HEADER TRANSCRIPTION 01-MAR-05 1Z05
TITLE CRYSTAL STRUCTURE OF THE ROK FAMILY TRANSCRIPTIONAL REGULATOR, HOMOLOG
TITLE 2 OF E.COLI MLC PROTEIN.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTIONAL REGULATOR, ROK FAMILY;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE O1 BIOVAR ELTOR;
SOURCE 3 ORGANISM_TAXID: 243277;
SOURCE 4 STRAIN: N16961;
SOURCE 5 GENE: AAF95155;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
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: PMCSG7
KEYWDS ROK FAMILY, TRANSCRIPTIONAL REGULATOR, STRUCTURAL GENOMICS, PSI,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS, MCSG, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR G.MINASOV,J.S.BRUNZELLE,L.SHUVALOVA,F.R.COLLART,W.F.ANDERSON,MIDWEST
AUTHOR 2 CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 5 27-JUN-18 1Z05 1 SEQADV
REVDAT 4 11-OCT-17 1Z05 1 REMARK
REVDAT 3 13-JUL-11 1Z05 1 VERSN
REVDAT 2 24-FEB-09 1Z05 1 VERSN
REVDAT 1 08-MAR-05 1Z05 0
JRNL AUTH G.MINASOV,J.S.BRUNZELLE,L.SHUVALOVA,F.R.COLLART,W.F.ANDERSON
JRNL TITL CRYSTAL STRUCTURE OF THE ROK FAMILY TRANSCRIPTIONAL
JRNL TITL 2 REGULATOR, HOMOLOG OF E.COLI MLC PROTEIN.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.9
REMARK 3 NUMBER OF REFLECTIONS : 31297
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1651
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2461
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.92
REMARK 3 BIN R VALUE (WORKING SET) : 0.2170
REMARK 3 BIN FREE R VALUE SET COUNT : 144
REMARK 3 BIN FREE R VALUE : 0.2800
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3045
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 396
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 31.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.58000
REMARK 3 B22 (A**2) : -1.58000
REMARK 3 B33 (A**2) : 3.16000
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): 0.181
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.161
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.106
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.110
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3287 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4480 ; 1.098 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 426 ; 5.292 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 149 ;38.184 ;24.899
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 573 ;13.897 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;13.076 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 511 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2490 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1582 ; 0.183 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2316 ; 0.295 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 320 ; 0.118 ; 0.200
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): 58 ; 0.188 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 22 ; 0.127 ; 0.200
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): 2132 ; 1.048 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3331 ; 1.671 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1288 ; 2.776 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1149 ; 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): 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 : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 14 A 82
REMARK 3 RESIDUE RANGE : A 395 A 405
REMARK 3 ORIGIN FOR THE GROUP (A): -7.5622 24.4556 16.6833
REMARK 3 T TENSOR
REMARK 3 T11: -0.2467 T22: -0.1168
REMARK 3 T33: -0.1675 T12: -0.0089
REMARK 3 T13: 0.0213 T23: 0.0277
REMARK 3 L TENSOR
REMARK 3 L11: 6.1598 L22: 4.7606
REMARK 3 L33: 5.2451 L12: -2.0575
REMARK 3 L13: 2.1239 L23: -2.5439
REMARK 3 S TENSOR
REMARK 3 S11: 0.0738 S12: 0.0499 S13: -0.0696
REMARK 3 S21: 0.2374 S22: 0.0345 S23: 0.3346
REMARK 3 S31: -0.1264 S32: -0.1312 S33: -0.1083
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 83 A 192
REMARK 3 ORIGIN FOR THE GROUP (A): 17.1221 20.1582 34.0140
REMARK 3 T TENSOR
REMARK 3 T11: -0.1140 T22: -0.2065
REMARK 3 T33: -0.2198 T12: -0.0059
REMARK 3 T13: -0.0586 T23: -0.0298
REMARK 3 L TENSOR
REMARK 3 L11: 2.8450 L22: 4.4043
REMARK 3 L33: 2.2518 L12: -0.3758
REMARK 3 L13: 1.0943 L23: -0.9767
REMARK 3 S TENSOR
REMARK 3 S11: -0.0600 S12: -0.0907 S13: 0.0719
REMARK 3 S21: 0.5190 S22: -0.0586 S23: -0.3053
REMARK 3 S31: -0.1488 S32: 0.1287 S33: 0.1185
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 193 A 394
REMARK 3 ORIGIN FOR THE GROUP (A): 21.2413 -3.3882 22.6964
REMARK 3 T TENSOR
REMARK 3 T11: -0.1324 T22: -0.1482
REMARK 3 T33: -0.1734 T12: -0.0160
REMARK 3 T13: -0.0017 T23: -0.0618
REMARK 3 L TENSOR
REMARK 3 L11: 2.3236 L22: 2.0743
REMARK 3 L33: 0.7874 L12: -1.7145
REMARK 3 L13: -0.6755 L23: 0.5043
REMARK 3 S TENSOR
REMARK 3 S11: 0.0769 S12: -0.0007 S13: 0.0535
REMARK 3 S21: -0.0307 S22: 0.0727 S23: -0.1438
REMARK 3 S31: -0.0478 S32: 0.1789 S33: -0.1495
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 1Z05 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032130.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-FEB-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 32-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : DIAMOND 111
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33945
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 200 DATA REDUNDANCY : 16.50
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 52.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 14.70
REMARK 200 R MERGE FOR SHELL (I) : 0.40200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX, SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL, 1.5M AMMONIUM SO4, 12%
REMARK 280 GLYCEROL, 5MM BETA-MERCAPTOETHANOL, PH 8.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 59.14550
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 46.85950
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 46.85950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 29.57275
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 46.85950
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 46.85950
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 88.71825
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 46.85950
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 46.85950
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 29.57275
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 46.85950
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 46.85950
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 88.71825
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 59.14550
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: PROBABLY A DIMER. THE SECON PART COULD BE GENERATED BY THE
REMARK 300 TWO FOLD AXIS: -Y,-X,-Z+1/2
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 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 59.14550
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 -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 SER A -16
REMARK 465 SER A -15
REMARK 465 GLY A -14
REMARK 465 VAL A -13
REMARK 465 ASP A -12
REMARK 465 LEU A -11
REMARK 465 GLY A -10
REMARK 465 THR A -9
REMARK 465 GLU A -8
REMARK 465 ASN A -7
REMARK 465 LEU A -6
REMARK 465 TYR A -5
REMARK 465 PHE A -4
REMARK 465 GLN A -3
REMARK 465 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 TYR A 2
REMARK 465 MET A 3
REMARK 465 ALA A 4
REMARK 465 GLN A 5
REMARK 465 PRO A 6
REMARK 465 GLY A 7
REMARK 465 HIS A 8
REMARK 465 ILE A 9
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 ASN A 80 70.14 -109.11
REMARK 500 ASP A 143 -113.40 -123.04
REMARK 500 ASP A 143 -114.55 -123.04
REMARK 500 HIS A 168 -57.79 75.03
REMARK 500 HIS A 219 -127.24 -150.96
REMARK 500 GLN A 251 55.84 -113.44
REMARK 500 TYR A 378 -52.00 -155.28
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 ZN A 406 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 245 ND1
REMARK 620 2 CYS A 255 SG 104.1
REMARK 620 3 CYS A 257 SG 110.1 103.7
REMARK 620 4 CYS A 262 SG 122.0 107.3 108.2
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 ZN A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 414
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC26690 RELATED DB: TARGETDB
DBREF 1Z05 A 1 405 UNP Q9KQJ1 Q9KQJ1_VIBCH 1 405
SEQADV 1Z05 MET A -23 UNP Q9KQJ1 INITIATING METHIONINE
SEQADV 1Z05 HIS A -22 UNP Q9KQJ1 EXPRESSION TAG
SEQADV 1Z05 HIS A -21 UNP Q9KQJ1 EXPRESSION TAG
SEQADV 1Z05 HIS A -20 UNP Q9KQJ1 EXPRESSION TAG
SEQADV 1Z05 HIS A -19 UNP Q9KQJ1 EXPRESSION TAG
SEQADV 1Z05 HIS A -18 UNP Q9KQJ1 EXPRESSION TAG
SEQADV 1Z05 HIS A -17 UNP Q9KQJ1 EXPRESSION TAG
SEQADV 1Z05 SER A -16 UNP Q9KQJ1 CLONING ARTIFACT
SEQADV 1Z05 SER A -15 UNP Q9KQJ1 CLONING ARTIFACT
SEQADV 1Z05 GLY A -14 UNP Q9KQJ1 CLONING ARTIFACT
SEQADV 1Z05 VAL A -13 UNP Q9KQJ1 CLONING ARTIFACT
SEQADV 1Z05 ASP A -12 UNP Q9KQJ1 CLONING ARTIFACT
SEQADV 1Z05 LEU A -11 UNP Q9KQJ1 CLONING ARTIFACT
SEQADV 1Z05 GLY A -10 UNP Q9KQJ1 CLONING ARTIFACT
SEQADV 1Z05 THR A -9 UNP Q9KQJ1 CLONING ARTIFACT
SEQADV 1Z05 GLU A -8 UNP Q9KQJ1 CLONING ARTIFACT
SEQADV 1Z05 ASN A -7 UNP Q9KQJ1 CLONING ARTIFACT
SEQADV 1Z05 LEU A -6 UNP Q9KQJ1 CLONING ARTIFACT
SEQADV 1Z05 TYR A -5 UNP Q9KQJ1 CLONING ARTIFACT
SEQADV 1Z05 PHE A -4 UNP Q9KQJ1 CLONING ARTIFACT
SEQADV 1Z05 GLN A -3 UNP Q9KQJ1 CLONING ARTIFACT
SEQADV 1Z05 SER A -2 UNP Q9KQJ1 CLONING ARTIFACT
SEQADV 1Z05 ASN A -1 UNP Q9KQJ1 CLONING ARTIFACT
SEQADV 1Z05 ALA A 0 UNP Q9KQJ1 CLONING ARTIFACT
SEQRES 1 A 429 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 429 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET TYR
SEQRES 3 A 429 MET ALA GLN PRO GLY HIS ILE ASP HIS ILE LYS GLN ILE
SEQRES 4 A 429 ASN ALA GLY ARG VAL TYR LYS LEU ILE ASP GLN LYS GLY
SEQRES 5 A 429 PRO ILE SER ARG ILE ASP LEU SER LYS GLU SER GLU LEU
SEQRES 6 A 429 ALA PRO ALA SER ILE THR LYS ILE THR ARG GLU LEU ILE
SEQRES 7 A 429 ASP ALA HIS LEU ILE HIS GLU THR THR VAL GLN GLU ALA
SEQRES 8 A 429 ILE SER ARG GLY ARG PRO ALA VAL GLY LEU GLN THR ASN
SEQRES 9 A 429 ASN LEU GLY TRP GLN PHE LEU SER MET ARG LEU GLY ARG
SEQRES 10 A 429 GLY TYR LEU THR ILE ALA LEU HIS GLU LEU GLY GLY GLU
SEQRES 11 A 429 VAL LEU ILE ASP THR LYS ILE ASP ILE HIS GLU ILE ASP
SEQRES 12 A 429 GLN ASP ASP VAL LEU ALA ARG LEU LEU PHE GLU ILE GLU
SEQRES 13 A 429 GLU PHE PHE GLN THR TYR ALA ALA GLN LEU ASP ARG VAL
SEQRES 14 A 429 THR SER ILE ALA ILE THR LEU PRO GLY LEU VAL ASN SER
SEQRES 15 A 429 GLU GLN GLY ILE VAL LEU GLN MET PRO HIS TYR ASN VAL
SEQRES 16 A 429 LYS ASN LEU ALA LEU GLY PRO GLU ILE TYR LYS ALA THR
SEQRES 17 A 429 GLY LEU PRO VAL PHE VAL ALA ASN ASP THR ARG ALA TRP
SEQRES 18 A 429 ALA LEU ALA GLU LYS LEU PHE GLY HIS SER GLN ASP VAL
SEQRES 19 A 429 ASP ASN SER VAL LEU ILE SER ILE HIS HIS GLY LEU GLY
SEQRES 20 A 429 ALA GLY ILE VAL LEU ASP GLY ARG VAL LEU GLN GLY ARG
SEQRES 21 A 429 HIS GLY ASN ILE GLY GLU LEU GLY HIS ILE GLN ILE ASP
SEQRES 22 A 429 PRO GLN GLY LYS ARG CYS HIS CYS GLY ASN TYR GLY CYS
SEQRES 23 A 429 LEU GLU THR VAL ALA SER SER GLN ALA ILE ARG ASP GLN
SEQRES 24 A 429 VAL THR ALA ARG ILE GLN ALA GLY GLU PRO SER CYS LEU
SEQRES 25 A 429 ALA THR VAL GLU GLU ILE SER ILE GLU ASP ILE CYS ALA
SEQRES 26 A 429 ALA ALA ALA ASP GLY ASP PRO LEU ALA VAL ASP VAL ILE
SEQRES 27 A 429 GLN GLN LEU GLY ARG TYR LEU GLY ALA ALA ILE ALA ILE
SEQRES 28 A 429 VAL ILE ASN LEU PHE ASN PRO GLU LYS ILE LEU ILE GLY
SEQRES 29 A 429 GLY VAL ILE ASN GLN ALA LYS SER ILE LEU TYR PRO SER
SEQRES 30 A 429 ILE GLU GLN CYS ILE ARG GLU GLN SER LEU PRO VAL TYR
SEQRES 31 A 429 HIS GLN ASP LEU LYS LEU VAL GLU SER ARG PHE TYR LYS
SEQRES 32 A 429 GLN ALA THR MET PRO GLY ALA ALA LEU ILE LYS GLN ALA
SEQRES 33 A 429 LEU TYR ASP GLY LEU LEU LEU MET LYS VAL VAL GLU GLY
HET ZN A 406 1
HET SO4 A 407 5
HET SO4 A 408 5
HET SO4 A 409 5
HET SO4 A 410 5
HET SO4 A 411 5
HET SO4 A 412 5
HET BME A 413 4
HET GOL A 414 6
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
HETNAM BME BETA-MERCAPTOETHANOL
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 ZN ZN 2+
FORMUL 3 SO4 6(O4 S 2-)
FORMUL 9 BME C2 H6 O S
FORMUL 10 GOL C3 H8 O3
FORMUL 11 HOH *396(H2 O)
HELIX 1 1 ASP A 10 GLY A 28 1 19
HELIX 2 2 SER A 31 GLU A 40 1 10
HELIX 3 3 ALA A 42 ALA A 56 1 15
HELIX 4 4 THR A 63 GLY A 71 1 9
HELIX 5 5 ASP A 119 TYR A 138 1 20
HELIX 6 6 ALA A 175 GLY A 185 1 11
HELIX 7 7 ASP A 193 GLY A 205 1 13
HELIX 8 8 LEU A 263 SER A 268 1 6
HELIX 9 9 SER A 268 ALA A 282 1 15
HELIX 10 10 SER A 295 ASP A 305 1 11
HELIX 11 11 ASP A 307 ASN A 333 1 27
HELIX 12 12 GLY A 341 GLN A 345 5 5
HELIX 13 13 ALA A 346 SER A 362 1 17
HELIX 14 14 LEU A 363 GLN A 368 1 6
HELIX 15 15 THR A 382 ASP A 395 1 14
HELIX 16 16 GLY A 396 GLY A 405 1 10
SHEET 1 A 2 ILE A 59 THR A 62 0
SHEET 2 A 2 VAL A 75 THR A 79 -1 O GLN A 78 N HIS A 60
SHEET 1 B 5 VAL A 107 ASP A 114 0
SHEET 2 B 5 TYR A 95 GLU A 102 -1 N LEU A 100 O LEU A 108
SHEET 3 B 5 TRP A 84 GLY A 92 -1 N PHE A 86 O HIS A 101
SHEET 4 B 5 ARG A 144 LEU A 152 1 O ALA A 149 N MET A 89
SHEET 5 B 5 VAL A 188 ASN A 192 1 O PHE A 189 N ILE A 150
SHEET 1 C 2 LEU A 155 ASN A 157 0
SHEET 2 C 2 ILE A 162 GLN A 165 -1 O ILE A 162 N ASN A 157
SHEET 1 D 5 ARG A 231 VAL A 232 0
SHEET 2 D 5 LEU A 222 LEU A 228 -1 N LEU A 228 O ARG A 231
SHEET 3 D 5 SER A 213 ILE A 218 -1 N SER A 217 O GLY A 223
SHEET 4 D 5 LYS A 336 GLY A 340 1 O LEU A 338 N ILE A 216
SHEET 5 D 5 LYS A 371 GLU A 374 1 O VAL A 373 N ILE A 337
LINK SG ACYS A 357 S2 ABME A 413 1555 1555 1.94
LINK ZN ZN A 406 ND1 HIS A 245 1555 1555 2.13
LINK ZN ZN A 406 SG CYS A 255 1555 1555 2.46
LINK ZN ZN A 406 SG CYS A 257 1555 1555 2.32
LINK ZN ZN A 406 SG CYS A 262 1555 1555 2.27
CISPEP 1 GLY A 28 PRO A 29 0 -0.20
SITE 1 AC1 4 HIS A 245 CYS A 255 CYS A 257 CYS A 262
SITE 1 AC2 8 ARG A 90 GLY A 92 ARG A 93 TYR A 95
SITE 2 AC2 8 HIS A 219 HIS A 220 HOH A 521 HOH A 735
SITE 1 AC3 8 ARG A 93 HIS A 219 HIS A 220 GLY A 221
SITE 2 AC3 8 HOH A 437 HOH A 520 HOH A 722 HOH A 802
SITE 1 AC4 5 GLU A 355 ILE A 358 ARG A 359 HIS A 367
SITE 2 AC4 5 LEU A 370
SITE 1 AC5 6 PRO A 167 HIS A 168 HOH A 714 HOH A 716
SITE 2 AC5 6 HOH A 718 HOH A 775
SITE 1 AC6 4 THR A 47 ARG A 51 HOH A 509 HOH A 739
SITE 1 AC7 5 GLN A 316 ARG A 319 TYR A 320 HOH A 776
SITE 2 AC7 5 HOH A 777
SITE 1 AC8 7 GLN A 356 CYS A 357 GLU A 360 HOH A 454
SITE 2 AC8 7 HOH A 737 HOH A 749 HOH A 750
SITE 1 AC9 7 GLN A 345 ALA A 346 LYS A 347 SER A 348
SITE 2 AC9 7 HOH A 772 HOH A 785 HOH A 792
CRYST1 93.719 93.719 118.291 90.00 90.00 90.00 P 41 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010670 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010670 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008454 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
