HEADER TRANSFERASE 20-SEP-12 4H7O
TITLE CRYSTAL STRUCTURE OF SERINE ACETYLTRANSFERASE FROM VIBRIO CHOLERAE O1
TITLE 2 BIOVAR EL TOR N16961
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE ACETYLTRANSFERASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 EC: 2.3.1.30;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;
SOURCE 3 ORGANISM_TAXID: 243277;
SOURCE 4 STRAIN: N16961;
SOURCE 5 GENE: SERINE ACETYLTRANSFERASE (EC:2.3.1.30), VC_2649;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21(C)
KEYWDS ACETYLTRANSFERASE, CYSTEINE SYNTHASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.F.TARIQUE,S.A.ABDUL REHMAN,S.GOURINATH
REVDAT 3 20-SEP-23 4H7O 1 REMARK SEQADV LINK
REVDAT 2 24-JAN-18 4H7O 1 AUTHOR
REVDAT 1 02-OCT-13 4H7O 0
JRNL AUTH K.F TARIQUE,S.A.ABDUL REHMAN,S.GOURINATH
JRNL TITL CRYSTAL STRUCTURE OF SERINE ACETYLTRANSFERASE FROM VIBRIO
JRNL TITL 2 CHOLERAE O1 BIOVAR EL TOR N16961.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.17 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.17
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 38412
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2027
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) : 2.17
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2474
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.76
REMARK 3 BIN R VALUE (WORKING SET) : 0.2280
REMARK 3 BIN FREE R VALUE SET COUNT : 143
REMARK 3 BIN FREE R VALUE : 0.2750
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5817
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 281
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.18
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.24000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.24000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.32000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.264
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.196
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.128
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.935
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5976 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8106 ; 1.373 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 771 ; 6.188 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 249 ;36.018 ;23.976
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 987 ;14.832 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;16.264 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 927 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4512 ; 0.006 ; 0.021
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
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 4H7O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-OCT-12.
REMARK 100 THE DEPOSITION ID IS D_1000075122.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAY-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.953
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38412
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.170
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 7.700
REMARK 200 R MERGE (I) : 0.10400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.17
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.35600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.060
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: PDB ENTRY 1T3D
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG4000, 20% GLYCEROL, 0.03M
REMARK 280 MGCL2,CACL2, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 273K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
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 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 72.02000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.52000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 72.02000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 37.52000
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 24660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -169.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 -1.23027
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -73.41969
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 LYS A 2
REMARK 465 GLN A 3
REMARK 465 CYS A 4
REMARK 465 ARG A 263
REMARK 465 SER A 264
REMARK 465 GLN A 265
REMARK 465 THR A 266
REMARK 465 PHE A 267
REMARK 465 ILE A 268
REMARK 465 GLY A 269
REMARK 465 GLY A 270
REMARK 465 ASP A 271
REMARK 465 GLY A 272
REMARK 465 ILE A 273
REMARK 465 LEU A 274
REMARK 465 GLU A 275
REMARK 465 HIS A 276
REMARK 465 HIS A 277
REMARK 465 HIS A 278
REMARK 465 HIS A 279
REMARK 465 HIS A 280
REMARK 465 HIS A 281
REMARK 465 MET B 1
REMARK 465 LYS B 2
REMARK 465 GLN B 3
REMARK 465 CYS B 4
REMARK 465 ARG B 263
REMARK 465 SER B 264
REMARK 465 GLN B 265
REMARK 465 THR B 266
REMARK 465 PHE B 267
REMARK 465 ILE B 268
REMARK 465 GLY B 269
REMARK 465 GLY B 270
REMARK 465 ASP B 271
REMARK 465 GLY B 272
REMARK 465 ILE B 273
REMARK 465 LEU B 274
REMARK 465 GLU B 275
REMARK 465 HIS B 276
REMARK 465 HIS B 277
REMARK 465 HIS B 278
REMARK 465 HIS B 279
REMARK 465 HIS B 280
REMARK 465 HIS B 281
REMARK 465 MET C 1
REMARK 465 LYS C 2
REMARK 465 GLN C 3
REMARK 465 CYS C 4
REMARK 465 ARG C 263
REMARK 465 SER C 264
REMARK 465 GLN C 265
REMARK 465 THR C 266
REMARK 465 PHE C 267
REMARK 465 ILE C 268
REMARK 465 GLY C 269
REMARK 465 GLY C 270
REMARK 465 ASP C 271
REMARK 465 GLY C 272
REMARK 465 ILE C 273
REMARK 465 LEU C 274
REMARK 465 GLU C 275
REMARK 465 HIS C 276
REMARK 465 HIS C 277
REMARK 465 HIS C 278
REMARK 465 HIS C 279
REMARK 465 HIS C 280
REMARK 465 HIS C 281
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 TRP B 119 CE2 TRP B 119 CD2 0.076
REMARK 500 HIS C 109 CG HIS C 109 CD2 0.056
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 HIS A 158 -56.84 69.43
REMARK 500 ALA A 159 -26.19 85.67
REMARK 500 ARG A 192 12.89 -151.27
REMARK 500 HIS B 6 -67.18 -27.00
REMARK 500 HIS B 158 -60.90 74.38
REMARK 500 ALA B 159 -22.54 83.70
REMARK 500 ARG B 192 14.23 -159.93
REMARK 500 HIS C 158 -55.92 73.56
REMARK 500 ALA C 159 -20.70 80.57
REMARK 500 ARG C 192 15.00 -157.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PHE A 260 ASN A 261 -145.66
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 NA C 302 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 493 O
REMARK 620 2 VAL C 89 O 86.6
REMARK 620 3 ASP C 92 O 82.3 111.8
REMARK 620 4 VAL C 95 O 167.7 97.6 85.4
REMARK 620 5 HOH C 492 O 98.4 146.3 101.9 84.6
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYS A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARG A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYS A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARG B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYS B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARG C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 302
DBREF 4H7O A 1 273 UNP Q9KNT2 Q9KNT2_VIBCH 1 273
DBREF 4H7O B 1 273 UNP Q9KNT2 Q9KNT2_VIBCH 1 273
DBREF 4H7O C 1 273 UNP Q9KNT2 Q9KNT2_VIBCH 1 273
SEQADV 4H7O LEU A 274 UNP Q9KNT2 EXPRESSION TAG
SEQADV 4H7O GLU A 275 UNP Q9KNT2 EXPRESSION TAG
SEQADV 4H7O HIS A 276 UNP Q9KNT2 EXPRESSION TAG
SEQADV 4H7O HIS A 277 UNP Q9KNT2 EXPRESSION TAG
SEQADV 4H7O HIS A 278 UNP Q9KNT2 EXPRESSION TAG
SEQADV 4H7O HIS A 279 UNP Q9KNT2 EXPRESSION TAG
SEQADV 4H7O HIS A 280 UNP Q9KNT2 EXPRESSION TAG
SEQADV 4H7O HIS A 281 UNP Q9KNT2 EXPRESSION TAG
SEQADV 4H7O LEU B 274 UNP Q9KNT2 EXPRESSION TAG
SEQADV 4H7O GLU B 275 UNP Q9KNT2 EXPRESSION TAG
SEQADV 4H7O HIS B 276 UNP Q9KNT2 EXPRESSION TAG
SEQADV 4H7O HIS B 277 UNP Q9KNT2 EXPRESSION TAG
SEQADV 4H7O HIS B 278 UNP Q9KNT2 EXPRESSION TAG
SEQADV 4H7O HIS B 279 UNP Q9KNT2 EXPRESSION TAG
SEQADV 4H7O HIS B 280 UNP Q9KNT2 EXPRESSION TAG
SEQADV 4H7O HIS B 281 UNP Q9KNT2 EXPRESSION TAG
SEQADV 4H7O LEU C 274 UNP Q9KNT2 EXPRESSION TAG
SEQADV 4H7O GLU C 275 UNP Q9KNT2 EXPRESSION TAG
SEQADV 4H7O HIS C 276 UNP Q9KNT2 EXPRESSION TAG
SEQADV 4H7O HIS C 277 UNP Q9KNT2 EXPRESSION TAG
SEQADV 4H7O HIS C 278 UNP Q9KNT2 EXPRESSION TAG
SEQADV 4H7O HIS C 279 UNP Q9KNT2 EXPRESSION TAG
SEQADV 4H7O HIS C 280 UNP Q9KNT2 EXPRESSION TAG
SEQADV 4H7O HIS C 281 UNP Q9KNT2 EXPRESSION TAG
SEQRES 1 A 281 MET LYS GLN CYS ALA HIS THR LYS VAL TRP GLN THR ILE
SEQRES 2 A 281 VAL ALA GLU ALA ARG GLU GLN ALA GLU GLN GLU PRO MET
SEQRES 3 A 281 LEU ALA SER PHE TYR HIS ALA THR ILE ILE LYS HIS ASP
SEQRES 4 A 281 SER LEU LYS ALA ALA LEU SER TYR ILE LEU ALA ASN ARG
SEQRES 5 A 281 LEU ASN THR ALA SER MET PRO ALA MET ALA VAL ARG GLU
SEQRES 6 A 281 VAL ILE GLU GLU ALA PHE ALA ALA ASP PRO SER ILE SER
SEQRES 7 A 281 GLU ALA ALA ALA CYS ASP ILE CYS ALA THR VAL ASN ARG
SEQRES 8 A 281 ASP PRO ALA VAL SER MET TYR SER MET PRO LEU LEU TYR
SEQRES 9 A 281 LEU LYS GLY TYR HIS ALA LEU GLN GLY TYR ARG VAL ALA
SEQRES 10 A 281 ASN TRP LEU TRP ARG GLN GLY ARG LYS ALA LEU ALA THR
SEQRES 11 A 281 TYR PHE GLN ASN GLN ILE SER VAL ALA CYS GLN VAL ASP
SEQRES 12 A 281 ILE HIS PRO ALA ALA ARG ILE GLY ARG GLY ILE MET LEU
SEQRES 13 A 281 ASP HIS ALA THR GLY ILE VAL ILE GLY GLU THR ALA VAL
SEQRES 14 A 281 VAL GLU ASP ASP VAL SER ILE LEU GLN ASP VAL THR LEU
SEQRES 15 A 281 GLY GLY THR GLY LYS GLU CYS GLY ASP ARG HIS PRO LYS
SEQRES 16 A 281 ILE ARG GLU GLY VAL MET ILE GLY ALA GLY ALA LYS ILE
SEQRES 17 A 281 LEU GLY ASN ILE GLU VAL GLY GLU GLY ALA LYS ILE GLY
SEQRES 18 A 281 SER GLY SER VAL VAL LEU GLN ALA VAL PRO PRO HIS THR
SEQRES 19 A 281 THR VAL ALA GLY VAL PRO ALA ARG ILE VAL GLY ARG PRO
SEQRES 20 A 281 GLN SER ASP LYS PRO SER LEU ASP MET ASP GLN GLN PHE
SEQRES 21 A 281 ASN GLY ARG SER GLN THR PHE ILE GLY GLY ASP GLY ILE
SEQRES 22 A 281 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 281 MET LYS GLN CYS ALA HIS THR LYS VAL TRP GLN THR ILE
SEQRES 2 B 281 VAL ALA GLU ALA ARG GLU GLN ALA GLU GLN GLU PRO MET
SEQRES 3 B 281 LEU ALA SER PHE TYR HIS ALA THR ILE ILE LYS HIS ASP
SEQRES 4 B 281 SER LEU LYS ALA ALA LEU SER TYR ILE LEU ALA ASN ARG
SEQRES 5 B 281 LEU ASN THR ALA SER MET PRO ALA MET ALA VAL ARG GLU
SEQRES 6 B 281 VAL ILE GLU GLU ALA PHE ALA ALA ASP PRO SER ILE SER
SEQRES 7 B 281 GLU ALA ALA ALA CYS ASP ILE CYS ALA THR VAL ASN ARG
SEQRES 8 B 281 ASP PRO ALA VAL SER MET TYR SER MET PRO LEU LEU TYR
SEQRES 9 B 281 LEU LYS GLY TYR HIS ALA LEU GLN GLY TYR ARG VAL ALA
SEQRES 10 B 281 ASN TRP LEU TRP ARG GLN GLY ARG LYS ALA LEU ALA THR
SEQRES 11 B 281 TYR PHE GLN ASN GLN ILE SER VAL ALA CYS GLN VAL ASP
SEQRES 12 B 281 ILE HIS PRO ALA ALA ARG ILE GLY ARG GLY ILE MET LEU
SEQRES 13 B 281 ASP HIS ALA THR GLY ILE VAL ILE GLY GLU THR ALA VAL
SEQRES 14 B 281 VAL GLU ASP ASP VAL SER ILE LEU GLN ASP VAL THR LEU
SEQRES 15 B 281 GLY GLY THR GLY LYS GLU CYS GLY ASP ARG HIS PRO LYS
SEQRES 16 B 281 ILE ARG GLU GLY VAL MET ILE GLY ALA GLY ALA LYS ILE
SEQRES 17 B 281 LEU GLY ASN ILE GLU VAL GLY GLU GLY ALA LYS ILE GLY
SEQRES 18 B 281 SER GLY SER VAL VAL LEU GLN ALA VAL PRO PRO HIS THR
SEQRES 19 B 281 THR VAL ALA GLY VAL PRO ALA ARG ILE VAL GLY ARG PRO
SEQRES 20 B 281 GLN SER ASP LYS PRO SER LEU ASP MET ASP GLN GLN PHE
SEQRES 21 B 281 ASN GLY ARG SER GLN THR PHE ILE GLY GLY ASP GLY ILE
SEQRES 22 B 281 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 281 MET LYS GLN CYS ALA HIS THR LYS VAL TRP GLN THR ILE
SEQRES 2 C 281 VAL ALA GLU ALA ARG GLU GLN ALA GLU GLN GLU PRO MET
SEQRES 3 C 281 LEU ALA SER PHE TYR HIS ALA THR ILE ILE LYS HIS ASP
SEQRES 4 C 281 SER LEU LYS ALA ALA LEU SER TYR ILE LEU ALA ASN ARG
SEQRES 5 C 281 LEU ASN THR ALA SER MET PRO ALA MET ALA VAL ARG GLU
SEQRES 6 C 281 VAL ILE GLU GLU ALA PHE ALA ALA ASP PRO SER ILE SER
SEQRES 7 C 281 GLU ALA ALA ALA CYS ASP ILE CYS ALA THR VAL ASN ARG
SEQRES 8 C 281 ASP PRO ALA VAL SER MET TYR SER MET PRO LEU LEU TYR
SEQRES 9 C 281 LEU LYS GLY TYR HIS ALA LEU GLN GLY TYR ARG VAL ALA
SEQRES 10 C 281 ASN TRP LEU TRP ARG GLN GLY ARG LYS ALA LEU ALA THR
SEQRES 11 C 281 TYR PHE GLN ASN GLN ILE SER VAL ALA CYS GLN VAL ASP
SEQRES 12 C 281 ILE HIS PRO ALA ALA ARG ILE GLY ARG GLY ILE MET LEU
SEQRES 13 C 281 ASP HIS ALA THR GLY ILE VAL ILE GLY GLU THR ALA VAL
SEQRES 14 C 281 VAL GLU ASP ASP VAL SER ILE LEU GLN ASP VAL THR LEU
SEQRES 15 C 281 GLY GLY THR GLY LYS GLU CYS GLY ASP ARG HIS PRO LYS
SEQRES 16 C 281 ILE ARG GLU GLY VAL MET ILE GLY ALA GLY ALA LYS ILE
SEQRES 17 C 281 LEU GLY ASN ILE GLU VAL GLY GLU GLY ALA LYS ILE GLY
SEQRES 18 C 281 SER GLY SER VAL VAL LEU GLN ALA VAL PRO PRO HIS THR
SEQRES 19 C 281 THR VAL ALA GLY VAL PRO ALA ARG ILE VAL GLY ARG PRO
SEQRES 20 C 281 GLN SER ASP LYS PRO SER LEU ASP MET ASP GLN GLN PHE
SEQRES 21 C 281 ASN GLY ARG SER GLN THR PHE ILE GLY GLY ASP GLY ILE
SEQRES 22 C 281 LEU GLU HIS HIS HIS HIS HIS HIS
HET CYS A 301 7
HET ARG A 302 12
HET CYS A 303 7
HET ARG B 301 12
HET CYS B 302 7
HET ARG C 301 12
HET NA C 302 1
HETNAM CYS CYSTEINE
HETNAM ARG ARGININE
HETNAM NA SODIUM ION
FORMUL 4 CYS 3(C3 H7 N O2 S)
FORMUL 5 ARG 3(C6 H15 N4 O2 1+)
FORMUL 10 NA NA 1+
FORMUL 11 HOH *281(H2 O)
HELIX 1 1 ALA A 5 GLU A 24 1 20
HELIX 2 2 LEU A 27 ILE A 35 1 9
HELIX 3 3 SER A 40 ASN A 54 1 15
HELIX 4 4 PRO A 59 ASP A 74 1 16
HELIX 5 5 PRO A 75 ASP A 92 1 18
HELIX 6 6 TYR A 98 LEU A 105 1 8
HELIX 7 7 LEU A 105 GLN A 123 1 19
HELIX 8 8 ARG A 125 GLN A 141 1 17
HELIX 9 9 LYS A 251 ASP A 255 5 5
HELIX 10 10 HIS B 6 GLU B 24 1 19
HELIX 11 11 LEU B 27 ILE B 35 1 9
HELIX 12 12 SER B 40 ASN B 54 1 15
HELIX 13 13 PRO B 59 ASP B 74 1 16
HELIX 14 14 PRO B 75 ASP B 92 1 18
HELIX 15 15 TYR B 98 LEU B 105 1 8
HELIX 16 16 LEU B 105 GLN B 123 1 19
HELIX 17 17 ARG B 125 CYS B 140 1 16
HELIX 18 18 LYS B 251 ASP B 255 5 5
HELIX 19 19 HIS C 6 GLU C 24 1 19
HELIX 20 20 LEU C 27 ILE C 35 1 9
HELIX 21 21 SER C 40 ASN C 54 1 15
HELIX 22 22 PRO C 59 ASP C 74 1 16
HELIX 23 23 PRO C 75 ASP C 92 1 18
HELIX 24 24 TYR C 98 LEU C 105 1 8
HELIX 25 25 LEU C 105 GLN C 123 1 19
HELIX 26 26 ARG C 125 GLN C 141 1 17
HELIX 27 27 LYS C 251 MET C 256 1 6
SHEET 1 A 5 VAL A 142 ILE A 144 0
SHEET 2 A 5 ILE A 162 ILE A 164 1 O ILE A 162 N ASP A 143
SHEET 3 A 5 THR A 181 GLY A 183 1 O LEU A 182 N VAL A 163
SHEET 4 A 5 LYS A 207 LEU A 209 1 O ILE A 208 N GLY A 183
SHEET 5 A 5 VAL A 225 VAL A 226 1 O VAL A 226 N LYS A 207
SHEET 1 B 4 ARG A 149 ILE A 150 0
SHEET 2 B 4 VAL A 169 VAL A 170 1 O VAL A 170 N ARG A 149
SHEET 3 B 4 LYS A 195 ILE A 196 1 O ILE A 196 N VAL A 169
SHEET 4 B 4 GLU A 213 VAL A 214 1 O VAL A 214 N LYS A 195
SHEET 1 C 6 MET A 155 LEU A 156 0
SHEET 2 C 6 SER A 175 ILE A 176 1 O ILE A 176 N MET A 155
SHEET 3 C 6 MET A 201 ILE A 202 1 O ILE A 202 N SER A 175
SHEET 4 C 6 LYS A 219 ILE A 220 1 O ILE A 220 N MET A 201
SHEET 5 C 6 THR A 235 ALA A 237 1 O VAL A 236 N LYS A 219
SHEET 6 C 6 ARG A 242 GLY A 245 -1 O VAL A 244 N THR A 235
SHEET 1 D 5 VAL B 142 ILE B 144 0
SHEET 2 D 5 ILE B 162 ILE B 164 1 O ILE B 164 N ASP B 143
SHEET 3 D 5 THR B 181 GLY B 183 1 O LEU B 182 N VAL B 163
SHEET 4 D 5 LYS B 207 LEU B 209 1 O ILE B 208 N GLY B 183
SHEET 5 D 5 VAL B 225 VAL B 226 1 O VAL B 226 N LYS B 207
SHEET 1 E 4 ARG B 149 ILE B 150 0
SHEET 2 E 4 VAL B 169 VAL B 170 1 O VAL B 170 N ARG B 149
SHEET 3 E 4 LYS B 195 ILE B 196 1 O ILE B 196 N VAL B 169
SHEET 4 E 4 GLU B 213 VAL B 214 1 O VAL B 214 N LYS B 195
SHEET 1 F 6 MET B 155 LEU B 156 0
SHEET 2 F 6 SER B 175 ILE B 176 1 O ILE B 176 N MET B 155
SHEET 3 F 6 MET B 201 ILE B 202 1 O ILE B 202 N SER B 175
SHEET 4 F 6 LYS B 219 ILE B 220 1 O ILE B 220 N MET B 201
SHEET 5 F 6 THR B 235 ALA B 237 1 O VAL B 236 N LYS B 219
SHEET 6 F 6 ARG B 242 GLY B 245 -1 O VAL B 244 N THR B 235
SHEET 1 G 5 ASP C 143 ILE C 144 0
SHEET 2 G 5 VAL C 163 ILE C 164 1 O ILE C 164 N ASP C 143
SHEET 3 G 5 THR C 181 GLY C 183 1 O LEU C 182 N VAL C 163
SHEET 4 G 5 LYS C 207 LEU C 209 1 O ILE C 208 N GLY C 183
SHEET 5 G 5 VAL C 225 VAL C 226 1 O VAL C 226 N LYS C 207
SHEET 1 H 4 ARG C 149 ILE C 150 0
SHEET 2 H 4 VAL C 169 VAL C 170 1 O VAL C 170 N ARG C 149
SHEET 3 H 4 LYS C 195 ILE C 196 1 O ILE C 196 N VAL C 169
SHEET 4 H 4 GLU C 213 VAL C 214 1 O VAL C 214 N LYS C 195
SHEET 1 I 6 MET C 155 ASP C 157 0
SHEET 2 I 6 SER C 175 LEU C 177 1 O ILE C 176 N MET C 155
SHEET 3 I 6 MET C 201 ILE C 202 1 O ILE C 202 N SER C 175
SHEET 4 I 6 LYS C 219 ILE C 220 1 O ILE C 220 N MET C 201
SHEET 5 I 6 THR C 235 ALA C 237 1 O VAL C 236 N LYS C 219
SHEET 6 I 6 ARG C 242 GLY C 245 -1 O VAL C 244 N THR C 235
LINK O HOH A 493 NA NA C 302 1555 1555 2.39
LINK O VAL C 89 NA NA C 302 1555 1555 2.20
LINK O ASP C 92 NA NA C 302 1555 1555 2.29
LINK O VAL C 95 NA NA C 302 1555 1555 2.21
LINK NA NA C 302 O HOH C 492 1555 1555 2.22
CISPEP 1 VAL A 239 PRO A 240 0 -1.69
CISPEP 2 VAL B 239 PRO B 240 0 -5.01
CISPEP 3 PHE B 260 ASN B 261 0 1.82
CISPEP 4 VAL C 239 PRO C 240 0 -2.65
SITE 1 AC1 9 GLY A 184 ARG A 192 HIS A 193 HOH A 401
SITE 2 AC1 9 HOH A 444 ASP C 92 ASP C 157 HIS C 158
SITE 3 AC1 9 HOH C 430
SITE 1 AC2 10 THR A 55 ALA A 56 SER A 57 TYR A 131
SITE 2 AC2 10 GLN A 135 HOH A 464 PHE C 30 ASN C 51
SITE 3 AC2 10 ARG C 52 HOH C 452
SITE 1 AC3 10 ASP A 92 PRO A 93 ASP A 157 HIS A 158
SITE 2 AC3 10 HOH A 477 GLY B 184 ARG B 192 HIS B 193
SITE 3 AC3 10 HOH B 411 HOH B 446
SITE 1 AC4 10 PHE A 30 ASN A 51 HOH A 466 THR B 55
SITE 2 AC4 10 ALA B 56 SER B 57 TYR B 131 ASN B 134
SITE 3 AC4 10 GLN B 135 HOH B 469
SITE 1 AC5 10 ASP B 92 PRO B 93 ALA B 94 ASP B 157
SITE 2 AC5 10 HIS B 158 HOH B 436 GLY C 184 ARG C 192
SITE 3 AC5 10 HIS C 193 HOH C 419
SITE 1 AC6 5 ASN B 51 SER C 57 TYR C 131 ASN C 134
SITE 2 AC6 5 GLN C 135
SITE 1 AC7 5 HOH A 493 VAL C 89 ASP C 92 VAL C 95
SITE 2 AC7 5 HOH C 492
CRYST1 144.040 75.040 73.430 90.00 89.04 90.00 C 1 2 1 12
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 0.006943 0.000000 -0.000116 0.00000
SCALE2 0.000000 0.013326 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013620 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
