HEADER OXIDOREDUCTASE 14-FEB-14 4OZ7 TITLE METHANOBACTIN PRODUCTION BY METHANOTROPHIC BACTERIA AND THEIR TITLE 2 STRUCTURAL DIVERSITY FROM METHYLOSINUS STRAINS: INSIGHTS INTO COPPER TITLE 3 RELEASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: METHANOBACTIN; COMPND 3 CHAIN: A, B SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: METHYLOSINUS SPORIUM; SOURCE 3 ORGANISM_TAXID: 428; SOURCE 4 STRAIN: NR3K KEYWDS COPPER UPTAKE, PARTICULATE METHANE MONOOXYGENASE, OXIDOREDUCTASE EXPDTA X-RAY DIFFRACTION AUTHOR A.EL GHAZOUANI,A.BASLE,C.DENNISON REVDAT 1 20-MAY-15 4OZ7 0 JRNL AUTH A.EL GHAZOUANI,A.BASLE,C.DENNISON JRNL TITL METHANOBACTIN PRODUCTION BY METHANOTROPHIC BACTERIA AND JRNL TITL 2 THEIR STRUCTURAL DIVERSITY FROM METHYLOSINUS STRAINS: JRNL TITL 3 INSIGHTS INTO COPPER RELEASE JRNL REF TO BE PUBLISHED REMARK 2 REMARK 2 RESOLUTION. 1.65 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0049 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.16 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6 REMARK 3 NUMBER OF REFLECTIONS : 3512 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.222 REMARK 3 R VALUE (WORKING SET) : 0.221 REMARK 3 FREE R VALUE : 0.251 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.500 REMARK 3 FREE R VALUE TEST SET COUNT : 164 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.65 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69 REMARK 3 REFLECTION IN BIN (WORKING SET) : 233 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.08 REMARK 3 BIN R VALUE (WORKING SET) : 0.2430 REMARK 3 BIN FREE R VALUE SET COUNT : 12 REMARK 3 BIN FREE R VALUE : 0.1300 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 154 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 2 REMARK 3 SOLVENT ATOMS : 25 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 17.10 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.44 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.95000 REMARK 3 B22 (A**2) : 2.45000 REMARK 3 B33 (A**2) : -1.50000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.095 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.096 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.069 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.187 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 160 ; 0.012 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 206 ; 2.859 ; 2.363 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 12 ; 4.046 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 2 ;34.537 ;30.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 10 ; 9.969 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 22 ; 0.080 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 108 ; 0.004 ; 0.022 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 71 ; 0.795 ; 2.352 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 72 ; 1.281 ; 3.574 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 88 ; 0.842 ; 2.285 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 236 ; 3.993 ;22.208 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN REMARK 3 THE INPUT REMARK 4 REMARK 4 4OZ7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAR-14. REMARK 100 THE DEPOSITION ID IS D_1000200303. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 21-NOV-09 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7 REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID29 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL REMARK 200 WAVELENGTH OR RANGE (A) : 0.98 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 3677 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650 REMARK 200 RESOLUTION RANGE LOW (A) : 28.160 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 200 DATA REDUNDANCY : 6.000 REMARK 200 R MERGE (I) : 0.08700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74 REMARK 200 COMPLETENESS FOR SHELL (%) : 94.1 REMARK 200 DATA REDUNDANCY IN SHELL : 4.40 REMARK 200 R MERGE FOR SHELL (I) : 0.34200 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.58 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.1 M SODIUM MALONATE, 100 MM HEPES PH REMARK 280 7.0, 0.5% V/V JEFFAMINE ED-2001, 0.5% W/V OCTYL-BETA-D-GLUCOSIDE, REMARK 280 CRYSTAL WERE CRYOPROTECTED WITH THE ABOVE CONDITION REMARK 280 SUPPLEMENTED WITH 20% GLYCEROL., VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 293K 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 18.36000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 19.71000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 20.12000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 18.36000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 19.71000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 20.12000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 18.36000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 19.71000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 20.12000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 18.36000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 19.71000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 20.12000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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 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 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B 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 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 B 209 LIES ON A SPECIAL POSITION. 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 22W A 6 CA - C - N ANGL. DEV. = 21.9 DEGREES REMARK 500 22W A 6 O - C - N ANGL. DEV. = -15.7 DEGREES REMARK 500 22W B 6 CA - C - N ANGL. DEV. = 18.1 DEGREES REMARK 500 22W B 6 O - C - N ANGL. DEV. = -19.5 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 22W A 6 178.46 REMARK 500 22W B 6 -173.18 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 CU1 A 101 CU REMARK 620 N RES CSSEQI ATOM REMARK 620 1 22W A 6 S REMARK 620 2 22W A 6 NB 86.4 REMARK 620 3 22Q B 1 N 104.9 45.9 REMARK 620 4 22Q B 1 S 108.9 48.1 4.1 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CU1 B 101 CU REMARK 620 N RES CSSEQI ATOM REMARK 620 1 22W B 6 S REMARK 620 2 22W B 6 NB 87.3 REMARK 620 3 22Q A 1 N 100.6 52.5 REMARK 620 4 22Q A 1 S 104.8 53.8 4.2 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CU1 A 101 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CU1 B 101 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues 22W A 6 through REMARK 800 GLY A 7 bound to SER A 5 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues 22W B 6 through REMARK 800 GLY B 7 bound to SER B 5 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 22Q B 1 and ALA B 2 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4OZ8 RELATED DB: PDB DBREF 4OZ7 A 1 10 PDB 4OZ7 4OZ7 1 10 DBREF 4OZ7 B 1 10 PDB 4OZ7 4OZ7 1 10 SEQRES 1 A 10 22Q ALA SER CYS SER 22W GLY PRO ASN CYS SEQRES 1 B 10 22Q ALA SER CYS SER 22W GLY PRO ASN CYS HET 22Q A 1 14 HET 22W A 6 14 HET 22Q B 1 14 HET 22W B 6 14 HET CU1 A 101 1 HET CU1 B 101 1 HETNAM 22Q (3Z)-5-(2-METHYLPROPYL)-3-(SULFANYLMETHYLIDENE) HETNAM 2 22Q PYRAZINE-2,6(1H,3H)-DIONE HETNAM 22W 2-[(1S,2S)-1-AMINO-2-METHYLBUTYL]-4- HETNAM 2 22W (THIOXOMETHYLIDENE)-1,3-OXAZOL-5(4H)-ONE HETNAM CU1 COPPER (I) ION FORMUL 1 22Q 2(C9 H12 N2 O2 S) FORMUL 1 22W 2(C9 H12 N2 O2 S) FORMUL 3 CU1 2(CU 1+) FORMUL 5 HOH *25(H2 O) SSBOND 1 CYS A 4 CYS A 10 1555 1555 2.03 SSBOND 2 CYS B 4 CYS B 10 1555 1555 2.03 LINK C 22Q A 1 N ALA A 2 1555 1555 1.34 LINK C SER A 5 N 22W A 6 1555 1555 1.35 LINK C 22W A 6 N GLY A 7 1555 1555 1.34 LINK S 22W A 6 CU CU1 A 101 1555 1555 2.35 LINK NB 22W A 6 CU CU1 A 101 1555 1555 2.14 LINK C 22Q B 1 N ALA B 2 1555 1555 1.34 LINK C SER B 5 N 22W B 6 1555 1555 1.35 LINK C 22W B 6 N GLY B 7 1555 1555 1.34 LINK S 22W B 6 CU CU1 B 101 1555 1555 2.23 LINK NB 22W B 6 CU CU1 B 101 1555 1555 2.17 LINK N 22Q A 1 CU CU1 B 101 1555 6345 2.05 LINK S 22Q A 1 CU CU1 B 101 1555 6345 2.26 LINK N 22Q B 1 CU CU1 A 101 1555 6344 2.07 LINK S 22Q B 1 CU CU1 A 101 1555 6344 2.22 SITE 1 AC1 2 22W A 6 22Q B 1 SITE 1 AC2 2 22Q A 1 22W B 6 SITE 1 AC3 10 CYS A 4 SER A 5 PRO A 8 ASN A 9 SITE 2 AC3 10 CYS A 10 CU1 A 101 HOH A 203 22Q B 1 SITE 3 AC3 10 PRO B 8 HOH B 202 SITE 1 AC4 11 22Q A 1 SER A 5 PRO A 8 HOH A 201 SITE 2 AC4 11 CYS B 4 SER B 5 PRO B 8 ASN B 9 SITE 3 AC4 11 CYS B 10 CU1 B 101 HOH B 205 SITE 1 AC5 8 SER A 3 CYS A 4 SER A 5 22W A 6 SITE 2 AC5 8 CU1 A 101 SER B 3 HOH B 203 HOH B 210 CRYST1 36.720 39.420 40.240 90.00 90.00 90.00 I 2 2 2 16 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 0.027233 0.000000 0.000000 0.00000 SCALE2 0.000000 0.025368 0.000000 0.00000 SCALE3 0.000000 0.000000 0.024851 0.00000 HETATM 1 C 22Q A 1 -23.828 -13.217 15.763 1.00 22.06 C HETATM 2 N 22Q A 1 -23.121 -12.941 18.023 1.00 22.71 N HETATM 3 S 22Q A 1 -22.855 -11.890 15.256 1.00 20.75 S HETATM 4 C1 22Q A 1 -23.218 -13.160 19.348 1.00 23.29 C HETATM 5 N1 22Q A 1 -25.145 -14.553 18.944 1.00 23.83 N HETATM 6 C2 22Q A 1 -25.006 -14.299 17.577 1.00 23.25 C HETATM 7 O2 22Q A 1 -25.808 -14.814 16.800 1.00 24.43 O HETATM 8 O3 22Q A 1 -24.374 -14.201 21.044 1.00 24.70 O HETATM 9 C4 22Q A 1 -22.286 -12.553 20.203 1.00 23.16 C HETATM 10 C5 22Q A 1 -24.244 -13.974 19.842 1.00 23.86 C HETATM 11 C6 22Q A 1 -21.258 -13.470 20.901 1.00 23.48 C HETATM 12 C7 22Q A 1 -20.428 -14.268 19.885 1.00 23.53 C HETATM 13 C8 22Q A 1 -20.313 -12.611 21.746 1.00 24.07 C HETATM 14 CA 22Q A 1 -23.974 -13.474 17.130 1.00 22.47 C ATOM 15 N ALA A 2 -24.495 -13.859 14.799 1.00 22.22 N ATOM 16 CA ALA A 2 -24.523 -13.670 13.326 1.00 23.23 C ATOM 17 C ALA A 2 -25.897 -14.032 12.797 1.00 23.77 C ATOM 18 O ALA A 2 -26.601 -14.864 13.377 1.00 24.36 O ATOM 19 CB ALA A 2 -23.448 -14.513 12.654 1.00 23.25 C ATOM 20 N SER A 3 -26.288 -13.373 11.715 1.00 24.14 N ATOM 21 CA SER A 3 -27.520 -13.711 11.028 1.00 24.71 C ATOM 22 C SER A 3 -27.239 -13.863 9.542 1.00 24.52 C ATOM 23 O SER A 3 -26.257 -13.319 9.019 1.00 24.11 O ATOM 24 CB SER A 3 -28.609 -12.666 11.287 1.00 25.64 C ATOM 25 OG SER A 3 -28.214 -11.390 10.823 1.00 27.86 O ATOM 26 N CYS A 4 -28.088 -14.632 8.873 1.00 23.46 N ATOM 27 CA CYS A 4 -27.974 -14.805 7.442 1.00 22.85 C ATOM 28 C CYS A 4 -28.521 -13.570 6.743 1.00 23.04 C ATOM 29 O CYS A 4 -29.712 -13.255 6.843 1.00 24.32 O ATOM 30 CB CYS A 4 -28.719 -16.056 6.991 1.00 22.80 C ATOM 31 SG CYS A 4 -28.497 -16.362 5.233 1.00 22.64 S ATOM 32 N SER A 5 -27.638 -12.868 6.045 1.00 21.84 N ATOM 33 CA SER A 5 -27.989 -11.616 5.400 1.00 21.75 C ATOM 34 C SER A 5 -28.175 -11.813 3.905 1.00 21.22 C ATOM 35 O SER A 5 -28.727 -10.948 3.229 1.00 21.81 O ATOM 36 CB SER A 5 -26.910 -10.563 5.666 1.00 21.62 C ATOM 37 OG SER A 5 -25.630 -11.070 5.326 1.00 21.78 O HETATM 38 C 22W A 6 -27.414 -18.020 1.929 1.00 19.81 C HETATM 39 N 22W A 6 -27.560 -12.822 3.261 1.00 19.91 N HETATM 40 O 22W A 6 -29.323 -14.902 1.057 1.00 19.69 O HETATM 41 S 22W A 6 -25.985 -18.276 2.540 1.00 20.77 S HETATM 42 CA 22W A 6 -27.672 -13.105 1.800 1.00 19.45 C HETATM 43 CB 22W A 6 -26.389 -12.723 1.054 1.00 19.25 C HETATM 44 NB 22W A 6 -27.314 -15.567 1.929 1.00 19.45 N HETATM 45 CE 22W A 6 -28.045 -14.574 1.604 1.00 19.52 C HETATM 46 CF 22W A 6 -27.926 -16.652 1.686 1.00 19.71 C HETATM 47 O26 22W A 6 -30.098 -17.090 0.760 1.00 20.03 O HETATM 48 C83 22W A 6 -29.222 -16.327 1.121 1.00 19.58 C HETATM 49 CD1 22W A 6 -24.686 -10.900 0.836 1.00 19.41 C HETATM 50 CG1 22W A 6 -26.101 -11.235 1.259 1.00 19.40 C HETATM 51 CG2 22W A 6 -26.559 -13.015 -0.436 1.00 18.83 C ATOM 52 N GLY A 7 -28.167 -19.068 1.568 1.00 19.72 N ATOM 53 CA GLY A 7 -27.934 -20.478 1.978 1.00 20.70 C ATOM 54 C GLY A 7 -29.227 -21.235 2.211 1.00 21.41 C ATOM 55 O GLY A 7 -30.300 -20.629 2.234 1.00 21.11 O ATOM 56 N PRO A 8 -29.129 -22.566 2.391 1.00 22.28 N ATOM 57 CA PRO A 8 -30.287 -23.465 2.483 1.00 23.15 C ATOM 58 C PRO A 8 -31.247 -23.144 3.635 1.00 23.99 C ATOM 59 O PRO A 8 -32.462 -23.289 3.483 1.00 24.15 O ATOM 60 CB PRO A 8 -29.649 -24.850 2.671 1.00 22.80 C ATOM 61 CG PRO A 8 -28.278 -24.580 3.172 1.00 22.68 C ATOM 62 CD PRO A 8 -27.861 -23.311 2.490 1.00 22.57 C ATOM 63 N ASN A 9 -30.714 -22.706 4.769 1.00 25.02 N ATOM 64 CA ASN A 9 -31.567 -22.347 5.897 1.00 26.89 C ATOM 65 C ASN A 9 -31.508 -20.868 6.302 1.00 26.78 C ATOM 66 O ASN A 9 -31.736 -20.526 7.463 1.00 27.54 O ATOM 67 CB ASN A 9 -31.331 -23.284 7.099 1.00 29.04 C ATOM 68 CG ASN A 9 -29.865 -23.616 7.319 1.00 30.79 C ATOM 69 OD1 ASN A 9 -29.516 -24.767 7.584 1.00 32.54 O ATOM 70 ND2 ASN A 9 -29.000 -22.612 7.221 1.00 32.47 N ATOM 71 N CYS A 10 -31.218 -20.000 5.333 1.00 25.69 N ATOM 72 CA CYS A 10 -31.192 -18.557 5.553 1.00 25.73 C ATOM 73 C CYS A 10 -32.515 -18.061 6.139 1.00 27.03 C ATOM 74 O CYS A 10 -32.557 -17.420 7.190 1.00 28.38 O ATOM 75 CB CYS A 10 -30.897 -17.825 4.242 1.00 24.35 C ATOM 76 SG CYS A 10 -30.352 -16.115 4.453 1.00 23.18 S ATOM 77 OXT CYS A 10 -33.582 -18.304 5.576 1.00 28.08 O TER 78 CYS A 10 HETATM 79 C 22Q B 1 -31.369 -5.522 -15.614 1.00 21.08 C HETATM 80 N 22Q B 1 -31.268 -4.746 -17.864 1.00 20.78 N HETATM 81 S 22Q B 1 -29.946 -4.628 -15.217 1.00 20.20 S HETATM 82 C1 22Q B 1 -31.616 -4.787 -19.166 1.00 21.33 C HETATM 83 N1 22Q B 1 -33.054 -6.676 -18.697 1.00 21.34 N HETATM 84 C2 22Q B 1 -32.673 -6.600 -17.356 1.00 21.37 C HETATM 85 O2 22Q B 1 -33.154 -7.408 -16.562 1.00 21.48 O HETATM 86 O3 22Q B 1 -32.870 -5.855 -20.790 1.00 22.05 O HETATM 87 C4 22Q B 1 -31.032 -3.850 -20.028 1.00 21.61 C HETATM 88 C5 22Q B 1 -32.522 -5.764 -19.614 1.00 21.44 C HETATM 89 C6 22Q B 1 -31.930 -2.740 -20.607 1.00 22.02 C HETATM 90 C7 22Q B 1 -32.617 -1.938 -19.496 1.00 22.26 C HETATM 91 C8 22Q B 1 -31.065 -1.804 -21.453 1.00 22.14 C HETATM 92 CA 22Q B 1 -31.757 -5.614 -16.955 1.00 20.81 C ATOM 93 N ALA B 2 -31.881 -6.203 -14.584 1.00 22.30 N ATOM 94 CA ALA B 2 -31.432 -6.397 -13.182 1.00 23.07 C ATOM 95 C ALA B 2 -31.769 -7.804 -12.741 1.00 23.34 C ATOM 96 O ALA B 2 -32.653 -8.444 -13.312 1.00 23.65 O ATOM 97 CB ALA B 2 -32.089 -5.376 -12.265 1.00 23.16 C ATOM 98 N SER B 3 -31.045 -8.287 -11.740 1.00 23.85 N ATOM 99 CA SER B 3 -31.328 -9.581 -11.141 1.00 24.19 C ATOM 100 C SER B 3 -31.374 -9.448 -9.627 1.00 24.19 C ATOM 101 O SER B 3 -30.788 -8.526 -9.055 1.00 23.76 O ATOM 102 CB SER B 3 -30.285 -10.618 -11.558 1.00 25.31 C ATOM 103 OG SER B 3 -29.010 -10.294 -11.034 1.00 27.12 O ATOM 104 N CYS B 4 -32.096 -10.365 -8.991 1.00 23.50 N ATOM 105 CA CYS B 4 -32.190 -10.399 -7.545 1.00 23.56 C ATOM 106 C CYS B 4 -30.922 -11.010 -6.996 1.00 23.53 C ATOM 107 O CYS B 4 -30.681 -12.208 -7.147 1.00 25.01 O ATOM 108 CB CYS B 4 -33.396 -11.215 -7.098 1.00 23.24 C ATOM 109 SG CYS B 4 -33.590 -11.201 -5.306 1.00 23.23 S ATOM 110 N SER B 5 -30.105 -10.178 -6.369 1.00 23.12 N ATOM 111 CA SER B 5 -28.821 -10.620 -5.864 1.00 23.13 C ATOM 112 C SER B 5 -28.929 -11.043 -4.402 1.00 22.51 C ATOM 113 O SER B 5 -28.042 -11.731 -3.888 1.00 23.47 O ATOM 114 CB SER B 5 -27.784 -9.510 -6.036 1.00 22.91 C ATOM 115 OG SER B 5 -28.240 -8.308 -5.446 1.00 23.14 O HETATM 116 C 22W B 6 -34.956 -10.355 -1.926 1.00 20.07 C HETATM 117 N 22W B 6 -29.898 -10.501 -3.638 1.00 20.52 N HETATM 118 O 22W B 6 -31.797 -12.329 -1.378 1.00 20.12 O HETATM 119 S 22W B 6 -35.202 -8.879 -2.416 1.00 20.49 S HETATM 120 CA 22W B 6 -30.060 -10.639 -2.158 1.00 19.80 C HETATM 121 CB 22W B 6 -29.585 -9.389 -1.408 1.00 19.96 C HETATM 122 NB 22W B 6 -32.518 -10.264 -2.043 1.00 20.07 N HETATM 123 CE 22W B 6 -31.506 -11.013 -1.845 1.00 19.75 C HETATM 124 CF 22W B 6 -33.586 -10.897 -1.790 1.00 20.19 C HETATM 125 O26 22W B 6 -33.968 -13.140 -1.028 1.00 20.52 O HETATM 126 C83 22W B 6 -33.227 -12.234 -1.354 1.00 19.97 C HETATM 127 CD1 22W B 6 -27.572 -7.893 -1.098 1.00 20.36 C HETATM 128 CG1 22W B 6 -28.089 -9.199 -1.661 1.00 20.16 C HETATM 129 CG2 22W B 6 -29.836 -9.561 0.092 1.00 19.75 C ATOM 130 N GLY B 7 -35.931 -11.224 -1.623 1.00 19.80 N ATOM 131 CA GLY B 7 -37.377 -10.987 -1.876 1.00 21.62 C ATOM 132 C GLY B 7 -38.149 -12.288 -1.950 1.00 21.96 C ATOM 133 O GLY B 7 -37.550 -13.364 -1.888 1.00 21.60 O ATOM 134 N PRO B 8 -39.488 -12.197 -2.081 1.00 23.07 N ATOM 135 CA PRO B 8 -40.365 -13.376 -2.140 1.00 23.79 C ATOM 136 C PRO B 8 -40.040 -14.341 -3.284 1.00 24.76 C ATOM 137 O PRO B 8 -40.103 -15.557 -3.095 1.00 24.84 O ATOM 138 CB PRO B 8 -41.767 -12.767 -2.318 1.00 23.55 C ATOM 139 CG PRO B 8 -41.533 -11.366 -2.791 1.00 22.96 C ATOM 140 CD PRO B 8 -40.267 -10.945 -2.111 1.00 22.68 C ATOM 141 N ASN B 9 -39.681 -13.807 -4.450 1.00 26.02 N ATOM 142 CA ASN B 9 -39.396 -14.647 -5.614 1.00 26.93 C ATOM 143 C ASN B 9 -37.981 -14.464 -6.179 1.00 26.64 C ATOM 144 O ASN B 9 -37.777 -14.466 -7.392 1.00 27.17 O ATOM 145 CB ASN B 9 -40.467 -14.454 -6.696 1.00 29.18 C ATOM 146 CG ASN B 9 -40.506 -13.043 -7.245 1.00 31.31 C ATOM 147 OD1 ASN B 9 -40.058 -12.092 -6.601 1.00 33.53 O ATOM 148 ND2 ASN B 9 -41.047 -12.901 -8.449 1.00 32.83 N ATOM 149 N CYS B 10 -37.012 -14.335 -5.280 1.00 26.05 N ATOM 150 CA CYS B 10 -35.624 -14.057 -5.646 1.00 26.04 C ATOM 151 C CYS B 10 -34.984 -15.180 -6.470 1.00 27.45 C ATOM 152 O CYS B 10 -34.344 -14.935 -7.493 1.00 28.81 O ATOM 153 CB CYS B 10 -34.799 -13.795 -4.392 1.00 24.50 C ATOM 154 SG CYS B 10 -33.171 -13.108 -4.736 1.00 23.78 S ATOM 155 OXT CYS B 10 -35.090 -16.358 -6.133 1.00 28.88 O TER 156 CYS B 10 HETATM 157 CU CU1 A 101 -25.467 -16.015 2.915 1.00 19.71 CU HETATM 158 CU CU1 B 101 -33.082 -8.321 -2.839 1.00 19.83 CU HETATM 159 O HOH A 201 -33.876 -23.493 1.363 1.00 27.22 O HETATM 160 O HOH A 202 -24.355 -9.052 4.082 1.00 31.95 O HETATM 161 O HOH A 203 -32.872 -20.050 1.274 1.00 39.95 O HETATM 162 O HOH A 204 -28.731 -8.180 3.710 1.00 34.11 O HETATM 163 O HOH A 205 -28.629 -14.958 17.158 1.00 37.59 O HETATM 164 O HOH A 206 -30.090 -16.179 10.398 1.00 29.33 O HETATM 165 O HOH A 207 -26.339 -7.127 2.313 1.00 33.57 O HETATM 166 O HOH A 208 -27.926 -21.106 5.289 1.00 37.04 O HETATM 167 O HOH A 209 -29.378 -15.095 20.164 1.00 41.85 O HETATM 168 O HOH A 210 -27.185 -16.815 20.149 1.00 33.26 O HETATM 169 O HOH B 201 -26.116 -7.088 -4.556 1.00 31.74 O HETATM 170 O HOH B 202 -40.601 -17.054 -0.966 1.00 32.62 O HETATM 171 O HOH B 203 -31.339 -5.688 -23.247 1.00 39.78 O HETATM 172 O HOH B 204 -34.653 -18.737 -7.735 1.00 36.12 O HETATM 173 O HOH B 205 -36.670 -16.107 -2.754 1.00 37.69 O HETATM 174 O HOH B 206 -25.138 -10.743 -3.280 1.00 41.79 O HETATM 175 O HOH B 207 -36.121 -7.734 -21.812 1.00 38.76 O HETATM 176 O HOH B 208 -38.030 -18.230 0.128 1.00101.29 O HETATM 177 O HOH B 209 -36.720 -19.710 -9.622 0.50 45.79 O HETATM 178 O HOH B 210 -34.780 -8.762 -19.554 1.00 29.33 O HETATM 179 O HOH B 211 -33.199 -11.046 -19.678 1.00 35.36 O HETATM 180 O HOH B 212 -38.685 -10.355 -4.928 1.00 33.79 O HETATM 181 O HOH B 213 -35.496 -9.068 -10.534 1.00 45.91 O HETATM 182 O HOH B 214 -33.730 -2.422 -15.478 1.00 39.96 O HETATM 183 O HOH B 215 -33.926 -12.108 -10.526 1.00 38.36 O CONECT 1 3 14 15 CONECT 2 4 14 CONECT 3 1 CONECT 4 2 9 10 CONECT 5 6 10 CONECT 6 5 7 14 CONECT 7 6 CONECT 8 10 CONECT 9 4 11 CONECT 10 4 5 8 CONECT 11 9 12 13 CONECT 12 11 CONECT 13 11 CONECT 14 1 2 6 CONECT 15 1 CONECT 31 76 CONECT 34 39 CONECT 38 41 46 52 CONECT 39 34 42 CONECT 40 45 48 CONECT 41 38 157 CONECT 42 39 43 45 CONECT 43 42 50 51 CONECT 44 45 46 157 CONECT 45 40 42 44 CONECT 46 38 44 48 CONECT 47 48 CONECT 48 40 46 47 CONECT 49 50 CONECT 50 43 49 CONECT 51 43 CONECT 52 38 CONECT 76 31 CONECT 79 81 92 93 CONECT 80 82 92 CONECT 81 79 CONECT 82 80 87 88 CONECT 83 84 88 CONECT 84 83 85 92 CONECT 85 84 CONECT 86 88 CONECT 87 82 89 CONECT 88 82 83 86 CONECT 89 87 90 91 CONECT 90 89 CONECT 91 89 CONECT 92 79 80 84 CONECT 93 79 CONECT 109 154 CONECT 112 117 CONECT 116 119 124 130 CONECT 117 112 120 CONECT 118 123 126 CONECT 119 116 158 CONECT 120 117 121 123 CONECT 121 120 128 129 CONECT 122 123 124 158 CONECT 123 118 120 122 CONECT 124 116 122 126 CONECT 125 126 CONECT 126 118 124 125 CONECT 127 128 CONECT 128 121 127 CONECT 129 121 CONECT 130 116 CONECT 154 109 CONECT 157 41 44 CONECT 158 119 122 MASTER 352 0 6 0 0 0 10 6 181 2 68 2 END