HEADER HYDROLASE 21-MAY-09 3HJG
TITLE CRYSTAL STRUCTURE OF PUTATIVE ALPHA-RIBAZOLE-5'-PHOSPHATE PHOSPHATASE
TITLE 2 COBC FROM VIBRIO PARAHAEMOLYTICUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE ALPHA-RIBAZOLE-5'-PHOSPHATE PHOSPHATASE COBC;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO PARAHAEMOLYTICUS;
SOURCE 3 ORGANISM_TAXID: 670;
SOURCE 4 GENE: VP1307;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-CODON+RIL(STRATAGENE);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: BC-PSGX3(BC)
KEYWDS PHOSPHATASE, PSI-2, NYSGXRC, STRUCTURAL GENOMICS, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS,
KEYWDS 3 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.PATSKOVSKY,R.TORO,C.MORANO,M.RUTTER,M.IIZUKA,J.M.SAUDER,S.K.BURLEY,
AUTHOR 2 S.C.ALMO,NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS
AUTHOR 3 (NYSGXRC)
REVDAT 4 21-FEB-24 3HJG 1 REMARK
REVDAT 3 10-FEB-21 3HJG 1 AUTHOR JRNL REMARK SEQADV
REVDAT 2 21-NOV-18 3HJG 1 AUTHOR
REVDAT 1 02-JUN-09 3HJG 0
JRNL AUTH Y.PATSKOVSKY,R.TORO,C.MORANO,M.RUTTER,M.IIZUKA,J.M.SAUDER,
JRNL AUTH 2 S.K.BURLEY,S.C.ALMO
JRNL TITL CRYSTAL STRUCTURE OF PUTATIVE ALPHA-RIBAZOLE-5' -PHOSPHATE
JRNL TITL 2 PHOSPHATASE FROM VIBRIO PARAHAEMOLYTICUS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0034
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.5
REMARK 3 NUMBER OF REFLECTIONS : 26642
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) : 0.263
REMARK 3 R VALUE (WORKING SET) : 0.263
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.100
REMARK 3 FREE R VALUE TEST SET COUNT : 849
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 385
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 18.29
REMARK 3 BIN R VALUE (WORKING SET) : 0.5980
REMARK 3 BIN FREE R VALUE SET COUNT : 8
REMARK 3 BIN FREE R VALUE : 0.4960
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3186
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 127.9
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.25000
REMARK 3 B22 (A**2) : -4.25000
REMARK 3 B33 (A**2) : 8.50000
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): 0.371
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.285
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.338
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.729
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
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): 3285 ; 0.007 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4477 ; 1.153 ; 1.940
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 404 ; 6.920 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 151 ;39.260 ;24.834
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 551 ;20.321 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;16.030 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 507 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2465 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1463 ; 0.129 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2169 ; 0.298 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 155 ; 0.131 ; 0.500
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): 55 ; 0.078 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 2 ; 0.111 ; 0.500
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): 2063 ; 1.895 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3260 ; 3.504 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1394 ; 3.932 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1216 ; 6.262 ; 6.000
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 : 3
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 102 ; 0.72 ; 0.10
REMARK 3 TIGHT THERMAL 1 A (A**2): 102 ; 2.42 ; 5.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 436 ; 0.46 ; 0.10
REMARK 3 TIGHT THERMAL 2 A (A**2): 436 ; 4.91 ; 5.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 A (A): 676 ; 0.56 ; 0.10
REMARK 3 TIGHT THERMAL 3 A (A**2): 676 ; 3.82 ; 5.00
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 : 1.00
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 3HJG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAY-09.
REMARK 100 THE DEPOSITION ID IS D_1000053207.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-APR-09
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37362
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.610
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -0.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.13200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.61
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.94000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: DIFFRACTION DATA WERE CORRECTED AND TRUNCATED DUE TO
REMARK 200 ANISOTROPY
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 80.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% ISOPROPANOL, 2000 MM AMMONIUM
REMARK 280 SULFATE, 10% GLYCEROL, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 294K, PH 7.5
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 103.35850
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 53.60750
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 53.60750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 51.67925
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 53.60750
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 53.60750
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 155.03775
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 53.60750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 53.60750
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 51.67925
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 53.60750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 53.60750
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 155.03775
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 103.35850
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: 2480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 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 MET A -1
REMARK 465 SER A 0
REMARK 465 LEU A 1
REMARK 465 GLU A 204
REMARK 465 GLY A 205
REMARK 465 HIS A 206
REMARK 465 HIS A 207
REMARK 465 HIS A 208
REMARK 465 HIS A 209
REMARK 465 HIS A 210
REMARK 465 HIS A 211
REMARK 465 MET B -1
REMARK 465 SER B 0
REMARK 465 LEU B 1
REMARK 465 GLU B 204
REMARK 465 GLY B 205
REMARK 465 HIS B 206
REMARK 465 HIS B 207
REMARK 465 HIS B 208
REMARK 465 HIS B 209
REMARK 465 HIS B 210
REMARK 465 HIS B 211
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 PRO A 115 C - N - CA ANGL. DEV. = 11.0 DEGREES
REMARK 500 PRO B 115 C - N - CA ANGL. DEV. = 12.4 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 HIS A 98 -158.07 -94.14
REMARK 500 LYS A 100 59.09 -101.37
REMARK 500 PRO A 115 -56.00 -0.71
REMARK 500 ASP A 140 -168.14 57.37
REMARK 500 ASP A 187 -97.61 -136.04
REMARK 500 GLN A 189 166.91 49.84
REMARK 500 ARG A 195 -97.61 -75.92
REMARK 500 ARG A 195 -96.78 -76.52
REMARK 500 VAL A 202 -101.56 -121.18
REMARK 500 GLU B 81 -178.75 -65.50
REMARK 500 ASP B 83 81.72 58.98
REMARK 500 ASP B 88 -78.80 -127.70
REMARK 500 PRO B 91 55.31 -11.34
REMARK 500 PHE B 92 42.27 -83.66
REMARK 500 HIS B 98 48.53 -91.93
REMARK 500 LEU B 102 67.63 39.15
REMARK 500 PRO B 115 51.30 -14.68
REMARK 500 ASN B 116 -19.34 -166.26
REMARK 500 ASP B 140 -178.61 71.12
REMARK 500 THR B 146 -155.31 -150.12
REMARK 500 ASP B 187 -107.65 -144.05
REMARK 500 ARG B 195 -103.28 -79.71
REMARK 500 VAL B 202 -148.67 52.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 212
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 212
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 213
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 214
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-11293D RELATED DB: TARGETDB
DBREF 3HJG A 2 203 UNP Q87Q43 Q87Q43_VIBPA 2 203
DBREF 3HJG B 2 203 UNP Q87Q43 Q87Q43_VIBPA 2 203
SEQADV 3HJG MET A -1 UNP Q87Q43 EXPRESSION TAG
SEQADV 3HJG SER A 0 UNP Q87Q43 EXPRESSION TAG
SEQADV 3HJG LEU A 1 UNP Q87Q43 EXPRESSION TAG
SEQADV 3HJG GLU A 204 UNP Q87Q43 EXPRESSION TAG
SEQADV 3HJG GLY A 205 UNP Q87Q43 EXPRESSION TAG
SEQADV 3HJG HIS A 206 UNP Q87Q43 EXPRESSION TAG
SEQADV 3HJG HIS A 207 UNP Q87Q43 EXPRESSION TAG
SEQADV 3HJG HIS A 208 UNP Q87Q43 EXPRESSION TAG
SEQADV 3HJG HIS A 209 UNP Q87Q43 EXPRESSION TAG
SEQADV 3HJG HIS A 210 UNP Q87Q43 EXPRESSION TAG
SEQADV 3HJG HIS A 211 UNP Q87Q43 EXPRESSION TAG
SEQADV 3HJG MET B -1 UNP Q87Q43 EXPRESSION TAG
SEQADV 3HJG SER B 0 UNP Q87Q43 EXPRESSION TAG
SEQADV 3HJG LEU B 1 UNP Q87Q43 EXPRESSION TAG
SEQADV 3HJG GLU B 204 UNP Q87Q43 EXPRESSION TAG
SEQADV 3HJG GLY B 205 UNP Q87Q43 EXPRESSION TAG
SEQADV 3HJG HIS B 206 UNP Q87Q43 EXPRESSION TAG
SEQADV 3HJG HIS B 207 UNP Q87Q43 EXPRESSION TAG
SEQADV 3HJG HIS B 208 UNP Q87Q43 EXPRESSION TAG
SEQADV 3HJG HIS B 209 UNP Q87Q43 EXPRESSION TAG
SEQADV 3HJG HIS B 210 UNP Q87Q43 EXPRESSION TAG
SEQADV 3HJG HIS B 211 UNP Q87Q43 EXPRESSION TAG
SEQRES 1 A 213 MET SER LEU LYS THR LEU ASN ILE TYR LEU MET ARG HIS
SEQRES 2 A 213 GLY LYS VAL ASP ALA ALA PRO GLY LEU HIS GLY GLN THR
SEQRES 3 A 213 ASP LEU LYS VAL LYS GLU ALA GLU GLN GLN GLN ILE ALA
SEQRES 4 A 213 MET ALA TRP LYS THR LYS GLY TYR ASP VAL ALA GLY ILE
SEQRES 5 A 213 ILE SER SER PRO LEU SER ARG CYS HIS ASP LEU ALA GLN
SEQRES 6 A 213 ILE LEU ALA GLU GLN GLN LEU LEU PRO MET THR THR GLU
SEQRES 7 A 213 ASP ASP LEU GLN GLU MET ASP PHE GLY ASP PHE ASP GLY
SEQRES 8 A 213 MET PRO PHE ASP LEU LEU THR GLU HIS TRP LYS LYS LEU
SEQRES 9 A 213 ASP ALA PHE TRP GLN SER PRO ALA HIS HIS SER LEU PRO
SEQRES 10 A 213 ASN ALA GLU SER LEU SER THR PHE SER GLN ARG VAL SER
SEQRES 11 A 213 ARG ALA TRP SER GLN ILE ILE ASN ASP ILE ASN ASP ASN
SEQRES 12 A 213 LEU LEU ILE VAL THR HIS GLY GLY VAL ILE ARG ILE ILE
SEQRES 13 A 213 LEU ALA HIS VAL LEU GLY VAL ASP TRP ARG ASN PRO GLN
SEQRES 14 A 213 TRP TYR SER THR LEU ALA ILE GLY ASN ALA SER VAL THR
SEQRES 15 A 213 HIS ILE THR ILE THR ILE ASP ASP GLN ILE TYR ALA SER
SEQRES 16 A 213 VAL ARG SER ILE GLY VAL PRO LEU VAL GLU GLU GLY HIS
SEQRES 17 A 213 HIS HIS HIS HIS HIS
SEQRES 1 B 213 MET SER LEU LYS THR LEU ASN ILE TYR LEU MET ARG HIS
SEQRES 2 B 213 GLY LYS VAL ASP ALA ALA PRO GLY LEU HIS GLY GLN THR
SEQRES 3 B 213 ASP LEU LYS VAL LYS GLU ALA GLU GLN GLN GLN ILE ALA
SEQRES 4 B 213 MET ALA TRP LYS THR LYS GLY TYR ASP VAL ALA GLY ILE
SEQRES 5 B 213 ILE SER SER PRO LEU SER ARG CYS HIS ASP LEU ALA GLN
SEQRES 6 B 213 ILE LEU ALA GLU GLN GLN LEU LEU PRO MET THR THR GLU
SEQRES 7 B 213 ASP ASP LEU GLN GLU MET ASP PHE GLY ASP PHE ASP GLY
SEQRES 8 B 213 MET PRO PHE ASP LEU LEU THR GLU HIS TRP LYS LYS LEU
SEQRES 9 B 213 ASP ALA PHE TRP GLN SER PRO ALA HIS HIS SER LEU PRO
SEQRES 10 B 213 ASN ALA GLU SER LEU SER THR PHE SER GLN ARG VAL SER
SEQRES 11 B 213 ARG ALA TRP SER GLN ILE ILE ASN ASP ILE ASN ASP ASN
SEQRES 12 B 213 LEU LEU ILE VAL THR HIS GLY GLY VAL ILE ARG ILE ILE
SEQRES 13 B 213 LEU ALA HIS VAL LEU GLY VAL ASP TRP ARG ASN PRO GLN
SEQRES 14 B 213 TRP TYR SER THR LEU ALA ILE GLY ASN ALA SER VAL THR
SEQRES 15 B 213 HIS ILE THR ILE THR ILE ASP ASP GLN ILE TYR ALA SER
SEQRES 16 B 213 VAL ARG SER ILE GLY VAL PRO LEU VAL GLU GLU GLY HIS
SEQRES 17 B 213 HIS HIS HIS HIS HIS
HET SO4 A 212 5
HET SO4 B 212 5
HET SO4 B 213 5
HET SO4 B 214 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 4(O4 S 2-)
HELIX 1 1 LYS A 29 LYS A 43 1 15
HELIX 2 2 LEU A 55 LEU A 70 1 16
HELIX 3 3 ASP A 77 GLN A 80 5 4
HELIX 4 4 ASP A 93 HIS A 98 1 6
HELIX 5 5 LEU A 102 SER A 108 1 7
HELIX 6 6 PRO A 109 HIS A 112 5 4
HELIX 7 7 SER A 119 ILE A 138 1 20
HELIX 8 8 HIS A 147 LEU A 159 1 13
HELIX 9 9 PRO A 166 LEU A 172 1 7
HELIX 10 10 LEU B 20 GLY B 22 5 3
HELIX 11 11 LYS B 29 LYS B 43 1 15
HELIX 12 12 LEU B 55 GLN B 69 1 15
HELIX 13 13 SER B 119 ILE B 138 1 20
HELIX 14 14 HIS B 147 LEU B 159 1 13
HELIX 15 15 PRO B 166 THR B 171 1 6
SHEET 1 A 6 MET A 73 THR A 75 0
SHEET 2 A 6 ILE A 50 SER A 52 1 N SER A 52 O THR A 74
SHEET 3 A 6 LEU A 142 THR A 146 1 O LEU A 143 N ILE A 51
SHEET 4 A 6 THR A 3 ARG A 10 1 N TYR A 7 O ILE A 144
SHEET 5 A 6 SER A 178 ILE A 186 -1 O THR A 180 N LEU A 8
SHEET 6 A 6 ILE A 190 VAL A 194 -1 O TYR A 191 N THR A 185
SHEET 1 B 6 MET A 73 THR A 75 0
SHEET 2 B 6 ILE A 50 SER A 52 1 N SER A 52 O THR A 74
SHEET 3 B 6 LEU A 142 THR A 146 1 O LEU A 143 N ILE A 51
SHEET 4 B 6 THR A 3 ARG A 10 1 N TYR A 7 O ILE A 144
SHEET 5 B 6 SER A 178 ILE A 186 -1 O THR A 180 N LEU A 8
SHEET 6 B 6 VAL A 199 PRO A 200 -1 O VAL A 199 N VAL A 179
SHEET 1 C 6 MET B 73 THR B 75 0
SHEET 2 C 6 GLY B 49 SER B 52 1 N SER B 52 O THR B 74
SHEET 3 C 6 LEU B 142 THR B 146 1 O LEU B 143 N ILE B 51
SHEET 4 C 6 THR B 3 ARG B 10 1 N TYR B 7 O LEU B 142
SHEET 5 C 6 SER B 178 ILE B 186 -1 O ILE B 184 N LEU B 4
SHEET 6 C 6 ILE B 190 VAL B 194 -1 O SER B 193 N THR B 183
SHEET 1 D 6 MET B 73 THR B 75 0
SHEET 2 D 6 GLY B 49 SER B 52 1 N SER B 52 O THR B 74
SHEET 3 D 6 LEU B 142 THR B 146 1 O LEU B 143 N ILE B 51
SHEET 4 D 6 THR B 3 ARG B 10 1 N TYR B 7 O LEU B 142
SHEET 5 D 6 SER B 178 ILE B 186 -1 O ILE B 184 N LEU B 4
SHEET 6 D 6 VAL B 199 PRO B 200 -1 O VAL B 199 N VAL B 179
SHEET 1 E 2 VAL B 14 PRO B 18 0
SHEET 2 E 2 THR B 24 VAL B 28 -1 O ASP B 25 N ALA B 17
SITE 1 AC1 7 ARG A 10 HIS A 11 HIS A 21 ARG A 57
SITE 2 AC1 7 GLU A 81 HIS A 147 GLY A 148
SITE 1 AC2 2 ASP A 162 ASP B 162
SITE 1 AC3 3 HIS B 181 ARG B 195 SER B 196
SITE 1 AC4 6 ARG B 10 HIS B 11 ARG B 57 GLU B 81
SITE 2 AC4 6 HIS B 147 GLY B 148
CRYST1 107.215 107.215 206.717 90.00 90.00 90.00 P 41 21 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 0.009327 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009327 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004838 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
