HEADER STRUCTURAL GENOMICS 10-SEP-10 3OT1
TITLE CRYSTAL STRUCTURE OF VC2308 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 4-METHYL-5(B-HYDROXYETHYL)-THIAZOLE MONOPHOSPHATE
COMPND 3 BIOSYNTHESIS ENZYME;
COMPND 4 CHAIN: A;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: CYS AT RESIDUE 108;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: 4-METHYL-5(B-HYDROXYETHYL)-THIAZOLE MONOPHOSPHATE
COMPND 9 BIOSYNTHESIS ENZYME;
COMPND 10 CHAIN: B;
COMPND 11 ENGINEERED: YES;
COMPND 12 OTHER_DETAILS: CSX AT RESIDUE 108
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE O1 BIOVAR EL TOR;
SOURCE 3 ORGANISM_TAXID: 243277;
SOURCE 4 STRAIN: N16961;
SOURCE 5 GENE: VC2308, VC_2308;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 DE3 GOLD MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: MCSG7;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE O1 BIOVAR EL TOR;
SOURCE 13 ORGANISM_TAXID: 243277;
SOURCE 14 STRAIN: N16961;
SOURCE 15 GENE: VC2308, VC_2308;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21 DE3 GOLD MAGIC;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: MCSG7
KEYWDS CSGID, STRUCTURAL GENOMICS, VIBRIO CHOLERAE, CENTER FOR STRUCTURAL
KEYWDS 2 GENOMICS OF INFECTIOUS DISEASES, DJ-1 SUPERFAMILY, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR E.NIEDZIALKOWSKA,Z.WAWRZAK,M.CHRUSZCZ,P.POREBSKI,T.SKARINA,X.HUANG,
AUTHOR 2 S.GRIMSHAW,M.CYMBOROWSKI,A.SAVCHENKO,W.F.ANDERSON,W.MINOR,CENTER FOR
AUTHOR 3 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)
REVDAT 2 13-APR-22 3OT1 1 AUTHOR JRNL REMARK SEQADV
REVDAT 2 2 1 LINK
REVDAT 1 22-SEP-10 3OT1 0
JRNL AUTH E.NIEDZIALKOWSKA,Z.WAWRZAK,M.CHRUSZCZ,P.POREBSKI,T.SKARINA,
JRNL AUTH 2 X.HUANG,S.GRIMSHAW,M.CYMBOROWSKI,A.SAVCHENKO,W.F.ANDERSON,
JRNL AUTH 3 W.MINOR,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS
JRNL AUTH 4 DISEASES (CSGID)
JRNL TITL CRYSTAL STRUCTURE OF VC2308 PROTEIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.16 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.16
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 109812
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) : 0.145
REMARK 3 R VALUE (WORKING SET) : 0.144
REMARK 3 FREE R VALUE : 0.168
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5797
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) : 1.16
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.19
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7215
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.37
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE SET COUNT : 359
REMARK 3 BIN FREE R VALUE : 0.2890
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2927
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 579
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 8.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.24000
REMARK 3 B22 (A**2) : -0.25000
REMARK 3 B33 (A**2) : 0.49000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.037
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.021
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.981
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.963
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3236 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2120 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4447 ; 1.500 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5245 ; 2.334 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 460 ; 6.053 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 131 ;37.697 ;24.427
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 536 ;12.980 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;13.788 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 526 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3736 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 643 ; 0.005 ; 0.020
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): 2100 ; 1.297 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 850 ; 1.543 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3390 ; 1.932 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1136 ; 2.926 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1032 ; 4.236 ; 4.500
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): 3236 ; 1.373 ; 3.000
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 ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3OT1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-SEP-10.
REMARK 100 THE DEPOSITION ID IS D_1000061536.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUL-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : DIAMOND LAUE MONOCHROMATOR
REMARK 200 OPTICS : BERYLLIUM LENSES
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 115862
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.160
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 (%) : 97.8
REMARK 200 DATA REDUNDANCY : 9.120
REMARK 200 R MERGE (I) : 0.09400
REMARK 200 R SYM (I) : 0.09400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.16
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.5
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.61000
REMARK 200 R SYM FOR SHELL (I) : 0.61000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000 MLPHARE, SHELXD, DM, CCP4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TACSIMATE 35%, PHENOL 10MM, PH 7.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 32.19350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.79600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.34150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.79600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.19350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.34150
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MSE A 1
REMARK 465 GLU A 2
REMARK 465 GLN A 3
REMARK 465 GLY A 4
REMARK 465 MSE A 5
REMARK 465 SER A 205
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 MSE B 1
REMARK 465 GLU B 2
REMARK 465 GLN B 3
REMARK 465 GLY B 4
REMARK 465 ILE B 201
REMARK 465 ASP B 202
REMARK 465 ALA B 203
REMARK 465 GLN B 204
REMARK 465 SER B 205
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 117 CE NZ
REMARK 470 LYS B 117 CD CE NZ
REMARK 470 GLU B 196 CG CD OE1 OE2
REMARK 470 SER B 198 OG
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 CYS A 108 CA - CB - SG ANGL. DEV. = 6.9 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 CYS A 108 -125.84 64.85
REMARK 500 VAL A 114 -63.45 -106.39
REMARK 500 CSX B 108 -116.92 62.32
REMARK 500 CSX B 108 -120.41 68.03
REMARK 500 VAL B 114 -64.07 -106.26
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 B 207 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 40 O
REMARK 620 2 GLY B 42 O 124.5
REMARK 620 3 THR B 60 OG1 110.6 124.6
REMARK 620 4 GLU B 62 OE1 90.0 104.9 78.3
REMARK 620 5 HOH B 335 O 89.6 84.6 91.3 168.7
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 CL B 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 208
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: IDP04323 RELATED DB: TARGETDB
DBREF 3OT1 A 1 205 UNP Q9KPQ8 Q9KPQ8_VIBCH 1 205
DBREF 3OT1 B 1 205 UNP Q9KPQ8 Q9KPQ8_VIBCH 1 205
SEQADV 3OT1 SER A -2 UNP Q9KPQ8 EXPRESSION TAG
SEQADV 3OT1 ASN A -1 UNP Q9KPQ8 EXPRESSION TAG
SEQADV 3OT1 ALA A 0 UNP Q9KPQ8 EXPRESSION TAG
SEQADV 3OT1 SER B -2 UNP Q9KPQ8 EXPRESSION TAG
SEQADV 3OT1 ASN B -1 UNP Q9KPQ8 EXPRESSION TAG
SEQADV 3OT1 ALA B 0 UNP Q9KPQ8 EXPRESSION TAG
SEQRES 1 A 208 SER ASN ALA MSE GLU GLN GLY MSE SER LYS ARG ILE LEU
SEQRES 2 A 208 VAL PRO VAL ALA HIS GLY SER GLU GLU MSE GLU THR VAL
SEQRES 3 A 208 ILE ILE VAL ASP THR LEU VAL ARG ALA GLY PHE GLN VAL
SEQRES 4 A 208 THR MSE ALA ALA VAL GLY ASP LYS LEU GLN VAL GLN GLY
SEQRES 5 A 208 SER ARG GLY VAL TRP LEU THR ALA GLU GLN THR LEU GLU
SEQRES 6 A 208 ALA CYS SER ALA GLU ALA PHE ASP ALA LEU ALA LEU PRO
SEQRES 7 A 208 GLY GLY VAL GLY GLY ALA GLN ALA PHE ALA ASP SER THR
SEQRES 8 A 208 ALA LEU LEU ALA LEU ILE ASP ALA PHE SER GLN GLN GLY
SEQRES 9 A 208 LYS LEU VAL ALA ALA ILE CYS ALA THR PRO ALA LEU VAL
SEQRES 10 A 208 PHE ALA LYS GLN GLN LYS PHE VAL GLY ALA ARG MSE THR
SEQRES 11 A 208 CYS HIS PRO ASN PHE PHE ASP HIS ILE PRO SER GLU ARG
SEQRES 12 A 208 LEU SER ARG GLN ARG VAL CYS TYR TYR ALA THR GLN HIS
SEQRES 13 A 208 LEU LEU THR SER GLN GLY PRO GLY THR ALA LEU GLU PHE
SEQRES 14 A 208 ALA LEU ALA MSE ILE ALA LEU LEU ALA GLY VAL GLU LEU
SEQRES 15 A 208 ALA GLN HIS VAL ALA ALA PRO MSE VAL LEU HIS PRO GLN
SEQRES 16 A 208 GLN LEU THR GLU LEU SER GLY PHE ILE ASP ALA GLN SER
SEQRES 1 B 208 SER ASN ALA MSE GLU GLN GLY MSE SER LYS ARG ILE LEU
SEQRES 2 B 208 VAL PRO VAL ALA HIS GLY SER GLU GLU MSE GLU THR VAL
SEQRES 3 B 208 ILE ILE VAL ASP THR LEU VAL ARG ALA GLY PHE GLN VAL
SEQRES 4 B 208 THR MSE ALA ALA VAL GLY ASP LYS LEU GLN VAL GLN GLY
SEQRES 5 B 208 SER ARG GLY VAL TRP LEU THR ALA GLU GLN THR LEU GLU
SEQRES 6 B 208 ALA CYS SER ALA GLU ALA PHE ASP ALA LEU ALA LEU PRO
SEQRES 7 B 208 GLY GLY VAL GLY GLY ALA GLN ALA PHE ALA ASP SER THR
SEQRES 8 B 208 ALA LEU LEU ALA LEU ILE ASP ALA PHE SER GLN GLN GLY
SEQRES 9 B 208 LYS LEU VAL ALA ALA ILE CSX ALA THR PRO ALA LEU VAL
SEQRES 10 B 208 PHE ALA LYS GLN GLN LYS PHE VAL GLY ALA ARG MSE THR
SEQRES 11 B 208 CYS HIS PRO ASN PHE PHE ASP HIS ILE PRO SER GLU ARG
SEQRES 12 B 208 LEU SER ARG GLN ARG VAL CYS TYR TYR ALA THR GLN HIS
SEQRES 13 B 208 LEU LEU THR SER GLN GLY PRO GLY THR ALA LEU GLU PHE
SEQRES 14 B 208 ALA LEU ALA MSE ILE ALA LEU LEU ALA GLY VAL GLU LEU
SEQRES 15 B 208 ALA GLN HIS VAL ALA ALA PRO MSE VAL LEU HIS PRO GLN
SEQRES 16 B 208 GLN LEU THR GLU LEU SER GLY PHE ILE ASP ALA GLN SER
MODRES 3OT1 MSE A 20 MET SELENOMETHIONINE
MODRES 3OT1 MSE A 38 MET SELENOMETHIONINE
MODRES 3OT1 MSE A 126 MET SELENOMETHIONINE
MODRES 3OT1 MSE A 170 MET SELENOMETHIONINE
MODRES 3OT1 MSE A 187 MET SELENOMETHIONINE
MODRES 3OT1 MSE B 5 MET SELENOMETHIONINE
MODRES 3OT1 MSE B 20 MET SELENOMETHIONINE
MODRES 3OT1 MSE B 38 MET SELENOMETHIONINE
MODRES 3OT1 CSX B 108 CYS S-OXY CYSTEINE
MODRES 3OT1 MSE B 126 MET SELENOMETHIONINE
MODRES 3OT1 MSE B 170 MET SELENOMETHIONINE
MODRES 3OT1 MSE B 187 MET SELENOMETHIONINE
HET MSE A 20 13
HET MSE A 38 13
HET MSE A 126 8
HET MSE A 170 8
HET MSE A 187 16
HET MSE B 5 8
HET MSE B 20 13
HET MSE B 38 16
HET CSX B 108 13
HET MSE B 126 8
HET MSE B 170 8
HET MSE B 187 8
HET CL B 206 1
HET NA B 207 1
HET CL B 208 1
HETNAM MSE SELENOMETHIONINE
HETNAM CSX S-OXY CYSTEINE
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
FORMUL 1 MSE 11(C5 H11 N O2 SE)
FORMUL 2 CSX C3 H7 N O3 S
FORMUL 3 CL 2(CL 1-)
FORMUL 4 NA NA 1+
FORMUL 6 HOH *579(H2 O)
HELIX 1 1 GLU A 18 ALA A 32 1 15
HELIX 2 2 GLU A 62 CYS A 64 5 3
HELIX 3 3 SER A 65 PHE A 69 5 5
HELIX 4 4 GLY A 77 ASP A 86 1 10
HELIX 5 5 SER A 87 GLN A 100 1 14
HELIX 6 6 ALA A 109 VAL A 114 1 6
HELIX 7 7 HIS A 129 ILE A 136 5 8
HELIX 8 8 ALA A 150 GLN A 152 5 3
HELIX 9 9 GLY A 159 GLY A 161 5 3
HELIX 10 10 THR A 162 GLY A 176 1 15
HELIX 11 11 GLY A 176 ALA A 185 1 10
HELIX 12 12 PRO A 186 VAL A 188 5 3
HELIX 13 13 HIS A 190 GLY A 199 1 10
HELIX 14 14 GLU B 18 ALA B 32 1 15
HELIX 15 15 GLU B 62 CYS B 64 5 3
HELIX 16 16 SER B 65 PHE B 69 5 5
HELIX 17 17 GLY B 77 ASP B 86 1 10
HELIX 18 18 SER B 87 GLN B 100 1 14
HELIX 19 19 ALA B 109 VAL B 114 1 6
HELIX 20 20 HIS B 129 ILE B 136 5 8
HELIX 21 21 ALA B 150 GLN B 152 5 3
HELIX 22 22 GLY B 159 GLY B 161 5 3
HELIX 23 23 THR B 162 GLY B 176 1 15
HELIX 24 24 GLY B 176 ALA B 185 1 10
HELIX 25 25 PRO B 186 VAL B 188 5 3
HELIX 26 26 HIS B 190 THR B 195 5 6
SHEET 1 A 7 GLN A 59 THR A 60 0
SHEET 2 A 7 GLN A 35 ALA A 40 1 N ALA A 40 O GLN A 59
SHEET 3 A 7 ARG A 8 VAL A 13 1 N VAL A 11 O THR A 37
SHEET 4 A 7 ALA A 71 LEU A 74 1 O ALA A 73 N LEU A 10
SHEET 5 A 7 LEU A 103 ILE A 107 1 O ALA A 105 N LEU A 74
SHEET 6 A 7 LEU A 154 SER A 157 1 O LEU A 155 N VAL A 104
SHEET 7 A 7 VAL A 146 TYR A 149 -1 N TYR A 149 O LEU A 154
SHEET 1 B 2 GLN A 46 GLN A 48 0
SHEET 2 B 2 TRP A 54 THR A 56 -1 O LEU A 55 N VAL A 47
SHEET 1 C 7 GLN B 59 THR B 60 0
SHEET 2 C 7 GLN B 35 ALA B 40 1 N ALA B 40 O GLN B 59
SHEET 3 C 7 ARG B 8 VAL B 13 1 N VAL B 11 O THR B 37
SHEET 4 C 7 ALA B 71 LEU B 74 1 O ALA B 73 N LEU B 10
SHEET 5 C 7 LEU B 103 ILE B 107 1 O ALA B 105 N LEU B 74
SHEET 6 C 7 LEU B 154 SER B 157 1 O LEU B 155 N VAL B 104
SHEET 7 C 7 VAL B 146 TYR B 149 -1 N TYR B 149 O LEU B 154
SHEET 1 D 2 GLN B 46 GLN B 48 0
SHEET 2 D 2 TRP B 54 THR B 56 -1 O LEU B 55 N VAL B 47
LINK C GLU A 19 N MSE A 20 1555 1555 1.34
LINK C MSE A 20 N GLU A 21 1555 1555 1.33
LINK C THR A 37 N MSE A 38 1555 1555 1.33
LINK C MSE A 38 N ALA A 39 1555 1555 1.33
LINK C ARG A 125 N MSE A 126 1555 1555 1.33
LINK C MSE A 126 N THR A 127 1555 1555 1.33
LINK C ALA A 169 N MSE A 170 1555 1555 1.33
LINK C MSE A 170 N ILE A 171 1555 1555 1.32
LINK C PRO A 186 N AMSE A 187 1555 1555 1.29
LINK C PRO A 186 N BMSE A 187 1555 1555 1.34
LINK C AMSE A 187 N VAL A 188 1555 1555 1.34
LINK C BMSE A 187 N VAL A 188 1555 1555 1.33
LINK C MSE B 5 N ASER B 6 1555 1555 1.32
LINK C MSE B 5 N BSER B 6 1555 1555 1.33
LINK C GLU B 19 N MSE B 20 1555 1555 1.33
LINK C MSE B 20 N GLU B 21 1555 1555 1.33
LINK C THR B 37 N AMSE B 38 1555 1555 1.33
LINK C THR B 37 N BMSE B 38 1555 1555 1.33
LINK C AMSE B 38 N ALA B 39 1555 1555 1.34
LINK C BMSE B 38 N ALA B 39 1555 1555 1.34
LINK C ILE B 107 N ACSX B 108 1555 1555 1.33
LINK C ILE B 107 N BCSX B 108 1555 1555 1.33
LINK C ACSX B 108 N ALA B 109 1555 1555 1.33
LINK C BCSX B 108 N ALA B 109 1555 1555 1.32
LINK C ARG B 125 N MSE B 126 1555 1555 1.33
LINK C MSE B 126 N THR B 127 1555 1555 1.33
LINK C ALA B 169 N MSE B 170 1555 1555 1.33
LINK C MSE B 170 N ILE B 171 1555 1555 1.33
LINK C PRO B 186 N MSE B 187 1555 1555 1.33
LINK C MSE B 187 N VAL B 188 1555 1555 1.33
LINK O ALA B 40 NA NA B 207 1555 1555 2.29
LINK O GLY B 42 NA NA B 207 1555 1555 2.14
LINK OG1 THR B 60 NA NA B 207 1555 1555 2.28
LINK OE1 GLU B 62 NA NA B 207 1555 1555 2.27
LINK NA NA B 207 O HOH B 335 1555 1555 2.43
SITE 1 AC1 3 ARG B 51 GLY B 77 VAL B 78
SITE 1 AC2 6 ALA B 40 GLY B 42 THR B 60 LEU B 61
SITE 2 AC2 6 GLU B 62 HOH B 335
SITE 1 AC3 5 HIS A 129 HOH A 330 ARG B 31 PRO B 186
SITE 2 AC3 5 HOH B 301
CRYST1 64.387 64.683 81.592 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 0.015531 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015460 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012256 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
