HEADER HYDROLASE 14-DEC-16 5MOO TITLE JOINT X-RAY/NEUTRON STRUCTURE OF CATIONIC TRYPSIN IN COMPLEX WITH TITLE 2 ANILINE COMPND MOL_ID: 1; COMPND 2 MOLECULE: CATIONIC TRYPSIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: BETA-TRYPSIN; COMPND 5 EC: 3.4.21.4 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: BOVINE; SOURCE 4 ORGANISM_TAXID: 9913 KEYWDS HYDROGEN BONDING, PROTONATION, PROTEIN-LIGAND INTERACTION, HYDROLASE EXPDTA X-RAY DIFFRACTION; NEUTRON DIFFRACTION AUTHOR J.SCHIEBEL,T.E.SCHRADER,A.OSTERMANN,A.HEINE,G.KLEBE REVDAT 3 14-NOV-18 5MOO 1 REMARK REVDAT 2 23-AUG-17 5MOO 1 ATOM REVDAT 1 24-MAY-17 5MOO 0 JRNL AUTH J.SCHIEBEL,R.GASPARI,A.SANDNER,K.NGO,H.D.GERBER,A.CAVALLI, JRNL AUTH 2 A.OSTERMANN,A.HEINE,G.KLEBE JRNL TITL CHARGES SHIFT PROTONATION: NEUTRON DIFFRACTION REVEALS THAT JRNL TITL 2 ANILINE AND 2-AMINOPYRIDINE BECOME PROTONATED UPON BINDING JRNL TITL 3 TO TRYPSIN. JRNL REF ANGEW. CHEM. INT. ED. ENGL. V. 56 4887 2017 JRNL REFN ESSN 1521-3773 JRNL PMID 28371253 JRNL DOI 10.1002/ANIE.201701038 REMARK 2 REMARK 2 RESOLUTION. 1.44 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (DEV_2429) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 X-RAY DATA. REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.44 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.18 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3 REMARK 3 NUMBER OF REFLECTIONS : 38776 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.136 REMARK 3 R VALUE (WORKING SET) : 0.134 REMARK 3 FREE R VALUE : 0.160 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050 REMARK 3 FREE R VALUE TEST SET COUNT : 1959 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 44.2047 - 3.4736 0.99 2867 137 0.1142 0.1105 REMARK 3 2 3.4736 - 2.7572 1.00 2785 123 0.1260 0.1475 REMARK 3 3 2.7572 - 2.4087 1.00 2748 140 0.1135 0.1378 REMARK 3 4 2.4087 - 2.1885 1.00 2716 133 0.0909 0.1214 REMARK 3 5 2.1885 - 2.0317 1.00 2694 146 0.0856 0.1054 REMARK 3 6 2.0317 - 1.9119 1.00 2675 155 0.0809 0.1162 REMARK 3 7 1.9119 - 1.8161 1.00 2678 147 0.0804 0.1144 REMARK 3 8 1.8161 - 1.7371 1.00 2687 154 0.0772 0.1196 REMARK 3 9 1.7371 - 1.6702 1.00 2659 125 0.0737 0.1000 REMARK 3 10 1.6702 - 1.6126 1.00 2661 140 0.0838 0.1455 REMARK 3 11 1.6126 - 1.5621 0.99 2650 158 0.1086 0.1622 REMARK 3 12 1.5621 - 1.5175 0.98 2598 135 0.2152 0.2612 REMARK 3 13 1.5175 - 1.4775 0.98 2614 152 0.2930 0.2871 REMARK 3 14 1.4775 - 1.4415 0.68 1785 114 0.6638 0.6601 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.110 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.006 3758 REMARK 3 ANGLE : 1.085 6417 REMARK 3 CHIRALITY : 0.093 270 REMARK 3 PLANARITY : 0.006 790 REMARK 3 DIHEDRAL : 12.911 976 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 3 NEUTRON DATA. REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.43 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.09 REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 93.8 REMARK 3 NUMBER OF REFLECTIONS : 38317 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.171 REMARK 3 R VALUE (WORKING SET) : 0.170 REMARK 3 FREE R VALUE : 0.185 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990 REMARK 3 FREE R VALUE TEST SET COUNT : 1911 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 22.0946 - 3.4405 0.95 2833 131 0.1462 0.1456 REMARK 3 2 3.4405 - 2.7324 0.95 2719 123 0.1506 0.1684 REMARK 3 3 2.7324 - 2.3875 0.96 2682 133 0.1347 0.1460 REMARK 3 4 2.3875 - 2.1694 0.92 2562 127 0.1378 0.1570 REMARK 3 5 2.1694 - 2.0140 0.93 2546 136 0.1432 0.1525 REMARK 3 6 2.0140 - 1.8954 0.93 2553 151 0.1502 0.1687 REMARK 3 7 1.8954 - 1.8005 0.94 2594 136 0.1693 0.1756 REMARK 3 8 1.8005 - 1.7221 0.94 2580 132 0.1794 0.1874 REMARK 3 9 1.7221 - 1.6559 0.95 2622 136 0.1837 0.2125 REMARK 3 10 1.6559 - 1.5987 0.96 2635 138 0.1969 0.2123 REMARK 3 11 1.5987 - 1.5488 0.96 2628 145 0.2224 0.2350 REMARK 3 12 1.5488 - 1.5045 0.97 2617 150 0.2601 0.2667 REMARK 3 13 1.5045 - 1.4649 0.95 2569 150 0.2488 0.2986 REMARK 3 14 1.4649 - 1.4292 0.84 2266 123 0.2666 0.2866 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.110 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.006 3758 REMARK 3 ANGLE : 1.085 6417 REMARK 3 CHIRALITY : 0.093 270 REMARK 3 PLANARITY : 0.006 790 REMARK 3 DIHEDRAL : 12.911 976 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 5MOO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-DEC-16. REMARK 100 THE DEPOSITION ID IS D_1200002723. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-FEB-16 REMARK 200 TEMPERATURE (KELVIN) : 295 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : SEALED TUBE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : OTHER REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.54179 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38793 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.441 REMARK 200 RESOLUTION RANGE LOW (A) : 44.184 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3 REMARK 200 DATA REDUNDANCY : 7.361 REMARK 200 R MERGE (I) : 0.04500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 27.0100 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.44 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53 REMARK 200 COMPLETENESS FOR SHELL (%) : 84.6 REMARK 200 DATA REDUNDANCY IN SHELL : 6.03 REMARK 200 R MERGE FOR SHELL (I) : 0.22900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 9.860 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 4I8H REMARK 200 REMARK 200 REMARK: NULL REMARK 230 REMARK 230 EXPERIMENTAL DETAILS REMARK 230 EXPERIMENT TYPE : NEUTRON DIFFRACTION REMARK 230 DATE OF DATA COLLECTION : 22-JUL-16 REMARK 230 TEMPERATURE (KELVIN) : 295.0 REMARK 230 PH : 7.50 REMARK 230 NUMBER OF CRYSTALS USED : NULL REMARK 230 REMARK 230 NEUTRON SOURCE : NUCLEAR REACTOR REMARK 230 BEAMLINE : BIODIFF REMARK 230 WAVELENGTH OR RANGE (A) : 2.667 REMARK 230 MONOCHROMATOR : NULL REMARK 230 OPTICS : NULL REMARK 230 REMARK 230 DETECTOR TYPE : IMAGE PLATE REMARK 230 DETECTOR MANUFACTURER : MAATEL BIODIFF REMARK 230 INTENSITY-INTEGRATION SOFTWARE : XDS, HKL-2000 REMARK 230 DATA SCALING SOFTWARE : XDS, HKL-2000 REMARK 230 REMARK 230 NUMBER OF UNIQUE REFLECTIONS : 38342 REMARK 230 RESOLUTION RANGE HIGH (A) : 1.430 REMARK 230 RESOLUTION RANGE LOW (A) : 50.000 REMARK 230 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 230 REMARK 230 OVERALL. REMARK 230 COMPLETENESS FOR RANGE (%) : 93.8 REMARK 230 DATA REDUNDANCY : 2.500 REMARK 230 R MERGE (I) : 0.09800 REMARK 230 R SYM (I) : NULL REMARK 230 FOR THE DATA SET : 7.2530 REMARK 230 REMARK 230 IN THE HIGHEST RESOLUTION SHELL. REMARK 230 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.43 REMARK 230 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45 REMARK 230 COMPLETENESS FOR SHELL (%) : 82.1 REMARK 230 DATA REDUNDANCY IN SHELL : 1.60 REMARK 230 R MERGE FOR SHELL (I) : 0.38700 REMARK 230 R SYM FOR SHELL (I) : NULL REMARK 230 FOR SHELL : 1.858 REMARK 230 REMARK 230 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 230 SOFTWARE USED : PHASER REMARK 230 STARTING MODEL: 4I8H REMARK 230 REMARK 230 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.98 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 0.1 M HEPES PH REMARK 280 7.5, 16.5-17.0% (W/V) PEG 8000, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z 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 27.43750 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.72900 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.23600 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 33.72900 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.43750 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.23600 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 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 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: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 17960 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 8900 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 19.0 KCAL/MOL 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 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 109 CD CE NZ REMARK 470 LYS A 145 CE NZ REMARK 470 SER A 147 OG REMARK 470 LYS A 188A NZ REMARK 470 GLN A 192 CG CD OE1 NE2 REMARK 470 LYS A 222 CD CE NZ REMARK 470 LYS A 239 CE NZ REMARK 470 GLN A 240 CD OE1 NE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OE1 GLU A 77 D1 DOD A 401 1.60 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 OD1 ASP A 153 D2 DOD A 541 4445 1.57 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 ASP A 71 -76.38 -121.77 REMARK 500 REMARK 500 REMARK: NULL 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 CA A 301 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 70 OE1 REMARK 620 2 ASN A 72 O 90.2 REMARK 620 3 VAL A 75 O 164.0 81.6 REMARK 620 4 GLU A 80 OE2 102.6 160.6 89.1 REMARK 620 5 DOD A 401 O 87.4 87.9 105.9 78.3 REMARK 620 6 DOD A 443 O 80.2 103.0 88.2 93.6 163.4 REMARK 620 N 1 2 3 4 5 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue WOT A 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 303 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5MNA RELATED DB: PDB REMARK 900 REFINEMENT AGAINST ONLY THE X-RAY DIFFRACTION DATA RESULTED IN THIS REMARK 900 STRUCTURE REMARK 900 RELATED ID: 5MNY RELATED DB: PDB REMARK 900 REFINEMENT AGAINST ONLY THE NEUTRON DIFFRACTION DATA RESULTED IN REMARK 900 THIS STRUCTURE DBREF 5MOO A 16 245 UNP P00760 TRY1_BOVIN 24 246 SEQRES 1 A 223 ILE VAL GLY GLY TYR THR CYS GLY ALA ASN THR VAL PRO SEQRES 2 A 223 TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY SEQRES 3 A 223 GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA SEQRES 4 A 223 HIS CYS TYR LYS SER GLY ILE GLN VAL ARG LEU GLY GLU SEQRES 5 A 223 ASP ASN ILE ASN VAL VAL GLU GLY ASN GLU GLN PHE ILE SEQRES 6 A 223 SER ALA SER LYS SER ILE VAL HIS PRO SER TYR ASN SER SEQRES 7 A 223 ASN THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU LYS SEQRES 8 A 223 SER ALA ALA SER LEU ASN SER ARG VAL ALA SER ILE SER SEQRES 9 A 223 LEU PRO THR SER CYS ALA SER ALA GLY THR GLN CYS LEU SEQRES 10 A 223 ILE SER GLY TRP GLY ASN THR LYS SER SER GLY THR SER SEQRES 11 A 223 TYR PRO ASP VAL LEU LYS CYS LEU LYS ALA PRO ILE LEU SEQRES 12 A 223 SER ASP SER SER CYS LYS SER ALA TYR PRO GLY GLN ILE SEQRES 13 A 223 THR SER ASN MET PHE CYS ALA GLY TYR LEU GLU GLY GLY SEQRES 14 A 223 LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL SEQRES 15 A 223 CYS SER GLY LYS LEU GLN GLY ILE VAL SER TRP GLY SER SEQRES 16 A 223 GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS SEQRES 17 A 223 VAL CYS ASN TYR VAL SER TRP ILE LYS GLN THR ILE ALA SEQRES 18 A 223 SER ASN HET CA A 301 1 HET WOT A 302 11 HET SO4 A 303 5 HETNAM CA CALCIUM ION HETNAM WOT PHENYLAZANIUM HETNAM SO4 SULFATE ION FORMUL 2 CA CA 2+ FORMUL 3 WOT C6 H8 N 1+ FORMUL 4 SO4 O4 S 2- FORMUL 5 DOD *149(D2 O) HELIX 1 AA1 ALA A 55 TYR A 59 5 5 HELIX 2 AA2 SER A 164 TYR A 172 1 9 HELIX 3 AA3 TYR A 234 ASN A 245 1 12 SHEET 1 AA1 7 TYR A 20 THR A 21 0 SHEET 2 AA1 7 LYS A 156 PRO A 161 -1 O CYS A 157 N TYR A 20 SHEET 3 AA1 7 GLN A 135 GLY A 140 -1 N ILE A 138 O LEU A 158 SHEET 4 AA1 7 PRO A 198 CYS A 201 -1 O VAL A 200 N LEU A 137 SHEET 5 AA1 7 LYS A 204 TRP A 215 -1 O LYS A 204 N CYS A 201 SHEET 6 AA1 7 GLY A 226 LYS A 230 -1 O VAL A 227 N TRP A 215 SHEET 7 AA1 7 MET A 180 ALA A 183 -1 N PHE A 181 O TYR A 228 SHEET 1 AA2 7 GLN A 30 ASN A 34 0 SHEET 2 AA2 7 HIS A 40 ASN A 48 -1 O CYS A 42 N LEU A 33 SHEET 3 AA2 7 TRP A 51 SER A 54 -1 O VAL A 53 N SER A 45 SHEET 4 AA2 7 MET A 104 LEU A 108 -1 O ILE A 106 N VAL A 52 SHEET 5 AA2 7 GLN A 81 VAL A 90 -1 N ILE A 89 O LEU A 105 SHEET 6 AA2 7 GLN A 64 LEU A 67 -1 N LEU A 67 O GLN A 81 SHEET 7 AA2 7 GLN A 30 ASN A 34 -1 N SER A 32 O ARG A 66 SSBOND 1 CYS A 22 CYS A 157 1555 1555 2.03 SSBOND 2 CYS A 42 CYS A 58 1555 1555 2.04 SSBOND 3 CYS A 128 CYS A 232 1555 1555 2.01 SSBOND 4 CYS A 136 CYS A 201 1555 1555 2.01 SSBOND 5 CYS A 168 CYS A 182 1555 1555 2.02 SSBOND 6 CYS A 191 CYS A 220 1555 1555 2.02 LINK OE1 GLU A 70 CA CA A 301 1555 1555 2.23 LINK O ASN A 72 CA CA A 301 1555 1555 2.32 LINK O VAL A 75 CA CA A 301 1555 1555 2.27 LINK OE2 GLU A 80 CA CA A 301 1555 1555 2.33 LINK CA CA A 301 O DOD A 401 1555 1555 2.37 LINK CA CA A 301 O DOD A 443 1555 1555 2.31 SITE 1 AC1 6 GLU A 70 ASN A 72 VAL A 75 GLU A 80 SITE 2 AC1 6 DOD A 401 DOD A 443 SITE 1 AC2 8 ASP A 189 SER A 190 SER A 195 VAL A 213 SITE 2 AC2 8 TRP A 215 GLY A 219 DOD A 419 DOD A 486 SITE 1 AC3 5 HIS A 57 GLN A 192 GLY A 193 SER A 195 SITE 2 AC3 5 DOD A 480 CRYST1 54.875 58.472 67.458 90.00 90.00 90.00 P 21 21 21 4 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 0.018223 0.000000 0.000000 0.00000 SCALE2 0.000000 0.017102 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014824 0.00000