604 1.797 1.00 7.91 O ANISOU 581 O ALA A 73 611 796 1525 64 193 -213 O ATOM 582 CB ALA A 73 62.650 22.047 2.477 1.00 9.40 C ANISOU 582 CB ALA A 73 649 1301 1535 124 151 196 C ATOM 583 N THR A 74 59.634 21.382 1.513 1.00 7.19 N ANISOU 583 N THR A 74 617 774 1272 125 282 -119 N ATOM 584 CA THR A 74 58.185 21.490 1.809 1.00 7.28 C ANISOU 584 CA THR A 74 632 881 1185 41 174 -134 C ATOM 585 C THR A 74 57.739 20.316 2.627 1.00 6.88 C ANISOU 585 C THR A 74 584 793 1173 33 140 -229 C ATOM 586 O THR A 74 58.266 19.195 2.549 1.00 8.23 O ANISOU 586 O THR A 74 760 855 1435 165 266 -77 O ATOM 587 CB THR A 74 57.392 21.584 0.509 1.00 8.61 C ANISOU 587 CB THR A 74 855 1207 1130 31 126 -4 C ATOM 588 OG1 THR A 74 56.013 21.897 0.762 1.00 9.56 O ANISOU 588 OG1 THR A 74 804 1368 1369 111 -12 -1 O ATOM 589 CG2 THR A 74 57.435 20.344 -0.329 1.00 10.58 C ANISOU 589 CG2 THR A 74 955 1731 1237 -9 12 -429 C ATOM 590 N VAL A 75 56.687 20.561 3.435 1.00 7.26 N ANISOU 590 N VAL A 75 675 771 1243 49 212 -79 N ATOM 591 CA VAL A 75 56.039 19.492 4.232 1.00 7.57 C ANISOU 591 CA VAL A 75 643 800 1362 124 120 -16 C ATOM 592 C VAL A 75 54.542 19.796 4.300 1.00 7.81 C ANISOU 592 C VAL A 75 741 883 1269 41 217 -41 C ATOM 593 O VAL A 75 54.122 20.951 4.334 1.00 8.36 O ANISOU 593 O VAL A 75 693 804 1602 107 316 9 O ATOM 594 CB VAL A 75 56.720 19.411 5.618 1.00 9.31 C ANISOU 594 CB VAL A 75 1005 1187 1259 103 88 141 C ATOM 595 CG1 VAL A 75 56.549 20.635 6.480 1.00 9.91 C ANISOU 595 CG1 VAL A 75 929 1374 1370 -73 160 -73 C ATOM 596 CG2 VAL A 75 56.339 18.136 6.353 1.00 11.30 C ANISOU 596 CG2 VAL A 75 1359 1423 1404 -76 32 230 C ATOM 597 N SER A 76 53.747 18.718 4.336 1.00 7.99 N ANISOU 597 N SER A 76 610 825 1525 100 221 -41 N ATOM 598 CA SER A 76 52.292 18.831 4.461 1.00 9.27 C ANISOU 598 CA SER A 76 755 1041 1638 49 290 4 C ATOM 599 C SER A 76 51.748 17.731 5.384 1.00 9.23 C ANISOU 599 C SER A 76 716 965 1741 68 265 13 C ATOM 600 O SER A 76 52.318 16.636 5.448 1.00 10.61 O ANISOU 600 O SER A 76 894 909 2129 113 442 107 O ATOM 601 CB SER A 76 51.612 18.662 3.088 1.00 10.00 C ANISOU 601 CB SER A 76 914 1145 1646 60 145 -82 C ATOM 602 OG SER A 76 51.914 19.676 2.153 1.00 10.83 O ANISOU 602 OG SER A 76 961 1302 1752 60 174 40 O ATOM 603 N TYR A 77 50.609 18.029 6.028 1.00 8.90 N ANISOU 603 N TYR A 77 751 991 1555 -3 253 16 N ATOM 604 CA TYR A 77 49.978 17.052 6.894 1.00 8.74 C ANISOU 604 CA TYR A 77 688 943 1607 -49 160 68 C ATOM 605 C TYR A 77 48.447 17.301 6.867 1.00 7.90 C ANISOU 605 C TYR A 77 755 832 1342 -9 156 17 C ATOM 606 O TYR A 77 47.997 18.433 7.060 1.00 8.95 O ANISOU 606 O TYR A 77 807 883 1629 -18 171 -26 O ATOM 607 CB TYR A 77 50.525 17.129 8.317 1.00 9.30 C ANISOU 607 CB TYR A 77 832 997 1616 -80 31 10 C ATOM 608 CG TYR A 77 49.971 16.076 9.279 1.00 9.72 C ANISOU 608 CG TYR A 77 801 1274 1528 -148 -204 104 C ATOM 609 CD1 TYR A 77 50.232 14.733 9.053 1.00 11.75 C ANISOU 609 CD1 TYR A 77 1437 1189 1729 -186 -254 171 C ATOM 610 CD2 TYR A 77 49.218 16.442 10.390 1.00 10.79 C ANISOU 610 CD2 TYR A 77 754 1627 1619 -141 -137 198 C ATOM 611 CE1 TYR A 77 49.698 13.764 9.947 1.00 13.07 C ANISOU 611 CE1 TYR A 77 1762 1265 1817 -362 -316 67 C ATOM 612 CE2 TYR A 77 48.708 15.487 11.260 1.00 12.18 C ANISOU 612 CE2 TYR A 77 960 1934 1621 -110 -36 259 C ATOM 613 CZ TYR A 77 48.952 14.142 11.036 1.00 13.17 C ANISOU 613 CZ TYR A 77 1254 1794 1833 -355 -241 544 C ATOM 614 OH TYR A 77 48.485 13.200 11.901 1.00 17.97 O ANISOU 614 OH TYR A 77 2009 2286 2364 -507 -199 992 O ATOM 615 N ASP A 78 47.693 16.217 6.658 1.00 8.49 N ANISOU 615 N ASP A 78 742 906 1498 -45 104 112 N ATOM 616 CA ASP A 78 46.215 16.264 6.681 1.00 8.95 C ANISOU 616 CA ASP A 78 755 1079 1481 -110 25 115 C ATOM 617 C ASP A 78 45.739 16.329 8.134 1.00 9.38 C ANISOU 617 C ASP A 78 691 1212 1574 -125 23 293 C ATOM 618 O ASP A 78 45.953 15.387 8.902 1.00 11.36 O ANISOU 618 O ASP A 78 1036 1318 1855 79 248 476 O ATOM 619 CB ASP A 78 45.673 15.075 5.894 1.00 11.48 C ANISOU 619 CB ASP A 78 1118 1258 1879 -393 -82 186 C ATOM 620 CG AASP A 78 46.201 15.065 4.471 0.53 15.19 C ANISOU 620 CG AASP A 78 1746 2246 1637 307 -331 -330 C ATOM 621 CG BASP A 78 45.673 15.207 4.404 0.47 14.75 C ANISOU 621 CG BASP A 78 2004 1621 1841 -406 -653 -17 C ATOM 622 OD1AASP A 78 45.953 16.093 3.774 0.53 19.58 O ANISOU 622 OD1AASP A 78 3064 2481 1712 268 576 189 O ATOM 623 OD1BASP A 78 45.938 16.318 3.891 0.47 18.14 O ANISOU 623 OD1BASP A 78 2710 2281 1733 -1197 -798 447 O ATOM 624 OD2AASP A 78 46.981 14.187 4.014 0.53 23.37 O ANISOU 624 OD2AASP A 78 3153 2873 2634 843 127 -858 O ATOM 625 OD2BASP A 78 45.477 14.166 3.770 0.47 23.44 O ANISOU 625 OD2BASP A 78 3894 2271 2522 -1085 -1223 -453 O ATOM 626 N VAL A 79 45.065 17.400 8.501 1.00 8.99 N ANISOU 626 N VAL A 79 678 1245 1409 -12 57 202 N ATOM 627 CA VAL A 79 44.591 17.624 9.857 1.00 9.97 C ANISOU 627 CA VAL A 79 765 1561 1369 13 86 356 C ATOM 628 C VAL A 79 43.444 18.662 9.798 1.00 9.07 C ANISOU 628 C VAL A 79 691 1275 1393 -107 132 40 C ATOM 629 O VAL A 79 43.533 19.695 9.115 1.00 10.25 O ANISOU 629 O VAL A 79 789 1212 1798 -42 231 188 O ATOM 630 CB VAL A 79 45.726 18.139 10.800 1.00 11.53 C ANISOU 630 CB VAL A 79 824 2059 1389 89 41 91 C ATOM 631 CG1 VAL A 79 46.431 19.383 10.302 1.00 11.17 C ANISOU 631 CG1 VAL A 79 906 1743 1489 -20 -67 -334 C ATOM 632 CG2 VAL A 79 45.199 18.302 12.218 1.00 13.90 C ANISOU 632 CG2 VAL A 79 1353 2447 1350 323 3 75 C ATOM 633 N ASP A 80 42.350 18.292 10.487 1.00 9.46 N ANISOU 633 N ASP A 80 759 1212 1537 -27 116 158 N ATOM 634 CA ASP A 80 41.222 19.256 10.653 1.00 9.19 C ANISOU 634 CA ASP A 80 576 1231 1599 -60 42 25 C ATOM 635 C ASP A 80 41.486 20.110 11.872 1.00 9.29 C ANISOU 635 C ASP A 80 617 1477 1349 -26 57 105 C ATOM 636 O ASP A 80 41.305 19.657 12.998 1.00 10.12 O ANISOU 636 O ASP A 80 827 1432 1491 21 157 179 O ATOM 637 CB ASP A 80 39.903 18.498 10.815 1.00 10.64 C ANISOU 637 CB ASP A 80 773 1468 1701 -108 51 31 C ATOM 638 CG ASP A 80 38.721 19.466 10.771 1.00 12.20 C ANISOU 638 CG ASP A 80 661 1676 2185 -212 59 -41 C ATOM 639 OD1 ASP A 80 38.904 20.704 10.922 1.00 13.30 O ANISOU 639 OD1 ASP A 80 758 1646 2524 -47 -30 -150 O ATOM 640 OD2 ASP A 80 37.583 18.932 10.573 1.00 16.57 O ANISOU 640 OD2 ASP A 80 729 1960 3452 -166 -2 -392 O ATOM 641 N LEU A 81 41.993 21.332 11.652 1.00 9.63 N ANISOU 641 N LEU A 81 746 1514 1310 -278 -63 104 N ATOM 642 CA LEU A 81 42.356 22.182 12.770 1.00 10.19 C ANISOU 642 CA LEU A 81 956 1574 1247 -283 -65 173 C ATOM 643 C LEU A 81 41.201 22.553 13.671 1.00 11.10 C ANISOU 643 C LEU A 81 1138 1674 1302 -383 102 140 C ATOM 644 O LEU A 81 41.419 22.883 14.841 1.00 11.40 O ANISOU 644 O LEU A 81 1218 1647 1360 -299 91 114 O ATOM 645 CB LEU A 81 43.161 23.397 12.297 1.00 10.64 C ANISOU 645 CB LEU A 81 1067 1687 1190 -484 35 82 C ATOM 646 CG LEU A 81 44.553 23.055 11.736 1.00 10.98 C ANISOU 646 CG LEU A 81 1030 1840 1200 -502 -22 -36 C ATOM 647 CD1 LEU A 81 45.261 24.307 11.266 1.00 13.61 C ANISOU 647 CD1 LEU A 81 1318 2282 1445 -907 55 39 C ATOM 648 CD2 LEU A 81 45.450 22.301 12.730 1.00 13.16 C ANISOU 648 CD2 LEU A 81 1180 2246 1451 -303 -245 -111 C ATOM 649 N ASP A 82 39.955 22.485 13.165 1.00 10.45 N ANISOU 649 N ASP A 82 1086 1278 1509 -16 126 84 N ATOM 650 CA ASP A 82 38.824 22.752 14.064 1.00 11.31 C ANISOU 650 CA ASP A 82 1171 1286 1735 44 399 90 C ATOM 651 C ASP A 82 38.624 21.660 15.090 1.00 10.52 C ANISOU 651 C ASP A 82 877 1291 1730 -107 286 -26 C ATOM 652 O ASP A 82 37.889 21.914 16.041 1.00 12.13 O ANISOU 652 O ASP A 82 1204 1646 1645 -188 499 8 O ATOM 653 CB ASP A 82 37.626 23.018 13.186 1.00 15.15 C ANISOU 653 CB ASP A 82 1323 2203 2090 634 484 326 C ATOM 654 CG ASP A 82 37.807 24.395 12.500 1.00 23.35 C ANISOU 654 CG ASP A 82 1895 2637 4120 -624 -1449 1348 C ATOM 655 OD1 ASP A 82 38.497 25.304 13.034 1.00 23.64 O ANISOU 655 OD1 ASP A 82 2876 2343 3541 -14 -230 -237 O ATOM 656 OD2 ASP A 82 37.407 24.440 11.349 1.00 18.66 O ANISOU 656 OD2 ASP A 82 2064 1935 2914 -28 122 563 O ATOM 657 N ASN A 83 39.255 20.507 14.902 1.00 10.27 N ANISOU 657 N ASN A 83 890 1201 1714 -237 184 84 N ATOM 658 CA ASN A 83 39.240 19.467 15.901 1.00 11.12 C ANISOU 658 CA ASN A 83 933 1391 1797 -361 144 318 C ATOM 659 C ASN A 83 40.443 19.496 16.850 1.00 10.67 C ANISOU 659 C ASN A 83 1015 1309 1629 -277 188 205 C ATOM 660 O ASN A 83 40.550 18.621 17.751 1.00 15.32 O ANISOU 660 O ASN A 83 1466 2073 2138 -660 -144 785 O ATOM 661 CB ASN A 83 39.195 18.085 15.230 1.00 12.13 C ANISOU 661 CB ASN A 83 1217 1345 1934 -204 -126 286 C ATOM 662 CG ASN A 83 37.919 17.809 14.503 1.00 12.00 C ANISOU 662 CG ASN A 83 1071 1378 1999 -280 301 -48 C ATOM 663 OD1 ASN A 83 36.912 18.490 14.775 1.00 12.51 O ANISOU 663 OD1 ASN A 83 934 1628 2074 -280 154 113 O ATOM 664 ND2 ASN A 83 37.913 16.832 13.626 1.00 14.50 N ANISOU 664 ND2 ASN A 83 1324 1758 2293 -451 264 -319 N ATOM 665 N VAL A 84 41.343 20.399 16.645 1.00 9.92 N ANISOU 665 N VAL A 84 825 1064 1787 -109 122 145 N ATOM 666 CA VAL A 84 42.550 20.553 17.454 1.00 10.05 C ANISOU 666 CA VAL A 84 783 1187 1756 24 153 261 C ATOM 667 C VAL A 84 42.538 21.831 18.261 1.00 9.39 C ANISOU 667 C VAL A 84 823 1134 1522 -22 64 336 C ATOM 668 O VAL A 84 42.771 21.854 19.478 1.00 11.84 O ANISOU 668 O VAL A 84 1271 1454 1662 26 -61 334 O ATOM 669 CB VAL A 84 43.807 20.478 16.568 1.00 11.72 C ANISOU 669 CB VAL A 84 730 1454 2160 -17 238 22 C ATOM 670 CG1 VAL A 84 45.055 20.674 17.428 1.00 12.52 C ANISOU 670 CG1 VAL A 84 785 1722 2132 57 73 448 C ATOM 671 CG2 VAL A 84 43.854 19.224 15.728 1.00 13.04 C ANISOU 671 CG2 VAL A 84 1233 1719 1879 140 335 44 C ATOM 672 N LEU A 85 42.261 22.955 17.590 1.00 9.67 N ANISOU 672 N LEU A 85 716 1085 1783 -27 34 197 N ATOM 673 CA LEU A 85 42.347 24.294 18.194 1.00 9.47 C ANISOU 673 CA LEU A 85 767 1056 1685 45 55 224 C ATOM 674 C LEU A 85 40.971 24.833 18.568 1.00 9.84 C ANISOU 674 C LEU A 85 725 1187 1735 -57 125 172 C ATOM 675 O LEU A 85 39.953 24.428 17.976 1.00 11.21 O ANISOU 675 O LEU A 85 762 1353 2039 87 53 19 O ATOM 676 CB LEU A 85 42.943 25.258 17.155 1.00 9.58 C ANISOU 676 CB LEU A 85 753 1062 1734 7 105 224 C ATOM 677 CG LEU A 85 44.455 25.057 16.854 1.00 10.25 C ANISOU 677 CG LEU A 85 748 1112 1939 67 248 -21 C ATOM 678 CD1 LEU A 85 44.843 25.767 15.550 1.00 10.68 C ANISOU 678 CD1 LEU A 85 1047 1145 1765 -157 300 -260 C ATOM 679 CD2 LEU A 85 45.327 25.472 18.011 1.00 12.27 C ANISOU 679 CD2 LEU A 85 794 1640 2114 -40 -61 192 C ATOM 680 N PRO A 86 40.949 25.731 19.561 1.00 9.62 N ANISOU 680 N PRO A 86 811 1021 1733 63 150 243 N ATOM 681 CA PRO A 86 39.690 26.450 19.873 1.00 10.66 C ANISOU 681 CA PRO A 86 905 1327 1717 84 383 267 C ATOM 682 C PRO A 86 39.316 27.426 18.769 1.00 9.56 C ANISOU 682 C PRO A 86 774 1093 1677 29 176 105 C ATOM 683 O PRO A 86 40.094 27.712 17.829 1.00 10.89 O ANISOU 683 O PRO A 86 1014 1274 1748 86 377 289 O ATOM 684 CB PRO A 86 40.034 27.149 21.196 1.00 12.38 C ANISOU 684 CB PRO A 86 1360 1678 1551 273 409 357 C ATOM 685 CG PRO A 86 41.546 27.390 21.097 1.00 11.32 C ANISOU 685 CG PRO A 86 1247 1533 1414 125 171 76 C ATOM 686 CD PRO A 86 42.084 26.194 20.350 1.00 9.94 C ANISOU 686 CD PRO A 86 1046 1059 1577 62 65 260 C ATOM 687 N GLU A 87 38.085 27.959 18.832 1.00 9.45 N ANISOU 687 N GLU A 87 758 1190 1553 -27 150 79 N ATOM 688 CA GLU A 87 37.549 28.854 17.836 1.00 9.89 C ANISOU 688 CA GLU A 87 919 1050 1696 -104 -180 22 C ATOM 689 C GLU A 87 38.293 30.183 17.737 1.00 7.95 C ANISOU 689 C GLU A 87 470 1074 1402 36 -29 -18 C ATOM 690 O GLU A 87 38.353 30.794 16.652 1.00 8.96 O ANISOU 690 O GLU A 87 788 1181 1352 41 -10 -45 O ATOM 691 CB GLU A 87 36.030 29.111 18.235 1.00 16.90 C ANISOU 691 CB GLU A 87 693 1614 3957 -492 -540 698 C ATOM 692 CG GLU A 87 35.318 30.230 17.634 1.00 15.19 C ANISOU 692 CG GLU A 87 929 1546 3152 -54 292 126 C ATOM 693 CD GLU A 87 33.849 30.408 17.942 1.00 15.37 C ANISOU 693 CD GLU A 87 864 1747 3086 -96 358 -160 C ATOM 694 OE1 GLU A 87 33.258 29.603 18.742 1.00 16.25 O ANISOU 694 OE1 GLU A 87 791 2716 2514 39 287 198 O ATOM 695 OE2 GLU A 87 33.210 31.221 17.224 1.00 17.42 O ANISOU 695 OE2 GLU A 87 1146 2052 3258 64 631 209 O ATOM 696 N TRP A 88 38.790 30.675 18.876 1.00 7.44 N ANISOU 696 N TRP A 88 534 933 1292 25 102 67 N ATOM 697 CA TRP A 88 39.633 31.871 18.963 1.00 7.50 C ANISOU 697 CA TRP A 88 468 979 1334 9 46 111 C ATOM 698 C TRP A 88 41.043 31.419 19.408 1.00 7.28 C ANISOU 698 C TRP A 88 568 775 1355 15 -4 232 C ATOM 699 O TRP A 88 41.181 30.612 20.305 1.00 8.05 O ANISOU 699 O TRP A 88 590 1166 1228 33 39 241 O ATOM 700 CB TRP A 88 39.090 32.863 19.973 1.00 8.02 C ANISOU 700 CB TRP A 88 624 1119 1228 98 -15 63 C ATOM 701 CG TRP A 88 37.850 33.584 19.514 1.00 8.10 C ANISOU 701 CG TRP A 88 550 1173 1278 97 115 -7 C ATOM 702 CD1 TRP A 88 36.526 33.232 19.750 1.00 8.66 C ANISOU 702 CD1 TRP A 88 676 1176 1356 34 30 15 C ATOM 703 CD2 TRP A 88 37.805 34.782 18.733 1.00 7.93 C ANISOU 703 CD2 TRP A 88 602 931 1406 158 -61 -146 C ATOM 704 NE1 TRP A 88 35.678 34.156 19.165 1.00 9.47 N ANISOU 704 NE1 TRP A 88 607 1220 1682 98 106 -131 N ATOM 705 CE2 TRP A 88 36.432 35.124 18.543 1.00 8.33 C ANISOU 705 CE2 TRP A 88 679 976 1432 204 -49 -182 C ATOM 706 CE3 TRP A 88 38.771 35.618 18.190 1.00 8.04 C ANISOU 706 CE3 TRP A 88 672 1066 1242 149 56 -101 C ATOM 707 CZ2 TRP A 88 36.057 36.256 17.819 1.00 9.09 C ANISOU 707 CZ2 TRP A 88 792 1021 1557 270 -217 -191 C ATOM 708 CZ3 TRP A 88 38.405 36.751 17.503 1.00 9.47 C ANISOU 708 CZ3 TRP A 88 951 862 1696 155 52 -22 C ATOM 709 CH2 TRP A 88 37.067 37.080 17.321 1.00 9.67 C ANISOU 709 CH2 TRP A 88 1061 983 1540 273 -74 -106 C ATOM 710 N VAL A 89 42.051 31.995 18.721 1.00 7.25 N ANISOU 710 N VAL A 89 464 819 1403 34 21 217 N ATOM 711 CA VAL A 89 43.465 31.648 18.955 1.00 6.87 C ANISOU 711 CA VAL A 89 453 915 1178 83 20 107 C ATOM 712 C VAL A 89 44.304 32.909 18.996 1.00 6.85 C ANISOU 712 C VAL A 89 490 918 1131 63 47 39 C ATOM 713 O VAL A 89 43.862 33.999 18.579 1.00 7.59 O ANISOU 713 O VAL A 89 512 907 1395 23 -13 72 O ATOM 714 CB VAL A 89 43.985 30.680 17.864 1.00 7.16 C ANISOU 714 CB VAL A 89 437 948 1270 -12 17 54 C ATOM 715 CG1 VAL A 89 43.261 29.332 17.937 1.00 8.82 C ANISOU 715 CG1 VAL A 89 755 901 1613 -32 104 38 C ATOM 716 CG2 VAL A 89 43.900 31.320 16.503 1.00 7.93 C ANISOU 716 CG2 VAL A 89 599 1054 1288 136 25 272 C ATOM 717 N ARG A 90 45.559 32.764 19.406 1.00 6.84 N ANISOU 717 N ARG A 90 496 874 1165 45 5 91 N ATOM 718 CA ARG A 90 46.601 33.751 19.064 1.00 6.60 C ANISOU 718 CA ARG A 90 487 720 1237 6 42 94 C ATOM 719 C ARG A 90 47.603 33.054 18.133 1.00 6.82 C ANISOU 719 C ARG A 90 468 812 1248 183 -42 90 C ATOM 720 O ARG A 90 47.758 31.836 18.167 1.00 8.00 O ANISOU 720 O ARG A 90 608 822 1535 105 125 2 O ATOM 721 CB ARG A 90 47.256 34.412 20.265 1.00 7.70 C ANISOU 721 CB ARG A 90 505 983 1366 49 67 -31 C ATOM 722 CG ARG A 90 46.420 35.571 20.855 1.00 7.49 C ANISOU 722 CG ARG A 90 652 935 1188 83 89 21 C ATOM 723 CD ARG A 90 47.204 36.458 21.778 1.00 8.79 C ANISOU 723 CD ARG A 90 722 1138 1396 77 72 -119 C ATOM 724 NE ARG A 90 46.489 37.686 22.120 1.00 9.14 N ANISOU 724 NE ARG A 90 899 1144 1345 91 169 -56 N ATOM 725 CZ ARG A 90 45.718 37.895 23.183 1.00 10.66 C ANISOU 725 CZ ARG A 90 1589 1058 1305 152 284 -83 C ATOM 726 NH1 ARG A 90 45.490 36.912 24.030 1.00 14.87 N ANISOU 726 NH1 ARG A 90 2176 1872 1465 616 647 426 N ATOM 727 NH2 ARG A 90 45.101 39.060 23.340 1.00 15.32 N ANISOU 727 NH2 ARG A 90 2147 1401 2129 493 967 -3 N ATOM 728 N VAL A 91 48.278 33.878 17.317 1.00 6.71 N ANISOU 728 N VAL A 91 434 711 1340 62 64 19 N ATOM 729 CA VAL A 91 49.327 33.399 16.408 1.00 6.37 C ANISOU 729 CA VAL A 91 465 765 1132 57 3 -39 C ATOM 730 C VAL A 91 50.671 34.049 16.844 1.00 6.05 C ANISOU 730 C VAL A 91 453 822 967 106 28 12 C ATOM 731 O VAL A 91 50.694 35.156 17.379 1.00 6.59 O ANISOU 731 O VAL A 91 484 797 1159 150 -11 -33 O ATOM 732 CB VAL A 91 48.997 33.700 14.949 1.00 7.36 C ANISOU 732 CB VAL A 91 612 978 1135 56 -141 9 C ATOM 733 CG1 VAL A 91 47.700 32.969 14.573 1.00 9.86 C ANISOU 733 CG1 VAL A 91 963 1104 1586 -162 -521 163 C ATOM 734 CG2 VAL A 91 48.932 35.160 14.623 1.00 7.73 C ANISOU 734 CG2 VAL A 91 684 1006 1173 86 -64 90 C ATOM 735 N GLY A 92 51.763 33.292 16.621 1.00 5.73 N ANISOU 735 N GLY A 92 435 706 982 138 -28 -14 N ATOM 736 CA GLY A 92 53.038 33.747 17.117 1.00 6.42 C ANISOU 736 CA GLY A 92 386 863 1129 85 15 -45 C ATOM 737 C GLY A 92 54.233 33.101 16.440 1.00 5.79 C ANISOU 737 C GLY A 92 458 808 880 117 -54 34 C ATOM 738 O GLY A 92 54.111 32.184 15.623 1.00 5.87 O ANISOU 738 O GLY A 92 480 750 947 67 -49 -20 O ATOM 739 N LEU A 93 55.392 33.632 16.834 1.00 5.73 N ANISOU 739 N LEU A 93 427 781 914 155 -83 -110 N ATOM 740 CA LEU A 93 56.709 33.056 16.498 1.00 5.55 C ANISOU 740 CA LEU A 93 390 829 838 147 -52 -60 C ATOM 741 C LEU A 93 57.419 32.683 17.802 1.00 5.57 C ANISOU 741 C LEU A 93 445 730 888 150 -47 -28 C ATOM 742 O LEU A 93 57.342 33.448 18.778 1.00 6.84 O ANISOU 742 O LEU A 93 679 854 1003 257 -173 -81 O ATOM 743 CB LEU A 93 57.545 34.050 15.678 1.00 6.00 C ANISOU 743 CB LEU A 93 403 805 1016 34 -52 -2 C ATOM 744 CG LEU A 93 56.939 34.504 14.356 1.00 6.88 C ANISOU 744 CG LEU A 93 539 1030 980 44 -83 150 C ATOM 745 CD1 LEU A 93 57.742 35.626 13.732 1.00 7.78 C ANISOU 745 CD1 LEU A 93 689 946 1250 -10 -7 185 C ATOM 746 CD2 LEU A 93 56.813 33.358 13.369 1.00 9.50 C ANISOU 746 CD2 LEU A 93 1293 1223 1006 -339 -206 -5 C ATOM 747 N SER A 94 58.129 31.588 17.814 1.00 5.80 N ANISOU 747 N SER A 94 491 805 853 161 -94 -12 N ATOM 748 CA SER A 94 58.864 31.102 19.011 1.00 6.28 C ANISOU 748 CA SER A 94 516 946 864 251 -93 60 C ATOM 749 C SER A 94 60.254 30.642 18.553 1.00 5.80 C ANISOU 749 C SER A 94 481 819 850 184 -86 -38 C ATOM 750 O SER A 94 60.444 30.175 17.440 1.00 6.80 O ANISOU 750 O SER A 94 553 1131 836 246 -126 -116 O ATOM 751 CB SER A 94 58.121 29.922 19.635 1.00 6.94 C ANISOU 751 CB SER A 94 614 1010 947 268 -46 121 C ATOM 752 OG SER A 94 58.659 29.573 20.906 1.00 7.72 O ANISOU 752 OG SER A 94 904 1093 862 291 6 103 O ATOM 753 N ALA A 95 61.220 30.714 19.484 1.00 6.37 N ANISOU 753 N ALA A 95 563 989 807 286 -122 23 N ATOM 754 CA ALA A 95 62.548 30.139 19.190 1.00 6.09 C ANISOU 754 CA ALA A 95 477 871 909 182 -100 -26 C ATOM 755 C ALA A 95 63.246 29.849 20.519 1.00 5.67 C ANISOU 755 C ALA A 95 518 763 820 101 -49 11 C ATOM 756 O ALA A 95 62.885 30.365 21.588 1.00 7.04 O ANISOU 756 O ALA A 95 589 1127 893 218 -150 -2 O ATOM 757 CB ALA A 95 63.405 31.077 18.371 1.00 7.07 C ANISOU 757 CB ALA A 95 649 983 987 184 -34 89 C ATOM 758 N SER A 96 64.283 29.022 20.433 1.00 6.08 N ANISOU 758 N SER A 96 492 862 900 137 -122 79 N ATOM 759 CA SER A 96 65.051 28.640 21.607 1.00 6.28 C ANISOU 759 CA SER A 96 515 952 859 161 -111 -27 C ATOM 760 C SER A 96 66.491 28.300 21.216 1.00 6.06 C ANISOU 760 C SER A 96 555 745 947 111 -138 95 C ATOM 761 O SER A 96 66.834 28.049 20.071 1.00 6.67 O ANISOU 761 O SER A 96 530 1006 935 222 -103 13 O ATOM 762 CB SER A 96 64.408 27.437 22.307 1.00 6.73 C ANISOU 762 CB SER A 96 569 1053 871 189 -53 67 C ATOM 763 OG SER A 96 64.440 26.335 21.418 1.00 7.85 O ANISOU 763 OG SER A 96 818 1034 1057 11 -67 98 O ATOM 764 N THR A 97 67.314 28.311 22.284 1.00 6.83 N ANISOU 764 N THR A 97 491 1007 1034 222 -140 -18 N ATOM 765 CA THR A 97 68.679 27.766 22.304 1.00 6.59 C ANISOU 765 CA THR A 97 476 953 1013 168 -116 96 C ATOM 766 C THR A 97 68.804 26.913 23.562 1.00 6.85 C ANISOU 766 C THR A 97 505 963 1073 99 -152 64 C ATOM 767 O THR A 97 67.982 26.972 24.486 1.00 7.86 O ANISOU 767 O THR A 97 627 1187 1098 87 -53 255 O ATOM 768 CB THR A 97 69.730 28.890 22.267 1.00 7.00 C ANISOU 768 CB THR A 97 546 925 1123 74 -67 26 C ATOM 769 OG1 THR A 97 69.628 29.641 23.459 1.00 7.62 O ANISOU 769 OG1 THR A 97 669 1051 1103 75 -125 100 O ATOM 770 CG2 THR A 97 69.606 29.772 21.060 1.00 7.01 C ANISOU 770 CG2 THR A 97 668 800 1130 128 -128 62 C ATOM 771 N GLY A 98 69.867 26.080 23.602 1.00 7.90 N ANISOU 771 N GLY A 98 722 1033 1173 258 -103 283 N ATOM 772 CA GLY A 98 70.165 25.269 24.774 1.00 9.05 C ANISOU 772 CA GLY A 98 696 1285 1371 288 -66 292 C ATOM 773 C GLY A 98 71.653 25.349 25.129 1.00 8.50 C ANISOU 773 C GLY A 98 827 1250 1073 238 -116 215 C ATOM 774 O GLY A 98 72.184 26.465 25.219 1.00 9.93 O ANISOU 774 O GLY A 98 925 1310 1443 143 -236 72 O ATOM 775 N LEU A 99 72.299 24.196 25.203 1.00 9.33 N ANISOU 775 N LEU A 99 709 1334 1413 311 -119 459 N ATOM 776 CA LEU A 99 73.773 24.255 25.340 1.00 9.45 C ANISOU 776 CA LEU A 99 749 1458 1295 197 -145 207 C ATOM 777 C LEU A 99 74.398 24.587 23.982 1.00 9.67 C ANISOU 777 C LEU A 99 856 1418 1308 151 -107 232 C ATOM 778 O LEU A 99 75.457 25.169 23.950 1.00 16.50 O ANISOU 778 O LEU A 99 998 3765 1352 -629 -168 289 O ATOM 779 CB LEU A 99 74.309 23.001 25.996 1.00 10.07 C ANISOU 779 CB LEU A 99 849 1526 1355 288 -204 272 C ATOM 780 CG LEU A 99 73.726 22.672 27.359 1.00 11.32 C ANISOU 780 CG LEU A 99 1074 1825 1296 295 -183 245 C ATOM 781 CD1 LEU A 99 74.465 21.477 27.958 1.00 12.92 C ANISOU 781 CD1 LEU A 99 1283 1863 1643 91 -279 560 C ATOM 782 CD2 LEU A 99 73.726 23.805 28.392 1.00 14.87 C ANISOU 782 CD2 LEU A 99 1456 2420 1634 337 -131 -285 C ATOM 783 N TYR A 100 73.752 24.215 22.879 1.00 8.77 N ANISOU 783 N TYR A 100 720 1214 1317 114 -47 233 N ATOM 784 CA TYR A 100 74.094 24.672 21.527 1.00 7.73 C ANISOU 784 CA TYR A 100 562 1039 1264 138 -114 56 C ATOM 785 C TYR A 100 73.215 25.890 21.224 1.00 7.54 C ANISOU 785 C TYR A 100 588 1083 1123 82 -97 30 C ATOM 786 O TYR A 100 72.152 26.086 21.852 1.00 8.86 O ANISOU 786 O TYR A 100 628 1256 1401 262 13 205 O ATOM 787 CB TYR A 100 73.897 23.559 20.505 1.00 8.22 C ANISOU 787 CB TYR A 100 691 1020 1336 158 -192 96 C ATOM 788 CG TYR A 100 74.803 22.354 20.631 1.00 8.03 C ANISOU 788 CG TYR A 100 666 1042 1270 167 -193 18 C ATOM 789 CD1 TYR A 100 74.472 21.273 21.431 1.00 9.29 C ANISOU 789 CD1 TYR A 100 933 1040 1471 169 56 106 C ATOM 790 CD2 TYR A 100 76.019 22.281 19.951 1.00 9.14 C ANISOU 790 CD2 TYR A 100 869 1199 1320 256 -9 152 C ATOM 791 CE1 TYR A 100 75.292 20.140 21.530 1.00 11.50 C ANISOU 791 CE1 TYR A 100 1175 1216 1871 319 234 342 C ATOM 792 CE2 TYR A 100 76.848 21.182 20.068 1.00 9.91 C ANISOU 792 CE2 TYR A 100 900 1346 1427 357 262 109 C ATOM 793 CZ TYR A 100 76.473 20.086 20.822 1.00 10.43 C ANISOU 793 CZ TYR A 100 1152 1277 1434 439 69 190 C ATOM 794 OH TYR A 100 77.332 19.035 20.873 1.00 13.19 O ANISOU 794 OH TYR A 100 1689 1340 1858 832 364 270 O ATOM 795 N LYS A 101 73.634 26.777 20.310 1.00 7.92 N ANISOU 795 N LYS A 101 609 1036 1290 169 -105 44 N ATOM 796 CA LYS A 101 73.022 28.093 20.188 1.00 7.94 C ANISOU 796 CA LYS A 101 590 1029 1325 160 -44 77 C ATOM 797 C LYS A 101 73.102 28.662 18.782 1.00 7.39 C ANISOU 797 C LYS A 101 567 855 1319 118 -98 42 C ATOM 798 O LYS A 101 73.856 28.212 17.918 1.00 8.76 O ANISOU 798 O LYS A 101 799 1094 1353 186 55 35 O ATOM 799 CB LYS A 101 73.621 29.026 21.222 1.00 10.30 C ANISOU 799 CB LYS A 101 1140 1213 1465 165 -453 -20 C ATOM 800 CG LYS A 101 75.048 29.364 20.980 1.00 15.95 C ANISOU 800 CG LYS A 101 1578 2283 2050 -840 -719 680 C ATOM 801 CD LYS A 101 75.956 29.896 22.027 1.00 20.30 C ANISOU 801 CD LYS A 101 1229 3275 3017 -138 -720 -871 C ATOM 802 CE LYS A 101 77.363 30.062 21.572 1.00 21.29 C ANISOU 802 CE LYS A 101 1213 3801 2877 252 -480 -1061 C ATOM 803 NZ LYS A 101 78.285 28.895 21.352 1.00 19.87 N ANISOU 803 NZ LYS A 101 1390 2874 3101 -59 -237 -45 N ATOM 804 N GLU A 102 72.322 29.733 18.545 1.00 7.48 N ANISOU 804 N GLU A 102 568 1021 1184 85 -16 8 N ATOM 805 CA GLU A 102 72.196 30.467 17.298 1.00 7.18 C ANISOU 805 CA GLU A 102 515 894 1251 46 -26 78 C ATOM 806 C GLU A 102 71.455 31.742 17.545 1.00 7.30 C ANISOU 806 C GLU A 102 505 967 1232 -11 -30 58 C ATOM 807 O GLU A 102 70.718 31.825 18.574 1.00 7.82 O ANISOU 807 O GLU A 102 772 838 1287 118 69 70 O ATOM 808 CB GLU A 102 71.454 29.644 16.242 1.00 7.13 C ANISOU 808 CB GLU A 102 638 779 1227 77 -67 130 C ATOM 809 CG GLU A 102 69.939 29.504 16.526 1.00 6.72 C ANISOU 809 CG GLU A 102 552 857 1082 122 -66 99 C ATOM 810 CD GLU A 102 69.269 28.336 15.866 1.00 6.95 C ANISOU 810 CD GLU A 102 557 870 1151 40 -89 315 C ATOM 811 OE1 GLU A 102 69.863 27.359 15.466 1.00 7.55 O ANISOU 811 OE1 GLU A 102 694 758 1347 84 -119 76 O ATOM 812 OE2 GLU A 102 67.934 28.422 15.729 1.00 7.96 O ANISOU 812 OE2 GLU A 102 605 1018 1328 25 -170 57 O ATOM 813 N THR A 103 71.585 32.748 16.678 1.00 7.50 N ANISOU 813 N THR A 103 535 923 1322 81 17 90 N ATOM 814 CA THR A 103 70.638 33.864 16.654 1.00 8.09 C ANISOU 814 CA THR A 103 625 870 1503 22 -5 64 C ATOM 815 C THR A 103 69.307 33.346 16.024 1.00 7.14 C ANISOU 815 C THR A 103 801 764 1083 223 -78 71 C ATOM 816 O THR A 103 69.291 32.499 15.149 1.00 8.61 O ANISOU 816 O THR A 103 878 1083 1229 349 -96 -101 O ATOM 817 CB THR A 103 71.098 35.043 15.805 1.00 10.58 C ANISOU 817 CB THR A 103 929 1013 1977 76 187 240 C ATOM 818 OG1 THR A 103 71.156 34.677 14.390 1.00 11.85 O ANISOU 818 OG1 THR A 103 1012 1563 1817 110 192 461 O ATOM 819 CG2 THR A 103 72.447 35.536 16.186 1.00 11.95 C ANISOU 819 CG2 THR A 103 892 1021 2516 -50 93 431 C ATOM 820 N ASN A 104 68.216 33.929 16.524 1.00 7.21 N ANISOU 820 N ASN A 104 676 863 1132 215 -116 -24 N ATOM 821 CA ASN A 104 66.886 33.610 15.987 1.00 7.22 C ANISOU 821 CA ASN A 104 689 868 1119 177 -187 -143 C ATOM 822 C ASN A 104 66.174 34.921 15.632 1.00 7.46 C ANISOU 822 C ASN A 104 680 991 1093 219 -144 53 C ATOM 823 O ASN A 104 65.223 35.390 16.270 1.00 8.26 O ANISOU 823 O ASN A 104 880 1037 1146 314 -13 59 O ATOM 824 CB ASN A 104 66.106 32.780 16.974 1.00 7.65 C ANISOU 824 CB ASN A 104 672 903 1261 171 -171 -3 C ATOM 825 CG ASN A 104 66.688 31.388 17.181 1.00 7.27 C ANISOU 825 CG ASN A 104 488 1036 1170 94 -139 -28 C ATOM 826 OD1 ASN A 104 67.119 31.046 18.347 1.00 9.91 O ANISOU 826 OD1 ASN A 104 1048 1299 1324 337 -288 -58 O ATOM 827 ND2 ASN A 104 66.735 30.654 16.167 1.00 6.21 N ANISOU 827 ND2 ASN A 104 590 651 1059 227 -256 62 N ATOM 828 N THR A 105 66.708 35.551 14.573 1.00 7.15 N ANISOU 828 N THR A 105 605 871 1176 225 -117 -22 N ATOM 829 CA THR A 105 66.356 36.899 14.197 1.00 7.22 C ANISOU 829 CA THR A 105 551 972 1152 127 -81 37 C ATOM 830 C THR A 105 65.246 36.890 13.144 1.00 6.65 C ANISOU 830 C THR A 105 544 758 1161 92 -76 19 C ATOM 831 O THR A 105 65.356 36.235 12.116 1.00 8.19 O ANISOU 831 O THR A 105 677 1236 1121 355 -68 -163 O ATOM 832 CB THR A 105 67.594 37.626 13.617 1.00 8.34 C ANISOU 832 CB THR A 105 608 1088 1394 3 -62 -8 C ATOM 833 OG1 THR A 105 68.722 37.452 14.479 1.00 10.16 O ANISOU 833 OG1 THR A 105 636 1611 1519 -53 -102 -135 O ATOM 834 CG2 THR A 105 67.327 39.136 13.407 1.00 10.58 C ANISOU 834 CG2 THR A 105 949 1178 1793 -239 -68 258 C ATOM 835 N ILE A 106 64.171 37.641 13.426 1.00 6.81 N ANISOU 835 N ILE A 106 557 866 1101 135 -78 -110 N ATOM 836 CA ILE A 106 63.042 37.799 12.479 1.00 6.75 C ANISOU 836 CA ILE A 106 501 861 1139 100 -52 7 C ATOM 837 C ILE A 106 63.115 39.187 11.847 1.00 6.28 C ANISOU 837 C ILE A 106 451 736 1140 56 -39 5 C ATOM 838 O ILE A 106 63.147 40.215 12.568 1.00 7.02 O ANISOU 838 O ILE A 106 669 804 1130 67 1 -81 O ATOM 839 CB ILE A 106 61.705 37.585 13.236 1.00 6.66 C ANISOU 839 CB ILE A 106 555 856 1057 97 29 18 C ATOM 840 CG1 ILE A 106 61.640 36.228 13.925 1.00 7.22 C ANISOU 840 CG1 ILE A 106 640 900 1137 70 33 41 C ATOM 841 CG2 ILE A 106 60.527 37.793 12.275 1.00 7.06 C ANISOU 841 CG2 ILE A 106 601 859 1155 -8 -63 125 C ATOM 842 CD1 ILE A 106 61.738 35.030 13.018 1.00 8.52 C ANISOU 842 CD1 ILE A 106 991 805 1359 46 77 -4 C ATOM 843 N LEU A 107 63.163 39.186 10.520 1.00 6.39 N ANISOU 843 N LEU A 107 521 747 1100 63 -65 -42 N ATOM 844 CA LEU A 107 63.270 40.430 9.761 1.00 6.91 C ANISOU 844 CA LEU A 107 581 826 1153 36 -36 13 C ATOM 845 C LEU A 107 61.889 40.901 9.236 1.00 6.99 C ANISOU 845 C LEU A 107 516 805 1269 80 19 -2 C ATOM 846 O LEU A 107 61.700 42.107 9.018 1.00 8.84 O ANISOU 846 O LEU A 107 708 870 1699 25 -71 123 O ATOM 847 CB LEU A 107 64.206 40.236 8.549 1.00 8.67 C ANISOU 847 CB LEU A 107 638 1132 1443 47 163 172 C ATOM 848 CG ALEU A 107 65.661 39.995 8.867 0.77 10.36 C ANISOU 848 CG ALEU A 107 509 1482 1850 7 120 -67 C ATOM 849 CG BLEU A 107 65.632 40.727 8.556 0.23 17.22 C ANISOU 849 CG BLEU A 107 728 3771 1883 -356 252 -699 C ATOM 850 CD1ALEU A 107 66.015 38.719 9.480 0.77 24.74 C ANISOU 850 CD1ALEU A 107 965 2638 5566 752 406 1606 C ATOM 851 CD1BLEU A 107 66.290 40.768 9.907 0.23 8.99 C ANISOU 851 CD1BLEU A 107 181 1305 1845 239 276 411 C ATOM 852 CD2 LEU A 107 66.481 39.974 7.533 1.00 20.87 C ANISOU 852 CD2 LEU A 107 1040 4347 2345 94 567 -682 C ATOM 853 N SER A 108 60.934 39.984 9.112 1.00 6.75 N ANISOU 853 N SER A 108 440 818 1244 59 33 58 N ATOM 854 CA SER A 108 59.585 40.361 8.631 1.00 7.11 C ANISOU 854 CA SER A 108 468 783 1382 120 -18 239 C ATOM 855 C SER A 108 58.630 39.211 9.044 1.00 6.64 C ANISOU 855 C SER A 108 414 779 1268 119 -90 -37 C ATOM 856 O SER A 108 59.043 38.061 9.172 1.00 7.06 O ANISOU 856 O SER A 108 512 760 1343 141 -27 40 O ATOM 857 CB SER A 108 59.540 40.564 7.138 1.00 9.62 C ANISOU 857 CB SER A 108 666 1536 1362 197 -101 223 C ATOM 858 OG SER A 108 59.714 39.391 6.419 1.00 14.29 O ANISOU 858 OG SER A 108 1639 2027 1628 786 -182 -133 O ATOM 859 N TRP A 109 57.343 39.594 9.209 1.00 6.44 N ANISOU 859 N TRP A 109 467 670 1248 81 -27 2 N ATOM 860 CA TRP A 109 56.313 38.598 9.529 1.00 6.46 C ANISOU 860 CA TRP A 109 499 618 1277 105 -6 -38 C ATOM 861 C TRP A 109 54.975 39.159 9.013 1.00 6.45 C ANISOU 861 C TRP A 109 468 670 1251 78 -23 -36 C ATOM 862 O TRP A 109 54.603 40.282 9.389 1.00 7.24 O ANISOU 862 O TRP A 109 559 730 1395 123 -20 -95 O ATOM 863 CB TRP A 109 56.225 38.379 11.029 1.00 7.15 C ANISOU 863 CB TRP A 109 602 841 1207 84 -61 -86 C ATOM 864 CG TRP A 109 55.225 37.372 11.512 1.00 6.76 C ANISOU 864 CG TRP A 109 491 877 1138 79 10 -29 C ATOM 865 CD1 TRP A 109 54.723 36.293 10.850 1.00 7.23 C ANISOU 865 CD1 TRP A 109 615 837 1229 5 87 23 C ATOM 866 CD2 TRP A 109 54.594 37.317 12.813 1.00 7.21 C ANISOU 866 CD2 TRP A 109 752 811 1107 188 -55 -44 C ATOM 867 NE1 TRP A 109 53.829 35.583 11.623 1.00 7.60 N ANISOU 867 NE1 TRP A 109 673 891 1252 -54 95 -44 N ATOM 868 CE2 TRP A 109 53.729 36.218 12.833 1.00 7.58 C ANISOU 868 CE2 TRP A 109 668 877 1265 159 122 120 C ATOM 869 CE3 TRP A 109 54.640 38.141 13.928 1.00 9.27 C ANISOU 869 CE3 TRP A 109 1032 1225 1178 1 100 -139 C ATOM 870 CZ2 TRP A 109 52.967 35.921 13.977 1.00 8.53 C ANISOU 870 CZ2 TRP A 109 993 884 1282 168 182 29 C ATOM 871 CZ3 TRP A 109 53.861 37.844 15.054 1.00 10.77 C ANISOU 871 CZ3 TRP A 109 1659 1208 1125 -64 159 -13 C ATOM 872 CH2 TRP A 109 53.028 36.739 15.047 1.00 10.22 C ANISOU 872 CH2 TRP A 109 1348 1035 1405 104 280 -51 C ATOM 873 N SER A 110 54.258 38.370 8.238 1.00 6.74 N ANISOU 873 N SER A 110 418 701 1377 145 -43 -108 N ATOM 874 CA SER A 110 52.913 38.714 7.768 1.00 7.46 C ANISOU 874 CA SER A 110 447 765 1552 172 -127 -96 C ATOM 875 C SER A 110 51.968 37.529 8.014 1.00 6.96 C ANISOU 875 C SER A 110 501 711 1366 211 -107 -174 C ATOM 876 O SER A 110 52.368 36.392 8.075 1.00 7.52 O ANISOU 876 O SER A 110 509 727 1551 135 4 -224 O ATOM 877 CB ASER A 110 52.912 39.185 6.354 0.69 9.99 C ANISOU 877 CB ASER A 110 761 1175 1765 334 -169 317 C ATOM 878 CB BSER A 110 53.014 38.837 6.231 0.31 11.21 C ANISOU 878 CB BSER A 110 960 1668 1527 -698 -529 117 C ATOM 879 OG ASER A 110 53.191 38.119 5.488 0.69 12.17 O ANISOU 879 OG ASER A 110 1404 1689 1419 306 -42 165 O ATOM 880 OG BSER A 110 53.736 39.980 5.822 0.31 12.52 O ANISOU 880 OG BSER A 110 1360 1272 2009 -189 113 225 O ATOM 881 N PHE A 111 50.682 37.883 8.166 1.00 7.58 N ANISOU 881 N PHE A 111 396 730 1684 130 -65 -237 N ATOM 882 CA PHE A 111 49.655 36.892 8.440 1.00 7.36 C ANISOU 882 CA PHE A 111 457 799 1472 174 -56 -138 C ATOM 883 C PHE A 111 48.319 37.454 7.859 1.00 7.77 C ANISOU 883 C PHE A 111 430 888 1561 185 -24 -234 C ATOM 884 O PHE A 111 47.999 38.606 8.020 1.00 8.35 O ANISOU 884 O PHE A 111 469 846 1778 209 -146 -344 O ATOM 885 CB PHE A 111 49.505 36.730 9.927 1.00 8.20 C ANISOU 885 CB PHE A 111 573 994 1471 73 -16 -291 C ATOM 886 CG PHE A 111 48.422 35.762 10.356 1.00 7.84 C ANISOU 886 CG PHE A 111 604 955 1348 148 -6 -223 C ATOM 887 CD1 PHE A 111 48.591 34.398 10.365 1.00 9.01 C ANISOU 887 CD1 PHE A 111 664 1084 1593 194 -103 4 C ATOM 888 CD2 PHE A 111 47.157 36.247 10.762 1.00 8.60 C ANISOU 888 CD2 PHE A 111 666 1013 1509 145 100 -119 C ATOM 889 CE1 PHE A 111 47.584 33.520 10.701 1.00 8.37 C ANISOU 889 CE1 PHE A 111 860 1023 1220 153 -109 14 C ATOM 890 CE2 PHE A 111 46.155 35.379 11.151 1.00 8.89 C ANISOU 890 CE2 PHE A 111 836 1063 1394 162 120 -132 C ATOM 891 CZ PHE A 111 46.339 34.014 11.131 1.00 8.74 C ANISOU 891 CZ PHE A 111 804 1082 1354 66 -2 -78 C ATOM 892 N THR A 112 47.552 36.527 7.274 1.00 8.10 N ANISOU 892 N THR A 112 446 810 1745 163 -70 -334 N ATOM 893 CA THR A 112 46.184 36.842 6.796 1.00 8.48 C ANISOU 893 CA THR A 112 513 777 1853 194 -141 -262 C ATOM 894 C THR A 112 45.265 35.705 7.169 1.00 9.26 C ANISOU 894 C THR A 112 484 866 2080 187 -147 -380 C ATOM 895 O THR A 112 45.553 34.542 6.817 1.00 11.18 O ANISOU 895 O THR A 112 639 827 2678 93 116 -465 O ATOM 896 CB THR A 112 46.120 37.049 5.299 1.00 11.02 C ANISOU 896 CB THR A 112 986 1292 1803 -14 -348 -326 C ATOM 897 OG1 THR A 112 47.050 38.038 4.920 1.00 12.81 O ANISOU 897 OG1 THR A 112 1530 1431 1786 -241 -235 -75 O ATOM 898 CG2 THR A 112 44.696 37.455 4.850 1.00 15.70 C ANISOU 898 CG2 THR A 112 1421 1677 2718 359 -935 -185 C ATOM 899 N SER A 113 44.132 35.992 7.835 1.00 8.99 N ANISOU 899 N SER A 113 501 760 2069 141 -182 -290 N ATOM 900 CA SER A 113 43.082 35.047 8.128 1.00 9.58 C ANISOU 900 CA SER A 113 559 717 2275 125 -217 -244 C ATOM 901 C SER A 113 41.774 35.528 7.541 1.00 8.54 C ANISOU 901 C SER A 113 505 885 1772 89 -35 -260 C ATOM 902 O SER A 113 41.475 36.712 7.605 1.00 11.16 O ANISOU 902 O SER A 113 567 891 2679 188 -222 -323 O ATOM 903 CB ASER A 113 42.817 34.981 9.645 0.55 13.37 C ANISOU 903 CB ASER A 113 846 1770 2337 -72 -418 609 C ATOM 904 CB BSER A 113 42.982 34.676 9.586 0.45 10.52 C ANISOU 904 CB BSER A 113 781 640 2477 83 -373 171 C ATOM 905 OG ASER A 113 41.857 33.983 9.971 0.55 20.08 O ANISOU 905 OG ASER A 113 1896 2453 3094 -889 112 332 O ATOM 906 OG BSER A 113 42.681 35.800 10.392 0.45 11.87 O ANISOU 906 OG BSER A 113 963 1139 2296 -262 -26 -244 O ATOM 907 N LYS A 114 41.002 34.620 6.960 1.00 9.89 N ANISOU 907 N LYS A 114 566 815 2285 143 -268 -305 N ATOM 908 CA LYS A 114 39.708 34.980 6.353 1.00 10.90 C ANISOU 908 CA LYS A 114 662 1040 2336 198 -429 -124 C ATOM 909 C LYS A 114 38.655 33.952 6.764 1.00 10.29 C ANISOU 909 C LYS A 114 598 980 2237 170 -374 -425 C ATOM 910 O LYS A 114 38.904 32.749 6.850 1.00 15.55 O ANISOU 910 O LYS A 114 725 953 4084 227 -386 -417 O ATOM 911 CB LYS A 114 39.804 34.934 4.833 1.00 13.75 C ANISOU 911 CB LYS A 114 936 1810 2350 101 -285 -10 C ATOM 912 CG LYS A 114 40.804 35.877 4.252 1.00 17.58 C ANISOU 912 CG LYS A 114 1513 2270 2730 -259 37 -76 C ATOM 913 CD LYS A 114 40.503 36.391 2.878 1.00 32.26 C ANISOU 913 CD LYS A 114 3539 5575 2839 -2246 -84 1034 C ATOM 914 CE LYS A 114 41.704 37.154 2.337 1.00 39.89 C ANISOU 914 CE LYS A 114 5052 5052 5052 0 0 0 C ATOM 915 NZ LYS A 114 42.100 36.748 0.960 1.00107.14 N ANISOU 915 NZ LYS A 114 13569 13569 13569 0 0 0 N ATOM 916 N LEU A 115 37.452 34.460 6.981 1.00 9.75 N ANISOU 916 N LEU A 115 730 847 2037 46 -335 -217 N ATOM 917 CA LEU A 115 36.234 33.662 7.263 1.00 9.64 C ANISOU 917 CA LEU A 115 813 854 1904 87 -142 -68 C ATOM 918 C LEU A 115 35.194 34.159 6.253 1.00 9.64 C ANISOU 918 C LEU A 115 727 917 1929 -7 -182 33 C ATOM 919 O LEU A 115 34.778 35.316 6.382 1.00 12.95 O ANISOU 919 O LEU A 115 929 1006 2864 283 -443 -246 O ATOM 920 CB LEU A 115 35.625 33.846 8.654 1.00 12.54 C ANISOU 920 CB LEU A 115 1267 1495 1884 -235 -187 -111 C ATOM 921 CG LEU A 115 36.497 33.444 9.811 1.00 12.97 C ANISOU 921 CG LEU A 115 914 1982 1909 -166 -127 -306 C ATOM 922 CD1 LEU A 115 35.842 33.942 11.123 1.00 17.99 C ANISOU 922 CD1 LEU A 115 2927 1900 1839 -109 292 -346 C ATOM 923 CD2 LEU A 115 36.626 31.917 9.796 1.00 20.33 C ANISOU 923 CD2 LEU A 115 3290 2252 1992 1102 -700 -405 C ATOM 924 N LYS A 116 34.761 33.312 5.358 1.00 9.63 N ANISOU 924 N LYS A 116 1069 796 1704 -124 -207 156 N ATOM 925 CA LYS A 116 33.721 33.638 4.348 1.00 11.54 C ANISOU 925 CA LYS A 116 1067 1244 1966 -277 -466 254 C ATOM 926 C LYS A 116 32.416 32.998 4.782 1.00 10.54 C ANISOU 926 C LYS A 116 1109 1008 1789 -166 -296 47 C ATOM 927 O LYS A 116 32.411 31.768 4.920 1.00 12.86 O ANISOU 927 O LYS A 116 1278 1048 2438 -199 30 274 O ATOM 928 CB LYS A 116 34.182 33.169 2.994 1.00 14.13 C ANISOU 928 CB LYS A 116 1460 2100 1675 -324 -278 573 C ATOM 929 CG LYS A 116 35.441 33.770 2.426 1.00 21.02 C ANISOU 929 CG LYS A 116 1904 3303 2582 -407 172 1187 C ATOM 930 CD LYS A 116 35.988 33.267 1.106 1.00 29.44 C ANISOU 930 CD LYS A 116 2510 5864 2537 -928 570 765 C ATOM 931 CE LYS A 116 37.285 33.990 0.761 1.00 42.00 C ANISOU 931 CE LYS A 116 3085 5695 6785 31 2604 3067 C ATOM 932 NZ LYS A 116 37.672 33.771 -0.655 1.00 53.56 N ANISOU 932 NZ LYS A 116 6783 6783 6783 0 0 0 N ATOM 933 N SER A 117 31.372 33.793 5.050 1.00 11.74 N ANISOU 933 N SER A 117 1081 1012 2259 -125 -325 278 N ATOM 934 CA SER A 117 30.079 33.220 5.454 1.00 12.09 C ANISOU 934 CA SER A 117 1105 1620 1753 -167 -204 179 C ATOM 935 C SER A 117 29.174 32.952 4.253 1.00 10.62 C ANISOU 935 C SER A 117 931 1425 1580 -141 -8 366 C ATOM 936 O SER A 117 29.528 33.245 3.120 1.00 15.26 O ANISOU 936 O SER A 117 1387 2643 1623 -742 -57 171 O ATOM 937 CB SER A 117 29.372 34.140 6.448 1.00 14.54 C ANISOU 937 CB SER A 117 1463 2018 1909 0 -216 -146 C ATOM 938 OG SER A 117 29.105 35.374 5.859 1.00 21.51 O ANISOU 938 OG SER A 117 2803 2558 2609 894 338 357 O ATOM 939 N ASN A 118 28.041 32.421 4.440 1.00 10.56 N ANISOU 939 N ASN A 118 1071 1194 1649 -150 -53 113 N ATOM 940 CA ASN A 118 26.941 32.305 3.497 1.00 11.53 C ANISOU 940 CA ASN A 118 975 1642 1654 -24 24 142 C ATOM 941 C ASN A 118 26.058 33.534 3.365 1.00 12.69 C ANISOU 941 C ASN A 118 1271 1628 1803 74 -35 161 C ATOM 942 O ASN A 118 25.131 33.572 2.562 1.00 15.43 O ANISOU 942 O ASN A 118 1424 2265 2030 406 -211 62 O ATOM 943 CB ASN A 118 26.068 31.075 3.708 1.00 11.49 C ANISOU 943 CB ASN A 118 1103 1512 1641 -110 38 -243 C ATOM 944 CG ASN A 118 25.245 31.111 4.955 1.00 11.57 C ANISOU 944 CG ASN A 118 1052 1810 1425 -196 -120 -106 C ATOM 945 OD1 ASN A 118 24.030 30.622 4.966 1.00 13.89 O ANISOU 945 OD1 ASN A 118 1203 2010 1935 -315 13 2 O ATOM 946 ND2 ASN A 118 25.623 31.682 6.069 1.00 15.72 N ANISOU 946 ND2 ASN A 118 1546 2888 1389 -1069 247 -149 N ATOM 947 N SER A 119 26.261 34.589 4.118 1.00 15.64 N ANISOU 947 N SER A 119 1715 1723 2358 299 -95 -98 N ATOM 948 CA SER A 119 25.546 35.832 3.848 1.00 20.37 C ANISOU 948 CA SER A 119 2282 1617 3650 268 -669 -194 C ATOM 949 C SER A 119 26.149 36.524 2.627 1.00 24.85 C ANISOU 949 C SER A 119 2952 2155 4102 256 -1154 895 C ATOM 950 O SER A 119 27.323 36.341 2.301 1.00 36.92 O ANISOU 950 O SER A 119 2706 4819 6156 -892 -330 2422 O ATOM 951 CB SER A 119 25.675 36.601 5.184 1.00 28.58 C ANISOU 951 CB SER A 119 3970 2438 4183 1656 -1198 -957 C ATOM 952 OG SER A 119 25.012 35.799 6.162 1.00 59.30 O ANISOU 952 OG SER A 119 7510 7510 7510 0 0 0 O ATOM 953 N THR A 120 25.385 37.206 1.771 1.00 26.76 N ANISOU 953 N THR A 120 3389 3389 3389 0 0 0 N ATOM 954 CA THR A 120 25.961 37.834 0.565 1.00 69.81 C ANISOU 954 CA THR A 120 8842 8842 8842 0 0 0 C ATOM 955 C THR A 120 27.256 38.645 0.762 1.00 52.32 C ANISOU 955 C THR A 120 6626 6626 6626 0 0 0 C ATOM 956 O THR A 120 27.017 39.720 1.345 1.00 42.20 O ANISOU 956 O THR A 120 5345 5345 5345 0 0 0 O ATOM 957 CB THR A 120 25.023 38.931 -0.009 1.00 90.59 C ANISOU 957 CB THR A 120 11473 11473 11473 0 0 0 C ATOM 958 OG1 THR A 120 23.681 38.763 0.476 1.00 89.82 O ANISOU 958 OG1 THR A 120 11376 11376 11376 0 0 0 O ATOM 959 CG2 THR A 120 25.013 38.899 -1.538 1.00 58.98 C ANISOU 959 CG2 THR A 120 7470 7470 7470 0 0 0 C ATOM 960 N HIS A 121 28.456 38.261 0.504 1.00 71.28 N ANISOU 960 N HIS A 121 9028 9028 9028 0 0 0 N ATOM 961 CA HIS A 121 29.474 37.347 0.127 1.00 87.66 C ANISOU 961 CA HIS A 121 11102 11102 11102 0 0 0 C ATOM 962 C HIS A 121 29.853 36.193 1.067 1.00 95.45 C ANISOU 962 C HIS A 121 12089 12089 12089 0 0 0 C ATOM 963 O HIS A 121 29.891 35.065 0.566 1.00101.89 O ANISOU 963 O HIS A 121 12905 12905 12905 0 0 0 O ATOM 964 CB HIS A 121 30.843 37.974 -0.194 1.00 40.39 C ANISOU 964 CB HIS A 121 5115 5115 5115 0 0 0 C ATOM 965 CG HIS A 121 30.829 39.451 -0.430 1.00 91.95 C ANISOU 965 CG HIS A 121 11646 11646 11646 0 0 0 C ATOM 966 ND1 HIS A 121 30.596 40.360 0.586 1.00123.03 N ANISOU 966 ND1 HIS A 121 15582 15582 15582 0 0 0 N ATOM 967 CD2 HIS A 121 31.075 40.194 -1.543 1.00 57.84 C ANISOU 967 CD2 HIS A 121 7326 7326 7326 0 0 0 C ATOM 968 CE1 HIS A 121 30.664 41.586 0.106 1.00122.19 C ANISOU 968 CE1 HIS A 121 15476 15476 15476 0 0 0 C ATOM 969 NE2 HIS A 121 30.953 41.519 -1.186 1.00 93.81 N ANISOU 969 NE2 HIS A 121 11881 11881 11881 0 0 0 N ATOM 970 N GLU A 122 30.314 36.365 2.283 1.00 56.14 N ANISOU 970 N GLU A 122 7110 7110 7110 0 0 0 N ATOM 971 CA GLU A 122 30.408 37.602 3.045 1.00 30.84 C ANISOU 971 CA GLU A 122 3906 3906 3906 0 0 0 C ATOM 972 C GLU A 122 31.673 37.526 3.891 1.00 18.74 C ANISOU 972 C GLU A 122 2012 1860 3074 -711 -966 286 C ATOM 973 O GLU A 122 31.982 36.552 4.543 1.00 21.50 O ANISOU 973 O GLU A 122 3842 1392 2732 -347 85 11 O ATOM 974 CB GLU A 122 29.135 37.909 3.806 1.00 80.45 C ANISOU 974 CB GLU A 122 10189 10189 10189 0 0 0 C ATOM 975 CG GLU A 122 29.075 39.225 4.506 1.00 22.39 C ANISOU 975 CG GLU A 122 2836 2836 2836 0 0 0 C ATOM 976 CD GLU A 122 27.910 40.141 4.400 1.00 54.22 C ANISOU 976 CD GLU A 122 6867 6867 6867 0 0 0 C ATOM 977 OE1 GLU A 122 27.721 40.706 3.292 1.00 71.09 O ANISOU 977 OE1 GLU A 122 9004 9004 9004 0 0 0 O ATOM 978 OE2 GLU A 122 27.246 40.346 5.456 1.00 65.64 O ANISOU 978 OE2 GLU A 122 8313 8313 8313 0 0 0 O ATOM 979 N THR A 123 32.531 38.501 3.601 1.00 23.08 N ANISOU 979 N THR A 123 2604 2622 3326 -1312 -866 818 N ATOM 980 CA THR A 123 33.905 38.386 4.022 1.00 24.22 C ANISOU 980 CA THR A 123 2265 2616 4096 -1017 -533 -718 C ATOM 981 C THR A 123 34.293 39.033 5.342 1.00 19.02 C ANISOU 981 C THR A 123 1412 1460 4175 146 -675 -578 C ATOM 982 O THR A 123 33.965 40.182 5.735 1.00 19.17 O ANISOU 982 O THR A 123 1809 1282 4011 153 -163 -124 O ATOM 983 CB THR A 123 34.930 38.821 2.952 1.00 39.31 C ANISOU 983 CB THR A 123 4979 4979 4979 0 0 0 C ATOM 984 OG1 THR A 123 34.372 38.657 1.644 1.00 40.20 O ANISOU 984 OG1 THR A 123 5091 5091 5091 0 0 0 O ATOM 985 CG2 THR A 123 36.163 37.914 3.028 1.00113.78 C ANISOU 985 CG2 THR A 123 14410 14410 14410 0 0 0 C ATOM 986 N ASN A 124 35.027 38.228 6.127 1.00 19.01 N ANISOU 986 N ASN A 124 881 1297 4867 115 -880 -683 N ATOM 987 CA AASN A 124 35.595 38.743 7.398 0.26 21.85 C ANISOU 987 CA AASN A 124 2767 2767 2767 0 0 0 C ATOM 988 CA BASN A 124 35.625 38.753 7.359 0.74 14.74 C ANISOU 988 CA BASN A 124 520 664 4278 38 -379 -250 C ATOM 989 C ASN A 124 37.109 38.461 7.302 1.00 12.42 C ANISOU 989 C ASN A 124 659 847 3096 195 -345 -461 C ATOM 990 O ASN A 124 37.509 37.376 6.839 1.00 16.95 O ANISOU 990 O ASN A 124 805 1194 4281 211 -587 -1035 O ATOM 991 CB AASN A 124 35.078 38.227 8.723 0.26 16.99 C ANISOU 991 CB AASN A 124 826 604 4864 557 274 428 C ATOM 992 CB BASN A 124 35.023 37.954 8.499 0.74 17.80 C ANISOU 992 CB BASN A 124 795 818 4984 122 310 -171 C ATOM 993 CG AASN A 124 33.867 38.757 9.472 0.26 21.99 C ANISOU 993 CG AASN A 124 1197 1409 5544 -320 1436 293 C ATOM 994 CG BASN A 124 33.467 38.135 8.376 0.74 11.74 C ANISOU 994 CG BASN A 124 951 1115 2286 192 -148 -177 C ATOM 995 OD1AASN A 124 33.009 39.459 8.947 0.26 12.65 O ANISOU 995 OD1AASN A 124 1602 1602 1602 0 0 0 O ATOM 996 OD1BASN A 124 32.958 39.070 8.994 0.74 11.20 O ANISOU 996 OD1BASN A 124 744 784 2624 260 96 54 O ATOM 997 ND2AASN A 124 33.638 38.542 10.769 0.26 17.78 N ANISOU 997 ND2AASN A 124 584 1410 4596 320 -276 -701 N ATOM 998 ND2BASN A 124 32.814 37.228 7.741 0.74 16.47 N ANISOU 998 ND2BASN A 124 1133 1294 3677 -17 133 -710 N ATOM 999 N ALA A 125 37.972 39.373 7.731 1.00 9.51 N ANISOU 999 N ALA A 125 552 724 2249 122 -94 -151 N ATOM 1000 CA ALA A 125 39.427 39.155 7.591 1.00 9.04 C ANISOU 1000 CA ALA A 125 533 836 1982 127 -113 -83 C ATOM 1001 C ALA A 125 40.195 39.918 8.630 1.00 7.73 C ANISOU 1001 C ALA A 125 498 758 1609 137 85 16 C ATOM 1002 O ALA A 125 39.792 40.973 9.131 1.00 8.53 O ANISOU 1002 O ALA A 125 515 872 1776 185 -16 -84 O ATOM 1003 CB ALA A 125 39.859 39.713 6.221 1.00 12.33 C ANISOU 1003 CB ALA A 125 1054 1918 1597 -7 -98 -278 C ATOM 1004 N LEU A 126 41.404 39.370 8.926 1.00 7.96 N ANISOU 1004 N LEU A 126 507 646 1796 84 -27 -66 N ATOM 1005 CA LEU A 126 42.455 40.037 9.674 1.00 7.65 C ANISOU 1005 CA LEU A 126 577 803 1455 79 41 -87 C ATOM 1006 C LEU A 126 43.751 39.900 8.862 1.00 7.71 C ANISOU 1006 C LEU A 126 456 713 1687 189 -23 -99 C ATOM 1007 O LEU A 126 44.073 38.796 8.397 1.00 9.28 O ANISOU 1007 O LEU A 126 547 797 2095 97 99 -328 O ATOM 1008 CB LEU A 126 42.699 39.363 11.037 1.00 9.31 C ANISOU 1008 CB LEU A 126 832 1056 1563 156 -8 -26 C ATOM 1009 CG LEU A 126 43.922 39.977 11.793 1.00 10.16 C ANISOU 1009 CG LEU A 126 1086 1122 1558 190 -156 -100 C ATOM 1010 CD1 LEU A 126 43.610 41.377 12.259 1.00 11.39 C ANISOU 1010 CD1 LEU A 126 1431 1192 1600 297 -257 -171 C ATOM 1011 CD2 LEU A 126 44.268 39.020 12.922 1.00 12.41 C ANISOU 1011 CD2 LEU A 126 1185 1486 1927 452 -264 153 C ATOM 1012 N HIS A 127 44.490 40.990 8.718 1.00 7.51 N ANISOU 1012 N HIS A 127 480 708 1595 156 -48 -184 N ATOM 1013 CA HIS A 127 45.824 40.973 8.094 1.00 7.31 C ANISOU 1013 CA HIS A 127 473 845 1389 111 -26 -135 C ATOM 1014 C HIS A 127 46.749 41.871 8.867 1.00 6.52 C ANISOU 1014 C HIS A 127 511 682 1222 135 39 88 C ATOM 1015 O HIS A 127 46.399 42.993 9.241 1.00 7.78 O ANISOU 1015 O HIS A 127 514 789 1581 193 -58 -61 O ATOM 1016 CB HIS A 127 45.749 41.434 6.642 1.00 8.83 C ANISOU 1016 CB HIS A 127 815 1012 1446 167 -166 3 C ATOM 1017 CG HIS A 127 47.080 41.703 5.999 1.00 9.64 C ANISOU 1017 CG HIS A 127 780 1234 1559 80 -118 45 C ATOM 1018 ND1 HIS A 127 47.929 40.725 5.587 1.00 10.33 N ANISOU 1018 ND1 HIS A 127 1052 1310 1464 188 154 161 N ATOM 1019 CD2 HIS A 127 47.744 42.863 5.800 1.00 11.70 C ANISOU 1019 CD2 HIS A 127 1198 1324 1813 -10 113 207 C ATOM 1020 CE1 HIS A 127 49.045 41.331 5.074 1.00 10.72 C ANISOU 1020 CE1 HIS A 127 980 1572 1420 42 54 82 C ATOM 1021 NE2 HIS A 127 48.958 42.635 5.158 1.00 12.37 N ANISOU 1021 NE2 HIS A 127 1276 1678 1631 -85 110 138 N ATOM 1022 N PHE A 128 47.996 41.391 9.081 1.00 6.76 N ANISOU 1022 N PHE A 128 437 704 1365 123 -33 -57 N ATOM 1023 CA PHE A 128 49.046 42.278 9.544 1.00 6.51 C ANISOU 1023 CA PHE A 128 510 595 1308 99 -5 -61 C ATOM 1024 C PHE A 128 50.328 41.971 8.766 1.00 6.68 C ANISOU 1024 C PHE A 128 482 710 1284 146 -49 -37 C ATOM 1025 O PHE A 128 50.561 40.847 8.316 1.00 7.27 O ANISOU 1025 O PHE A 128 489 708 1496 98 7 -50 O ATOM 1026 CB PHE A 128 49.250 42.191 11.041 1.00 7.62 C ANISOU 1026 CB PHE A 128 726 809 1287 155 -27 -102 C ATOM 1027 CG PHE A 128 49.629 40.851 11.638 1.00 8.16 C ANISOU 1027 CG PHE A 128 944 885 1195 115 -207 -80 C ATOM 1028 CD1 PHE A 128 50.956 40.360 11.570 1.00 9.60 C ANISOU 1028 CD1 PHE A 128 903 974 1681 115 -492 110 C ATOM 1029 CD2 PHE A 128 48.706 39.992 12.222 1.00 9.01 C ANISOU 1029 CD2 PHE A 128 1211 974 1152 -7 -63 -73 C ATOM 1030 CE1 PHE A 128 51.306 39.164 12.116 1.00 10.89 C ANISOU 1030 CE1 PHE A 128 1387 717 1933 197 -852 -245 C ATOM 1031 CE2 PHE A 128 49.060 38.808 12.811 1.00 10.81 C ANISOU 1031 CE2 PHE A 128 1967 1094 946 -6 -130 -11 C ATOM 1032 CZ PHE A 128 50.372 38.364 12.741 1.00 11.38 C ANISOU 1032 CZ PHE A 128 2073 731 1415 174 -663 -79 C ATOM 1033 N MET A 129 51.176 42.997 8.702 1.00 7.48 N ANISOU 1033 N MET A 129 475 747 1549 115 46 -92 N ATOM 1034 CA MET A 129 52.507 42.881 8.038 1.00 7.37 C ANISOU 1034 CA MET A 129 496 756 1480 81 68 -105 C ATOM 1035 C MET A 129 53.471 43.756 8.800 1.00 7.48 C ANISOU 1035 C MET A 129 501 777 1494 78 65 26 C ATOM 1036 O MET A 129 53.297 44.976 8.921 1.00 9.16 O ANISOU 1036 O MET A 129 590 718 2089 158 -111 -37 O ATOM 1037 CB MET A 129 52.440 43.286 6.571 1.00 9.37 C ANISOU 1037 CB MET A 129 846 1159 1467 -87 17 -45 C ATOM 1038 CG MET A 129 53.794 43.313 5.888 1.00 12.14 C ANISOU 1038 CG MET A 129 1310 1225 1965 11 646 -74 C ATOM 1039 SD MET A 129 53.688 43.583 4.119 1.00 18.02 S ANISOU 1039 SD MET A 129 1996 2652 2030 -275 412 155 S ATOM 1040 CE MET A 129 52.949 42.064 3.587 1.00 23.27 C ANISOU 1040 CE MET A 129 3243 3490 1891 -1162 -161 116 C ATOM 1041 N PHE A 130 54.554 43.086 9.301 1.00 7.56 N ANISOU 1041 N PHE A 130 573 696 1533 106 -7 -53 N ATOM 1042 CA PHE A 130 55.688 43.759 9.914 1.00 7.65 C ANISOU 1042 CA PHE A 130 601 792 1443 179 -34 -206 C ATOM 1043 C PHE A 130 56.893 43.600 8.964 1.00 8.42 C ANISOU 1043 C PHE A 130 552 912 1656 111 32 -46 C ATOM 1044 O PHE A 130 57.323 42.470 8.677 1.00 9.70 O ANISOU 1044 O PHE A 130 643 868 2083 156 221 85 O ATOM 1045 CB PHE A 130 56.088 43.126 11.223 1.00 8.39 C ANISOU 1045 CB PHE A 130 692 897 1522 159 -105 -118 C ATOM 1046 CG PHE A 130 55.060 43.159 12.349 1.00 8.56 C ANISOU 1046 CG PHE A 130 795 853 1523 137 -107 -161 C ATOM 1047 CD1 PHE A 130 54.104 42.164 12.486 1.00 9.38 C ANISOU 1047 CD1 PHE A 130 1049 988 1439 -62 13 -180 C ATOM 1048 CD2 PHE A 130 55.118 44.111 13.341 1.00 11.26 C ANISOU 1048 CD2 PHE A 130 1233 1258 1683 -259 210 -331 C ATOM 1049 CE1 PHE A 130 53.185 42.177 13.483 1.00 10.40 C ANISOU 1049 CE1 PHE A 130 1161 1190 1502 -138 33 -220 C ATOM 1050 CE2 PHE A 130 54.218 44.131 14.370 1.00 13.56 C ANISOU 1050 CE2 PHE A 130 1968 1307 1752 -525 500 -493 C ATOM 1051 CZ PHE A 130 53.190 43.188 14.413 1.00 10.16 C ANISOU 1051 CZ PHE A 130 1166 1161 1438 -62 82 -148 C ATOM 1052 N ASN A 131 57.505 44.707 8.579 1.00 9.92 N ANISOU 1052 N ASN A 131 837 862 1977 118 179 -57 N ATOM 1053 CA ASN A 131 58.829 44.691 7.899 1.00 10.85 C ANISOU 1053 CA ASN A 131 943 989 2087 130 407 123 C ATOM 1054 C ASN A 131 59.848 45.438 8.735 1.00 11.34 C ANISOU 1054 C ASN A 131 948 1031 2222 84 309 325 C ATOM 1055 O ASN A 131 61.017 45.555 8.338 1.00 16.62 O ANISOU 1055 O ASN A 131 919 2128 3112 -26 330 173 O ATOM 1056 CB ASN A 131 58.756 45.226 6.494 1.00 14.79 C ANISOU 1056 CB ASN A 131 1591 1829 2061 5 281 249 C ATOM 1057 CG ASN A 131 58.438 44.086 5.558 1.00 16.49 C ANISOU 1057 CG ASN A 131 2012 1948 2152 290 167 6 C ATOM 1058 OD1 ASN A 131 59.261 43.199 5.376 1.00 19.00 O ANISOU 1058 OD1 ASN A 131 2166 2150 2727 497 583 206 O ATOM 1059 ND2 ASN A 131 57.309 44.229 4.930 1.00 19.01 N ANISOU 1059 ND2 ASN A 131 2128 2157 2758 345 -147 -246 N ATOM 1060 N GLN A 132 59.521 45.828 9.902 1.00 13.61 N ANISOU 1060 N GLN A 132 914 1735 2395 -328 152 -170 N ATOM 1061 CA GLN A 132 60.433 46.383 10.882 1.00 14.94 C ANISOU 1061 CA GLN A 132 1071 2203 2261 -516 -105 383 C ATOM 1062 C GLN A 132 59.732 46.268 12.198 1.00 14.27 C ANISOU 1062 C GLN A 132 892 2121 2273 -202 5 126 C ATOM 1063 O GLN A 132 58.508 46.011 12.329 1.00 15.19 O ANISOU 1063 O GLN A 132 749 1973 2908 -107 -56 213 O ATOM 1064 CB GLN A 132 60.695 47.812 10.538 1.00 17.03 C ANISOU 1064 CB GLN A 132 1729 2069 2511 -830 -205 -24 C ATOM 1065 CG GLN A 132 59.555 48.789 10.680 1.00 19.75 C ANISOU 1065 CG GLN A 132 2564 2256 2498 -51 -994 -6 C ATOM 1066 CD GLN A 132 59.901 50.236 10.384 1.00 37.52 C ANISOU 1066 CD GLN A 132 4097 2262 7545 -224 -697 293 C ATOM 1067 OE1 GLN A 132 59.334 51.124 11.020 1.00 36.37 O ANISOU 1067 OE1 GLN A 132 4606 4606 4606 0 0 0 O ATOM 1068 NE2 GLN A 132 60.888 50.534 9.540 1.00 71.26 N ANISOU 1068 NE2 GLN A 132 9025 9025 9025 0 0 0 N ATOM 1069 N PHE A 133 60.521 46.349 13.238 1.00 12.31 N ANISOU 1069 N PHE A 133 700 1551 2309 -56 34 46 N ATOM 1070 CA PHE A 133 60.072 46.213 14.590 1.00 11.83 C ANISOU 1070 CA PHE A 133 628 1500 2256 6 -7 -102 C ATOM 1071 C PHE A 133 60.751 47.281 15.446 1.00 14.37 C ANISOU 1071 C PHE A 133 949 1772 2605 -196 52 -362 C ATOM 1072 O PHE A 133 61.957 47.498 15.393 1.00 20.97 O ANISOU 1072 O PHE A 133 1046 3169 3556 -630 357 -1383 O ATOM 1073 CB PHE A 133 60.430 44.852 15.100 1.00 12.14 C ANISOU 1073 CB PHE A 133 741 1585 2174 62 -196 -105 C ATOM 1074 CG PHE A 133 59.872 43.656 14.351 1.00 9.78 C ANISOU 1074 CG PHE A 133 695 1307 1624 186 -37 129 C ATOM 1075 CD1 PHE A 133 60.542 43.105 13.241 1.00 10.30 C ANISOU 1075 CD1 PHE A 133 691 1325 1802 279 105 145 C ATOM 1076 CD2 PHE A 133 58.674 43.067 14.692 1.00 9.90 C ANISOU 1076 CD2 PHE A 133 744 1250 1675 69 39 -6 C ATOM 1077 CE1 PHE A 133 60.021 42.054 12.526 1.00 10.54 C ANISOU 1077 CE1 PHE A 133 832 1421 1652 406 82 53 C ATOM 1078 CE2 PHE A 133 58.159 42.009 13.972 1.00 9.81 C ANISOU 1078 CE2 PHE A 133 765 1142 1728 200 28 -28 C ATOM 1079 CZ PHE A 133 58.824 41.488 12.890 1.00 9.96 C ANISOU 1079 CZ PHE A 133 761 1223 1707 403 -91 -4 C ATOM 1080 N SER A 134 59.992 48.073 16.114 1.00 15.35 N ANISOU 1080 N SER A 134 1191 1297 3202 -234 205 -345 N ATOM 1081 CA SER A 134 60.611 49.133 16.866 1.00 19.09 C ANISOU 1081 CA SER A 134 1617 1509 3948 -288 -134 -612 C ATOM 1082 C SER A 134 60.751 48.732 18.316 1.00 15.92 C ANISOU 1082 C SER A 134 837 1314 3749 -109 -4 -965 C ATOM 1083 O SER A 134 60.195 47.725 18.762 1.00 17.50 O ANISOU 1083 O SER A 134 1310 1277 3898 -82 -358 -617 O ATOM 1084 CB SER A 134 59.813 50.410 16.533 1.00 25.65 C ANISOU 1084 CB SER A 134 2887 1348 5271 -161 -1285 -623 C ATOM 1085 OG SER A 134 58.723 50.227 17.419 1.00 37.48 O ANISOU 1085 OG SER A 134 1581 3298 9009 324 -148 -2187 O ATOM 1086 N LYS A 135 61.438 49.476 19.176 1.00 18.89 N ANISOU 1086 N LYS A 135 1028 1748 4223 -207 -247 -950 N ATOM 1087 CA LYS A 135 61.686 49.326 20.534 1.00 20.24 C ANISOU 1087 CA LYS A 135 1376 2005 4121 246 -389 -1424 C ATOM 1088 C LYS A 135 60.515 49.006 21.401 1.00 23.87 C ANISOU 1088 C LYS A 135 1792 3417 3637 15 -172 -1953 C ATOM 1089 O LYS A 135 60.618 48.245 22.371 1.00 40.24 O ANISOU 1089 O LYS A 135 2542 7993 4379 -878 -511 336 O ATOM 1090 CB LYS A 135 62.512 50.614 20.850 1.00 28.37 C ANISOU 1090 CB LYS A 135 2301 2591 5622 -246 -793 -1914 C ATOM 1091 CG LYS A 135 63.478 51.084 19.778 1.00 50.31 C ANISOU 1091 CG LYS A 135 4625 5026 8993 -3110 1569 -2894 C ATOM 1092 CD LYS A 135 63.434 51.548 18.336 1.00 39.89 C ANISOU 1092 CD LYS A 135 5052 5052 5052 0 0 0 C ATOM 1093 CE LYS A 135 62.217 52.504 18.049 1.00 54.70 C ANISOU 1093 CE LYS A 135 6928 6928 6928 0 0 0 C ATOM 1094 NZ LYS A 135 62.335 52.807 16.588 1.00 97.89 N ANISOU 1094 NZ LYS A 135 12398 12398 12398 0 0 0 N ATOM 1095 N ASP A 136 59.381 49.725 21.123 1.00 26.66 N ANISOU 1095 N ASP A 136 1087 3033 5759 -49 -336 -3355 N ATOM 1096 CA ASP A 136 58.073 49.589 21.830 1.00 18.58 C ANISOU 1096 CA ASP A 136 1627 2079 3180 162 -836 -1313 C ATOM 1097 C ASP A 136 56.980 49.227 20.837 1.00 12.73 C ANISOU 1097 C ASP A 136 1162 1304 2251 -4 -346 -430 C ATOM 1098 O ASP A 136 56.169 50.034 20.439 1.00 16.20 O ANISOU 1098 O ASP A 136 1552 1187 3264 170 -523 -419 O ATOM 1099 CB ASP A 136 57.773 50.864 22.617 1.00 22.86 C ANISOU 1099 CB ASP A 136 1460 3198 3811 88 -256 -2212 C ATOM 1100 CG ASP A 136 56.464 50.704 23.410 1.00 19.43 C ANISOU 1100 CG ASP A 136 2023 2390 2789 -31 -384 -1054 C ATOM 1101 OD1 ASP A 136 56.116 49.590 23.911 1.00 31.92 O ANISOU 1101 OD1 ASP A 136 5435 3220 3172 -1038 -547 -295 O ATOM 1102 OD2 ASP A 136 55.774 51.708 23.519 1.00 24.62 O ANISOU 1102 OD2 ASP A 136 1930 3594 3601 863 -28 -1028 O ATOM 1103 N GLN A 137 56.947 47.932 20.507 1.00 10.80 N ANISOU 1103 N GLN A 137 947 1206 1848 131 -153 -429 N ATOM 1104 CA GLN A 137 56.075 47.408 19.456 1.00 10.03 C ANISOU 1104 CA GLN A 137 757 1104 1857 102 -98 -344 C ATOM 1105 C GLN A 137 54.788 46.904 20.116 1.00 9.75 C ANISOU 1105 C GLN A 137 943 1020 1652 136 -193 -278 C ATOM 1106 O GLN A 137 54.613 45.755 20.477 1.00 10.28 O ANISOU 1106 O GLN A 137 864 969 1976 110 -255 -72 O ATOM 1107 CB GLN A 137 56.824 46.286 18.678 1.00 10.51 C ANISOU 1107 CB GLN A 137 783 1191 1919 207 -179 -369 C ATOM 1108 CG GLN A 137 56.090 45.868 17.434 1.00 10.90 C ANISOU 1108 CG GLN A 137 838 1343 1859 0 -67 -366 C ATOM 1109 CD GLN A 137 56.111 46.950 16.375 1.00 10.40 C ANISOU 1109 CD GLN A 137 867 1158 1830 17 63 -349 C ATOM 1110 OE1 GLN A 137 57.154 47.543 16.021 1.00 13.64 O ANISOU 1110 OE1 GLN A 137 834 1933 2286 -185 169 -328 O ATOM 1111 NE2 GLN A 137 54.934 47.270 15.839 1.00 10.58 N ANISOU 1111 NE2 GLN A 137 804 1020 2097 125 103 -228 N ATOM 1112 N LYS A 138 53.852 47.866 20.322 1.00 8.71 N ANISOU 1112 N LYS A 138 922 1019 1286 131 -33 -116 N ATOM 1113 CA LYS A 138 52.709 47.669 21.201 1.00 9.11 C ANISOU 1113 CA LYS A 138 990 1053 1334 112 -93 -98 C ATOM 1114 C LYS A 138 51.728 46.618 20.717 1.00 9.07 C ANISOU 1114 C LYS A 138 882 1021 1458 94 9 -89 C ATOM 1115 O LYS A 138 50.943 46.128 21.546 1.00 11.22 O ANISOU 1115 O LYS A 138 1431 1144 1585 -80 223 -68 O ATOM 1116 CB LYS A 138 51.946 48.985 21.466 1.00 9.24 C ANISOU 1116 CB LYS A 138 1026 1086 1311 168 60 6 C ATOM 1117 CG LYS A 138 52.781 50.044 22.212 1.00 10.10 C ANISOU 1117 CG LYS A 138 1133 1296 1313 129 -66 -250 C ATOM 1118 CD LYS A 138 51.857 51.166 22.717 1.00 11.09 C ANISOU 1118 CD LYS A 138 1332 1317 1460 328 73 -135 C ATOM 1119 CE LYS A 138 52.530 52.326 23.368 1.00 15.25 C ANISOU 1119 CE LYS A 138 1826 1646 2178 230 223 -652 C ATOM 1120 NZ LYS A 138 53.283 51.885 24.573 1.00 19.90 N ANISOU 1120 NZ LYS A 138 1941 2866 2567 317 -523 -1208 N ATOM 1121 N ASP A 139 51.687 46.292 19.429 1.00 8.60 N ANISOU 1121 N ASP A 139 728 1037 1421 115 -84 -163 N ATOM 1122 CA ASP A 139 50.862 45.260 18.891 1.00 8.44 C ANISOU 1122 CA ASP A 139 728 990 1408 84 54 -53 C ATOM 1123 C ASP A 139 51.465 43.872 18.896 1.00 7.91 C ANISOU 1123 C ASP A 139 655 981 1294 16 -33 -48 C ATOM 1124 O ASP A 139 50.861 42.938 18.316 1.00 8.30 O ANISOU 1124 O ASP A 139 697 920 1460 58 -72 27 O ATOM 1125 CB ASP A 139 50.306 45.641 17.507 1.00 8.69 C ANISOU 1125 CB ASP A 139 749 1019 1453 154 -94 -113 C ATOM 1126 CG ASP A 139 51.390 45.942 16.523 1.00 8.62 C ANISOU 1126 CG ASP A 139 712 921 1563 163 -87 210 C ATOM 1127 OD1 ASP A 139 52.594 45.951 16.877 1.00 9.55 O ANISOU 1127 OD1 ASP A 139 678 1292 1567 111 -2 -103 O ATOM 1128 OD2 ASP A 139 51.002 46.164 15.336 1.00 9.67 O ANISOU 1128 OD2 ASP A 139 805 1339 1440 259 3 -53 O ATOM 1129 N LEU A 140 52.599 43.669 19.604 1.00 8.58 N ANISOU 1129 N LEU A 140 853 817 1510 95 -140 -105 N ATOM 1130 CA LEU A 140 53.162 42.375 19.882 1.00 7.95 C ANISOU 1130 CA LEU A 140 816 867 1265 111 -83 -221 C ATOM 1131 C LEU A 140 53.206 42.142 21.373 1.00 8.21 C ANISOU 1131 C LEU A 140 855 893 1297 131 -191 -214 C ATOM 1132 O LEU A 140 53.588 43.033 22.146 1.00 11.21 O ANISOU 1132 O LEU A 140 1611 1158 1387 -145 -279 -320 O ATOM 1133 CB LEU A 140 54.573 42.207 19.296 1.00 8.94 C ANISOU 1133 CB LEU A 140 765 1048 1500 20 -109 -205 C ATOM 1134 CG LEU A 140 54.683 42.175 17.785 1.00 8.75 C ANISOU 1134 CG LEU A 140 854 1002 1387 57 91 -87 C ATOM 1135 CD1 LEU A 140 56.170 42.045 17.381 1.00 11.28 C ANISOU 1135 CD1 LEU A 140 1014 1320 1845 -2 243 -125 C ATOM 1136 CD2 LEU A 140 53.879 41.037 17.197 1.00 10.28 C ANISOU 1136 CD2 LEU A 140 1237 1195 1380 -70 42 -190 C ATOM 1137 N ILE A 141 52.862 40.933 21.788 1.00 8.08 N ANISOU 1137 N ILE A 141 746 1021 1226 158 -116 -137 N ATOM 1138 CA ILE A 141 53.059 40.426 23.122 1.00 7.98 C ANISOU 1138 CA ILE A 141 702 1053 1205 231 -62 -173 C ATOM 1139 C ILE A 141 54.378 39.644 23.127 1.00 7.79 C ANISOU 1139 C ILE A 141 677 1224 986 199 9 -307 C ATOM 1140 O ILE A 141 54.489 38.585 22.529 1.00 8.79 O ANISOU 1140 O ILE A 141 772 1263 1222 255 -124 -351 O ATOM 1141 CB ILE A 141 51.909 39.482 23.541 1.00 9.36 C ANISOU 1141 CB ILE A 141 828 1242 1400 83 68 33 C ATOM 1142 CG1 ILE A 141 50.549 40.210 23.471 1.00 11.34 C ANISOU 1142 CG1 ILE A 141 671 1906 1624 66 -19 -177 C ATOM 1143 CG2 ILE A 141 52.173 38.923 24.914 1.00 11.90 C ANISOU 1143 CG2 ILE A 141 944 1913 1553 43 112 178 C ATOM 1144 CD1 ILE A 141 49.371 39.263 23.490 1.00 13.79 C ANISOU 1144 CD1 ILE A 141 799 2031 2279 -65 114 127 C ATOM 1145 N LEU A 142 55.401 40.207 23.802 1.00 8.47 N ANISOU 1145 N LEU A 142 697 1224 1217 239 -115 -308 N ATOM 1146 CA LEU A 142 56.714 39.549 23.869 1.00 8.21 C ANISOU 1146 CA LEU A 142 777 982 1285 238 -141 -123 C ATOM 1147 C LEU A 142 56.785 38.706 25.119 1.00 8.30 C ANISOU 1147 C LEU A 142 710 1260 1107 220 -26 -268 C ATOM 1148 O LEU A 142 56.367 39.152 26.204 1.00 10.60 O ANISOU 1148 O LEU A 142 1273 1481 1175 444 30 -361 O ATOM 1149 CB LEU A 142 57.864 40.577 23.834 1.00 9.35 C ANISOU 1149 CB LEU A 142 760 1165 1540 83 -173 -241 C ATOM 1150 CG LEU A 142 57.904 41.504 22.616 1.00 9.60 C ANISOU 1150 CG LEU A 142 825 1042 1691 134 -42 -188 C ATOM 1151 CD1 LEU A 142 59.075 42.463 22.724 1.00 12.29 C ANISOU 1151 CD1 LEU A 142 1170 1478 1905 -175 -185 27 C ATOM 1152 CD2 LEU A 142 57.921 40.723 21.287 1.00 10.38 C ANISOU 1152 CD2 LEU A 142 1049 1277 1520 123 -20 -105 C ATOM 1153 N GLN A 143 57.313 37.518 24.996 1.00 7.52 N ANISOU 1153 N GLN A 143 661 1106 1020 191 -105 -171 N ATOM 1154 CA GLN A 143 57.433 36.558 26.098 1.00 8.13 C ANISOU 1154 CA GLN A 143 770 1328 915 221 -122 -236 C ATOM 1155 C GLN A 143 58.900 36.108 26.199 1.00 7.46 C ANISOU 1155 C GLN A 143 826 1079 858 250 -90 -85 C ATOM 1156 O GLN A 143 59.615 35.968 25.205 1.00 8.17 O ANISOU 1156 O GLN A 143 754 1233 1041 275 -118 -151 O ATOM 1157 CB GLN A 143 56.510 35.348 25.925 1.00 8.51 C ANISOU 1157 CB GLN A 143 786 1283 1083 310 -81 -2 C ATOM 1158 CG GLN A 143 55.037 35.780 25.836 1.00 9.52 C ANISOU 1158 CG GLN A 143 735 1350 1442 276 -22 -164 C ATOM 1159 CD GLN A 143 54.079 34.634 25.686 1.00 8.74 C ANISOU 1159 CD GLN A 143 703 1443 1094 252 57 -184 C ATOM 1160 OE1 GLN A 143 54.379 33.597 25.099 1.00 9.55 O ANISOU 1160 OE1 GLN A 143 766 1339 1434 209 43 -118 O ATOM 1161 NE2 GLN A 143 52.845 34.797 26.219 1.00 9.91 N ANISOU 1161 NE2 GLN A 143 810 1385 1475 245 49 -155 N ATOM 1162 N GLY A 144 59.321 35.865 27.436 1.00 9.25 N ANISOU 1162 N GLY A 144 831 1594 1001 329 -105 -156 N ATOM 1163 CA GLY A 144 60.683 35.285 27.633 1.00 9.92 C ANISOU 1163 CA GLY A 144 784 1683 1208 259 -221 -6 C ATOM 1164 C GLY A 144 61.727 36.336 27.254 1.00 9.07 C ANISOU 1164 C GLY A 144 910 1496 956 242 -116 -215 C ATOM 1165 O GLY A 144 61.683 37.518 27.660 1.00 10.82 O ANISOU 1165 O GLY A 144 1058 1689 1263 285 -173 -496 O ATOM 1166 N ASP A 145 62.722 35.881 26.483 1.00 8.87 N ANISOU 1166 N ASP A 145 809 1350 1129 256 -212 -250 N ATOM 1167 CA ASP A 145 63.867 36.709 26.139 1.00 9.25 C ANISOU 1167 CA ASP A 145 811 1383 1234 225 -217 -218 C ATOM 1168 C ASP A 145 63.683 37.556 24.869 1.00 9.21 C ANISOU 1168 C ASP A 145 788 1255 1372 153 -226 -183 C ATOM 1169 O ASP A 145 64.595 38.246 24.455 1.00 9.90 O ANISOU 1169 O ASP A 145 818 1511 1339 30 -242 -232 O ATOM 1170 CB ASP A 145 65.095 35.771 25.945 1.00 9.78 C ANISOU 1170 CB ASP A 145 775 1457 1393 293 -264 -201 C ATOM 1171 CG ASP A 145 65.585 35.130 27.210 1.00 11.27 C ANISOU 1171 CG ASP A 145 944 1941 1290 433 -199 -209 C ATOM 1172 OD1 ASP A 145 65.381 35.731 28.297 1.00 16.47 O ANISOU 1172 OD1 ASP A 145 1748 2988 1367 1170 -498 -409 O ATOM 1173 OD2 ASP A 145 66.194 34.035 27.120 1.00 11.61 O ANISOU 1173 OD2 ASP A 145 1149 1830 1321 445 -242 20 O ATOM 1174 N ALA A 146 62.478 37.512 24.247 1.00 8.61 N ANISOU 1174 N ALA A 146 761 1286 1145 185 -175 -221 N ATOM 1175 CA ALA A 146 62.288 38.217 22.979 1.00 8.52 C ANISOU 1175 CA ALA A 146 756 1242 1160 135 -168 -241 C ATOM 1176 C ALA A 146 62.381 39.703 23.166 1.00 8.84 C ANISOU 1176 C ALA A 146 809 1198 1268 228 -189 -258 C ATOM 1177 O ALA A 146 61.797 40.233 24.142 1.00 10.21 O ANISOU 1177 O ALA A 146 1110 1391 1282 242 -40 -330 O ATOM 1178 CB ALA A 146 60.915 37.797 22.394 1.00 9.46 C ANISOU 1178 CB ALA A 146 818 1426 1262 145 -305 -145 C ATOM 1179 N THR A 147 62.997 40.395 22.220 1.00 8.92 N ANISOU 1179 N THR A 147 840 1151 1313 105 -103 -273 N ATOM 1180 CA THR A 147 63.100 41.854 22.191 1.00 9.68 C ANISOU 1180 CA THR A 147 1005 1120 1461 67 -139 -306 C ATOM 1181 C THR A 147 62.869 42.344 20.768 1.00 9.24 C ANISOU 1181 C THR A 147 905 1115 1403 216 -80 -363 C ATOM 1182 O THR A 147 63.066 41.643 19.786 1.00 10.43 O ANISOU 1182 O THR A 147 1130 1228 1507 305 -86 -416 O ATOM 1183 CB THR A 147 64.468 42.341 22.707 1.00 11.86 C ANISOU 1183 CB THR A 147 1232 1206 1956 82 -411 -371 C ATOM 1184 OG1 THR A 147 65.499 41.858 21.831 1.00 13.63 O ANISOU 1184 OG1 THR A 147 974 1664 2411 33 -218 -373 O ATOM 1185 CG2 THR A 147 64.707 41.938 24.142 1.00 15.05 C ANISOU 1185 CG2 THR A 147 1550 2000 2028 161 -705 -463 C ATOM 1186 N THR A 148 62.443 43.629 20.662 1.00 10.73 N ANISOU 1186 N THR A 148 1141 1186 1650 271 -230 -375 N ATOM 1187 CA THR A 148 62.279 44.291 19.403 1.00 10.46 C ANISOU 1187 CA THR A 148 1145 1134 1599 205 -161 -392 C ATOM 1188 C THR A 148 63.092 45.537 19.335 1.00 11.91 C ANISOU 1188 C THR A 148 1056 1240 2120 176 -103 -425 C ATOM 1189 O THR A 148 63.318 46.202 20.375 1.00 14.73 O ANISOU 1189 O THR A 148 1547 1510 2400 -144 -99 -641 O ATOM 1190 CB THR A 148 60.778 44.648 19.095 1.00 10.91 C ANISOU 1190 CB THR A 148 1137 1296 1608 156 -240 -190 C ATOM 1191 OG1 THR A 148 60.232 45.390 20.178 1.00 12.34 O ANISOU 1191 OG1 THR A 148 1161 1415 1995 243 -177 -429 O ATOM 1192 CG2 THR A 148 59.948 43.400 18.858 1.00 11.30 C ANISOU 1192 CG2 THR A 148 1108 1350 1729 46 -131 -308 C ATOM 1193 N GLY A 149 63.510 45.950 18.150 1.00 13.53 N ANISOU 1193 N GLY A 149 1097 1541 2375 -92 75 -317 N ATOM 1194 CA GLY A 149 64.113 47.219 17.906 1.00 16.32 C ANISOU 1194 CA GLY A 149 1188 1688 3172 -133 -76 -44 C ATOM 1195 C GLY A 149 65.616 47.167 17.668 1.00 19.18 C ANISOU 1195 C GLY A 149 1247 1450 4412 -169 209 -441 C ATOM 1196 O GLY A 149 66.142 48.159 17.138 1.00 25.26 O ANISOU 1196 O GLY A 149 1460 1883 6017 -94 812 112 O ATOM 1197 N THR A 150 66.300 46.098 18.014 1.00 17.43 N ANISOU 1197 N THR A 150 1098 1794 3568 53 -148 -681 N ATOM 1198 CA THR A 150 67.761 46.063 17.722 1.00 19.78 C ANISOU 1198 CA THR A 150 1048 2156 4126 -185 -50 -839 C ATOM 1199 C THR A 150 67.946 45.857 16.204 1.00 18.14 C ANISOU 1199 C THR A 150 848 1781 4092 -195 49 -533 C ATOM 1200 O THR A 150 67.479 44.865 15.637 1.00 17.32 O ANISOU 1200 O THR A 150 1034 1708 3675 -148 -92 -383 O ATOM 1201 CB THR A 150 68.423 44.933 18.529 1.00 25.14 C ANISOU 1201 CB THR A 150 1132 3820 4364 278 -846 -326 C ATOM 1202 OG1 THR A 150 68.236 45.257 19.914 1.00 31.69 O ANISOU 1202 OG1 THR A 150 1698 5779 4266 -488 -947 -398 O ATOM 1203 CG2 THR A 150 69.900 44.826 18.216 1.00 28.58 C ANISOU 1203 CG2 THR A 150 1135 3580 5875 -92 -346 246 C ATOM 1204 N ASP A 151 68.563 46.867 15.578 1.00 21.39 N ANISOU 1204 N ASP A 151 1061 2020 4847 -399 289 -438 N ATOM 1205 CA ASP A 151 68.686 46.962 14.137 1.00 21.13 C ANISOU 1205 CA ASP A 151 1143 1709 4979 -364 611 -123 C ATOM 1206 C ASP A 151 67.291 46.883 13.515 1.00 21.14 C ANISOU 1206 C ASP A 151 1230 2146 4457 -199 579 72 C ATOM 1207 O ASP A 151 67.102 46.464 12.385 1.00 20.78 O ANISOU 1207 O ASP A 151 1425 2288 3987 -327 806 639 O ATOM 1208 CB ASP A 151 69.562 45.809 13.583 1.00 27.89 C ANISOU 1208 CB ASP A 151 1681 3196 5459 658 1365 94 C ATOM 1209 CG ASP A 151 70.778 46.558 13.022 1.00 44.03 C ANISOU 1209 CG ASP A 151 5576 5576 5576 0 0 0 C ATOM 1210 OD1 ASP A 151 70.628 47.201 11.959 1.00 44.47 O ANISOU 1210 OD1 ASP A 151 5632 5632 5632 0 0 0 O ATOM 1211 OD2 ASP A 151 71.695 46.669 13.860 1.00 68.57 O ANISOU 1211 OD2 ASP A 151 8684 8684 8684 0 0 0 O ATOM 1212 N GLY A 152 66.237 47.317 14.196 1.00 20.16 N ANISOU 1212 N GLY A 152 1281 1078 5112 -248 677 -231 N ATOM 1213 CA GLY A 152 64.900 47.252 13.647 1.00 16.36 C ANISOU 1213 CA GLY A 152 1498 1225 3340 26 700 212 C ATOM 1214 C GLY A 152 64.285 45.839 13.559 1.00 13.03 C ANISOU 1214 C GLY A 152 818 1212 2800 135 309 423 C ATOM 1215 O GLY A 152 63.306 45.643 12.815 1.00 14.35 O ANISOU 1215 O GLY A 152 949 1552 2816 296 155 486 O ATOM 1216 N ASN A 153 64.864 44.841 14.185 1.00 12.07 N ANISOU 1216 N ASN A 153 859 985 2627 9 7 -28 N ATOM 1217 CA ASN A 153 64.430 43.433 14.027 1.00 10.05 C ANISOU 1217 CA ASN A 153 724 979 2019 -157 7 174 C ATOM 1218 C ASN A 153 63.797 42.901 15.293 1.00 9.06 C ANISOU 1218 C ASN A 153 698 933 1726 50 -122 -61 C ATOM 1219 O ASN A 153 63.885 43.533 16.367 1.00 10.99 O ANISOU 1219 O ASN A 153 963 1158 1951 -110 62 -290 O ATOM 1220 CB ASN A 153 65.640 42.571 13.643 1.00 10.46 C ANISOU 1220 CB ASN A 153 926 1093 1859 -59 93 26 C ATOM 1221 CG ASN A 153 66.279 42.991 12.341 1.00 12.96 C ANISOU 1221 CG ASN A 153 920 1702 2182 -88 159 323 C ATOM 1222 OD1 ASN A 153 65.556 43.342 11.399 1.00 15.76 O ANISOU 1222 OD1 ASN A 153 1210 2522 2107 -26 212 598 O ATOM 1223 ND2 ASN A 153 67.584 42.801 12.250 1.00 14.91 N ANISOU 1223 ND2 ASN A 153 1051 2027 2448 134 421 455 N ATOM 1224 N LEU A 154 63.183 41.721 15.194 1.00 8.13 N ANISOU 1224 N LEU A 154 754 984 1275 -74 -30 39 N ATOM 1225 CA LEU A 154 62.685 40.976 16.336 1.00 7.51 C ANISOU 1225 CA LEU A 154 785 747 1251 44 -16 -182 C ATOM 1226 C LEU A 154 63.709 39.869 16.631 1.00 7.59 C ANISOU 1226 C LEU A 154 707 922 1183 44 15 -47 C ATOM 1227 O LEU A 154 63.958 38.976 15.821 1.00 9.74 O ANISOU 1227 O LEU A 154 1138 1173 1300 466 -236 -343 O ATOM 1228 CB LEU A 154 61.292 40.392 15.962 1.00 7.55 C ANISOU 1228 CB LEU A 154 700 840 1260 101 -66 -52 C ATOM 1229 CG LEU A 154 60.752 39.273 16.850 1.00 8.16 C ANISOU 1229 CG LEU A 154 802 979 1243 -12 93 -111 C ATOM 1230 CD1 LEU A 154 60.555 39.607 18.298 1.00 10.02 C ANISOU 1230 CD1 LEU A 154 938 1557 1217 -37 -17 -118 C ATOM 1231 CD2 LEU A 154 59.422 38.762 16.249 1.00 9.11 C ANISOU 1231 CD2 LEU A 154 789 1197 1388 -72 -19 -89 C ATOM 1232 N GLU A 155 64.346 39.956 17.814 1.00 8.13 N ANISOU 1232 N GLU A 155 735 881 1396 111 -112 -331 N ATOM 1233 CA GLU A 155 65.337 38.938 18.257 1.00 8.07 C ANISOU 1233 CA GLU A 155 665 903 1423 68 -130 -190 C ATOM 1234 C GLU A 155 64.599 38.021 19.208 1.00 7.81 C ANISOU 1234 C GLU A 155 681 1029 1186 203 -12 -264 C ATOM 1235 O GLU A 155 64.316 38.399 20.338 1.00 8.87 O ANISOU 1235 O GLU A 155 977 986 1324 107 -42 -226 O ATOM 1236 CB GLU A 155 66.535 39.615 18.944 1.00 8.98 C ANISOU 1236 CB GLU A 155 843 1117 1368 88 -160 -295 C ATOM 1237 CG GLU A 155 67.420 40.411 18.017 1.00 10.73 C ANISOU 1237 CG GLU A 155 856 1282 1840 -139 -123 -174 C ATOM 1238 CD GLU A 155 68.303 39.619 17.070 1.00 10.28 C ANISOU 1238 CD GLU A 155 811 1318 1681 -8 -88 69 C ATOM 1239 OE1 GLU A 155 68.100 38.367 16.926 1.00 9.67 O ANISOU 1239 OE1 GLU A 155 822 1316 1446 -7 -11 20 O ATOM 1240 OE2 GLU A 155 69.216 40.245 16.508 1.00 12.89 O ANISOU 1240 OE2 GLU A 155 1114 1269 2392 -95 209 -17 O ATOM 1241 N LEU A 156 64.240 36.804 18.810 1.00 7.04 N ANISOU 1241 N LEU A 156 652 904 1053 164 -103 -98 N ATOM 1242 CA LEU A 156 63.455 35.932 19.642 1.00 7.50 C ANISOU 1242 CA LEU A 156 675 1038 1068 278 -93 -71 C ATOM 1243 C LEU A 156 64.227 35.416 20.865 1.00 7.93 C ANISOU 1243 C LEU A 156 732 1188 1017 115 -27 -120 C ATOM 1244 O LEU A 156 63.650 35.247 21.934 1.00 9.93 O ANISOU 1244 O LEU A 156 861 1687 1130 332 -58 -41 O ATOM 1245 CB LEU A 156 62.869 34.791 18.857 1.00 7.12 C ANISOU 1245 CB LEU A 156 593 893 1155 164 -139 66 C ATOM 1246 CG LEU A 156 61.766 35.164 17.849 1.00 7.46 C ANISOU 1246 CG LEU A 156 689 1039 1037 162 -104 78 C ATOM 1247 CD1 LEU A 156 61.505 34.043 16.870 1.00 8.34 C ANISOU 1247 CD1 LEU A 156 742 1214 1135 56 -202 -78 C ATOM 1248 CD2 LEU A 156 60.460 35.529 18.593 1.00 8.84 C ANISOU 1248 CD2 LEU A 156 671 1199 1405 264 -105 -54 C ATOM 1249 N THR A 157 65.529 35.161 20.679 1.00 7.53 N ANISOU 1249 N THR A 157 696 1090 1006 212 -153 -35 N ATOM 1250 CA THR A 157 66.379 34.700 21.770 1.00 7.65 C ANISOU 1250 CA THR A 157 758 1050 1028 117 -124 71 C ATOM 1251 C THR A 157 67.493 35.730 22.019 1.00 8.49 C ANISOU 1251 C THR A 157 823 1153 1168 63 -188 -94 C ATOM 1252 O THR A 157 67.779 36.631 21.231 1.00 9.32 O ANISOU 1252 O THR A 157 1044 1083 1327 -73 -246 -6 O ATOM 1253 CB THR A 157 66.905 33.291 21.493 1.00 8.15 C ANISOU 1253 CB THR A 157 860 1026 1136 129 -304 -60 C ATOM 1254 OG1 THR A 157 67.496 33.230 20.199 1.00 9.27 O ANISOU 1254 OG1 THR A 157 1020 1235 1179 299 -74 -91 O ATOM 1255 CG2 THR A 157 65.819 32.265 21.586 1.00 9.07 C ANISOU 1255 CG2 THR A 157 998 1118 1246 2 -188 -49 C ATOM 1256 N ARG A 158 68.134 35.570 23.202 1.00 9.06 N ANISOU 1256 N ARG A 158 834 1270 1253 -43 -270 -39 N ATOM 1257 CA ARG A 158 69.076 36.597 23.671 1.00 10.59 C ANISOU 1257 CA ARG A 158 980 1513 1432 -139 -323 -132 C ATOM 1258 C ARG A 158 70.349 36.624 22.838 1.00 10.45 C ANISOU 1258 C ARG A 158 972 1290 1612 -68 -315 -206 C ATOM 1259 O ARG A 158 70.944 35.587 22.519 1.00 11.09 O ANISOU 1259 O ARG A 158 862 1312 1937 18 -289 -98 O ATOM 1260 CB ARG A 158 69.359 36.360 25.145 1.00 16.92 C ANISOU 1260 CB ARG A 158 1403 3351 1518 -836 -637 -150 C ATOM 1261 CG ARG A 158 69.983 37.511 25.870 1.00 18.86 C ANISOU 1261 CG ARG A 158 2062 3028 1898 -208 -457 -906 C ATOM 1262 CD ARG A 158 69.078 38.685 26.138 1.00 23.79 C ANISOU 1262 CD ARG A 158 3326 3394 2096 703 321 287 C ATOM 1263 NE ARG A 158 68.002 38.384 27.076 1.00 19.41 N ANISOU 1263 NE ARG A 158 2320 2402 2473 334 -165 103 N ATOM 1264 CZ ARG A 158 66.926 39.158 27.299 1.00 21.24 C ANISOU 1264 CZ ARG A 158 2630 2407 2835 600 -289 -455 C ATOM 1265 NH1 ARG A 158 66.671 40.268 26.681 1.00 29.20 N ANISOU 1265 NH1 ARG A 158 5485 3024 2311 1860 -943 -564 N ATOM 1266 NH2 ARG A 158 66.082 38.743 28.225 1.00 24.70 N ANISOU 1266 NH2 ARG A 158 1956 3983 3211 137 -315 -827 N ATOM 1267 N VAL A 159 70.791 37.843 22.556 1.00 12.18 N ANISOU 1267 N VAL A 159 970 1423 2120 -237 -299 -44 N ATOM 1268 CA VAL A 159 72.012 38.154 21.809 1.00 12.79 C ANISOU 1268 CA VAL A 159 869 1609 2260 -169 -240 -75 C ATOM 1269 C VAL A 159 72.795 39.141 22.660 1.00 15.31 C ANISOU 1269 C VAL A 159 1021 1639 3016 -332 -73 -428 C ATOM 1270 O VAL A 159 72.225 40.110 23.141 1.00 18.96 O ANISOU 1270 O VAL A 159 1428 1850 3750 -368 98 -893 O ATOM 1271 CB VAL A 159 71.742 38.629 20.388 1.00 14.52 C ANISOU 1271 CB VAL A 159 1151 1697 2534 -97 -180 430 C ATOM 1272 CG1 VAL A 159 73.038 38.731 19.573 1.00 20.61 C ANISOU 1272 CG1 VAL A 159 1569 2895 3172 -107 292 1049 C ATOM 1273 CG2 VAL A 159 70.828 37.741 19.570 1.00 15.48 C ANISOU 1273 CG2 VAL A 159 1651 2008 2076 -136 -231 116 C ATOM 1274 N SER A 160 74.067 38.903 22.843 1.00 17.27 N ANISOU 1274 N SER A 160 1034 2319 3046 -379 -253 -856 N ATOM 1275 CA SER A 160 74.926 39.702 23.653 1.00 24.22 C ANISOU 1275 CA SER A 160 1613 2669 4693 -654 -939 -1084 C ATOM 1276 C SER A 160 75.148 41.005 22.902 1.00 29.07 C ANISOU 1276 C SER A 160 2868 3200 4703 -1686 -515 -1091 C ATOM 1277 O SER A 160 74.891 41.216 21.727 1.00 26.87 O ANISOU 1277 O SER A 160 2410 3217 4332 -1439 475 -995 O ATOM 1278 CB SER A 160 76.211 38.892 23.986 1.00 26.95 C ANISOU 1278 CB SER A 160 1319 4991 3676 205 -732 -2042 C ATOM 1279 OG SER A 160 77.071 39.111 22.894 1.00 34.81 O ANISOU 1279 OG SER A 160 2870 4643 5388 -902 812 -2401 O ATOM 1280 N SER A 161 75.653 41.977 23.662 1.00 31.68 N ANISOU 1280 N SER A 161 4012 4012 4012 0 0 0 N ATOM 1281 CA SER A 161 75.844 43.341 23.224 1.00 45.50 C ANISOU 1281 CA SER A 161 5763 5763 5763 0 0 0 C ATOM 1282 C SER A 161 76.744 43.428 22.006 1.00 36.62 C ANISOU 1282 C SER A 161 4638 4638 4638 0 0 0 C ATOM 1283 O SER A 161 76.561 44.218 21.087 1.00 40.80 O ANISOU 1283 O SER A 161 5167 5167 5167 0 0 0 O ATOM 1284 CB SER A 161 76.448 44.174 24.361 1.00 42.95 C ANISOU 1284 CB SER A 161 5440 5440 5440 0 0 0 C ATOM 1285 OG SER A 161 75.866 45.462 24.388 1.00 43.89 O ANISOU 1285 OG SER A 161 5559 5559 5559 0 0 0 O ATOM 1286 N ASN A 162 77.616 42.441 21.893 1.00 33.11 N ANISOU 1286 N ASN A 162 4193 4193 4193 0 0 0 N ATOM 1287 CA ASN A 162 78.471 42.260 20.736 1.00 71.32 C ANISOU 1287 CA ASN A 162 9033 9033 9033 0 0 0 C ATOM 1288 C ASN A 162 77.909 41.494 19.544 1.00 52.40 C ANISOU 1288 C ASN A 162 6637 6637 6637 0 0 0 C ATOM 1289 O ASN A 162 78.609 41.209 18.557 1.00 36.54 O ANISOU 1289 O ASN A 162 4628 4628 4628 0 0 0 O ATOM 1290 CB ASN A 162 79.724 41.494 21.243 1.00 71.44 C ANISOU 1290 CB ASN A 162 9048 9048 9048 0 0 0 C ATOM 1291 CG ASN A 162 79.506 40.035 20.826 1.00 47.69 C ANISOU 1291 CG ASN A 162 6040 6040 6040 0 0 0 C ATOM 1292 OD1 ASN A 162 79.386 39.263 21.766 1.00 44.41 O ANISOU 1292 OD1 ASN A 162 5625 5625 5625 0 0 0 O ATOM 1293 ND2 ASN A 162 79.451 39.921 19.502 1.00 45.83 N ANISOU 1293 ND2 ASN A 162 5804 5804 5804 0 0 0 N ATOM 1294 N GLY A 163 76.660 41.066 19.639 1.00 34.34 N ANISOU 1294 N GLY A 163 3651 2644 6430 -1645 2188 -517 N ATOM 1295 CA GLY A 163 76.012 40.245 18.652 1.00 31.91 C ANISOU 1295 CA GLY A 163 4560 2026 5238 -764 1078 504 C ATOM 1296 C GLY A 163 76.233 38.744 18.797 1.00 25.30 C ANISOU 1296 C GLY A 163 2821 2058 4497 -392 1019 242 C ATOM 1297 O GLY A 163 75.656 38.016 17.971 1.00 27.34 O ANISOU 1297 O GLY A 163 4329 2187 3614 -246 805 349 O ATOM 1298 N SER A 164 76.824 38.193 19.848 1.00 24.04 N ANISOU 1298 N SER A 164 2339 2180 4391 -918 850 76 N ATOM 1299 CA SER A 164 76.969 36.722 19.923 1.00 21.27 C ANISOU 1299 CA SER A 164 1344 2267 4271 -686 251 175 C ATOM 1300 C SER A 164 75.701 36.084 20.456 1.00 14.47 C ANISOU 1300 C SER A 164 1129 1551 2683 -335 -89 -120 C ATOM 1301 O SER A 164 75.182 36.634 21.455 1.00 16.98 O ANISOU 1301 O SER A 164 1406 1725 3163 -398 -117 -661 O ATOM 1302 CB ASER A 164 78.045 36.323 20.941 0.53 26.30 C ANISOU 1302 CB ASER A 164 1292 3285 5169 -962 -426 -15 C ATOM 1303 CB BSER A 164 78.299 36.342 20.532 0.47 26.93 C ANISOU 1303 CB BSER A 164 1251 3444 5285 -1058 -122 499 C ATOM 1304 OG ASER A 164 79.285 36.878 20.624 0.53 36.28 O ANISOU 1304 OG ASER A 164 1198 6519 5728 -1691 700 -2507 O ATOM 1305 OG BSER A 164 78.307 36.209 21.937 0.47 31.29 O ANISOU 1305 OG BSER A 164 1920 4681 4992 742 -778 -1421 O ATOM 1306 N PRO A 165 75.143 35.052 19.839 1.00 12.30 N ANISOU 1306 N PRO A 165 945 1570 2042 -218 -21 25 N ATOM 1307 CA PRO A 165 74.001 34.418 20.486 1.00 11.16 C ANISOU 1307 CA PRO A 165 878 1378 1880 -129 -185 -10 C ATOM 1308 C PRO A 165 74.342 33.792 21.798 1.00 11.13 C ANISOU 1308 C PRO A 165 892 1331 1901 -21 -179 -28 C ATOM 1309 O PRO A 165 75.430 33.267 21.994 1.00 14.50 O ANISOU 1309 O PRO A 165 1090 2190 2094 444 -204 5 O ATOM 1310 CB PRO A 165 73.544 33.434 19.414 1.00 13.01 C ANISOU 1310 CB PRO A 165 1173 1717 1930 -354 -93 -169 C ATOM 1311 CG PRO A 165 74.816 33.068 18.653 1.00 14.34 C ANISOU 1311 CG PRO A 165 1180 2013 2121 -247 85 -198 C ATOM 1312 CD PRO A 165 75.526 34.378 18.607 1.00 14.53 C ANISOU 1312 CD PRO A 165 1297 1977 2111 -213 145 -34 C ATOM 1313 N GLN A 166 73.338 33.756 22.707 1.00 10.88 N ANISOU 1313 N GLN A 166 810 1367 1853 -166 -371 111 N ATOM 1314 CA GLN A 166 73.506 33.080 23.976 1.00 11.27 C ANISOU 1314 CA GLN A 166 858 1595 1722 -58 -418 41 C ATOM 1315 C GLN A 166 72.761 31.764 24.034 1.00 10.11 C ANISOU 1315 C GLN A 166 676 1599 1472 58 -113 110 C ATOM 1316 O GLN A 166 71.670 31.581 23.420 1.00 10.69 O ANISOU 1316 O GLN A 166 823 1612 1525 -17 -314 -59 O ATOM 1317 CB GLN A 166 72.986 33.957 25.108 1.00 14.25 C ANISOU 1317 CB GLN A 166 1608 1794 1878 -151 -352 -214 C ATOM 1318 CG GLN A 166 73.764 35.297 25.059 1.00 24.10 C ANISOU 1318 CG GLN A 166 2447 1862 4622 -535 -808 -696 C ATOM 1319 CD GLN A 166 75.252 35.191 25.199 1.00 29.67 C ANISOU 1319 CD GLN A 166 2340 5778 2876 -1597 -1034 -314 C ATOM 1320 OE1 GLN A 166 75.784 34.775 26.233 1.00 37.95 O ANISOU 1320 OE1 GLN A 166 3969 6690 3404 307 -1671 -776 O ATOM 1321 NE2 GLN A 166 75.956 35.464 24.083 1.00 62.01 N ANISOU 1321 NE2 GLN A 166 7854 7854 7854 0 0 0 N ATOM 1322 N GLY A 167 73.297 30.827 24.779 1.00 11.16 N ANISOU 1322 N GLY A 167 714 1546 1874 25 -291 154 N ATOM 1323 CA GLY A 167 72.655 29.649 25.155 1.00 10.79 C ANISOU 1323 CA GLY A 167 857 1429 1711 86 -214 13 C ATOM 1324 C GLY A 167 71.525 29.758 26.152 1.00 10.38 C ANISOU 1324 C GLY A 167 783 1569 1495 147 -303 103 C ATOM 1325 O GLY A 167 71.333 30.824 26.752 1.00 11.12 O ANISOU 1325 O GLY A 167 1031 1487 1601 88 -225 49 O ATOM 1326 N SER A 168 70.802 28.664 26.363 1.00 9.35 N ANISOU 1326 N SER A 168 842 1464 1160 201 -297 20 N ATOM 1327 CA SER A 168 69.765 28.555 27.394 1.00 10.03 C ANISOU 1327 CA SER A 168 996 1567 1154 347 -162 304 C ATOM 1328 C SER A 168 68.769 29.681 27.354 1.00 8.95 C ANISOU 1328 C SER A 168 968 1200 1148 155 -206 47 C ATOM 1329 O SER A 168 68.383 30.264 28.395 1.00 12.91 O ANISOU 1329 O SER A 168 1768 1934 1083 736 -315 -12 O ATOM 1330 CB SER A 168 70.452 28.444 28.784 1.00 11.80 C ANISOU 1330 CB SER A 168 1418 1763 1190 381 -263 117 C ATOM 1331 OG SER A 168 71.350 27.344 28.820 1.00 14.42 O ANISOU 1331 OG SER A 168 1420 2283 1640 674 -358 485 O ATOM 1332 N SER A 169 68.257 29.993 26.151 1.00 8.65 N ANISOU 1332 N SER A 169 766 1364 1078 254 -205 2 N ATOM 1333 CA SER A 169 67.374 31.132 25.933 1.00 8.21 C ANISOU 1333 CA SER A 169 840 1124 1080 156 -251 3 C ATOM 1334 C SER A 169 66.091 30.624 25.268 1.00 7.87 C ANISOU 1334 C SER A 169 741 1272 904 235 -159 -102 C ATOM 1335 O SER A 169 66.073 29.686 24.474 1.00 8.53 O ANISOU 1335 O SER A 169 731 1294 1137 209 -130 -122 O ATOM 1336 CB SER A 169 68.093 32.170 25.058 1.00 8.71 C ANISOU 1336 CB SER A 169 774 1226 1229 143 -140 -6 C ATOM 1337 OG SER A 169 67.258 33.332 24.798 1.00 9.08 O ANISOU 1337 OG SER A 169 915 1152 1298 167 -185 75 O ATOM 1338 N VAL A 170 64.977 31.324 25.572 1.00 8.26 N ANISOU 1338 N VAL A 170 773 1260 1028 285 -274 -197 N ATOM 1339 CA VAL A 170 63.672 31.037 24.912 1.00 7.83 C ANISOU 1339 CA VAL A 170 564 1315 1022 127 -140 -182 C ATOM 1340 C VAL A 170 62.940 32.349 24.807 1.00 7.83 C ANISOU 1340 C VAL A 170 648 1301 954 79 -99 -195 C ATOM 1341 O VAL A 170 62.950 33.153 25.766 1.00 8.61 O ANISOU 1341 O VAL A 170 750 1466 974 217 -182 -307 O ATOM 1342 CB VAL A 170 62.958 29.894 25.687 1.00 10.43 C ANISOU 1342 CB VAL A 170 939 1782 1142 43 -27 185 C ATOM 1343 CG1 VAL A 170 62.698 30.260 27.148 1.00 11.71 C ANISOU 1343 CG1 VAL A 170 981 2013 1344 36 22 148 C ATOM 1344 CG2 VAL A 170 61.713 29.388 24.973 1.00 10.57 C ANISOU 1344 CG2 VAL A 170 919 1464 1533 94 -99 111 C ATOM 1345 N GLY A 171 62.239 32.609 23.715 1.00 8.35 N ANISOU 1345 N GLY A 171 656 1437 1002 390 -215 -185 N ATOM 1346 CA GLY A 171 61.436 33.794 23.566 1.00 8.58 C ANISOU 1346 CA GLY A 171 754 1353 1071 314 -273 -317 C ATOM 1347 C GLY A 171 60.392 33.617 22.477 1.00 7.19 C ANISOU 1347 C GLY A 171 607 1167 891 234 -92 -18 C ATOM 1348 O GLY A 171 60.566 32.833 21.545 1.00 7.49 O ANISOU 1348 O GLY A 171 675 1105 994 316 -132 -181 O ATOM 1349 N ARG A 172 59.295 34.396 22.622 1.00 6.81 N ANISOU 1349 N ARG A 172 682 976 867 210 -153 -105 N ATOM 1350 CA ARG A 172 58.179 34.334 21.693 1.00 6.38 C ANISOU 1350 CA ARG A 172 552 984 829 181 -139 -80 C ATOM 1351 C ARG A 172 57.611 35.723 21.447 1.00 6.36 C ANISOU 1351 C ARG A 172 624 933 799 164 -64 -60 C ATOM 1352 O ARG A 172 57.746 36.619 22.286 1.00 7.43 O ANISOU 1352 O ARG A 172 707 1080 967 230 -113 -145 O ATOM 1353 CB ARG A 172 57.063 33.400 22.154 1.00 6.65 C ANISOU 1353 CB ARG A 172 634 965 867 240 -73 -135 C ATOM 1354 CG ARG A 172 57.567 32.109 22.750 1.00 7.84 C ANISOU 1354 CG ARG A 172 827 1083 996 198 80 35 C ATOM 1355 CD ARG A 172 56.596 30.955 22.865 1.00 8.04 C ANISOU 1355 CD ARG A 172 773 1073 1134 252 114 26 C ATOM 1356 NE ARG A 172 55.413 31.326 23.615 1.00 8.19 N ANISOU 1356 NE ARG A 172 716 1263 1056 221 56 69 N ATOM 1357 CZ ARG A 172 54.397 30.496 23.891 1.00 8.26 C ANISOU 1357 CZ ARG A 172 711 1280 1069 271 29 194 C ATOM 1358 NH1 ARG A 172 54.520 29.212 23.645 1.00 9.06 N ANISOU 1358 NH1 ARG A 172 747 1249 1362 281 104 192 N ATOM 1359 NH2 ARG A 172 53.330 31.092 24.370 1.00 9.01 N ANISOU 1359 NH2 ARG A 172 805 1348 1184 328 52 4 N ATOM 1360 N ALA A 173 56.928 35.896 20.300 1.00 6.59 N ANISOU 1360 N ALA A 173 526 980 938 160 -108 -99 N ATOM 1361 CA ALA A 173 56.168 37.093 20.003 1.00 6.56 C ANISOU 1361 CA ALA A 173 497 952 984 169 -107 -151 C ATOM 1362 C ALA A 173 54.803 36.645 19.468 1.00 6.50 C ANISOU 1362 C ALA A 173 540 892 977 101 -46 -95 C ATOM 1363 O ALA A 173 54.737 35.877 18.519 1.00 7.42 O ANISOU 1363 O ALA A 173 520 1084 1146 175 -106 -285 O ATOM 1364 CB ALA A 173 56.878 37.940 18.945 1.00 8.11 C ANISOU 1364 CB ALA A 173 649 987 1368 32 -29 37 C ATOM 1365 N LEU A 174 53.732 37.167 20.095 1.00 6.48 N ANISOU 1365 N LEU A 174 513 869 1019 147 -44 -137 N ATOM 1366 CA LEU A 174 52.361 36.854 19.677 1.00 6.49 C ANISOU 1366 CA LEU A 174 526 836 1042 83 -75 -125 C ATOM 1367 C LEU A 174 51.683 38.133 19.196 1.00 6.65 C ANISOU 1367 C LEU A 174 601 837 1025 160 -1 -16 C ATOM 1368 O LEU A 174 51.840 39.217 19.801 1.00 7.46 O ANISOU 1368 O LEU A 174 734 1004 1026 170 -139 -90 O ATOM 1369 CB LEU A 174 51.503 36.211 20.765 1.00 7.68 C ANISOU 1369 CB LEU A 174 635 962 1247 65 -58 0 C ATOM 1370 CG LEU A 174 52.000 34.860 21.300 1.00 9.05 C ANISOU 1370 CG LEU A 174 742 1372 1242 111 -43 294 C ATOM 1371 CD1 LEU A 174 53.147 34.917 22.252 1.00 13.52 C ANISOU 1371 CD1 LEU A 174 1742 1513 1756 -373 -861 509 C ATOM 1372 CD2 LEU A 174 50.869 34.076 21.937 1.00 17.27 C ANISOU 1372 CD2 LEU A 174 926 1960 3515 74 0 1592 C ATOM 1373 N PHE A 175 50.857 38.029 18.127 1.00 6.93 N ANISOU 1373 N PHE A 175 559 898 1111 108 -85 -101 N ATOM 1374 CA PHE A 175 50.120 39.216 17.710 1.00 6.64 C ANISOU 1374 CA PHE A 175 530 801 1131 99 -24 -1 C ATOM 1375 C PHE A 175 49.085 39.578 18.814 1.00 6.87 C ANISOU 1375 C PHE A 175 536 827 1184 100 -82 -42 C ATOM 1376 O PHE A 175 48.448 38.693 19.409 1.00 7.49 O ANISOU 1376 O PHE A 175 634 869 1272 114 79 32 O ATOM 1377 CB PHE A 175 49.479 39.043 16.326 1.00 7.20 C ANISOU 1377 CB PHE A 175 646 906 1117 71 -89 -75 C ATOM 1378 CG PHE A 175 48.876 40.358 15.808 1.00 7.91 C ANISOU 1378 CG PHE A 175 827 1052 1052 111 -162 -31 C ATOM 1379 CD1 PHE A 175 49.724 41.406 15.449 1.00 8.71 C ANISOU 1379 CD1 PHE A 175 985 1012 1229 66 -121 44 C ATOM 1380 CD2 PHE A 175 47.504 40.534 15.690 1.00 8.94 C ANISOU 1380 CD2 PHE A 175 841 1330 1141 290 -104 22 C ATOM 1381 CE1 PHE A 175 49.227 42.626 15.028 1.00 10.72 C ANISOU 1381 CE1 PHE A 175 1267 1251 1453 282 -85 266 C ATOM 1382 CE2 PHE A 175 47.020 41.751 15.231 1.00 10.56 C ANISOU 1382 CE2 PHE A 175 995 1538 1381 442 -173 116 C ATOM 1383 CZ PHE A 175 47.859 42.800 14.916 1.00 11.71 C ANISOU 1383 CZ PHE A 175 1345 1268 1727 379 -138 13 C ATOM 1384 N TYR A 176 48.885 40.870 19.037 1.00 7.33 N ANISOU 1384 N TYR A 176 555 847 1316 55 103 -41 N ATOM 1385 CA TYR A 176 48.077 41.293 20.171 1.00 8.50 C ANISOU 1385 CA TYR A 176 739 1100 1311 -10 71 -217 C ATOM 1386 C TYR A 176 46.601 40.875 20.066 1.00 8.30 C ANISOU 1386 C TYR A 176 653 814 1608 176 158 9 C ATOM 1387 O TYR A 176 46.003 40.494 21.077 1.00 9.97 O ANISOU 1387 O TYR A 176 899 1125 1671 69 305 -63 O ATOM 1388 CB TYR A 176 48.172 42.826 20.326 1.00 10.62 C ANISOU 1388 CB TYR A 176 980 1138 1818 -115 332 -491 C ATOM 1389 CG TYR A 176 47.770 43.380 21.621 1.00 10.66 C ANISOU 1389 CG TYR A 176 886 1406 1658 137 50 -426 C ATOM 1390 CD1 TYR A 176 46.467 43.796 21.856 1.00 12.29 C ANISOU 1390 CD1 TYR A 176 1391 1470 1693 729 292 156 C ATOM 1391 CD2 TYR A 176 48.667 43.697 22.618 1.00 18.68 C ANISOU 1391 CD2 TYR A 176 1683 2870 2369 556 -433 -1384 C ATOM 1392 CE1 TYR A 176 46.016 44.328 23.010 1.00 16.69 C ANISOU 1392 CE1 TYR A 176 2226 1543 2415 434 950 -276 C ATOM 1393 CE2 TYR A 176 48.208 44.292 23.781 1.00 23.30 C ANISOU 1393 CE2 TYR A 176 2755 3473 2408 -105 84 -1634 C ATOM 1394 CZ TYR A 176 46.894 44.594 24.019 1.00 24.66 C ANISOU 1394 CZ TYR A 176 3366 3441 2331 719 692 -1424 C ATOM 1395 OH TYR A 176 46.381 45.196 25.135 1.00 36.37 O ANISOU 1395 OH TYR A 176 4932 4929 3618 -132 1758 -2751 O ATOM 1396 N ALA A 177 46.021 41.011 18.868 1.00 8.45 N ANISOU 1396 N ALA A 177 508 955 1667 -8 105 25 N ATOM 1397 CA ALA A 177 44.572 40.679 18.753 1.00 9.64 C ANISOU 1397 CA ALA A 177 485 835 2251 46 -36 -60 C ATOM 1398 C ALA A 177 44.388 39.158 18.691 1.00 9.56 C ANISOU 1398 C ALA A 177 467 903 2171 91 8 -92 C ATOM 1399 O ALA A 177 45.079 38.445 17.947 1.00 10.18 O ANISOU 1399 O ALA A 177 724 974 2073 193 -75 -265 O ATOM 1400 CB ALA A 177 43.988 41.305 17.518 1.00 11.68 C ANISOU 1400 CB ALA A 177 687 1019 2624 147 -214 124 C ATOM 1401 N PRO A 178 43.329 38.629 19.353 1.00 9.29 N ANISOU 1401 N PRO A 178 647 868 1926 71 -113 22 N ATOM 1402 CA PRO A 178 42.864 37.264 19.099 1.00 9.88 C ANISOU 1402 CA PRO A 178 890 913 1858 -85 -357 76 C ATOM 1403 C PRO A 178 42.395 37.151 17.660 1.00 8.27 C ANISOU 1403 C PRO A 178 570 820 1673 29 -90 240 C ATOM 1404 O PRO A 178 41.898 38.117 17.054 1.00 9.47 O ANISOU 1404 O PRO A 178 783 891 1835 74 -117 171 O ATOM 1405 CB PRO A 178 41.710 37.113 20.048 1.00 13.36 C ANISOU 1405 CB PRO A 178 1762 1593 1597 -750 -160 100 C ATOM 1406 CG PRO A 178 41.544 38.293 20.860 1.00 21.75 C ANISOU 1406 CG PRO A 178 2113 1436 4511 -465 1849 -436 C ATOM 1407 CD PRO A 178 42.436 39.361 20.276 1.00 11.64 C ANISOU 1407 CD PRO A 178 847 1174 2293 -3 265 -87 C ATOM 1408 N VAL A 179 42.467 35.947 17.098 1.00 8.13 N ANISOU 1408 N VAL A 179 660 876 1476 5 -82 280 N ATOM 1409 CA VAL A 179 42.173 35.606 15.726 1.00 8.02 C ANISOU 1409 CA VAL A 179 686 888 1399 83 67 360 C ATOM 1410 C VAL A 179 41.033 34.558 15.693 1.00 7.90 C ANISOU 1410 C VAL A 179 644 946 1337 171 20 109 C ATOM 1411 O VAL A 179 41.079 33.545 16.425 1.00 7.63 O ANISOU 1411 O VAL A 179 632 860 1336 73 -10 114 O ATOM 1412 CB VAL A 179 43.444 35.046 15.036 1.00 9.55 C ANISOU 1412 CB VAL A 179 778 1039 1723 98 255 243 C ATOM 1413 CG1 VAL A 179 43.118 34.713 13.589 1.00 12.28 C ANISOU 1413 CG1 VAL A 179 1023 1773 1755 -233 363 23 C ATOM 1414 CG2 VAL A 179 44.599 36.024 15.145 1.00 10.82 C ANISOU 1414 CG2 VAL A 179 722 1429 1860 -91 134 218 C ATOM 1415 N HIS A 180 40.019 34.834 14.878 1.00 8.46 N ANISOU 1415 N HIS A 180 699 923 1512 10 -56 172 N ATOM 1416 CA HIS A 180 38.860 33.957 14.784 1.00 8.49 C ANISOU 1416 CA HIS A 180 800 882 1466 122 -114 54 C ATOM 1417 C HIS A 180 39.039 32.974 13.624 1.00 8.89 C ANISOU 1417 C HIS A 180 881 1068 1346 112 -62 -39 C ATOM 1418 O HIS A 180 39.044 33.360 12.486 1.00 12.60 O ANISOU 1418 O HIS A 180 1892 1293 1482 173 -91 49 O ATOM 1419 CB HIS A 180 37.633 34.870 14.527 1.00 9.57 C ANISOU 1419 CB HIS A 180 731 989 1827 107 -210 -31 C ATOM 1420 CG HIS A 180 36.340 34.244 14.977 1.00 9.43 C ANISOU 1420 CG HIS A 180 729 1089 1678 3 -178 -317 C ATOM 1421 ND1 HIS A 180 35.146 34.923 14.751 1.00 11.09 N ANISOU 1421 ND1 HIS A 180 704 1179 2226 135 -276 -363 N ATOM 1422 CD2 HIS A 180 36.065 33.127 15.644 1.00 10.20 C ANISOU 1422 CD2 HIS A 180 621 1319 1840 20 -19 -140 C ATOM 1423 CE1 HIS A 180 34.216 34.210 15.355 1.00 11.25 C ANISOU 1423 CE1 HIS A 180 820 1317 2032 97 -299 -474 C ATOM 1424 NE2 HIS A 180 34.675 33.118 15.896 1.00 10.97 N ANISOU 1424 NE2 HIS A 180 716 1427 1920 75 -7 -427 N ATOM 1425 N ILE A 181 39.267 31.675 13.927 1.00 9.39 N ANISOU 1425 N ILE A 181 919 1098 1461 63 128 -128 N ATOM 1426 CA ILE A 181 39.592 30.678 12.928 1.00 9.56 C ANISOU 1426 CA ILE A 181 1012 1142 1387 162 170 -24 C ATOM 1427 C ILE A 181 38.457 29.739 12.590 1.00 10.26 C ANISOU 1427 C ILE A 181 1194 1204 1404 79 136 -189 C ATOM 1428 O ILE A 181 38.513 29.000 11.595 1.00 12.45 O ANISOU 1428 O ILE A 181 1669 1384 1562 10 210 -285 O ATOM 1429 CB ILE A 181 40.910 29.917 13.230 1.00 11.68 C ANISOU 1429 CB ILE A 181 998 1219 2112 233 292 114 C ATOM 1430 CG1 ILE A 181 40.811 29.105 14.498 1.00 10.84 C ANISOU 1430 CG1 ILE A 181 1026 1285 1705 216 21 -37 C ATOM 1431 CG2 ILE A 181 42.072 30.887 13.158 1.00 12.13 C ANISOU 1431 CG2 ILE A 181 998 1556 1942 54 81 57 C ATOM 1432 CD1 ILE A 181 41.887 28.051 14.624 1.00 13.96 C ANISOU 1432 CD1 ILE A 181 1626 1643 1905 534 -249 -254 C ATOM 1433 N TRP A 182 37.370 29.779 13.329 1.00 10.98 N ANISOU 1433 N TRP A 182 1086 1472 1511 -244 88 -257 N ATOM 1434 CA TRP A 182 36.170 29.008 13.063 1.00 11.27 C ANISOU 1434 CA TRP A 182 1291 1403 1484 -310 -20 -76 C ATOM 1435 C TRP A 182 34.991 29.862 13.431 1.00 10.86 C ANISOU 1435 C TRP A 182 1100 1268 1655 -383 -222 -80 C ATOM 1436 O TRP A 182 35.030 30.575 14.455 1.00 11.99 O ANISOU 1436 O TRP A 182 1220 1471 1753 -68 -296 -262 O ATOM 1437 CB TRP A 182 36.112 27.690 13.825 1.00 11.99 C ANISOU 1437 CB TRP A 182 1403 1316 1724 -211 -99 -129 C ATOM 1438 CG TRP A 182 34.816 26.911 13.583 1.00 12.92 C ANISOU 1438 CG TRP A 182 1797 1250 1741 -447 -241 59 C ATOM 1439 CD1 TRP A 182 34.533 26.077 12.551 1.00 17.54 C ANISOU 1439 CD1 TRP A 182 2640 1768 2090 -1053 -106 -226 C ATOM 1440 CD2 TRP A 182 33.597 27.020 14.318 1.00 12.70 C ANISOU 1440 CD2 TRP A 182 1401 1133 2172 -482 -309 248 C ATOM 1441 NE1 TRP A 182 33.244 25.592 12.642 1.00 18.06 N ANISOU 1441 NE1 TRP A 182 2736 1958 2000 -1241 -612 213 N ATOM 1442 CE2 TRP A 182 32.652 26.149 13.733 1.00 15.31 C ANISOU 1442 CE2 TRP A 182 1895 1703 2075 -806 -737 534 C ATOM 1443 CE3 TRP A 182 33.196 27.684 15.489 1.00 13.13 C ANISOU 1443 CE3 TRP A 182 1188 1400 2278 -220 -237 181 C ATOM 1444 CZ2 TRP A 182 31.350 25.986 14.216 1.00 17.24 C ANISOU 1444 CZ2 TRP A 182 1639 1943 2805 -910 -905 763 C ATOM 1445 CZ3 TRP A 182 31.940 27.531 16.026 1.00 14.78 C ANISOU 1445 CZ3 TRP A 182 1295 1919 2262 -289 -186 617 C ATOM 1446 CH2 TRP A 182 31.035 26.678 15.384 1.00 17.35 C ANISOU 1446 CH2 TRP A 182 1467 2191 2772 -637 -505 966 C ATOM 1447 N GLU A 183 33.906 29.830 12.679 1.00 10.73 N ANISOU 1447 N GLU A 183 1194 1337 1445 -343 -136 -18 N ATOM 1448 CA GLU A 183 32.660 30.463 13.067 1.00 10.66 C ANISOU 1448 CA GLU A 183 1177 1242 1533 -269 -221 -36 C ATOM 1449 C GLU A 183 31.556 29.629 12.462 1.00 9.74 C ANISOU 1449 C GLU A 183 1151 1096 1364 -252 -86 101 C ATOM 1450 O GLU A 183 31.689 29.035 11.388 1.00 9.87 O ANISOU 1450 O GLU A 183 1184 1201 1273 -143 -104 -27 O ATOM 1451 CB GLU A 183 32.643 31.916 12.618 1.00 14.54 C ANISOU 1451 CB GLU A 183 1782 1203 2403 -403 -462 145 C ATOM 1452 CG GLU A 183 31.624 32.816 13.293 1.00 17.26 C ANISOU 1452 CG GLU A 183 2286 1391 2718 -45 -576 -166 C ATOM 1453 CD GLU A 183 30.293 32.798 12.631 1.00 18.02 C ANISOU 1453 CD GLU A 183 1985 1850 2844 -77 -159 193 C ATOM 1454 OE1 GLU A 183 30.188 32.531 11.422 1.00 24.15 O ANISOU 1454 OE1 GLU A 183 2865 2519 3564 391 -1285 -998 O ATOM 1455 OE2 GLU A 183 29.304 33.033 13.336 1.00 29.00 O ANISOU 1455 OE2 GLU A 183 2185 3597 4965 84 713 -100 O ATOM 1456 N SER A 184 30.411 29.561 13.146 1.00 10.91 N ANISOU 1456 N SER A 184 1189 1296 1558 -241 19 -226 N ATOM 1457 CA SER A 184 29.361 28.637 12.733 1.00 9.69 C ANISOU 1457 CA SER A 184 1061 1134 1397 -184 -168 82 C ATOM 1458 C SER A 184 28.787 28.891 11.341 1.00 9.59 C ANISOU 1458 C SER A 184 1102 1097 1355 -435 0 100 C ATOM 1459 O SER A 184 28.271 27.927 10.709 1.00 9.99 O ANISOU 1459 O SER A 184 1429 960 1315 -311 -175 148 O ATOM 1460 CB SER A 184 28.254 28.613 13.803 1.00 11.78 C ANISOU 1460 CB SER A 184 1299 1690 1377 -200 57 -40 C ATOM 1461 OG SER A 184 27.573 29.868 13.867 1.00 13.32 O ANISOU 1461 OG SER A 184 1243 1887 1808 -107 -12 -223 O ATOM 1462 N SER A 185 28.803 30.117 10.859 1.00 9.12 N ANISOU 1462 N SER A 185 956 909 1515 -230 54 72 N ATOM 1463 CA SER A 185 28.291 30.463 9.531 1.00 10.38 C ANISOU 1463 CA SER A 185 921 1228 1698 -151 -11 224 C ATOM 1464 C SER A 185 29.355 30.385 8.435 1.00 9.76 C ANISOU 1464 C SER A 185 995 1136 1487 -155 -124 273 C ATOM 1465 O SER A 185 29.033 30.590 7.254 1.00 10.51 O ANISOU 1465 O SER A 185 1057 1314 1523 -125 -175 101 O ATOM 1466 CB ASER A 185 27.572 31.811 9.477 0.59 12.18 C ANISOU 1466 CB ASER A 185 1121 1285 2107 -25 -73 204 C ATOM 1467 CB BSER A 185 27.768 31.921 9.612 0.41 14.39 C ANISOU 1467 CB BSER A 185 1053 1454 2826 254 455 710 C ATOM 1468 OG ASER A 185 28.473 32.874 9.356 0.59 19.44 O ANISOU 1468 OG ASER A 185 2190 1214 3801 -489 1085 -364 O ATOM 1469 OG BSER A 185 26.594 31.988 10.430 0.41 16.62 O ANISOU 1469 OG BSER A 185 1962 1454 2742 88 1067 480 O ATOM 1470 N ALA A 186 30.638 30.144 8.795 1.00 9.89 N ANISOU 1470 N ALA A 186 940 1226 1498 -105 -132 -145 N ATOM 1471 CA ALA A 186 31.668 30.168 7.780 1.00 10.06 C ANISOU 1471 CA ALA A 186 1062 1195 1472 -117 -48 -106 C ATOM 1472 C ALA A 186 31.493 28.973 6.829 1.00 9.85 C ANISOU 1472 C ALA A 186 1369 954 1328 -46 -121 29 C ATOM 1473 O ALA A 186 31.279 27.841 7.293 1.00 14.09 O ANISOU 1473 O ALA A 186 2374 1195 1654 -231 11 197 O ATOM 1474 CB ALA A 186 33.052 30.171 8.456 1.00 14.36 C ANISOU 1474 CB ALA A 186 916 2676 1730 -106 77 -744 C ATOM 1475 N VAL A 187 31.621 29.237 5.548 1.00 8.45 N ANISOU 1475 N VAL A 187 773 987 1371 -76 50 1 N ATOM 1476 CA VAL A 187 31.646 28.227 4.520 1.00 9.43 C ANISOU 1476 CA VAL A 187 818 1274 1402 -164 23 -73 C ATOM 1477 C VAL A 187 33.068 27.896 4.064 1.00 9.00 C ANISOU 1477 C VAL A 187 865 1090 1381 -60 92 -170 C ATOM 1478 O VAL A 187 33.323 26.797 3.561 1.00 11.00 O ANISOU 1478 O VAL A 187 986 1278 1810 -167 123 -305 O ATOM 1479 CB VAL A 187 30.733 28.549 3.325 1.00 11.06 C ANISOU 1479 CB VAL A 187 930 1758 1410 159 -40 -309 C ATOM 1480 CG1 VAL A 187 29.320 28.906 3.820 1.00 14.18 C ANISOU 1480 CG1 VAL A 187 859 2658 1738 177 -133 -477 C ATOM 1481 CG2 VAL A 187 31.315 29.652 2.473 1.00 15.05 C ANISOU 1481 CG2 VAL A 187 1357 2545 1676 153 -140 462 C ATOM 1482 N VAL A 188 34.014 28.824 4.248 1.00 10.25 N ANISOU 1482 N VAL A 188 813 1169 1816 -154 6 -130 N ATOM 1483 CA VAL A 188 35.442 28.574 4.068 1.00 12.31 C ANISOU 1483 CA VAL A 188 756 1840 1965 -66 44 -759 C ATOM 1484 C VAL A 188 36.201 29.475 5.045 1.00 9.50 C ANISOU 1484 C VAL A 188 806 1090 1624 -128 108 -166 C ATOM 1485 O VAL A 188 35.846 30.639 5.226 1.00 12.03 O ANISOU 1485 O VAL A 188 1343 1101 2015 70 -376 -34 O ATOM 1486 CB AVAL A 188 35.976 28.859 2.665 0.68 16.10 C ANISOU 1486 CB AVAL A 188 1080 2943 1942 -281 259 -1078 C ATOM 1487 CB BVAL A 188 35.988 28.173 2.732 0.32 23.47 C ANISOU 1487 CB BVAL A 188 1378 5325 1996 -70 119 -1603 C ATOM 1488 CG1AVAL A 188 35.577 30.146 2.095 0.68 20.86 C ANISOU 1488 CG1AVAL A 188 1581 3646 2501 -593 438 148 C ATOM 1489 CG1BVAL A 188 35.182 28.463 1.463 0.32 12.14 C ANISOU 1489 CG1BVAL A 188 900 1790 1810 -595 731 -757 C ATOM 1490 CG2 VAL A 188 37.471 28.536 2.531 1.00 23.96 C ANISOU 1490 CG2 VAL A 188 1217 5572 2090 273 337 -1215 C ATOM 1491 N ALA A 189 37.197 28.906 5.704 1.00 10.43 N ANISOU 1491 N ALA A 189 550 993 2320 -54 72 -383 N ATOM 1492 CA ALA A 189 38.095 29.645 6.580 1.00 10.04 C ANISOU 1492 CA ALA A 189 610 1110 2002 -6 100 -465 C ATOM 1493 C ALA A 189 39.527 29.324 6.074 1.00 9.95 C ANISOU 1493 C ALA A 189 535 1069 2083 35 6 -474 C ATOM 1494 O ALA A 189 39.827 28.207 5.707 1.00 12.36 O ANISOU 1494 O ALA A 189 679 1017 2883 -85 357 -575 O ATOM 1495 CB ALA A 189 37.971 29.150 8.000 1.00 13.47 C ANISOU 1495 CB ALA A 189 1131 1757 2102 90 265 -344 C ATOM 1496 N SER A 190 40.390 30.309 6.061 1.00 9.40 N ANISOU 1496 N SER A 190 571 851 2064 51 -10 -370 N ATOM 1497 CA SER A 190 41.772 30.090 5.628 1.00 9.46 C ANISOU 1497 CA SER A 190 514 922 2071 37 13 -236 C ATOM 1498 C SER A 190 42.711 30.973 6.390 1.00 10.54 C ANISOU 1498 C SER A 190 536 890 2482 79 -112 -281 C ATOM 1499 O SER A 190 42.346 32.023 6.925 1.00 11.00 O ANISOU 1499 O SER A 190 589 874 2613 190 -122 -418 O ATOM 1500 CB SER A 190 41.866 30.420 4.137 1.00 11.66 C ANISOU 1500 CB SER A 190 854 1390 2076 186 170 -217 C ATOM 1501 OG SER A 190 41.602 31.799 3.920 1.00 14.93 O ANISOU 1501 OG SER A 190 1475 1617 2442 118 -48 265 O ATOM 1502 N PHE A 191 44.000 30.554 6.402 1.00 10.00 N ANISOU 1502 N PHE A 191 491 946 2269 112 -47 -567 N ATOM 1503 CA PHE A 191 45.039 31.441 6.911 1.00 10.69 C ANISOU 1503 CA PHE A 191 517 900 2543 35 -33 -440 C ATOM 1504 C PHE A 191 46.305 31.188 6.063 1.00 10.62 C ANISOU 1504 C PHE A 191 449 1003 2483 198 -101 -505 C ATOM 1505 O PHE A 191 46.547 30.114 5.474 1.00 10.65 O ANISOU 1505 O PHE A 191 572 868 2506 142 -124 -407 O ATOM 1506 CB PHE A 191 45.290 31.377 8.408 1.00 12.68 C ANISOU 1506 CB PHE A 191 768 1413 2517 161 -117 -913 C ATOM 1507 CG PHE A 191 45.770 30.037 8.984 1.00 13.45 C ANISOU 1507 CG PHE A 191 980 1912 2091 283 -335 -642 C ATOM 1508 CD1 PHE A 191 47.135 29.695 8.902 1.00 15.51 C ANISOU 1508 CD1 PHE A 191 1072 1864 2811 457 -363 -443 C ATOM 1509 CD2 PHE A 191 44.894 29.142 9.602 1.00 14.05 C ANISOU 1509 CD2 PHE A 191 1297 1564 2344 185 -230 -771 C ATOM 1510 CE1 PHE A 191 47.590 28.469 9.406 1.00 14.22 C ANISOU 1510 CE1 PHE A 191 1373 1769 2128 312 -415 -395 C ATOM 1511 CE2 PHE A 191 45.324 27.959 10.174 1.00 15.28 C ANISOU 1511 CE2 PHE A 191 1584 2164 1914 455 -147 -463 C ATOM 1512 CZ PHE A 191 46.648 27.614 9.995 1.00 14.63 C ANISOU 1512 CZ PHE A 191 1353 1880 2188 167 -138 -708 C ATOM 1513 N GLU A 192 47.120 32.220 6.066 1.00 10.50 N ANISOU 1513 N GLU A 192 437 939 2514 130 -50 -563 N ATOM 1514 CA GLU A 192 48.475 32.173 5.461 1.00 12.00 C ANISOU 1514 CA GLU A 192 443 1166 2837 82 11 -935 C ATOM 1515 C GLU A 192 49.410 33.032 6.317 1.00 9.71 C ANISOU 1515 C GLU A 192 506 782 2312 147 -29 -343 C ATOM 1516 O GLU A 192 49.009 34.019 6.892 1.00 12.00 O ANISOU 1516 O GLU A 192 509 1211 2728 259 -177 -961 O ATOM 1517 CB AGLU A 192 48.483 32.608 4.030 0.70 17.24 C ANISOU 1517 CB AGLU A 192 1014 2886 2490 -670 91 -1106 C ATOM 1518 CB BGLU A 192 48.457 32.533 3.992 0.30 27.37 C ANISOU 1518 CB BGLU A 192 3466 3466 3466 0 0 0 C ATOM 1519 CG AGLU A 192 48.264 34.012 3.591 0.70 27.39 C ANISOU 1519 CG AGLU A 192 1803 4669 3680 1073 -279 996 C ATOM 1520 CG BGLU A 192 47.984 33.963 3.827 0.30 13.82 C ANISOU 1520 CG BGLU A 192 921 2239 1960 80 -54 -709 C ATOM 1521 CD AGLU A 192 48.451 34.176 2.081 0.70 32.99 C ANISOU 1521 CD AGLU A 192 3253 4905 4068 -649 1500 708 C ATOM 1522 CD BGLU A 192 48.413 34.558 2.492 0.30 18.59 C ANISOU 1522 CD BGLU A 192 1410 3662 1818 -626 -554 -377 C ATOM 1523 OE1AGLU A 192 47.538 33.795 1.310 0.70 35.46 O ANISOU 1523 OE1AGLU A 192 4184 5747 3211 1673 94 595 O ATOM 1524 OE1BGLU A 192 49.562 34.297 2.089 0.30 25.32 O ANISOU 1524 OE1BGLU A 192 2777 3806 2799 507 1056 450 O ATOM 1525 OE2AGLU A 192 49.507 34.658 1.610 0.70 41.62 O ANISOU 1525 OE2AGLU A 192 5271 5271 5271 0 0 0 O ATOM 1526 OE2BGLU A 192 47.649 35.324 1.893 0.30 24.57 O ANISOU 1526 OE2BGLU A 192 2390 5014 1701 223 -595 -10 O ATOM 1527 N ALA A 193 50.649 32.542 6.466 1.00 8.58 N ANISOU 1527 N ALA A 193 483 864 1831 30 143 -358 N ATOM 1528 CA ALA A 193 51.647 33.304 7.162 1.00 7.89 C ANISOU 1528 CA ALA A 193 437 892 1596 48 87 -267 C ATOM 1529 C ALA A 193 52.967 33.224 6.386 1.00 7.36 C ANISOU 1529 C ALA A 193 412 712 1604 151 59 -156 C ATOM 1530 O ALA A 193 53.263 32.213 5.736 1.00 8.09 O ANISOU 1530 O ALA A 193 536 828 1635 39 107 -311 O ATOM 1531 CB ALA A 193 51.885 32.763 8.565 1.00 10.13 C ANISOU 1531 CB ALA A 193 948 1349 1457 226 298 -190 C ATOM 1532 N THR A 194 53.748 34.257 6.527 1.00 7.39 N ANISOU 1532 N THR A 194 451 847 1441 82 72 -255 N ATOM 1533 CA THR A 194 55.114 34.308 5.927 1.00 6.98 C ANISOU 1533 CA THR A 194 412 914 1262 54 56 -271 C ATOM 1534 C THR A 194 56.026 34.955 6.953 1.00 7.07 C ANISOU 1534 C THR A 194 531 816 1272 55 44 -242 C ATOM 1535 O THR A 194 55.658 35.955 7.598 1.00 8.57 O ANISOU 1535 O THR A 194 603 968 1605 176 -52 -496 O ATOM 1536 CB THR A 194 55.131 35.122 4.611 1.00 9.65 C ANISOU 1536 CB THR A 194 850 1442 1283 -71 -33 -87 C ATOM 1537 OG1 THR A 194 54.257 34.596 3.657 1.00 12.98 O ANISOU 1537 OG1 THR A 194 1362 1904 1546 23 -414 -68 O ATOM 1538 CG2 THR A 194 56.561 35.222 4.076 1.00 13.86 C ANISOU 1538 CG2 THR A 194 1129 2143 1864 -139 323 243 C ATOM 1539 N PHE A 195 57.256 34.457 7.122 1.00 7.06 N ANISOU 1539 N PHE A 195 426 863 1326 116 33 -337 N ATOM 1540 CA PHE A 195 58.229 35.187 7.888 1.00 7.25 C ANISOU 1540 CA PHE A 195 462 923 1301 58 45 -256 C ATOM 1541 C PHE A 195 59.613 35.013 7.249 1.00 6.73 C ANISOU 1541 C PHE A 195 450 887 1158 153 25 -275 C ATOM 1542 O PHE A 195 59.904 33.999 6.593 1.00 8.03 O ANISOU 1542 O PHE A 195 519 1016 1443 62 98 -340 O ATOM 1543 CB PHE A 195 58.239 34.818 9.374 1.00 7.96 C ANISOU 1543 CB PHE A 195 570 1081 1297 46 104 -400 C ATOM 1544 CG PHE A 195 58.623 33.411 9.718 1.00 7.62 C ANISOU 1544 CG PHE A 195 625 1129 1067 55 48 -203 C ATOM 1545 CD1 PHE A 195 57.713 32.360 9.766 1.00 8.75 C ANISOU 1545 CD1 PHE A 195 585 1245 1412 31 163 -215 C ATOM 1546 CD2 PHE A 195 59.967 33.085 10.069 1.00 8.54 C ANISOU 1546 CD2 PHE A 195 598 1285 1282 32 15 -67 C ATOM 1547 CE1 PHE A 195 58.085 31.073 10.134 1.00 9.38 C ANISOU 1547 CE1 PHE A 195 931 1292 1254 -50 226 -39 C ATOM 1548 CE2 PHE A 195 60.342 31.821 10.395 1.00 9.01 C ANISOU 1548 CE2 PHE A 195 751 1317 1272 102 22 -81 C ATOM 1549 CZ PHE A 195 59.416 30.813 10.471 1.00 9.67 C ANISOU 1549 CZ PHE A 195 846 1426 1310 105 190 144 C ATOM 1550 N THR A 196 60.460 36.026 7.431 1.00 7.09 N ANISOU 1550 N THR A 196 434 973 1221 96 52 -257 N ATOM 1551 CA THR A 196 61.849 36.006 6.979 1.00 6.64 C ANISOU 1551 CA THR A 196 471 894 1097 84 58 -159 C ATOM 1552 C THR A 196 62.732 36.010 8.222 1.00 6.10 C ANISOU 1552 C THR A 196 487 704 1070 19 127 -62 C ATOM 1553 O THR A 196 62.442 36.708 9.191 1.00 7.62 O ANISOU 1553 O THR A 196 553 1058 1211 91 26 -226 O ATOM 1554 CB ATHR A 196 62.185 37.147 6.036 0.68 7.28 C ANISOU 1554 CB ATHR A 196 738 968 990 129 105 -97 C ATOM 1555 CB BTHR A 196 62.379 36.448 5.672 0.32 16.77 C ANISOU 1555 CB BTHR A 196 1213 3537 1462 -956 -80 958 C ATOM 1556 OG1ATHR A 196 62.211 38.377 6.605 0.68 10.85 O ANISOU 1556 OG1ATHR A 196 1252 1069 1701 65 99 -123 O ATOM 1557 OG1BTHR A 196 63.460 37.387 5.605 0.32 8.62 O ANISOU 1557 OG1BTHR A 196 774 1254 1165 95 233 13 O ATOM 1558 CG2ATHR A 196 61.247 37.066 4.848 0.68 10.31 C ANISOU 1558 CG2ATHR A 196 1240 1274 1305 187 -351 232 C ATOM 1559 CG2BTHR A 196 61.336 36.972 4.697 0.32 14.12 C ANISOU 1559 CG2BTHR A 196 2085 2173 975 -976 -761 -99 C ATOM 1560 N PHE A 197 63.793 35.187 8.159 1.00 6.65 N ANISOU 1560 N PHE A 197 567 859 1039 140 36 -54 N ATOM 1561 CA PHE A 197 64.579 34.914 9.343 1.00 6.78 C ANISOU 1561 CA PHE A 197 500 978 1035 131 77 -41 C ATOM 1562 C PHE A 197 66.091 34.876 8.964 1.00 6.62 C ANISOU 1562 C PHE A 197 520 899 1035 2 29 9 C ATOM 1563 O PHE A 197 66.461 34.549 7.865 1.00 8.28 O ANISOU 1563 O PHE A 197 551 1315 1201 20 165 -293 O ATOM 1564 CB PHE A 197 64.146 33.573 9.989 1.00 7.83 C ANISOU 1564 CB PHE A 197 615 1092 1195 -19 78 82 C ATOM 1565 CG PHE A 197 64.268 32.398 9.035 1.00 7.35 C ANISOU 1565 CG PHE A 197 666 936 1122 -29 40 145 C ATOM 1566 CD1 PHE A 197 63.231 32.040 8.172 1.00 7.46 C ANISOU 1566 CD1 PHE A 197 615 1096 1052 -30 -16 190 C ATOM 1567 CD2 PHE A 197 65.423 31.647 9.002 1.00 8.71 C ANISOU 1567 CD2 PHE A 197 725 1016 1485 86 -171 26 C ATOM 1568 CE1 PHE A 197 63.376 31.009 7.287 1.00 8.34 C ANISOU 1568 CE1 PHE A 197 1018 824 1250 -84 -217 267 C ATOM 1569 CE2 PHE A 197 65.572 30.601 8.130 1.00 9.80 C ANISOU 1569 CE2 PHE A 197 954 867 1812 164 -270 -91 C ATOM 1570 CZ PHE A 197 64.535 30.277 7.244 1.00 10.09 C ANISOU 1570 CZ PHE A 197 1107 1036 1598 45 -249 -64 C ATOM 1571 N LEU A 198 66.891 35.105 10.015 1.00 7.33 N ANISOU 1571 N LEU A 198 537 1047 1132 123 -1 43 N ATOM 1572 CA LEU A 198 68.360 35.014 9.906 1.00 7.85 C ANISOU 1572 CA LEU A 198 445 1116 1347 87 38 86 C ATOM 1573 C LEU A 198 68.838 34.211 11.125 1.00 8.16 C ANISOU 1573 C LEU A 198 512 1210 1302 149 8 6 C ATOM 1574 O LEU A 198 68.803 34.717 12.252 1.00 8.99 O ANISOU 1574 O LEU A 198 887 1056 1388 166 -39 18 O ATOM 1575 CB LEU A 198 68.998 36.391 9.842 1.00 9.92 C ANISOU 1575 CB LEU A 198 691 1264 1720 -68 53 106 C ATOM 1576 CG LEU A 198 70.423 36.543 9.333 1.00 22.40 C ANISOU 1576 CG LEU A 198 911 1898 5494 -611 413 340 C ATOM 1577 CD1 LEU A 198 70.929 37.959 9.581 1.00 22.75 C ANISOU 1577 CD1 LEU A 198 1367 1742 5321 -602 209 711 C ATOM 1578 CD2 LEU A 198 71.312 35.417 9.307 1.00 29.12 C ANISOU 1578 CD2 LEU A 198 1130 2423 7238 -337 1955 -1783 C ATOM 1579 N ILE A 199 69.270 32.984 10.859 1.00 8.07 N ANISOU 1579 N ILE A 199 627 1230 1134 223 -91 70 N ATOM 1580 CA ILE A 199 69.811 32.078 11.879 1.00 8.23 C ANISOU 1580 CA ILE A 199 592 1274 1185 185 -3 117 C ATOM 1581 C ILE A 199 71.349 32.051 11.625 1.00 8.55 C ANISOU 1581 C ILE A 199 632 1312 1225 287 35 161 C ATOM 1582 O ILE A 199 71.780 31.595 10.554 1.00 9.63 O ANISOU 1582 O ILE A 199 801 1386 1381 326 175 70 O ATOM 1583 CB ILE A 199 69.229 30.685 11.845 1.00 8.27 C ANISOU 1583 CB ILE A 199 787 1170 1107 238 -61 106 C ATOM 1584 CG1 ILE A 199 67.700 30.731 12.213 1.00 8.77 C ANISOU 1584 CG1 ILE A 199 785 1193 1272 143 -54 95 C ATOM 1585 CG2 ILE A 199 69.975 29.757 12.808 1.00 9.95 C ANISOU 1585 CG2 ILE A 199 966 1311 1412 230 -224 242 C ATOM 1586 CD1 ILE A 199 66.953 29.474 11.886 1.00 10.45 C ANISOU 1586 CD1 ILE A 199 1168 977 1727 84 -330 115 C ATOM 1587 N LYS A 200 72.089 32.534 12.608 1.00 10.09 N ANISOU 1587 N LYS A 200 628 1851 1258 306 -104 161 N ATOM 1588 CA LYS A 200 73.572 32.589 12.506 1.00 12.86 C ANISOU 1588 CA LYS A 200 577 2762 1427 259 4 495 C ATOM 1589 C LYS A 200 74.141 31.994 13.783 1.00 9.57 C ANISOU 1589 C LYS A 200 547 1672 1328 100 -26 77 C ATOM 1590 O LYS A 200 73.645 32.193 14.885 1.00 9.93 O ANISOU 1590 O LYS A 200 772 1542 1367 249 84 193 O ATOM 1591 CB LYS A 200 74.067 34.044 12.465 1.00 19.49 C ANISOU 1591 CB LYS A 200 980 3038 3204 -129 96 1743 C ATOM 1592 CG LYS A 200 75.511 34.275 12.206 1.00 33.11 C ANISOU 1592 CG LYS A 200 1274 4772 6225 -767 406 619 C ATOM 1593 CD LYS A 200 76.271 33.441 11.187 1.00 59.59 C ANISOU 1593 CD LYS A 200 7547 7547 7547 0 0 0 C ATOM 1594 CE LYS A 200 77.677 33.981 10.898 1.00 75.31 C ANISOU 1594 CE LYS A 200 9538 9538 9538 0 0 0 C ATOM 1595 NZ LYS A 200 78.590 32.879 10.483 1.00 71.71 N ANISOU 1595 NZ LYS A 200 9082 9082 9082 0 0 0 N ATOM 1596 N SER A 201 75.254 31.318 13.633 1.00 10.90 N ANISOU 1596 N SER A 201 700 1876 1463 330 -34 50 N ATOM 1597 CA SER A 201 75.940 30.785 14.788 1.00 10.42 C ANISOU 1597 CA SER A 201 714 1632 1515 173 -74 63 C ATOM 1598 C SER A 201 77.414 30.794 14.532 1.00 10.70 C ANISOU 1598 C SER A 201 749 1669 1549 263 -181 62 C ATOM 1599 O SER A 201 77.823 30.468 13.411 1.00 11.74 O ANISOU 1599 O SER A 201 770 2034 1544 82 -94 16 O ATOM 1600 CB SER A 201 75.469 29.385 15.018 1.00 11.86 C ANISOU 1600 CB SER A 201 775 1622 1998 108 -119 69 C ATOM 1601 OG SER A 201 76.002 28.778 16.212 1.00 15.98 O ANISOU 1601 OG SER A 201 1121 2261 2540 328 190 810 O ATOM 1602 N PRO A 202 78.236 30.979 15.582 1.00 12.46 N ANISOU 1602 N PRO A 202 890 1916 1813 211 -219 -314 N ATOM 1603 CA PRO A 202 79.700 30.757 15.429 1.00 13.49 C ANISOU 1603 CA PRO A 202 755 2127 2118 101 -334 -122 C ATOM 1604 C PRO A 202 80.052 29.314 15.302 1.00 13.55 C ANISOU 1604 C PRO A 202 756 2048 2216 176 -117 386 C ATOM 1605 O PRO A 202 81.241 29.055 15.085 1.00 17.75 O ANISOU 1605 O PRO A 202 983 2542 3052 335 292 307 O ATOM 1606 CB PRO A 202 80.292 31.477 16.649 1.00 18.83 C ANISOU 1606 CB PRO A 202 1388 3292 2298 60 -639 -503 C ATOM 1607 CG PRO A 202 79.194 31.318 17.680 1.00 20.57 C ANISOU 1607 CG PRO A 202 1447 3927 2249 407 -556 -967 C ATOM 1608 CD PRO A 202 77.916 31.452 16.928 1.00 13.74 C ANISOU 1608 CD PRO A 202 1530 1851 1709 369 -276 -136 C ATOM 1609 N ASP A 203 79.178 28.349 15.472 1.00 14.38 N ANISOU 1609 N ASP A 203 930 1940 2460 367 -171 512 N ATOM 1610 CA ASP A 203 79.392 26.976 15.701 1.00 13.05 C ANISOU 1610 CA ASP A 203 1148 1925 1764 268 -185 318 C ATOM 1611 C ASP A 203 78.927 26.120 14.505 1.00 13.60 C ANISOU 1611 C ASP A 203 953 2318 1768 404 -101 183 C ATOM 1612 O ASP A 203 77.990 26.442 13.775 1.00 14.20 O ANISOU 1612 O ASP A 203 1179 2278 1804 288 -191 344 O ATOM 1613 CB ASP A 203 78.645 26.496 16.978 1.00 14.84 C ANISOU 1613 CB ASP A 203 1441 2196 1863 -18 70 222 C ATOM 1614 CG ASP A 203 78.986 27.281 18.220 1.00 15.81 C ANISOU 1614 CG ASP A 203 1240 2707 1913 168 39 -9 C ATOM 1615 OD1 ASP A 203 80.208 27.537 18.478 1.00 16.41 O ANISOU 1615 OD1 ASP A 203 1217 2167 2695 220 -84 -204 O ATOM 1616 OD2 ASP A 203 78.005 27.716 18.916 1.00 17.81 O ANISOU 1616 OD2 ASP A 203 1685 2261 2655 -313 658 -273 O ATOM 1617 N SER A 204 79.626 25.015 14.344 1.00 13.15 N ANISOU 1617 N SER A 204 877 2229 1768 287 49 110 N ATOM 1618 CA SER A 204 79.235 24.019 13.313 1.00 13.39 C ANISOU 1618 CA SER A 204 728 2829 1404 306 99 -116 C ATOM 1619 C SER A 204 77.878 23.356 13.598 1.00 12.36 C ANISOU 1619 C SER A 204 827 2491 1262 336 4 161 C ATOM 1620 O SER A 204 77.269 22.787 12.687 1.00 16.66 O ANISOU 1620 O SER A 204 877 3805 1491 242 68 -545 O ATOM 1621 CB ASER A 204 80.283 22.881 13.311 0.69 12.18 C ANISOU 1621 CB ASER A 204 855 2249 1409 88 64 62 C ATOM 1622 CB BSER A 204 80.330 23.022 12.979 0.31 15.91 C ANISOU 1622 CB BSER A 204 996 2926 1973 582 201 -192 C ATOM 1623 OG ASER A 204 81.524 23.319 12.783 0.69 15.05 O ANISOU 1623 OG ASER A 204 718 3290 1570 384 279 -43 O ATOM 1624 OG BSER A 204 80.834 22.384 14.131 0.31 33.36 O ANISOU 1624 OG BSER A 204 3277 5377 3706 2263 796 2257 O ATOM 1625 N HIS A 205 77.391 23.412 14.785 1.00 10.35 N ANISOU 1625 N HIS A 205 884 1475 1478 196 226 -123 N ATOM 1626 CA HIS A 205 76.161 22.801 15.264 1.00 8.80 C ANISOU 1626 CA HIS A 205 705 1207 1349 196 7 -47 C ATOM 1627 C HIS A 205 75.269 23.891 15.879 1.00 8.68 C ANISOU 1627 C HIS A 205 714 1298 1203 158 55 12 C ATOM 1628 O HIS A 205 75.203 24.023 17.118 1.00 10.20 O ANISOU 1628 O HIS A 205 1069 1539 1173 293 17 -98 O ATOM 1629 CB HIS A 205 76.462 21.687 16.259 1.00 10.52 C ANISOU 1629 CB HIS A 205 954 1655 1289 443 162 137 C ATOM 1630 CG HIS A 205 77.338 20.622 15.678 1.00 10.38 C ANISOU 1630 CG HIS A 205 1075 1388 1383 400 67 145 C ATOM 1631 ND1 HIS A 205 76.885 19.674 14.773 1.00 12.19 N ANISOU 1631 ND1 HIS A 205 1052 1371 2094 257 58 -52 N ATOM 1632 CD2 HIS A 205 78.629 20.331 15.873 1.00 12.60 C ANISOU 1632 CD2 HIS A 205 1157 1729 1784 560 -64 -238 C ATOM 1633 CE1 HIS A 205 77.917 18.919 14.410 1.00 12.81 C ANISOU 1633 CE1 HIS A 205 1063 1291 2393 167 259 -241 C ATOM 1634 NE2 HIS A 205 78.995 19.313 15.097 1.00 12.43 N ANISOU 1634 NE2 HIS A 205 1177 1373 2054 374 138 -35 N ATOM 1635 N PRO A 206 74.507 24.626 15.062 1.00 8.45 N ANISOU 1635 N PRO A 206 634 1215 1281 176 149 39 N ATOM 1636 CA PRO A 206 73.528 25.571 15.628 1.00 8.65 C ANISOU 1636 CA PRO A 206 753 1025 1428 95 234 121 C ATOM 1637 C PRO A 206 72.400 24.800 16.323 1.00 7.48 C ANISOU 1637 C PRO A 206 640 979 1153 175 9 48 C ATOM 1638 O PRO A 206 72.095 23.654 16.022 1.00 8.00 O ANISOU 1638 O PRO A 206 711 999 1253 124 136 0 O ATOM 1639 CB PRO A 206 72.981 26.294 14.384 1.00 11.40 C ANISOU 1639 CB PRO A 206 1137 1309 1778 312 392 475 C ATOM 1640 CG PRO A 206 73.234 25.347 13.285 1.00 17.25 C ANISOU 1640 CG PRO A 206 2347 2557 1488 1565 -48 226 C ATOM 1641 CD PRO A 206 74.503 24.612 13.615 1.00 10.19 C ANISOU 1641 CD PRO A 206 896 1579 1300 398 254 265 C ATOM 1642 N ALA A 207 71.721 25.501 17.252 1.00 6.79 N ANISOU 1642 N ALA A 207 529 814 1175 106 30 40 N ATOM 1643 CA ALA A 207 70.463 24.970 17.844 1.00 6.31 C ANISOU 1643 CA ALA A 207 480 900 958 165 -45 60 C ATOM 1644 C ALA A 207 69.708 26.155 18.391 1.00 6.43 C ANISOU 1644 C ALA A 207 453 834 1098 114 -37 139 C ATOM 1645 O ALA A 207 70.302 27.193 18.734 1.00 6.74 O ANISOU 1645 O ALA A 207 519 873 1104 99 -43 67 O ATOM 1646 CB ALA A 207 70.762 23.968 18.960 1.00 7.04 C ANISOU 1646 CB ALA A 207 561 912 1136 151 -64 58 C ATOM 1647 N ASP A 208 68.357 26.022 18.614 1.00 6.32 N ANISOU 1647 N ASP A 208 503 789 1052 118 -110 56 N ATOM 1648 CA ASP A 208 67.536 24.838 18.399 1.00 6.27 C ANISOU 1648 CA ASP A 208 474 846 1002 84 -49 176 C ATOM 1649 C ASP A 208 66.515 24.971 17.267 1.00 6.20 C ANISOU 1649 C ASP A 208 520 852 926 119 -52 30 C ATOM 1650 O ASP A 208 66.061 23.942 16.717 1.00 6.86 O ANISOU 1650 O ASP A 208 627 868 1047 139 -84 86 O ATOM 1651 CB ASP A 208 66.794 24.453 19.708 1.00 6.84 C ANISOU 1651 CB ASP A 208 590 1000 943 17 -70 1 C ATOM 1652 CG ASP A 208 67.736 23.575 20.558 1.00 8.13 C ANISOU 1652 CG ASP A 208 791 1162 1061 -21 -83 216 C ATOM 1653 OD1 ASP A 208 67.693 22.309 20.369 1.00 9.05 O ANISOU 1653 OD1 ASP A 208 867 1207 1281 51 -77 192 O ATOM 1654 OD2 ASP A 208 68.480 24.127 21.395 1.00 8.96 O ANISOU 1654 OD2 ASP A 208 840 1396 1083 155 -120 24 O ATOM 1655 N GLY A 209 66.117 26.199 16.931 1.00 6.33 N ANISOU 1655 N GLY A 209 597 822 925 212 -121 -30 N ATOM 1656 CA GLY A 209 65.212 26.426 15.809 1.00 6.64 C ANISOU 1656 CA GLY A 209 588 879 992 247 -185 -10 C ATOM 1657 C GLY A 209 64.208 27.569 16.103 1.00 5.73 C ANISOU 1657 C GLY A 209 509 689 927 93 -68 7 C ATOM 1658 O GLY A 209 64.232 28.207 17.134 1.00 6.53 O ANISOU 1658 O GLY A 209 654 857 911 224 -169 -37 O ATOM 1659 N ILE A 210 63.362 27.756 15.080 1.00 5.75 N ANISOU 1659 N ILE A 210 494 758 880 155 -72 9 N ATOM 1660 CA ILE A 210 62.299 28.785 15.080 1.00 5.75 C ANISOU 1660 CA ILE A 210 498 757 876 133 -63 -31 C ATOM 1661 C ILE A 210 61.001 28.087 14.687 1.00 5.79 C ANISOU 1661 C ILE A 210 465 829 851 134 -62 -52 C ATOM 1662 O ILE A 210 61.020 27.219 13.814 1.00 7.27 O ANISOU 1662 O ILE A 210 508 955 1233 103 -59 -299 O ATOM 1663 CB ILE A 210 62.595 29.922 14.067 1.00 6.17 C ANISOU 1663 CB ILE A 210 623 728 936 55 -18 3 C ATOM 1664 CG1 ILE A 210 63.914 30.641 14.396 1.00 7.29 C ANISOU 1664 CG1 ILE A 210 629 1096 975 -40 -69 73 C ATOM 1665 CG2 ILE A 210 61.446 30.966 13.990 1.00 7.46 C ANISOU 1665 CG2 ILE A 210 640 849 1276 109 -33 140 C ATOM 1666 CD1 ILE A 210 64.328 31.737 13.434 1.00 8.28 C ANISOU 1666 CD1 ILE A 210 702 1091 1274 -37 -7 233 C ATOM 1667 N ALA A 211 59.875 28.505 15.246 1.00 5.77 N ANISOU 1667 N ALA A 211 426 770 943 137 -75 -90 N ATOM 1668 CA ALA A 211 58.573 27.950 14.841 1.00 5.95 C ANISOU 1668 CA ALA A 211 513 731 961 56 -57 -123 C ATOM 1669 C ALA A 211 57.557 29.104 14.682 1.00 5.73 C ANISOU 1669 C ALA A 211 489 765 872 91 -74 -42 C ATOM 1670 O ALA A 211 57.541 30.079 15.434 1.00 7.21 O ANISOU 1670 O ALA A 211 605 988 1080 230 -194 -259 O ATOM 1671 CB ALA A 211 58.043 26.964 15.877 1.00 7.47 C ANISOU 1671 CB ALA A 211 660 922 1184 49 42 102 C ATOM 1672 N PHE A 212 56.660 28.923 13.702 1.00 5.51 N ANISOU 1672 N PHE A 212 464 738 840 131 -43 -24 N ATOM 1673 CA PHE A 212 55.371 29.670 13.644 1.00 5.54 C ANISOU 1673 CA PHE A 212 391 760 901 73 5 0 C ATOM 1674 C PHE A 212 54.337 28.797 14.341 1.00 5.68 C ANISOU 1674 C PHE A 212 500 690 914 112 -39 -19 C ATOM 1675 O PHE A 212 54.255 27.582 14.074 1.00 6.96 O ANISOU 1675 O PHE A 212 644 827 1110 110 134 22 O ATOM 1676 CB PHE A 212 54.971 29.899 12.177 1.00 6.18 C ANISOU 1676 CB PHE A 212 496 840 953 60 -43 108 C ATOM 1677 CG PHE A 212 53.520 30.439 12.083 1.00 6.65 C ANISOU 1677 CG PHE A 212 593 974 895 167 -136 -7 C ATOM 1678 CD1 PHE A 212 53.203 31.745 12.411 1.00 7.84 C ANISOU 1678 CD1 PHE A 212 667 1002 1235 197 -58 88 C ATOM 1679 CD2 PHE A 212 52.490 29.579 11.696 1.00 7.85 C ANISOU 1679 CD2 PHE A 212 600 1066 1244 42 -220 -8 C ATOM 1680 CE1 PHE A 212 51.883 32.212 12.330 1.00 8.36 C ANISOU 1680 CE1 PHE A 212 790 943 1365 274 -35 85 C ATOM 1681 CE2 PHE A 212 51.183 30.034 11.650 1.00 9.17 C ANISOU 1681 CE2 PHE A 212 684 1278 1437 10 -139 -95 C ATOM 1682 CZ PHE A 212 50.875 31.333 11.952 1.00 8.85 C ANISOU 1682 CZ PHE A 212 615 1336 1327 203 -130 81 C ATOM 1683 N PHE A 213 53.561 29.383 15.248 1.00 5.67 N ANISOU 1683 N PHE A 213 445 689 969 58 54 87 N ATOM 1684 CA PHE A 213 52.593 28.566 16.013 1.00 6.12 C ANISOU 1684 CA PHE A 213 461 792 1016 97 17 126 C ATOM 1685 C PHE A 213 51.260 29.318 16.149 1.00 5.83 C ANISOU 1685 C PHE A 213 523 695 943 62 126 69 C ATOM 1686 O PHE A 213 51.133 30.521 16.019 1.00 6.55 O ANISOU 1686 O PHE A 213 451 830 1149 89 35 49 O ATOM 1687 CB PHE A 213 53.167 28.178 17.388 1.00 6.45 C ANISOU 1687 CB PHE A 213 591 818 980 76 92 182 C ATOM 1688 CG PHE A 213 53.278 29.301 18.385 1.00 6.79 C ANISOU 1688 CG PHE A 213 616 1006 895 154 -13 152 C ATOM 1689 CD1 PHE A 213 54.340 30.180 18.438 1.00 6.59 C ANISOU 1689 CD1 PHE A 213 581 926 934 151 10 126 C ATOM 1690 CD2 PHE A 213 52.285 29.459 19.349 1.00 8.91 C ANISOU 1690 CD2 PHE A 213 854 1270 1177 -84 166 -95 C ATOM 1691 CE1 PHE A 213 54.425 31.190 19.375 1.00 6.98 C ANISOU 1691 CE1 PHE A 213 710 1049 827 69 -55 115 C ATOM 1692 CE2 PHE A 213 52.362 30.449 20.297 1.00 11.50 C ANISOU 1692 CE2 PHE A 213 985 2040 1235 -262 381 -553 C ATOM 1693 CZ PHE A 213 53.450 31.339 20.332 1.00 8.91 C ANISOU 1693 CZ PHE A 213 799 1442 1062 92 18 -149 C ATOM 1694 N ILE A 214 50.255 28.460 16.460 1.00 6.22 N ANISOU 1694 N ILE A 214 478 736 1092 83 98 26 N ATOM 1695 CA ILE A 214 48.874 28.900 16.743 1.00 6.40 C ANISOU 1695 CA ILE A 214 463 768 1141 78 76 36 C ATOM 1696 C ILE A 214 48.491 28.202 18.032 1.00 6.95 C ANISOU 1696 C ILE A 214 491 850 1236 140 100 28 C ATOM 1697 O ILE A 214 48.757 27.007 18.251 1.00 7.79 O ANISOU 1697 O ILE A 214 718 881 1286 181 227 160 O ATOM 1698 CB ILE A 214 47.929 28.446 15.590 1.00 7.03 C ANISOU 1698 CB ILE A 214 579 802 1224 41 -15 63 C ATOM 1699 CG1 ILE A 214 48.468 28.830 14.216 1.00 8.70 C ANISOU 1699 CG1 ILE A 214 793 1275 1158 -58 10 204 C ATOM 1700 CG2 ILE A 214 46.527 29.032 15.870 1.00 8.37 C ANISOU 1700 CG2 ILE A 214 591 1056 1455 -1 -41 60 C ATOM 1701 CD1 ILE A 214 47.630 28.465 13.049 1.00 17.60 C ANISOU 1701 CD1 ILE A 214 1111 4141 1271 -543 -93 -88 C ATOM 1702 N SER A 215 47.898 28.969 18.968 1.00 7.14 N ANISOU 1702 N SER A 215 609 910 1127 152 120 133 N ATOM 1703 CA SER A 215 47.676 28.521 20.299 1.00 8.38 C ANISOU 1703 CA SER A 215 702 1279 1125 351 122 90 C ATOM 1704 C SER A 215 46.365 29.070 20.886 1.00 7.35 C ANISOU 1704 C SER A 215 647 996 1081 155 105 256 C ATOM 1705 O SER A 215 45.767 30.005 20.373 1.00 7.29 O ANISOU 1705 O SER A 215 606 914 1183 183 195 180 O ATOM 1706 CB ASER A 215 48.800 29.099 21.213 0.71 9.18 C ANISOU 1706 CB ASER A 215 751 1491 1162 136 187 60 C ATOM 1707 CB BSER A 215 48.841 28.615 21.275 0.29 9.37 C ANISOU 1707 CB BSER A 215 782 1453 1238 434 -25 169 C ATOM 1708 OG ASER A 215 48.801 30.512 21.347 0.71 9.56 O ANISOU 1708 OG ASER A 215 770 1431 1343 109 15 132 O ATOM 1709 OG BSER A 215 48.754 27.797 22.447 0.29 9.95 O ANISOU 1709 OG BSER A 215 764 1964 959 178 4 94 O ATOM 1710 N ASN A 216 45.956 28.493 22.014 1.00 8.37 N ANISOU 1710 N ASN A 216 806 1042 1252 244 250 313 N ATOM 1711 CA ASN A 216 44.976 29.182 22.856 1.00 8.38 C ANISOU 1711 CA ASN A 216 647 1310 1149 104 179 156 C ATOM 1712 C ASN A 216 45.403 30.613 23.113 1.00 8.47 C ANISOU 1712 C ASN A 216 695 1316 1126 115 80 4 C ATOM 1713 O ASN A 216 46.606 30.924 23.188 1.00 8.99 O ANISOU 1713 O ASN A 216 642 1542 1146 142 86 93 O ATOM 1714 CB ASN A 216 44.765 28.382 24.153 1.00 10.70 C ANISOU 1714 CB ASN A 216 948 1807 1209 179 332 355 C ATOM 1715 CG ASN A 216 46.025 27.963 24.835 1.00 11.91 C ANISOU 1715 CG ASN A 216 1301 1824 1290 318 180 368 C ATOM 1716 OD1 ASN A 216 46.817 27.195 24.296 1.00 14.26 O ANISOU 1716 OD1 ASN A 216 1707 2090 1487 941 48 449 O ATOM 1717 ND2 ASN A 216 46.225 28.412 26.066 1.00 13.14 N ANISOU 1717 ND2 ASN A 216 1249 2328 1293 129 203 287 N ATOM 1718 N ILE A 217 44.420 31.518 23.294 1.00 8.51 N ANISOU 1718 N ILE A 217 606 1352 1198 112 147 114 N ATOM 1719 CA ILE A 217 44.724 32.955 23.368 1.00 8.77 C ANISOU 1719 CA ILE A 217 753 1278 1221 30 73 225 C ATOM 1720 C ILE A 217 45.629 33.304 24.519 1.00 8.86 C ANISOU 1720 C ILE A 217 837 1194 1252 219 133 47 C ATOM 1721 O ILE A 217 46.403 34.266 24.446 1.00 10.16 O ANISOU 1721 O ILE A 217 939 1352 1475 37 -64 28 O ATOM 1722 CB ILE A 217 43.425 33.802 23.371 1.00 10.00 C ANISOU 1722 CB ILE A 217 915 1437 1354 262 86 2 C ATOM 1723 CG1 ILE A 217 42.522 33.548 24.589 1.00 11.67 C ANISOU 1723 CG1 ILE A 217 980 2036 1308 424 33 45 C ATOM 1724 CG2 ILE A 217 42.681 33.668 22.052 1.00 10.38 C ANISOU 1724 CG2 ILE A 217 890 1527 1430 159 -45 288 C ATOM 1725 CD1 ILE A 217 41.325 34.509 24.619 1.00 14.58 C ANISOU 1725 CD1 ILE A 217 1318 2526 1559 791 162 -239 C ATOM 1726 N ASP A 218 45.545 32.552 25.626 1.00 9.65 N ANISOU 1726 N ASP A 218 721 1677 1175 285 31 80 N ATOM 1727 CA ASP A 218 46.299 32.820 26.843 1.00 10.06 C ANISOU 1727 CA ASP A 218 850 1676 1203 304 107 -55 C ATOM 1728 C ASP A 218 47.610 31.988 26.900 1.00 9.88 C ANISOU 1728 C ASP A 218 870 1689 1101 272 -8 30 C ATOM 1729 O ASP A 218 48.190 31.862 27.995 1.00 12.19 O ANISOU 1729 O ASP A 218 1154 2229 1133 436 -5 18 O ATOM 1730 CB ASP A 218 45.427 32.537 28.066 1.00 12.95 C ANISOU 1730 CB ASP A 218 1043 2572 1182 379 156 -92 C ATOM 1731 CG AASP A 218 44.976 31.100 28.163 0.65 15.97 C ANISOU 1731 CG AASP A 218 1343 3169 1406 -345 621 256 C ATOM 1732 CG BASP A 218 44.619 31.276 28.124 0.35 16.05 C ANISOU 1732 CG BASP A 218 1535 3817 597 -720 -203 417 C ATOM 1733 OD1 ASP A 218 44.556 30.502 27.136 1.00 14.55 O ANISOU 1733 OD1 ASP A 218 1611 2077 1705 55 539 282 O ATOM 1734 OD2AASP A 218 44.967 30.353 29.141 0.65 20.62 O ANISOU 1734 OD2AASP A 218 2162 3579 1900 -1201 -266 675 O ATOM 1735 OD2BASP A 218 43.845 31.299 29.108 0.35 17.12 O ANISOU 1735 OD2BASP A 218 2171 2361 1811 360 786 374 O ATOM 1736 N SER A 219 48.106 31.481 25.807 1.00 9.06 N ANISOU 1736 N SER A 219 684 1464 1210 206 87 29 N ATOM 1737 CA SER A 219 49.339 30.669 25.812 1.00 10.08 C ANISOU 1737 CA SER A 219 667 1536 1535 170 149 123 C ATOM 1738 C SER A 219 50.521 31.464 26.385 1.00 9.56 C ANISOU 1738 C SER A 219 714 1565 1264 189 93 242 C ATOM 1739 O SER A 219 50.740 32.638 26.058 1.00 9.92 O ANISOU 1739 O SER A 219 799 1513 1363 156 -54 98 O ATOM 1740 CB SER A 219 49.608 30.245 24.378 1.00 12.58 C ANISOU 1740 CB SER A 219 788 1934 1938 214 249 -598 C ATOM 1741 OG SER A 219 50.718 29.342 24.257 1.00 14.03 O ANISOU 1741 OG SER A 219 964 1847 2389 278 173 -416 O ATOM 1742 N SER A 220 51.364 30.719 27.086 1.00 9.71 N ANISOU 1742 N SER A 220 750 1343 1507 203 26 206 N ATOM 1743 CA SER A 220 52.594 31.244 27.697 1.00 10.12 C ANISOU 1743 CA SER A 220 857 1573 1318 258 -19 119 C ATOM 1744 C SER A 220 53.719 30.210 27.508 1.00 9.11 C ANISOU 1744 C SER A 220 859 1465 1054 166 68 355 C ATOM 1745 O SER A 220 53.455 29.033 27.279 1.00 10.33 O ANISOU 1745 O SER A 220 828 1488 1514 199 -7 179 O ATOM 1746 CB ASER A 220 52.353 31.558 29.158 0.72 12.22 C ANISOU 1746 CB ASER A 220 1153 1928 1449 587 -148 -37 C ATOM 1747 CB BSER A 220 52.333 31.274 29.220 0.28 11.86 C ANISOU 1747 CB BSER A 220 707 2178 1509 -280 291 -204 C ATOM 1748 OG ASER A 220 51.946 30.376 29.836 0.72 14.45 O ANISOU 1748 OG ASER A 220 1239 2866 1249 297 306 448 O ATOM 1749 OG BSER A 220 51.417 32.224 29.713 0.28 14.47 O ANISOU 1749 OG BSER A 220 1130 2641 1591 228 193 -240 O ATOM 1750 N ILE A 221 54.957 30.670 27.666 1.00 9.12 N ANISOU 1750 N ILE A 221 771 1392 1215 260 -26 146 N ATOM 1751 CA ILE A 221 56.104 29.742 27.502 1.00 8.62 C ANISOU 1751 CA ILE A 221 865 1336 995 274 46 152 C ATOM 1752 C ILE A 221 56.018 28.690 28.585 1.00 9.33 C ANISOU 1752 C ILE A 221 815 1597 1046 342 80 224 C ATOM 1753 O ILE A 221 55.997 29.004 29.799 1.00 10.57 O ANISOU 1753 O ILE A 221 1136 1774 1009 362 111 200 O ATOM 1754 CB ILE A 221 57.443 30.537 27.636 1.00 9.53 C ANISOU 1754 CB ILE A 221 769 1564 1201 259 -22 218 C ATOM 1755 CG1 ILE A 221 57.602 31.523 26.480 1.00 8.65 C ANISOU 1755 CG1 ILE A 221 852 1273 1081 299 20 162 C ATOM 1756 CG2 ILE A 221 58.615 29.542 27.661 1.00 9.55 C ANISOU 1756 CG2 ILE A 221 828 1265 1447 189 -84 221 C ATOM 1757 CD1 ILE A 221 58.753 32.480 26.616 1.00 10.25 C ANISOU 1757 CD1 ILE A 221 841 1463 1496 239 20 133 C ATOM 1758 N PRO A 222 56.052 27.391 28.253 1.00 9.34 N ANISOU 1758 N PRO A 222 889 1531 1040 337 129 317 N ATOM 1759 CA PRO A 222 56.043 26.356 29.274 1.00 9.86 C ANISOU 1759 CA PRO A 222 898 1612 1142 272 109 312 C ATOM 1760 C PRO A 222 57.360 26.369 30.071 1.00 9.83 C ANISOU 1760 C PRO A 222 1040 1601 1002 253 109 422 C ATOM 1761 O PRO A 222 58.455 26.604 29.540 1.00 10.07 O ANISOU 1761 O PRO A 222 986 1645 1100 334 61 324 O ATOM 1762 CB PRO A 222 55.887 25.041 28.532 1.00 11.25 C ANISOU 1762 CB PRO A 222 1106 1600 1461 146 67 277 C ATOM 1763 CG PRO A 222 55.272 25.465 27.222 1.00 11.96 C ANISOU 1763 CG PRO A 222 1318 1797 1315 118 48 173 C ATOM 1764 CD PRO A 222 55.882 26.802 26.936 1.00 9.98 C ANISOU 1764 CD PRO A 222 949 1648 1100 204 93 154 C ATOM 1765 N SER A 223 57.301 26.060 31.359 1.00 11.51 N ANISOU 1765 N SER A 223 1160 2087 1018 433 169 241 N ATOM 1766 CA SER A 223 58.488 25.905 32.157 1.00 13.02 C ANISOU 1766 CA SER A 223 1422 2473 931 679 117 214 C ATOM 1767 C SER A 223 59.439 24.868 31.495 1.00 11.05 C ANISOU 1767 C SER A 223 1244 1771 1078 411 66 485 C ATOM 1768 O SER A 223 59.051 23.781 31.060 1.00 12.93 O ANISOU 1768 O SER A 223 1296 1835 1661 253 164 483 O ATOM 1769 CB ASER A 223 58.143 25.315 33.538 0.32 18.13 C ANISOU 1769 CB ASER A 223 2123 3571 1024 1128 233 599 C ATOM 1770 CB BSER A 223 58.111 25.357 33.559 0.68 17.14 C ANISOU 1770 CB BSER A 223 1842 3379 1129 1386 188 646 C ATOM 1771 OG ASER A 223 57.218 26.116 34.225 0.32 18.70 O ANISOU 1771 OG ASER A 223 1182 4414 1334 175 202 -595 O ATOM 1772 OG BSER A 223 59.276 25.328 34.385 0.68 20.30 O ANISOU 1772 OG BSER A 223 2175 4257 1091 973 -57 376 O ATOM 1773 N GLY A 224 60.745 25.182 31.492 1.00 11.87 N ANISOU 1773 N GLY A 224 1077 2145 1176 419 70 292 N ATOM 1774 CA GLY A 224 61.718 24.263 31.016 1.00 11.34 C ANISOU 1774 CA GLY A 224 1194 1880 1128 305 -114 290 C ATOM 1775 C GLY A 224 61.729 23.993 29.539 1.00 10.62 C ANISOU 1775 C GLY A 224 971 1941 1023 558 93 412 C ATOM 1776 O GLY A 224 62.203 22.905 29.124 1.00 14.23 O ANISOU 1776 O GLY A 224 1697 2264 1313 1137 27 252 O ATOM 1777 N SER A 225 61.216 24.875 28.702 1.00 9.66 N ANISOU 1777 N SER A 225 970 1550 1059 288 -8 347 N ATOM 1778 CA SER A 225 61.068 24.661 27.282 1.00 8.57 C ANISOU 1778 CA SER A 225 899 1246 1032 272 -45 253 C ATOM 1779 C SER A 225 62.158 25.286 26.435 1.00 7.78 C ANISOU 1779 C SER A 225 728 1187 970 301 0 129 C ATOM 1780 O SER A 225 61.984 25.532 25.216 1.00 8.96 O ANISOU 1780 O SER A 225 761 1560 999 212 -65 277 O ATOM 1781 CB SER A 225 59.664 25.104 26.795 1.00 9.12 C ANISOU 1781 CB SER A 225 760 1467 1154 243 -16 89 C ATOM 1782 OG SER A 225 59.469 26.490 26.966 1.00 9.72 O ANISOU 1782 OG SER A 225 948 1494 1159 403 -12 240 O ATOM 1783 N THR A 226 63.321 25.539 27.051 1.00 8.28 N ANISOU 1783 N THR A 226 784 1304 979 270 -29 112 N ATOM 1784 CA THR A 226 64.520 25.871 26.279 1.00 7.74 C ANISOU 1784 CA THR A 226 835 1103 930 91 -83 47 C ATOM 1785 C THR A 226 64.908 24.695 25.391 1.00 7.10 C ANISOU 1785 C THR A 226 618 1074 938 141 -67 211 C ATOM 1786 O THR A 226 64.337 23.614 25.430 1.00 7.27 O ANISOU 1786 O THR A 226 688 1004 1001 125 16 123 O ATOM 1787 CB THR A 226 65.659 26.203 27.287 1.00 8.46 C ANISOU 1787 CB THR A 226 917 1134 1084 77 -122 31 C ATOM 1788 OG1 THR A 226 65.733 25.195 28.279 1.00 9.21 O ANISOU 1788 OG1 THR A 226 1008 1346 1057 80 -230 55 O ATOM 1789 CG2 THR A 226 65.477 27.563 27.951 1.00 10.04 C ANISOU 1789 CG2 THR A 226 1393 1261 1066 -139 -99 -4 C ATOM 1790 N GLY A 227 65.906 24.922 24.532 1.00 7.30 N ANISOU 1790 N GLY A 227 806 935 963 92 -22 130 N ATOM 1791 CA GLY A 227 66.520 23.833 23.811 1.00 7.22 C ANISOU 1791 CA GLY A 227 707 956 1014 119 -32 59 C ATOM 1792 C GLY A 227 65.520 23.118 22.891 1.00 6.57 C ANISOU 1792 C GLY A 227 660 880 897 45 -17 225 C ATOM 1793 O GLY A 227 64.807 23.773 22.090 1.00 7.06 O ANISOU 1793 O GLY A 227 684 935 999 86 -48 195 O ATOM 1794 N ARG A 228 65.501 21.812 22.945 1.00 6.81 N ANISOU 1794 N ARG A 228 596 971 959 174 -49 150 N ATOM 1795 CA ARG A 228 64.788 20.994 21.970 1.00 6.94 C ANISOU 1795 CA ARG A 228 571 993 1008 190 -53 51 C ATOM 1796 C ARG A 228 63.257 21.226 21.976 1.00 6.48 C ANISOU 1796 C ARG A 228 566 877 958 136 -26 204 C ATOM 1797 O ARG A 228 62.593 20.792 21.025 1.00 7.54 O ANISOU 1797 O ARG A 228 635 1083 1076 123 -50 -84 O ATOM 1798 CB ARG A 228 65.055 19.504 22.212 1.00 7.86 C ANISOU 1798 CB ARG A 228 618 1014 1279 179 -35 134 C ATOM 1799 CG ARG A 228 64.495 18.938 23.525 1.00 8.69 C ANISOU 1799 CG ARG A 228 772 999 1448 77 20 318 C ATOM 1800 CD ARG A 228 64.738 17.480 23.739 1.00 9.24 C ANISOU 1800 CD ARG A 228 985 1178 1261 97 -258 232 C ATOM 1801 NE ARG A 228 66.188 17.214 23.896 1.00 8.64 N ANISOU 1801 NE ARG A 228 1068 1077 1056 343 -163 97 N ATOM 1802 CZ ARG A 228 66.741 16.027 23.709 1.00 10.83 C ANISOU 1802 CZ ARG A 228 1669 1418 927 655 -119 -31 C ATOM 1803 NH1 ARG A 228 65.956 14.983 23.458 1.00 13.21 N ANISOU 1803 NH1 ARG A 228 2294 1087 1512 495 -66 338 N ATOM 1804 NH2 ARG A 228 68.057 15.911 23.774 1.00 13.83 N ANISOU 1804 NH2 ARG A 228 1767 1937 1421 1080 10 171 N ATOM 1805 N LEU A 229 62.717 21.810 23.030 1.00 6.23 N ANISOU 1805 N LEU A 229 557 848 904 142 -36 177 N ATOM 1806 CA LEU A 229 61.241 22.046 23.150 1.00 7.63 C ANISOU 1806 CA LEU A 229 554 1164 1110 141 -13 298 C ATOM 1807 C LEU A 229 60.757 23.313 22.493 1.00 6.95 C ANISOU 1807 C LEU A 229 589 1029 956 140 -37 153 C ATOM 1808 O LEU A 229 59.511 23.527 22.452 1.00 7.41 O ANISOU 1808 O LEU A 229 553 1035 1160 161 -14 256 O ATOM 1809 CB LEU A 229 60.845 21.853 24.603 1.00 7.91 C ANISOU 1809 CB LEU A 229 689 1069 1172 184 73 338 C ATOM 1810 CG LEU A 229 61.153 20.500 25.237 1.00 8.52 C ANISOU 1810 CG LEU A 229 700 1177 1280 156 -35 386 C ATOM 1811 CD1 LEU A 229 60.667 20.455 26.694 1.00 10.36 C ANISOU 1811 CD1 LEU A 229 1044 1491 1304 122 65 587 C ATOM 1812 CD2 LEU A 229 60.585 19.391 24.434 1.00 9.47 C ANISOU 1812 CD2 LEU A 229 894 1204 1412 -1 -49 449 C ATOM 1813 N LEU A 230 61.656 24.171 21.986 1.00 6.75 N ANISOU 1813 N LEU A 230 574 876 1049 61 -55 171 N ATOM 1814 CA LEU A 230 61.351 25.246 21.053 1.00 6.60 C ANISOU 1814 CA LEU A 230 580 883 984 62 -65 161 C ATOM 1815 C LEU A 230 60.477 26.326 21.645 1.00 6.82 C ANISOU 1815 C LEU A 230 609 986 931 64 -102 190 C ATOM 1816 O LEU A 230 59.864 27.131 20.905 1.00 7.67 O ANISOU 1816 O LEU A 230 746 1089 1007 237 -145 137 O ATOM 1817 CB LEU A 230 60.750 24.709 19.722 1.00 7.46 C ANISOU 1817 CB LEU A 230 673 1114 979 65 -147 67 C ATOM 1818 CG LEU A 230 61.685 23.829 18.930 1.00 8.96 C ANISOU 1818 CG LEU A 230 1011 1348 963 312 -66 98 C ATOM 1819 CD1 LEU A 230 60.948 23.189 17.760 1.00 12.30 C ANISOU 1819 CD1 LEU A 230 1472 1652 1435 -90 -31 -349 C ATOM 1820 CD2 LEU A 230 62.912 24.620 18.406 1.00 12.96 C ANISOU 1820 CD2 LEU A 230 913 2414 1474 -77 223 -396 C ATOM 1821 N GLY A 231 60.394 26.420 22.992 1.00 6.46 N ANISOU 1821 N GLY A 231 630 799 964 105 -94 173 N ATOM 1822 CA GLY A 231 59.491 27.372 23.663 1.00 7.69 C ANISOU 1822 CA GLY A 231 708 1081 1060 193 -5 121 C ATOM 1823 C GLY A 231 57.998 27.007 23.531 1.00 7.36 C ANISOU 1823 C GLY A 231 721 1020 987 88 0 268 C ATOM 1824 O GLY A 231 57.179 27.852 23.902 1.00 8.46 O ANISOU 1824 O GLY A 231 786 1122 1229 247 95 203 O ATOM 1825 N LEU A 232 57.697 25.814 23.034 1.00 7.82 N ANISOU 1825 N LEU A 232 638 1129 1132 197 -53 114 N ATOM 1826 CA LEU A 232 56.323 25.424 22.709 1.00 8.21 C ANISOU 1826 CA LEU A 232 654 962 1425 110 -45 287 C ATOM 1827 C LEU A 232 55.693 24.384 23.631 1.00 8.35 C ANISOU 1827 C LEU A 232 678 1208 1209 209 14 320 C ATOM 1828 O LEU A 232 54.483 24.447 23.863 1.00 9.56 O ANISOU 1828 O LEU A 232 730 1429 1385 176 53 461 O ATOM 1829 CB LEU A 232 56.272 24.891 21.270 1.00 9.26 C ANISOU 1829 CB LEU A 232 782 1511 1139 -61 -179 522 C ATOM 1830 CG LEU A 232 56.632 25.841 20.144 1.00 11.73 C ANISOU 1830 CG LEU A 232 982 1970 1394 -574 -463 830 C ATOM 1831 CD1 LEU A 232 56.605 25.067 18.809 1.00 15.85 C ANISOU 1831 CD1 LEU A 232 1263 3425 1184 -990 -247 500 C ATOM 1832 CD2 LEU A 232 55.709 27.035 20.112 1.00 15.43 C ANISOU 1832 CD2 LEU A 232 1343 1996 2379 -404 -592 1437 C ATOM 1833 N PHE A 233 56.493 23.421 24.094 1.00 8.07 N ANISOU 1833 N PHE A 233 696 1080 1215 121 -7 303 N ATOM 1834 CA PHE A 233 55.966 22.252 24.783 1.00 8.98 C ANISOU 1834 CA PHE A 233 789 1226 1314 67 -27 350 C ATOM 1835 C PHE A 233 56.595 22.047 26.130 1.00 9.10 C ANISOU 1835 C PHE A 233 930 1118 1323 178 172 480 C ATOM 1836 O PHE A 233 57.776 22.416 26.345 1.00 9.96 O ANISOU 1836 O PHE A 233 847 1599 1246 181 -52 437 O ATOM 1837 CB PHE A 233 56.219 20.986 23.934 1.00 9.59 C ANISOU 1837 CB PHE A 233 922 1154 1478 147 2 384 C ATOM 1838 CG PHE A 233 55.528 21.043 22.590 1.00 10.68 C ANISOU 1838 CG PHE A 233 1405 987 1565 202 -269 192 C ATOM 1839 CD1 PHE A 233 54.105 20.856 22.581 1.00 12.81 C ANISOU 1839 CD1 PHE A 233 1389 1320 2038 229 -524 9 C ATOM 1840 CD2 PHE A 233 56.176 21.343 21.409 1.00 12.93 C ANISOU 1840 CD2 PHE A 233 1859 1445 1487 415 -141 193 C ATOM 1841 CE1 PHE A 233 53.411 21.025 21.375 1.00 14.40 C ANISOU 1841 CE1 PHE A 233 1681 1248 2407 416 -812 -174 C ATOM 1842 CE2 PHE A 233 55.452 21.458 20.178 1.00 14.30 C ANISOU 1842 CE2 PHE A 233 2450 1377 1471 658 -338 -158 C ATOM 1843 CZ PHE A 233 54.081 21.284 20.212 1.00 16.63 C ANISOU 1843 CZ PHE A 233 2360 1821 1984 1017 -707 -228 C ATOM 1844 N PRO A 234 55.846 21.500 27.084 1.00 10.87 N ANISOU 1844 N PRO A 234 1117 1527 1386 69 86 595 N ATOM 1845 CA PRO A 234 56.410 21.294 28.457 1.00 12.57 C ANISOU 1845 CA PRO A 234 1640 1760 1259 32 207 613 C ATOM 1846 C PRO A 234 57.266 20.067 28.563 1.00 12.10 C ANISOU 1846 C PRO A 234 1380 1793 1309 -58 -203 502 C ATOM 1847 O PRO A 234 57.945 19.849 29.576 1.00 14.11 O ANISOU 1847 O PRO A 234 1910 1849 1471 -118 -313 618 O ATOM 1848 CB PRO A 234 55.154 21.181 29.349 1.00 15.72 C ANISOU 1848 CB PRO A 234 2044 2113 1667 -104 690 397 C ATOM 1849 CG PRO A 234 54.114 20.616 28.409 1.00 15.51 C ANISOU 1849 CG PRO A 234 1496 2195 2056 37 591 603 C ATOM 1850 CD PRO A 234 54.401 21.174 27.023 1.00 13.83 C ANISOU 1850 CD PRO A 234 1070 1937 2117 13 364 832 C ATOM 1851 N ASP A 235 57.156 19.119 27.628 1.00 11.50 N ANISOU 1851 N ASP A 235 1250 1728 1285 107 -94 649 N ATOM 1852 CA ASP A 235 57.870 17.857 27.654 1.00 11.80 C ANISOU 1852 CA ASP A 235 1116 1751 1504 107 -154 672 C ATOM 1853 C ASP A 235 57.942 17.353 26.210 1.00 10.59 C ANISOU 1853 C ASP A 235 892 1342 1690 -117 -233 565 C ATOM 1854 O ASP A 235 57.428 17.990 25.294 1.00 10.33 O ANISOU 1854 O ASP A 235 901 1434 1493 21 -184 384 O ATOM 1855 CB ASP A 235 57.234 16.870 28.631 1.00 14.37 C ANISOU 1855 CB ASP A 235 1568 1903 1853 -136 -162 912 C ATOM 1856 CG ASP A 235 55.793 16.637 28.250 1.00 16.59 C ANISOU 1856 CG ASP A 235 1493 2614 2041 -248 63 1135 C ATOM 1857 OD1 ASP A 235 55.477 16.379 27.060 1.00 15.12 O ANISOU 1857 OD1 ASP A 235 1218 2130 2255 -150 -85 882 O ATOM 1858 OD2 ASP A 235 54.925 16.679 29.166 1.00 22.70 O ANISOU 1858 OD2 ASP A 235 1932 3782 2696 -381 585 337 O ATOM 1859 N ALA A 236 58.608 16.205 26.062 1.00 12.64 N ANISOU 1859 N ALA A 236 1077 1680 1926 224 -9 567 N ATOM 1860 CA ALA A 236 58.797 15.618 24.745 1.00 13.27 C ANISOU 1860 CA ALA A 236 1149 1959 1808 296 -21 579 C ATOM 1861 C ALA A 236 57.815 14.525 24.407 1.00 15.95 C ANISOU 1861 C ALA A 236 1417 2230 2265 298 -434 225 C ATOM 1862 O ALA A 236 58.070 13.700 23.525 1.00 18.73 O ANISOU 1862 O ALA A 236 2313 2420 2207 394 -368 119 O ATOM 1863 CB ALA A 236 60.219 15.084 24.576 1.00 18.85 C ANISOU 1863 CB ALA A 236 1389 2489 3106 564 90 -187 C ATOM 1864 N ASN A 237 56.686 14.475 25.136 1.00 14.14 N ANISOU 1864 N ASN A 237 1494 1547 2199 -82 -436 626 N ATOM 1865 CA ASN A 237 55.705 13.457 24.856 1.00 16.73 C ANISOU 1865 CA ASN A 237 2150 1620 2429 -420 -822 875 C ATOM 1866 C ASN A 237 55.134 13.625 23.463 1.00 15.98 C ANISOU 1866 C ASN A 237 1962 1566 2394 6 -677 378 C ATOM 1867 O ASN A 237 54.932 14.731 22.975 1.00 15.50 O ANISOU 1867 O ASN A 237 1853 1607 2284 -261 -662 722 O ATOM 1868 CB ASN A 237 54.660 13.413 25.939 1.00 23.13 C ANISOU 1868 CB ASN A 237 2438 3506 2628 -1594 -528 828 C ATOM 1869 CG ASN A 237 55.080 12.973 27.327 1.00 31.32 C ANISOU 1869 CG ASN A 237 3119 5519 2969 -877 -167 1743 C ATOM 1870 OD1 ASN A 237 54.209 13.123 28.215 1.00 37.27 O ANISOU 1870 OD1 ASN A 237 4720 4720 4720 0 0 0 O ATOM 1871 ND2 ASN A 237 56.281 12.460 27.504 1.00 33.14 N ANISOU 1871 ND2 ASN A 237 3743 5252 3286 -325 -237 2343 N ATOM 1872 OXT ASN A 237 54.754 12.556 22.898 1.00 21.61 O ANISOU 1872 OXT ASN A 237 3812 1638 2559 -389 -1265 527 O TER 1873 ASN A 237 HETATM 1874 MN MN A 239 62.148 18.271 15.073 1.00 6.45 MN ANISOU 1874 MN MN A 239 566 800 1023 82 -75 95 MN HETATM 1875 CA CA A 240 65.495 19.343 17.381 1.00 6.37 CA ANISOU 1875 CA CA A 240 574 779 1009 135 -68 112 CA HETATM 1876 O HOH A 241 69.797 24.313 -3.624 1.00 9.19 O ANISOU 1876 O HOH A 241 849 1291 1267 191 201 -151 O HETATM 1877 O HOH A 242 41.756 30.382 22.989 1.00 9.93 O ANISOU 1877 O HOH A 242 822 1484 1373 -18 9 126 O HETATM 1878 O HOH A 243 72.792 21.681 14.210 1.00 10.20 O ANISOU 1878 O HOH A 243 787 1541 1452 198 33 -81 O HETATM 1879 O HOH A 244 55.753 17.286 23.188 1.00 10.75 O ANISOU 1879 O HOH A 244 1001 1350 1632 4 -137 421 O HETATM 1880 O HOH A 245 76.116 25.880 19.070 1.00 10.98 O ANISOU 1880 O HOH A 245 854 1516 1698 239 40 59 O HETATM 1881 O HOH A 246 64.142 21.633 27.450 1.00 10.80 O ANISOU 1881 O HOH A 246 1193 1369 1439 284 229 393 O HETATM 1882 O HOH A 247 53.423 16.680 16.496 1.00 8.98 O ANISOU 1882 O HOH A 247 781 977 1570 91 -75 275 O HETATM 1883 O HOH A 248 69.339 25.718 1.138 1.00 9.46 O ANISOU 1883 O HOH A 248 1124 1304 1076 -11 26 -149 O HETATM 1884 O HOH A 249 67.710 36.049 18.403 1.00 9.31 O ANISOU 1884 O HOH A 249 861 1211 1380 133 -155 -112 O HETATM 1885 O HOH A 250 47.337 36.674 17.762 1.00 8.20 O ANISOU 1885 O HOH A 250 659 845 1535 108 97 12 O HETATM 1886 O HOH A 251 40.045 37.332 13.410 1.00 11.95 O ANISOU 1886 O HOH A 251 1314 1355 1760 38 -130 416 O HETATM 1887 O HOH A 252 68.655 20.258 21.809 1.00 9.31 O ANISOU 1887 O HOH A 252 957 1184 1308 56 -39 78 O HETATM 1888 O HOH A 253 66.239 22.868 2.008 1.00 9.06 O ANISOU 1888 O HOH A 253 876 1466 1018 90 -54 -70 O HETATM 1889 O HOH A 254 66.234 39.154 22.493 1.00 11.84 O ANISOU 1889 O HOH A 254 1026 1846 1518 -176 -212 -279 O HETATM 1890 O HOH A 255 44.419 23.251 3.439 1.00 10.30 O ANISOU 1890 O HOH A 255 896 1214 1705 93 -96 -92 O HETATM 1891 O HOH A 256 54.280 19.701 0.807 1.00 11.47 O ANISOU 1891 O HOH A 256 904 1519 1827 41 179 -79 O HETATM 1892 O HOH A 257 63.436 27.725 -4.310 1.00 12.27 O ANISOU 1892 O HOH A 257 853 1632 2061 -26 -69 316 O HETATM 1893 O HOH A 258 61.130 19.023 0.673 1.00 15.81 O ANISOU 1893 O HOH A 258 2458 1491 1911 724 501 -464 O HETATM 1894 O HOH A 259 34.736 20.074 13.862 1.00 13.82 O ANISOU 1894 O HOH A 259 1223 1758 2141 54 332 179 O HETATM 1895 O HOH A 260 71.786 26.125 -4.360 1.00 14.22 O ANISOU 1895 O HOH A 260 972 1681 2617 90 481 -235 O HETATM 1896 O HOH A 261 48.403 46.968 14.763 1.00 11.91 O ANISOU 1896 O HOH A 261 1114 1510 1789 297 -242 -167 O HETATM 1897 O HOH A 262 67.938 21.761 -1.139 1.00 12.18 O ANISOU 1897 O HOH A 262 1273 1842 1398 378 81 -278 O HETATM 1898 O HOH A 263 69.502 31.120 8.164 1.00 14.69 O ANISOU 1898 O HOH A 263 940 2622 1883 441 106 216 O HETATM 1899 O HOH A 264 70.745 22.946 22.519 1.00 10.32 O ANISOU 1899 O HOH A 264 1048 1263 1514 109 -198 128 O HETATM 1900 O HOH A 265 51.913 47.722 13.519 1.00 11.98 O ANISOU 1900 O HOH A 265 1209 1402 1828 117 252 -159 O HETATM 1901 O HOH A 266 60.175 14.537 16.005 1.00 13.28 O ANISOU 1901 O HOH A 266 1323 1285 2313 74 356 18 O HETATM 1902 O HOH A 267 64.359 20.558 -3.356 1.00 11.39 O ANISOU 1902 O HOH A 267 988 1505 1729 107 4 -27 O HETATM 1903 O HOH A 268 67.250 20.236 -3.609 1.00 11.07 O ANISOU 1903 O HOH A 268 1054 1513 1535 351 235 38 O HETATM 1904 O HOH A 269 70.766 21.792 25.127 1.00 11.19 O ANISOU 1904 O HOH A 269 1208 1604 1336 61 -26 -52 O HETATM 1905 O HOH A 270 25.417 32.605 0.193 1.00 15.90 O ANISOU 1905 O HOH A 270 1533 1780 2581 124 -251 -275 O HETATM 1906 O HOH A 271 52.982 27.002 24.713 1.00 12.92 O ANISOU 1906 O HOH A 271 1502 1642 1642 -34 42 404 O HETATM 1907 O HOH A 272 69.782 18.905 6.041 1.00 16.50 O ANISOU 1907 O HOH A 272 1858 2051 2206 845 -699 -366 O HETATM 1908 O HOH A 273 53.564 12.912 17.894 1.00 14.66 O ANISOU 1908 O HOH A 273 1245 1682 2505 -249 -167 557 O HETATM 1909 O HOH A 274 53.944 18.066 25.430 1.00 17.50 O ANISOU 1909 O HOH A 274 1608 2559 2317 505 213 746 O HETATM 1910 O HOH A 275 55.398 33.457 28.819 1.00 12.66 O ANISOU 1910 O HOH A 275 1357 1872 1462 47 115 15 O HETATM 1911 O HOH A 276 27.131 28.521 6.686 1.00 17.92 O ANISOU 1911 O HOH A 276 2045 2787 1809 -628 -197 -492 O HETATM 1912 O HOH A 277 62.663 23.930 -5.257 1.00 11.39 O ANISOU 1912 O HOH A 277 1138 1522 1559 120 60 -199 O HETATM 1913 O HOH A 278 38.699 26.133 15.606 1.00 18.12 O ANISOU 1913 O HOH A 278 2442 1628 2644 -657 -755 84 O HETATM 1914 O HOH A 279 70.083 15.385 21.128 1.00 14.27 O ANISOU 1914 O HOH A 279 1523 2120 1645 1008 -34 196 O HETATM 1915 O HOH A 280 64.737 34.466 1.817 1.00 15.88 O ANISOU 1915 O HOH A 280 1681 2448 1755 -505 155 141 O HETATM 1916 O HOH A 281 52.299 37.072 28.005 1.00 18.27 O ANISOU 1916 O HOH A 281 2504 2568 1698 959 294 -662 O HETATM 1917 O HOH A 282 65.493 27.110 3.143 1.00 16.35 O ANISOU 1917 O HOH A 282 1437 2610 2012 488 159 498 O HETATM 1918 O HOH A 283 42.142 24.400 -2.624 1.00 22.07 O ANISOU 1918 O HOH A 283 3364 2989 1825 1611 537 757 O HETATM 1919 O HOH A 284 37.697 30.008 21.891 1.00 14.10 O ANISOU 1919 O HOH A 284 1287 1875 2063 166 271 103 O HETATM 1920 O HOH A 285 69.959 34.037 20.160 1.00 12.53 O ANISOU 1920 O HOH A 285 1160 1569 1913 39 104 -96 O HETATM 1921 O HOH A 286 69.716 23.883 -0.886 1.00 11.99 O ANISOU 1921 O HOH A 286 1409 1684 1352 345 214 -319 O HETATM 1922 O HOH A 287 58.209 45.801 22.022 1.00 14.62 O ANISOU 1922 O HOH A 287 1359 1838 2221 399 -86 -334 O HETATM 1923 O HOH A 288 65.440 21.235 -0.124 1.00 11.48 O ANISOU 1923 O HOH A 288 1166 1714 1377 289 -136 -149 O HETATM 1924 O HOH A 289 68.840 40.061 22.807 1.00 16.00 O ANISOU 1924 O HOH A 289 1047 1744 3136 102 -172 -515 O HETATM 1925 O HOH A 290 68.969 42.447 14.913 1.00 19.59 O ANISOU 1925 O HOH A 290 1763 1767 3731 -147 -929 287 O HETATM 1926 O HOH A 291 49.077 34.792 25.341 1.00 15.61 O ANISOU 1926 O HOH A 291 1078 1551 3155 79 -397 -44 O HETATM 1927 O HOH A 292 25.586 29.910 12.002 1.00 15.23 O ANISOU 1927 O HOH A 292 1098 2120 2428 -529 196 -134 O HETATM 1928 O HOH A 293 60.264 30.398 0.640 1.00 16.40 O ANISOU 1928 O HOH A 293 1486 2726 1866 554 -117 -592 O HETATM 1929 O HOH A 294 62.302 20.633 30.782 1.00 15.66 O ANISOU 1929 O HOH A 294 1490 2519 1793 482 -73 561 O HETATM 1930 O HOH A 295 49.492 14.726 19.094 1.00 21.14 O ANISOU 1930 O HOH A 295 2598 1584 3651 -206 1201 417 O HETATM 1931 O HOH A 296 69.628 25.339 28.425 1.00 16.42 O ANISOU 1931 O HOH A 296 1901 2229 1955 315 -143 11 O HETATM 1932 O HOH A 297 62.031 44.912 23.323 1.00 18.78 O ANISOU 1932 O HOH A 297 2433 2246 2279 266 -34 -1054 O HETATM 1933 O HOH A 298 62.446 14.020 6.842 1.00 20.47 O ANISOU 1933 O HOH A 298 2499 2498 2586 793 7 -398 O HETATM 1934 O HOH A 299 66.531 25.500 1.112 1.00 14.10 O ANISOU 1934 O HOH A 299 1365 2161 1697 -66 -91 -315 O HETATM 1935 O HOH A 300 39.525 23.994 9.741 1.00 24.55 O ANISOU 1935 O HOH A 300 1579 5165 2353 1471 756 1395 O HETATM 1936 O HOH A 301 35.276 37.442 13.592 1.00 15.30 O ANISOU 1936 O HOH A 301 1134 1639 2898 140 -199 -117 O HETATM 1937 O HOH A 302 65.512 43.420 18.990 1.00 15.81 O ANISOU 1937 O HOH A 302 1321 1591 2948 -36 -193 -474 O HETATM 1938 O HOH A 303 52.346 27.025 29.082 1.00 15.53 O ANISOU 1938 O HOH A 303 1808 2080 1865 246 -196 552 O HETATM 1939 O HOH A 304 71.690 29.552 -1.618 1.00 16.66 O ANISOU 1939 O HOH A 304 1689 2215 2269 -612 -472 708 O HETATM 1940 O HOH A 305 55.773 44.751 22.997 1.00 14.88 O ANISOU 1940 O HOH A 305 1742 1621 2150 275 -719 -306 O HETATM 1941 O HOH A 306 53.525 12.026 20.542 1.00 23.14 O ANISOU 1941 O HOH A 306 2948 2773 2853 -1197 -1015 1252 O HETATM 1942 O HOH A 307 74.703 25.903 7.249 1.00 19.17 O ANISOU 1942 O HOH A 307 1958 2352 2793 569 -489 -466 O HETATM 1943 O HOH A 308 55.045 16.168 3.414 1.00 15.90 O ANISOU 1943 O HOH A 308 1600 1303 2989 237 268 -339 O HETATM 1944 O HOH A 309 36.835 24.530 16.614 1.00 20.28 O ANISOU 1944 O HOH A 309 1505 3301 2707 -907 -168 -608 O HETATM 1945 O HOH A 310 50.991 21.606 25.019 1.00 16.87 O ANISOU 1945 O HOH A 310 1412 2359 2480 14 90 161 O HETATM 1946 O HOH A 311 77.137 26.024 11.071 1.00 22.01 O ANISOU 1946 O HOH A 311 2490 3139 2528 600 190 877 O HETATM 1947 O HOH A 312 63.183 44.221 10.024 1.00 17.93 O ANISOU 1947 O HOH A 312 2260 1383 2999 207 -756 -79 O HETATM 1948 O HOH A 313 65.667 25.729 31.022 1.00 18.05 O ANISOU 1948 O HOH A 313 3482 1855 1352 582 -217 183 O HETATM 1949 O HOH A 314 69.503 13.496 22.950 1.00 13.64 O ANISOU 1949 O HOH A 314 1267 1798 1989 306 45 185 O HETATM 1950 O HOH A 315 35.250 20.284 11.051 1.00 14.41 O ANISOU 1950 O HOH A 315 917 2171 2251 -114 12 117 O HETATM 1951 O HOH A 316 29.656 32.793 0.555 1.00 23.28 O ANISOU 1951 O HOH A 316 2058 4537 2032 425 400 -798 O HETATM 1952 O HOH A 317 26.896 30.194 16.575 1.00 16.77 O ANISOU 1952 O HOH A 317 1834 2166 2213 -45 191 -425 O HETATM 1953 O HOH A 318 55.378 42.851 25.050 1.00 14.76 O ANISOU 1953 O HOH A 318 1783 1649 2038 264 89 -602 O HETATM 1954 O HOH A 319 62.946 15.293 2.660 1.00 17.77 O ANISOU 1954 O HOH A 319 2186 2206 2192 207 -130 -1146 O HETATM 1955 O HOH A 320 45.294 26.478 1.610 1.00 26.53 O ANISOU 1955 O HOH A 320 2306 4926 2601 -1700 750 -354 O HETATM 1956 O HOH A 321 36.276 26.597 20.770 1.00 16.16 O ANISOU 1956 O HOH A 321 1377 2239 2371 -345 418 592 O HETATM 1957 O HOH A 322 48.833 13.553 6.045 1.00 17.96 O ANISOU 1957 O HOH A 322 1931 1426 3298 291 -394 -482 O HETATM 1958 O HOH A 323 67.060 53.597 21.337 1.00 24.59 O ANISOU 1958 O HOH A 323 4342 1918 2853 -502 3 769 O HETATM 1959 O HOH A 324 80.784 19.026 11.661 1.00 23.52 O ANISOU 1959 O HOH A 324 2314 3513 2889 194 -7 -1133 O HETATM 1960 O HOH A 325 50.219 54.747 23.647 1.00 19.69 O ANISOU 1960 O HOH A 325 1423 2856 3016 616 -333 174 O HETATM 1961 O HOH A 326 72.311 22.547 7.260 1.00 20.90 O ANISOU 1961 O HOH A 326 2049 2752 2945 411 273 338 O HETATM 1962 O HOH A 327 60.134 25.162 -4.992 1.00 15.88 O ANISOU 1962 O HOH A 327 1347 1905 2633 182 302 187 O HETATM 1963 O HOH A 328 60.194 39.309 26.271 1.00 20.65 O ANISOU 1963 O HOH A 328 2277 2830 2547 722 291 -321 O HETATM 1964 O HOH A 329 31.582 26.699 9.684 1.00 19.69 O ANISOU 1964 O HOH A 329 3920 1349 2026 -38 475 237 O HETATM 1965 O HOH A 330 37.003 26.911 10.248 1.00 17.65 O ANISOU 1965 O HOH A 330 2855 2014 1670 -291 -58 -482 O HETATM 1966 O HOH A 331 52.455 23.894 25.616 1.00 16.83 O ANISOU 1966 O HOH A 331 1129 2951 2155 428 365 506 O HETATM 1967 O HOH A 332 53.088 34.958 29.853 1.00 25.70 O ANISOU 1967 O HOH A 332 2886 4317 2320 1519 -30 -438 O HETATM 1968 O HOH A 333 43.849 33.591 4.461 1.00 20.49 O ANISOU 1968 O HOH A 333 1871 2885 2836 -394 -193 -141 O HETATM 1969 O HOH A 334 75.683 31.471 26.289 1.00 23.88 O ANISOU 1969 O HOH A 334 1801 3058 3992 -110 -1575 271 O HETATM 1970 O HOH A 335 67.571 9.461 25.262 1.00 24.20 O ANISOU 1970 O HOH A 335 2671 4457 1839 399 -448 -239 O HETATM 1971 O HOH A 336 49.456 29.342 29.324 1.00 21.66 O ANISOU 1971 O HOH A 336 2212 3859 1957 -900 181 -129 O HETATM 1972 O HOH A 337 30.615 30.656 15.829 1.00 17.23 O ANISOU 1972 O HOH A 337 1684 2729 1972 -579 369 -535 O HETATM 1973 O HOH A 338 28.922 26.490 7.387 1.00 18.09 O ANISOU 1973 O HOH A 338 1892 2204 2609 -536 -226 -126 O HETATM 1974 O HOH A 339 43.420 16.816 3.116 1.00 26.34 O ANISOU 1974 O HOH A 339 3581 2502 3676 1132 -1018 -1129 O HETATM 1975 O HOH A 340 78.302 24.982 20.739 1.00 18.35 O ANISOU 1975 O HOH A 340 1369 2744 2687 259 -226 -312 O HETATM 1976 O HOH A 341 50.379 36.900 4.899 1.00 34.46 O ANISOU 1976 O HOH A 341 4718 5366 2686 -3004 132 359 O HETATM 1977 O HOH A 342 68.302 33.935 28.909 1.00 23.80 O ANISOU 1977 O HOH A 342 2653 3817 2351 950 -1193 -430 O HETATM 1978 O HOH A 343 68.297 26.158 31.154 1.00 32.99 O ANISOU 1978 O HOH A 343 3396 7029 1800 -1642 -910 453 O HETATM 1979 O HOH A 344 63.365 18.194 1.589 1.00 24.93 O ANISOU 1979 O HOH A 344 3916 3298 2022 1565 -1029 -1278 O HETATM 1980 O HOH A 345 42.462 16.253 6.664 1.00 25.24 O ANISOU 1980 O HOH A 345 1932 2585 4838 204 -312 -672 O HETATM 1981 O HOH A 346 42.271 15.546 11.587 1.00 25.95 O ANISOU 1981 O HOH A 346 2477 2971 4167 495 1045 2154 O HETATM 1982 O HOH A 347 50.314 44.374 3.495 1.00 22.08 O ANISOU 1982 O HOH A 347 2786 2900 2495 -874 517 353 O HETATM 1983 O HOH A 348 71.761 17.784 22.122 1.00 15.52 O ANISOU 1983 O HOH A 348 1529 2088 2133 103 303 -14 O HETATM 1984 O HOH A 349 57.638 12.532 7.763 1.00 25.44 O ANISOU 1984 O HOH A 349 2575 1531 5322 -292 1151 -1181 O HETATM 1985 O HOH A 350 69.481 31.074 30.932 1.00 23.02 O ANISOU 1985 O HOH A 350 3917 2369 2246 222 -859 54 O HETATM 1986 O HOH A 351 54.192 39.226 27.877 1.00 25.77 O ANISOU 1986 O HOH A 351 2238 5159 2152 -399 627 -1687 O HETATM 1987 O HOH A 352 57.523 35.916 29.656 1.00 28.91 O ANISOU 1987 O HOH A 352 2308 6340 2065 1679 1051 1626 O HETATM 1988 O HOH A 353 58.376 12.588 15.031 1.00 18.85 O ANISOU 1988 O HOH A 353 1689 1521 3775 474 -1039 -89 O HETATM 1989 O HOH A 354 73.934 27.969 28.116 1.00 21.39 O ANISOU 1989 O HOH A 354 1620 2770 3537 397 -300 250 O HETATM 1990 O HOH A 355 55.708 31.547 30.941 1.00 23.01 O ANISOU 1990 O HOH A 355 2992 2979 2554 198 -365 228 O HETATM 1991 O HOH A 356 37.740 40.316 11.871 1.00 31.67 O ANISOU 1991 O HOH A 356 2394 6488 2856 1861 -140 -844 O HETATM 1992 O HOH A 357 42.775 19.664 21.240 1.00 21.41 O ANISOU 1992 O HOH A 357 1822 2576 3535 464 193 514 O HETATM 1993 O HOH A 358 57.603 21.655 31.726 1.00 31.53 O ANISOU 1993 O HOH A 358 4675 4663 2346 -2373 810 -430 O HETATM 1994 O HOH A 359 38.563 31.755 3.567 1.00 24.93 O ANISOU 1994 O HOH A 359 2544 3316 3379 -400 -643 144 O HETATM 1995 O HOH A 360 74.172 19.368 14.342 1.00 21.72 O ANISOU 1995 O HOH A 360 1273 1892 4884 357 -585 -765 O HETATM 1996 O HOH A 361 30.673 30.104 19.632 1.00 21.55 O ANISOU 1996 O HOH A 361 1199 3050 3737 77 99 -481 O HETATM 1997 O HOH A 362 32.040 24.617 4.500 1.00 27.64 O ANISOU 1997 O HOH A 362 1896 2009 6339 -426 1728 4 O HETATM 1998 O HOH A 363 42.042 29.369 26.940 1.00 25.86 O ANISOU 1998 O HOH A 363 2668 4980 1933 -1122 701 -276 O HETATM 1999 O HOH A 364 57.664 15.042 3.983 1.00 19.92 O ANISOU 1999 O HOH A 364 2004 2372 3004 415 -529 -597 O HETATM 2000 O HOH A 365 60.309 18.596 30.480 1.00 26.54 O ANISOU 2000 O HOH A 365 2554 3916 3366 315 -585 1817 O HETATM 2001 O HOH A 366 70.661 33.272 28.026 1.00 24.06 O ANISOU 2001 O HOH A 366 2715 2849 3353 -124 -523 -867 O HETATM 2002 O HOH A 367 69.734 41.915 20.837 1.00 25.14 O ANISOU 2002 O HOH A 367 2453 3103 3760 -151 654 -245 O HETATM 2003 O HOH A 368 56.838 38.570 5.754 1.00 27.22 O ANISOU 2003 O HOH A 368 3728 2704 3654 -1503 1334 -1454 O HETATM 2004 O HOH A 369 73.694 14.453 13.002 1.00 25.62 O ANISOU 2004 O HOH A 369 2131 2342 5020 -33 1396 -990 O HETATM 2005 O HOH A 370 54.664 25.590 32.497 1.00 30.99 O ANISOU 2005 O HOH A 370 1855 6352 3277 967 1116 2569 O HETATM 2006 O HOH A 371 35.223 26.937 7.843 1.00 21.49 O ANISOU 2006 O HOH A 371 2081 2795 3086 -436 813 -597 O HETATM 2007 O HOH A 372 61.940 43.102 6.169 1.00 22.58 O ANISOU 2007 O HOH A 372 1902 3407 3059 -58 456 -570 O HETATM 2008 O HOH A 373 47.102 20.365 25.864 1.00 30.24 O ANISOU 2008 O HOH A 373 4499 2582 4126 -32 -123 206 O HETATM 2009 O HOH A 374 69.433 35.769 1.743 1.00 24.25 O ANISOU 2009 O HOH A 374 3410 3329 2246 -558 933 437 O HETATM 2010 O HOH A 375 71.258 20.481 21.298 1.00 12.24 O ANISOU 2010 O HOH A 375 993 1816 1726 82 27 -326 O HETATM 2011 O HOH A 376 41.157 28.196 24.612 1.00 15.77 O ANISOU 2011 O HOH A 376 1909 2164 1772 -220 378 525 O HETATM 2012 O HOH A 377 40.071 35.673 11.183 1.00 15.21 O ANISOU 2012 O HOH A 377 1548 1942 2147 377 333 47 O HETATM 2013 O HOH A 378 51.489 19.155 26.037 1.00 21.70 O ANISOU 2013 O HOH A 378 1463 2832 3746 45 -134 782 O HETATM 2014 O HOH A 379 35.059 30.665 22.402 1.00 21.00 O ANISOU 2014 O HOH A 379 1461 2908 3411 53 620 652 O HETATM 2015 O HOH A 380 64.317 25.457 -6.924 1.00 15.29 O ANISOU 2015 O HOH A 380 1510 2171 1987 12 -59 85 O HETATM 2016 O HOH A 381 55.020 17.049 0.983 1.00 21.46 O ANISOU 2016 O HOH A 381 2382 2216 3353 215 215 -312 O HETATM 2017 O HOH A 382 74.297 17.108 12.494 1.00 24.74 O ANISOU 2017 O HOH A 382 2418 2457 4293 676 308 578 O HETATM 2018 O HOH A 383 73.521 26.937 -2.481 1.00 28.91 O ANISOU 2018 O HOH A 383 2116 4933 3665 568 -230 -2512 O HETATM 2019 O HOH A 384 74.815 25.086 10.022 1.00 25.21 O ANISOU 2019 O HOH A 384 3052 3145 3143 -612 -674 201 O HETATM 2020 O HOH A 385 29.539 33.187 15.868 1.00 31.77 O ANISOU 2020 O HOH A 385 3959 2570 5242 355 597 -438 O HETATM 2021 O HOH A 386 71.224 38.992 15.186 1.00 29.77 O ANISOU 2021 O HOH A 386 2632 2637 5762 474 2022 166 O HETATM 2022 O HOH A 387 37.122 16.515 9.613 1.00 30.45 O ANISOU 2022 O HOH A 387 2930 2850 5502 -1319 -848 -87 O HETATM 2023 O HOH A 388 53.806 19.561 -2.106 1.00 24.07 O ANISOU 2023 O HOH A 388 1782 4035 3102 809 -84 -856 O HETATM 2024 O HOH A 389 52.061 44.527 23.838 1.00 26.88 O ANISOU 2024 O HOH A 389 2334 4701 2927 890 -445 -1481 O HETATM 2025 O HOH A 390 53.863 28.377 31.413 1.00 23.97 O ANISOU 2025 O HOH A 390 2409 3348 3126 745 1048 676 O HETATM 2026 O HOH A 391 38.537 22.150 18.767 1.00 30.01 O ANISOU 2026 O HOH A 391 3688 4013 3420 -2179 385 -822 O HETATM 2027 O HOH A 392 75.704 27.215 25.969 1.00 25.21 O ANISOU 2027 O HOH A 392 2781 2796 3767 -365 754 -285 O HETATM 2028 O HOH A 393 71.206 35.415 -0.216 1.00 29.62 O ANISOU 2028 O HOH A 393 3466 3898 3612 -1643 1324 -1507 O HETATM 2029 O HOH A 394 57.377 49.950 14.446 1.00 26.12 O ANISOU 2029 O HOH A 394 1475 2106 6097 -123 -585 649 O HETATM 2030 O HOH A 395 72.893 19.496 3.599 1.00 38.53 O ANISOU 2030 O HOH A 395 3995 7558 2726 2469 687 -362 O HETATM 2031 O HOH A 396 72.241 20.120 6.385 1.00 27.74 O ANISOU 2031 O HOH A 396 2933 4095 3251 -1179 261 -88 O HETATM 2032 O HOH A 397 68.969 28.916 32.562 1.00 26.56 O ANISOU 2032 O HOH A 397 3354 3781 2706 1019 -457 1297 O HETATM 2033 O HOH A 398 53.309 42.680 26.771 1.00 36.56 O ANISOU 2033 O HOH A 398 3101 5933 4516 1328 969 -846 O HETATM 2034 O HOH A 399 59.806 14.038 27.818 1.00 35.69 O ANISOU 2034 O HOH A 399 3862 4696 4669 1828 1354 1902 O HETATM 2035 O HOH A 400 56.152 53.787 21.745 1.00 29.37 O ANISOU 2035 O HOH A 400 1916 3024 5942 781 -387 -765 O HETATM 2036 O HOH A 401 49.832 10.868 15.755 1.00 29.93 O ANISOU 2036 O HOH A 401 3876 2093 5121 -969 -503 -22 O HETATM 2037 O HOH A 402 46.647 30.278 31.115 1.00 32.76 O ANISOU 2037 O HOH A 402 3004 7032 2105 -321 -535 679 O HETATM 2038 O HOH A 403 42.842 33.465 30.531 1.00 28.69 O ANISOU 2038 O HOH A 403 2436 6374 1822 271 247 -109 O HETATM 2039 O HOH A 404 50.923 18.352 28.728 1.00 30.78 O ANISOU 2039 O HOH A 404 2767 4557 4081 462 1116 1913 O HETATM 2040 O HOH A 405 56.735 52.492 19.418 1.00 31.04 O ANISOU 2040 O HOH A 405 1058 4556 5887 -198 -962 331 O HETATM 2041 O HOH A 406 64.205 46.948 10.374 1.00 25.86 O ANISOU 2041 O HOH A 406 2407 2281 4894 -503 -874 638 O HETATM 2042 O HOH A 407 49.727 18.010 24.161 1.00 32.01 O ANISOU 2042 O HOH A 407 3057 6335 2470 -1409 -488 960 O HETATM 2043 O HOH A 408 68.141 37.790 1.199 1.00 27.76 O ANISOU 2043 O HOH A 408 3564 3292 3431 -662 89 -685 O HETATM 2044 O HOH A 409 58.256 40.561 27.718 1.00 29.21 O ANISOU 2044 O HOH A 409 3451 4737 2638 1235 -1028 -1565 O HETATM 2045 O HOH A 410 66.167 21.437 18.237 1.00 7.69 O ANISOU 2045 O HOH A 410 766 949 1134 133 25 -7 O HETATM 2046 O HOH A 411 63.430 19.497 18.648 1.00 8.23 O ANISOU 2046 O HOH A 411 610 1396 1044 74 -81 177 O HETATM 2047 O HOH A 412 61.049 18.677 17.007 1.00 7.41 O ANISOU 2047 O HOH A 412 662 996 1089 75 -74 257 O HETATM 2048 O HOH A 413 60.719 16.761 14.410 1.00 8.68 O ANISOU 2048 O HOH A 413 756 1073 1385 19 -185 -45 O HETATM 2049 O HOH A 414 51.670 24.570 28.148 1.00 15.85 O ANISOU 2049 O HOH A 414 1539 2194 2142 68 -107 280 O HETATM 2050 O HOH A 415 52.337 23.260 30.518 1.00 25.35 O ANISOU 2050 O HOH A 415 2870 4451 2071 1583 -25 64 O HETATM 2051 O HOH A 416 71.395 36.701 3.370 1.00 22.83 O ANISOU 2051 O HOH A 416 1887 3097 3477 79 849 1416 O HETATM 2052 O HOH A 417 46.642 12.739 8.462 1.00 25.97 O ANISOU 2052 O HOH A 417 3147 1545 4932 94 -1191 -197 O HETATM 2053 O HOH A 418 68.960 11.644 21.089 1.00 24.38 O ANISOU 2053 O HOH A 418 2257 3425 3354 -775 -168 -576 O HETATM 2054 O HOH A 419 38.256 28.141 24.179 1.00 23.43 O ANISOU 2054 O HOH A 419 2149 3624 2908 276 232 601 O HETATM 2055 O HOH A 420 60.660 21.087 33.252 1.00 34.56 O ANISOU 2055 O HOH A 420 3716 4679 4414 -746 -472 995 O HETATM 2056 O HOH A 421 38.531 31.819 26.314 1.00 34.49 O ANISOU 2056 O HOH A 421 3491 5636 3654 1202 342 217 O HETATM 2057 O HOH A 422 40.487 32.448 31.846 1.00 34.95 O ANISOU 2057 O HOH A 422 1837 9287 1829 685 67 -535 O HETATM 2058 O HOH A 423 67.799 43.347 21.677 1.00 37.83 O ANISOU 2058 O HOH A 423 2590 5701 5727 -1154 -1524 688 O HETATM 2059 O HOH A 424 64.745 9.805 15.482 1.00 21.58 O ANISOU 2059 O HOH A 424 3075 1940 2983 1 -401 70 O HETATM 2060 O HOH A 425 33.864 27.989 20.722 1.00 34.04 O ANISOU 2060 O HOH A 425 2220 4136 6259 951 1216 1928 O HETATM 2061 O HOH A 426 62.578 50.101 13.618 1.00 29.55 O ANISOU 2061 O HOH A 426 3081 2218 5652 303 671 303 O HETATM 2062 O HOH A 427 52.034 29.566 32.073 1.00 26.13 O ANISOU 2062 O HOH A 427 2288 5010 2386 1454 690 1157 O HETATM 2063 O HOH A 428 68.782 41.554 25.123 1.00 31.20 O ANISOU 2063 O HOH A 428 2522 4431 4607 377 -1202 -39 O HETATM 2064 O HOH A 429 73.532 31.248 0.022 1.00 27.91 O ANISOU 2064 O HOH A 429 2768 3870 3704 -1461 724 -446 O HETATM 2065 O HOH A 430 35.411 22.998 10.020 1.00 28.51 O ANISOU 2065 O HOH A 430 2482 3472 4613 -1459 -524 1081 O HETATM 2066 O HOH A 431 31.591 32.560 18.142 1.00 20.96 O ANISOU 2066 O HOH A 431 1184 2478 4104 -262 803 -1212 O HETATM 2067 O HOH A 432 51.208 15.225 26.154 1.00 30.59 O ANISOU 2067 O HOH A 432 3396 4672 3267 825 812 1078 O HETATM 2068 O HOH A 433 34.854 24.401 5.262 1.00 27.70 O ANISOU 2068 O HOH A 433 2008 2656 5600 -91 810 -301 O HETATM 2069 O HOH A 434 54.490 10.504 16.577 1.00 32.25 O ANISOU 2069 O HOH A 434 4905 2262 4783 341 463 -187 O HETATM 2070 O HOH A 435 71.339 31.879 0.260 1.00 46.24 O ANISOU 2070 O HOH A 435 5856 5856 5856 0 0 0 O HETATM 2071 O HOH A 436 25.234 33.741 7.806 1.00 31.52 O ANISOU 2071 O HOH A 436 3763 3343 4576 974 -1379 -1832 O HETATM 2072 O HOH A 437 74.766 30.222 28.701 1.00 40.67 O ANISOU 2072 O HOH A 437 5151 5151 5151 0 0 0 O HETATM 2073 O HOH A 438 49.714 30.724 32.159 1.00 27.04 O ANISOU 2073 O HOH A 438 2816 4718 2487 -378 445 -586 O HETATM 2074 O HOH A 439 40.227 26.729 10.975 1.00 29.02 O ANISOU 2074 O HOH A 439 2730 4047 3977 -544 10 -1812 O HETATM 2075 O HOH A 440 41.240 29.183 9.554 1.00 38.34 O ANISOU 2075 O HOH A 440 4856 4856 4856 0 0 0 O HETATM 2076 O HOH A 441 45.511 29.733 2.622 1.00 30.08 O ANISOU 2076 O HOH A 441 2790 5432 2923 1255 -258 424 O HETATM 2077 O HOH A 442 44.878 14.299 11.325 1.00 28.50 O ANISOU 2077 O HOH A 442 3514 4272 2778 256 752 795 O HETATM 2078 O HOH A 443 49.735 21.098 22.566 1.00 14.46 O ANISOU 2078 O HOH A 443 1748 1899 1711 556 119 442 O HETATM 2079 O HOH A 444 26.141 40.565 8.489 1.00 17.30 O ANISOU 2079 O HOH A 444 1265 2229 2915 -278 -208 0 O HETATM 2080 O HOH A 445 50.608 18.695 -0.328 1.00 21.56 O ANISOU 2080 O HOH A 445 2993 2711 2285 651 -445 -72 O HETATM 2081 O HOH A 446 48.548 28.597 31.280 1.00 21.42 O ANISOU 2081 O HOH A 446 2373 4230 1335 663 97 -364 O HETATM 2082 O HOH A 447 29.797 37.808 6.792 1.00 23.60 O ANISOU 2082 O HOH A 447 2446 2971 3327 89 122 -754 O HETATM 2083 O HOH A 448 54.741 47.142 24.147 1.00 30.58 O ANISOU 2083 O HOH A 448 4066 3169 4097 1672 -1729 -1051 O HETATM 2084 O HOH A 449 61.229 42.735 25.451 1.00 31.84 O ANISOU 2084 O HOH A 449 4572 3436 3790 30 281 -1506 O HETATM 2085 O HOH A 450 57.553 16.624 2.294 1.00 30.80 O ANISOU 2085 O HOH A 450 4371 2307 4735 125 -1437 346 O HETATM 2086 O HOH A 451 37.554 31.830 -2.483 1.00 39.77 O ANISOU 2086 O HOH A 451 3303 3967 7468 -1943 -191 131 O HETATM 2087 O HOH A 452 44.702 27.268 29.277 1.00 37.37 O ANISOU 2087 O HOH A 452 3885 5648 4315 311 1315 1249 O HETATM 2088 O HOH A 453 77.773 26.312 22.899 1.00 28.09 O ANISOU 2088 O HOH A 453 2726 3741 3941 -1302 558 219 O HETATM 2089 O HOH A 454 71.537 11.770 7.863 1.00 41.11 O ANISOU 2089 O HOH A 454 5207 5207 5207 0 0 0 O HETATM 2090 O HOH A 455 32.682 22.680 6.028 1.00 37.12 O ANISOU 2090 O HOH A 455 4701 4701 4701 0 0 0 O HETATM 2091 O HOH A 456 53.120 38.553 2.525 1.00 37.71 O ANISOU 2091 O HOH A 456 4776 4776 4776 0 0 0 O HETATM 2092 O HOH A 457 53.279 31.434 32.543 1.00 36.79 O ANISOU 2092 O HOH A 457 4015 6301 3319 -1316 -162 1152 O HETATM 2093 O HOH A 458 41.974 34.245 28.182 1.00 33.41 O ANISOU 2093 O HOH A 458 3371 4264 4746 211 769 1488 O HETATM 2094 O HOH A 459 51.611 34.927 3.758 1.00 34.21 O ANISOU 2094 O HOH A 459 2500 5179 4997 -443 -1360 1914 O HETATM 2095 O HOH A 460 50.644 39.427 2.308 1.00 46.02 O ANISOU 2095 O HOH A 460 5829 5829 5829 0 0 0 O HETATM 2096 O HOH A 461 73.007 16.544 9.648 1.00 37.55 O ANISOU 2096 O HOH A 461 4756 4756 4756 0 0 0 O HETATM 2097 O HOH A 462 72.387 32.812 -1.555 1.00 35.96 O ANISOU 2097 O HOH A 462 5844 4354 3128 -880 -609 -1015 O HETATM 2098 O HOH A 463 66.001 36.689 0.726 1.00 36.75 O ANISOU 2098 O HOH A 463 5788 3518 4314 -2520 -171 779 O HETATM 2099 O HOH A 464 76.948 17.225 11.610 1.00 33.74 O ANISOU 2099 O HOH A 464 3003 4602 4897 -186 634 380 O HETATM 2100 O HOH A 465 54.754 36.635 1.088 1.00 46.95 O ANISOU 2100 O HOH A 465 5946 5946 5946 0 0 0 O HETATM 2101 O HOH A 466 61.570 27.843 32.584 1.00 27.60 O ANISOU 2101 O HOH A 466 2999 3603 3626 -291 -509 -1107 O HETATM 2102 O HOH A 467 64.817 33.664 30.762 1.00 44.58 O ANISOU 2102 O HOH A 467 5646 5646 5646 0 0 0 O HETATM 2103 O HOH A 468 69.328 38.395 -1.050 1.00 41.67 O ANISOU 2103 O HOH A 468 5278 5278 5278 0 0 0 O HETATM 2104 O HOH A 469 34.686 27.940 10.008 1.00 27.26 O ANISOU 2104 O HOH A 469 2882 3641 3577 -677 -775 562 O HETATM 2105 O HOH A 470 61.638 16.133 0.207 1.00 40.19 O ANISOU 2105 O HOH A 470 5090 5090 5090 0 0 0 O HETATM 2106 O HOH A 471 50.670 27.320 31.190 1.00 43.20 O ANISOU 2106 O HOH A 471 5471 5471 5471 0 0 0 O HETATM 2107 O HOH A 472 40.165 15.187 13.213 1.00 29.78 O ANISOU 2107 O HOH A 472 2984 2402 5651 233 1953 605 O HETATM 2108 O HOH A 473 44.972 34.748 1.994 1.00 35.42 O ANISOU 2108 O HOH A 473 3720 4462 4944 -403 586 138 O HETATM 2109 O HOH A 474 47.255 26.739 29.643 1.00 33.96 O ANISOU 2109 O HOH A 474 4821 4432 3332 -159 1827 917 O HETATM 2110 O HOH A 475 68.266 44.107 24.816 1.00 33.56 O ANISOU 2110 O HOH A 475 4250 4250 4250 0 0 0 O HETATM 2111 O HOH A 476 65.715 46.447 21.617 1.00 34.18 O ANISOU 2111 O HOH A 476 2949 4895 4822 -168 -817 -1001 O HETATM 2112 O HOH A 477 56.871 16.402 -1.001 1.00 31.03 O ANISOU 2112 O HOH A 477 2593 4302 4604 152 1450 -1083 O HETATM 2113 O HOH A 478 52.358 10.906 11.649 1.00 30.77 O ANISOU 2113 O HOH A 478 4359 2055 4990 -1404 986 -130 O HETATM 2114 O HOH A 479 66.468 45.654 10.330 1.00 30.16 O ANISOU 2114 O HOH A 479 1886 4435 4854 213 915 1922 O HETATM 2115 O HOH A 480 52.500 16.191 28.777 1.00 34.30 O ANISOU 2115 O HOH A 480 3433 4207 5069 -161 825 1388 O HETATM 2116 O HOH A 481 71.779 41.701 25.460 1.00 37.93 O ANISOU 2116 O HOH A 481 3154 6402 4500 1838 78 -285 O HETATM 2117 O HOH A 482 75.049 36.781 8.230 1.00 25.52 O ANISOU 2117 O HOH A 482 2626 3272 3561 -557 -328 -615 O HETATM 2118 O HOH A 483 72.442 35.543 27.479 1.00 34.06 O ANISOU 2118 O HOH A 483 4206 3857 4559 706 -1631 -1758 O HETATM 2119 O HOH A 484 64.056 49.798 11.252 1.00 32.39 O ANISOU 2119 O HOH A 484 3757 3673 4575 787 -942 1029 O HETATM 2120 O HOH A 485 35.665 39.102 12.053 1.00 35.62 O ANISOU 2120 O HOH A 485 3183 6829 3186 2735 -993 -733 O HETATM 2121 O HOH A 486 40.610 31.424 27.502 1.00 30.51 O ANISOU 2121 O HOH A 486 3826 4971 2509 -919 586 340 O HETATM 2122 O HOH A 487 73.560 22.783 10.216 1.00 36.66 O ANISOU 2122 O HOH A 487 4184 3289 6112 -1011 926 -1485 O HETATM 2123 O HOH A 488 75.374 29.405 2.571 1.00 34.39 O ANISOU 2123 O HOH A 488 2712 5894 4138 -1525 893 -877 O HETATM 2124 O HOH A 489 66.447 51.025 11.970 1.00 35.40 O ANISOU 2124 O HOH A 489 4483 4483 4483 0 0 0 O HETATM 2125 O HOH A 490 70.787 41.781 18.276 1.00 27.57 O ANISOU 2125 O HOH A 490 3491 3179 3548 -972 -1006 -18 O HETATM 2126 O HOH A 491 57.314 42.895 27.089 1.00 35.44 O ANISOU 2126 O HOH A 491 3771 5224 4138 787 -1303 -1818 O HETATM 2127 O HOH A 492 52.196 15.532 23.632 1.00 35.63 O ANISOU 2127 O HOH A 492 3316 6259 3628 1101 792 697 O HETATM 2128 O HOH A 493 59.952 11.145 13.317 1.00 36.22 O ANISOU 2128 O HOH A 493 2050 5539 5833 34 -580 -2456 O HETATM 2129 O HOH A 494 58.118 10.528 16.483 1.00 38.41 O ANISOU 2129 O HOH A 494 4865 4865 4865 0 0 0 O HETATM 2130 O HOH A 495 51.776 20.193 31.079 1.00 33.29 O ANISOU 2130 O HOH A 495 3657 5303 3377 -878 1252 931 O HETATM 2131 O HOH A 496 73.608 10.126 8.333 1.00 34.43 O ANISOU 2131 O HOH A 496 3475 3601 5683 -309 -1084 1226 O HETATM 2132 O HOH A 497 55.800 20.365 -4.191 1.00 44.71 O ANISOU 2132 O HOH A 497 5663 5663 5663 0 0 0 O HETATM 2133 O HOH A 498 51.209 34.056 31.167 1.00 38.41 O ANISOU 2133 O HOH A 498 4865 4865 4865 0 0 0 O HETATM 2134 O HOH A 499 50.075 11.000 12.939 1.00 38.51 O ANISOU 2134 O HOH A 499 4877 4877 4877 0 0 0 O HETATM 2135 O HOH A 500 65.786 30.725 29.807 1.00 38.03 O ANISOU 2135 O HOH A 500 4817 4817 4817 0 0 0 O HETATM 2136 O HOH A 501 69.897 48.921 17.254 1.00 30.70 O ANISOU 2136 O HOH A 501 4629 2553 4195 -1070 -230 -237 O HETATM 2137 O HOH A 502 70.840 36.548 -4.492 1.00 35.13 O ANISOU 2137 O HOH A 502 4556 3542 4919 -353 11 52 O HETATM 2138 O HOH A 503 77.197 29.229 25.817 1.00 41.33 O ANISOU 2138 O HOH A 503 5235 5235 5235 0 0 0 O HETATM 2139 O HOH A 504 62.649 40.637 4.849 1.00 37.51 O ANISOU 2139 O HOH A 504 4751 4751 4751 0 0 0 O HETATM 2140 O HOH A 505 59.732 12.274 10.243 1.00 32.59 O ANISOU 2140 O HOH A 505 5020 2966 4090 384 306 238 O HETATM 2141 O HOH A 506 78.165 19.780 11.282 1.00 33.10 O ANISOU 2141 O HOH A 506 3447 4697 4122 1159 -951 -119 O HETATM 2142 O HOH A 507 75.783 36.802 15.266 1.00 31.50 O ANISOU 2142 O HOH A 507 3332 4107 4235 383 486 236 O HETATM 2143 O HOH A 508 47.230 14.492 14.260 1.00 40.63 O ANISOU 2143 O HOH A 508 5146 5146 5146 0 0 0 O HETATM 2144 O HOH A 509 30.814 30.037 22.097 1.00 37.92 O ANISOU 2144 O HOH A 509 4803 4803 4803 0 0 0 O HETATM 2145 O HOH A 510 49.725 46.483 2.110 1.00 35.28 O ANISOU 2145 O HOH A 510 4468 4468 4468 0 0 0 O HETATM 2146 O HOH A 511 34.331 21.234 6.702 1.00 37.55 O ANISOU 2146 O HOH A 511 4756 4756 4756 0 0 0 O HETATM 2147 O HOH A 512 51.679 50.486 26.228 1.00 38.71 O ANISOU 2147 O HOH A 512 5182 6422 2739 -26 959 -46 O HETATM 2148 O HOH A 513 26.927 33.477 12.512 1.00 36.00 O ANISOU 2148 O HOH A 513 4559 4559 4559 0 0 0 O HETATM 2149 O HOH A 514 53.666 19.501 32.720 1.00 34.83 O ANISOU 2149 O HOH A 514 4426 5188 3293 -203 601 1117 O HETATM 2150 O HOH A 515 73.173 42.786 17.813 1.00 56.61 O ANISOU 2150 O HOH A 515 7170 7170 7170 0 0 0 O HETATM 2151 O HOH A 516 65.157 50.730 16.303 1.00 36.97 O ANISOU 2151 O HOH A 516 5956 3690 4053 292 1106 645 O HETATM 2152 O HOH A 517 57.967 52.343 9.638 1.00 44.75 O ANISOU 2152 O HOH A 517 5668 5668 5668 0 0 0 O HETATM 2153 O HOH A 518 59.200 17.245 0.854 1.00 44.92 O ANISOU 2153 O HOH A 518 5689 5689 5689 0 0 0 O HETATM 2154 O HOH A 519 48.171 27.531 33.270 1.00 43.05 O ANISOU 2154 O HOH A 519 5452 5452 5452 0 0 0 O HETATM 2155 O HOH A 520 29.553 32.707 19.184 1.00 41.84 O ANISOU 2155 O HOH A 520 5299 5299 5299 0 0 0 O HETATM 2156 O HOH A 521 43.859 37.792 26.296 1.00 34.60 O ANISOU 2156 O HOH A 521 4054 4704 4063 -179 2148 -1023 O HETATM 2157 O HOH A 522 39.535 30.577 0.870 1.00 41.94 O ANISOU 2157 O HOH A 522 5312 5312 5312 0 0 0 O HETATM 2158 O HOH A 523 53.960 55.206 25.238 1.00 42.79 O ANISOU 2158 O HOH A 523 5419 5419 5419 0 0 0 O HETATM 2159 O HOH A 524 70.153 41.094 10.753 1.00 35.54 O ANISOU 2159 O HOH A 524 4501 4501 4501 0 0 0 O HETATM 2160 O HOH A 525 55.132 21.937 33.025 1.00 36.19 O ANISOU 2160 O HOH A 525 4584 4584 4584 0 0 0 O HETATM 2161 O HOH A 526 79.988 26.019 25.527 1.00 44.97 O ANISOU 2161 O HOH A 526 5696 5696 5696 0 0 0 O HETATM 2162 O HOH A 527 60.999 14.411 1.836 1.00 36.11 O ANISOU 2162 O HOH A 527 4573 4573 4573 0 0 0 O HETATM 2163 O HOH A 528 75.836 29.267 4.815 1.00 46.39 O ANISOU 2163 O HOH A 528 5875 5875 5875 0 0 0 O HETATM 2164 O HOH A 529 59.588 46.033 24.215 1.00 32.19 O ANISOU 2164 O HOH A 529 3660 4492 3776 1240 -1372 -1216 O HETATM 2165 O HOH A 530 37.100 26.121 23.420 1.00 47.25 O ANISOU 2165 O HOH A 530 5984 5984 5984 0 0 0 O HETATM 2166 O HOH A 531 56.592 23.155 -2.513 1.00 43.34 O ANISOU 2166 O HOH A 531 5489 5489 5489 0 0 0 O HETATM 2167 O HOH A 532 44.748 24.753 26.202 1.00 43.87 O ANISOU 2167 O HOH A 532 5556 5556 5556 0 0 0 O HETATM 2168 O HOH A 533 54.806 17.531 31.313 1.00 48.03 O ANISOU 2168 O HOH A 533 6083 6083 6083 0 0 0 O HETATM 2169 O HOH A 534 44.775 35.260 31.055 0.50 54.47 O ANISOU 2169 O HOH A 534 6899 6899 6899 0 0 0 O HETATM 2170 O HOH A 535 56.047 41.018 6.345 1.00 38.37 O ANISOU 2170 O HOH A 535 2696 7443 4078 -839 -470 804 O HETATM 2171 O HOH A 536 49.198 20.391 32.201 1.00 43.27 O ANISOU 2171 O HOH A 536 5480 5480 5480 0 0 0 O HETATM 2172 O HOH A 537 71.144 37.161 -1.730 1.00 35.16 O ANISOU 2172 O HOH A 537 4453 4453 4453 0 0 0 O HETATM 2173 O HOH A 538 40.831 31.527 9.256 1.00 41.75 O ANISOU 2173 O HOH A 538 5288 5288 5288 0 0 0 O HETATM 2174 O HOH A 539 77.988 24.910 25.532 1.00 53.45 O ANISOU 2174 O HOH A 539 6770 6770 6770 0 0 0 O HETATM 2175 O HOH A 540 77.335 29.345 30.013 1.00 37.56 O ANISOU 2175 O HOH A 540 4757 4757 4757 0 0 0 O HETATM 2176 O HOH A 541 55.457 9.686 23.682 1.00 41.81 O ANISOU 2176 O HOH A 541 5295 5295 5295 0 0 0 O HETATM 2177 O HOH A 542 48.599 17.607 29.091 1.00 45.28 O ANISOU 2177 O HOH A 542 5735 5735 5735 0 0 0 O HETATM 2178 O HOH A 543 71.660 42.861 14.587 1.00 42.37 O ANISOU 2178 O HOH A 543 5366 5366 5366 0 0 0 O HETATM 2179 O HOH A 544 44.775 23.336 0.000 0.50 28.18 O ANISOU 2179 O HOH A 544 1389 3327 5728 0 -137 0 O HETATM 2180 O HOH A 545 64.424 41.588 27.582 1.00 46.47 O ANISOU 2180 O HOH A 545 5885 5885 5885 0 0 0 O HETATM 2181 O HOH A 546 70.924 23.700 11.367 1.00 49.24 O ANISOU 2181 O HOH A 546 6236 6236 6236 0 0 0 O HETATM 2182 O HOH A 547 22.596 37.649 3.564 1.00 34.92 O ANISOU 2182 O HOH A 547 4423 4423 4423 0 0 0 O HETATM 2183 O HOH A 548 73.385 18.003 7.918 1.00 37.54 O ANISOU 2183 O HOH A 548 4754 4754 4754 0 0 0 O HETATM 2184 O HOH A 549 77.278 34.277 15.204 1.00 39.84 O ANISOU 2184 O HOH A 549 5046 5046 5046 0 0 0 O HETATM 2185 O HOH A 550 65.831 44.930 26.125 1.00 36.74 O ANISOU 2185 O HOH A 550 4653 4653 4653 0 0 0 O HETATM 2186 O HOH A 551 76.709 26.315 6.004 1.00 40.97 O ANISOU 2186 O HOH A 551 5189 5189 5189 0 0 0 O HETATM 2187 O HOH A 552 31.479 31.870 23.510 1.00 38.44 O ANISOU 2187 O HOH A 552 4868 4868 4868 0 0 0 O HETATM 2188 O HOH A 553 47.181 11.095 10.534 1.00 40.90 O ANISOU 2188 O HOH A 553 5180 5180 5180 0 0 0 O HETATM 2189 O HOH A 554 55.807 37.763 30.321 1.00 38.66 O ANISOU 2189 O HOH A 554 4896 4896 4896 0 0 0 O HETATM 2190 O HOH A 555 25.137 34.047 10.203 1.00 45.00 O ANISOU 2190 O HOH A 555 5699 5699 5699 0 0 0 O HETATM 2191 O HOH A 556 66.646 6.869 25.376 1.00 36.60 O ANISOU 2191 O HOH A 556 4635 4635 4635 0 0 0 O HETATM 2192 O HOH A 557 47.573 19.475 23.808 1.00 43.30 O ANISOU 2192 O HOH A 557 5484 5484 5484 0 0 0 O HETATM 2193 O HOH A 558 55.159 26.421 35.531 1.00 53.90 O ANISOU 2193 O HOH A 558 6827 6827 6827 0 0 0 O HETATM 2194 O HOH A 559 83.458 30.557 14.651 1.00 49.80 O ANISOU 2194 O HOH A 559 6307 6307 6307 0 0 0 O CONECT 56 1874 CONECT 73 1875 CONECT 74 1874 1875 CONECT 85 1875 CONECT 107 1875 CONECT 142 1874 CONECT 143 1875 CONECT 187 1874 CONECT 1874 56 74 142 187 CONECT 1874 2047 2048 CONECT 1875 73 74 85 107 CONECT 1875 143 2045 2046 CONECT 2045 1875 CONECT 2046 1875 CONECT 2047 1874 CONECT 2048 1874 MASTER 371 0 2 4 15 0 4 6 2193 1 16 19 END