HEADER PROTEIN TRANSPORT 12-MAY-03 1P9R
TITLE CRYSTAL STRUCTURE OF VIBRIO CHOLERAE PUTATIVE NTPASE EPSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GENERAL SECRETION PATHWAY PROTEIN E;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL TRUNCATION OF RESIDUES 1-90;
COMPND 5 SYNONYM: TYPE II TRAFFIC WARDEN ATPASE, CHOLERA TOXIN
COMPND 6 SECRETION PROTEIN EPSE;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;
SOURCE 3 ORGANISM_TAXID: 666;
SOURCE 4 GENE: EPSE OR VC2732;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: M15;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE70
KEYWDS BACTERIAL TYPE II SECRETION SYSTEM CYTOPLASMIC PROTEIN -
KEYWDS 2 GSPE, PUTATIVE ATPASE/ ATP BINDING PROTEIN, METALLOPROTEIN
KEYWDS 3 (METAL-CYS4 SITE), PROTEIN TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.ROBIEN,B.E.KRUMM,M.SANDKVIST,W.G.J.HOL
REVDAT 2 24-FEB-09 1P9R 1 VERSN
REVDAT 1 14-OCT-03 1P9R 0
JRNL AUTH M.A.ROBIEN,B.E.KRUMM,M.SANDKVIST,W.G.J.HOL
JRNL TITL CRYSTAL STRUCTURE OF THE EXTRACELLULAR PROTEIN
JRNL TITL 2 SECRETION NTPASE EPSE OF VIBRIO CHOLERAE
JRNL REF J.MOL.BIOL. V. 333 657 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 14556751
JRNL DOI 10.1016/J.JMB.2003.07.015
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 84.9
REMARK 3 NUMBER OF REFLECTIONS : 15262
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) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 808
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 804
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2150
REMARK 3 BIN FREE R VALUE SET COUNT : 47
REMARK 3 BIN FREE R VALUE : 0.2850
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2932
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 111
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 48.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.76000
REMARK 3 B22 (A**2) : 0.76000
REMARK 3 B33 (A**2) : -1.14000
REMARK 3 B12 (A**2) : 0.38000
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): 0.571
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.318
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.123
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.110
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.920
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2972 ; 0.011 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4005 ; 1.374 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 374 ; 6.155 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 475 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2171 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1276 ; 0.221 ; 0.200
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): 194 ; 0.164 ; 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): 68 ; 0.231 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 15 ; 0.168 ; 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): 1874 ; 1.657 ; 2.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3029 ; 3.125 ; 6.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1098 ; 4.223 ; 5.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 976 ; 6.127 ; 8.000
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 : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1P9R COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-03.
REMARK 100 THE RCSB ID CODE IS RCSB019185.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-AUG-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9748
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : KOHZU: DOUBLE CRYSTAL: SI(111)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM, ELVES
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18982
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 60.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 12.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 13.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.65300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE V. 2.02
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 200,3-
REMARK 280 MORPHOLINOPROPANESULFONATE, AMMONIUM ACETATE, AMP-PNP, PH 7.2,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.42033
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 110.84067
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 83.13050
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 138.55083
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 27.71017
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 55.42033
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 110.84067
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 138.55083
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 83.13050
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 27.71017
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 MSE A 91
REMARK 465 GLU A 92
REMARK 465 ASP A 93
REMARK 465 ILE A 94
REMARK 465 GLY A 95
REMARK 465 ALA A 96
REMARK 465 ASP A 97
REMARK 465 SER A 98
REMARK 465 ASP A 99
REMARK 465 LEU A 108
REMARK 465 PRO A 109
REMARK 465 GLN A 110
REMARK 465 ASN A 111
REMARK 465 GLU A 112
REMARK 465 ASP A 113
REMARK 465 LEU A 114
REMARK 465 LEU A 115
REMARK 465 GLU A 116
REMARK 465 SER A 117
REMARK 465 GLU A 118
REMARK 465 ASP A 119
REMARK 465 ASP A 120
REMARK 465 ARG A 201
REMARK 465 ILE A 202
REMARK 465 GLY A 203
REMARK 465 GLY A 204
REMARK 465 ARG A 205
REMARK 465 ASP A 415
REMARK 465 SER A 416
REMARK 465 LYS A 417
REMARK 465 LYS A 418
REMARK 465 LYS A 419
REMARK 465 ARG A 501
REMARK 465 SER A 502
REMARK 465 HIS A 503
REMARK 465 HIS A 504
REMARK 465 HIS A 505
REMARK 465 HIS A 506
REMARK 465 HIS A 507
REMARK 465 HIS A 508
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 ARG A 162 NE - CZ - NH2 ANGL. DEV. = -3.0 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 GLU A 148 -65.59 -19.70
REMARK 500 LYS A 184 62.29 61.53
REMARK 500 LEU A 226 88.48 44.03
REMARK 500 ASP A 300 103.90 82.56
REMARK 500 THR A 428 -102.16 59.94
REMARK 500 ASN A 434 -100.52 -138.55
REMARK 500 HIS A 435 104.95 -51.08
REMARK 500 LYS A 436 163.94 74.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 880 DISTANCE = 7.25 ANGSTROMS
REMARK 525 HOH A 886 DISTANCE = 5.56 ANGSTROMS
REMARK 525 HOH A 896 DISTANCE = 8.04 ANGSTROMS
REMARK 525 HOH A 900 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH A 902 DISTANCE = 5.42 ANGSTROMS
REMARK 525 HOH A 909 DISTANCE = 8.35 ANGSTROMS
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 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 397 SG
REMARK 620 2 CYS A 400 SG 113.9
REMARK 620 3 CYS A 430 SG 112.7 109.3
REMARK 620 4 CYS A 433 SG 117.1 87.1 113.9
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 601
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1P9R RELATED DB: PDB
REMARK 900 1P9R IS THE SAME PROTEIN WITH BOUND NUCLEOTIDE ANALOG
DBREF 1P9R A 91 498 UNP P37093 GSPE_VIBCH 91 498
SEQADV 1P9R MSE A 91 UNP P37093 MET 91 MODIFIED RESIDUE
SEQADV 1P9R MSE A 130 UNP P37093 MET 130 MODIFIED RESIDUE
SEQADV 1P9R MSE A 182 UNP P37093 MET 182 MODIFIED RESIDUE
SEQADV 1P9R MSE A 214 UNP P37093 MET 214 MODIFIED RESIDUE
SEQADV 1P9R MSE A 224 UNP P37093 MET 224 MODIFIED RESIDUE
SEQADV 1P9R MSE A 241 UNP P37093 MET 241 MODIFIED RESIDUE
SEQADV 1P9R MSE A 313 UNP P37093 MET 313 MODIFIED RESIDUE
SEQADV 1P9R MSE A 331 UNP P37093 MET 331 MODIFIED RESIDUE
SEQADV 1P9R MSE A 355 UNP P37093 MET 355 MODIFIED RESIDUE
SEQADV 1P9R MSE A 373 UNP P37093 MET 373 MODIFIED RESIDUE
SEQADV 1P9R MSE A 467 UNP P37093 MET 467 MODIFIED RESIDUE
SEQADV 1P9R MSE A 497 UNP P37093 MET 497 MODIFIED RESIDUE
SEQADV 1P9R GLY A 499 UNP P37093 EXPRESSION TAG
SEQADV 1P9R SER A 500 UNP P37093 EXPRESSION TAG
SEQADV 1P9R ARG A 501 UNP P37093 EXPRESSION TAG
SEQADV 1P9R SER A 502 UNP P37093 EXPRESSION TAG
SEQADV 1P9R HIS A 503 UNP P37093 EXPRESSION TAG
SEQADV 1P9R HIS A 504 UNP P37093 EXPRESSION TAG
SEQADV 1P9R HIS A 505 UNP P37093 EXPRESSION TAG
SEQADV 1P9R HIS A 506 UNP P37093 EXPRESSION TAG
SEQADV 1P9R HIS A 507 UNP P37093 EXPRESSION TAG
SEQADV 1P9R HIS A 508 UNP P37093 EXPRESSION TAG
SEQRES 1 A 418 MSE GLU ASP ILE GLY ALA ASP SER ASP ASP PHE PHE SER
SEQRES 2 A 418 LEU ALA GLU GLU LEU PRO GLN ASN GLU ASP LEU LEU GLU
SEQRES 3 A 418 SER GLU ASP ASP ALA PRO ILE ILE LYS LEU ILE ASN ALA
SEQRES 4 A 418 MSE LEU GLY GLU ALA ILE LYS GLU GLY ALA SER ASP ILE
SEQRES 5 A 418 HIS ILE GLU THR PHE GLU LYS THR LEU SER ILE ARG PHE
SEQRES 6 A 418 ARG VAL ASP GLY VAL LEU ARG GLU VAL LEU ALA PRO SER
SEQRES 7 A 418 ARG LYS LEU SER SER LEU LEU VAL SER ARG VAL LYS VAL
SEQRES 8 A 418 MSE ALA LYS LEU ASP ILE ALA GLU LYS ARG VAL PRO GLN
SEQRES 9 A 418 ASP GLY ARG ILE SER LEU ARG ILE GLY GLY ARG ALA VAL
SEQRES 10 A 418 ASP VAL ARG VAL SER THR MSE PRO SER SER HIS GLY GLU
SEQRES 11 A 418 ARG VAL VAL MSE ARG LEU LEU ASP LYS ASN ALA THR ARG
SEQRES 12 A 418 LEU ASP LEU HIS SER LEU GLY MSE THR ALA HIS ASN HIS
SEQRES 13 A 418 ASP ASN PHE ARG ARG LEU ILE LYS ARG PRO HIS GLY ILE
SEQRES 14 A 418 ILE LEU VAL THR GLY PRO THR GLY SER GLY LYS SER THR
SEQRES 15 A 418 THR LEU TYR ALA GLY LEU GLN GLU LEU ASN SER SER GLU
SEQRES 16 A 418 ARG ASN ILE LEU THR VAL GLU ASP PRO ILE GLU PHE ASP
SEQRES 17 A 418 ILE ASP GLY ILE GLY GLN THR GLN VAL ASN PRO ARG VAL
SEQRES 18 A 418 ASP MSE THR PHE ALA ARG GLY LEU ARG ALA ILE LEU ARG
SEQRES 19 A 418 GLN ASP PRO ASP VAL VAL MSE VAL GLY GLU ILE ARG ASP
SEQRES 20 A 418 LEU GLU THR ALA GLN ILE ALA VAL GLN ALA SER LEU THR
SEQRES 21 A 418 GLY HIS LEU VAL MSE SER THR LEU HIS THR ASN THR ALA
SEQRES 22 A 418 VAL GLY ALA VAL THR ARG LEU ARG ASP MSE GLY ILE GLU
SEQRES 23 A 418 PRO PHE LEU ILE SER SER SER LEU LEU GLY VAL LEU ALA
SEQRES 24 A 418 GLN ARG LEU VAL ARG THR LEU CYS PRO ASP CYS LYS GLU
SEQRES 25 A 418 PRO TYR GLU ALA ASP LYS GLU GLN ARG LYS LEU PHE ASP
SEQRES 26 A 418 SER LYS LYS LYS GLU PRO LEU ILE LEU TYR ARG ALA THR
SEQRES 27 A 418 GLY CYS PRO LYS CYS ASN HIS LYS GLY TYR ARG GLY ARG
SEQRES 28 A 418 THR GLY ILE HIS GLU LEU LEU LEU VAL ASP ASP ALA LEU
SEQRES 29 A 418 GLN GLU LEU ILE HIS SER GLU ALA GLY GLU GLN ALA MSE
SEQRES 30 A 418 GLU LYS HIS ILE ARG ALA THR THR PRO SER ILE ARG ASP
SEQRES 31 A 418 ASP GLY LEU ASP LYS VAL ARG GLN GLY ILE THR SER LEU
SEQRES 32 A 418 GLU GLU VAL MSE ARG GLY SER ARG SER HIS HIS HIS HIS
SEQRES 33 A 418 HIS HIS
MODRES 1P9R MSE A 130 MET SELENOMETHIONINE
MODRES 1P9R MSE A 182 MET SELENOMETHIONINE
MODRES 1P9R MSE A 214 MET SELENOMETHIONINE
MODRES 1P9R MSE A 224 MET SELENOMETHIONINE
MODRES 1P9R MSE A 241 MET SELENOMETHIONINE
MODRES 1P9R MSE A 313 MET SELENOMETHIONINE
MODRES 1P9R MSE A 331 MET SELENOMETHIONINE
MODRES 1P9R MSE A 355 MET SELENOMETHIONINE
MODRES 1P9R MSE A 373 MET SELENOMETHIONINE
MODRES 1P9R MSE A 467 MET SELENOMETHIONINE
MODRES 1P9R MSE A 497 MET SELENOMETHIONINE
HET MSE A 130 8
HET MSE A 182 8
HET MSE A 214 8
HET MSE A 224 8
HET MSE A 241 8
HET MSE A 313 8
HET MSE A 331 8
HET MSE A 355 8
HET MSE A 373 8
HET MSE A 467 8
HET MSE A 497 8
HET ZN A 601 1
HET CL A 602 1
HETNAM MSE SELENOMETHIONINE
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
FORMUL 1 MSE 11(C5 H11 N O2 SE)
FORMUL 2 ZN ZN 2+
FORMUL 3 CL CL 1-
FORMUL 4 HOH *111(H2 O)
HELIX 1 1 ASP A 100 GLU A 107 1 8
HELIX 2 2 ALA A 121 GLY A 138 1 18
HELIX 3 3 SER A 168 LYS A 170 5 3
HELIX 4 4 LEU A 171 ALA A 183 1 13
HELIX 5 5 ASP A 235 LEU A 239 5 5
HELIX 6 6 THR A 242 LYS A 254 1 13
HELIX 7 7 GLY A 269 ASN A 282 1 14
HELIX 8 8 ASN A 308 ASP A 312 5 5
HELIX 9 9 THR A 314 LEU A 323 1 10
HELIX 10 10 ARG A 324 ASP A 326 5 3
HELIX 11 11 ASP A 337 THR A 350 1 14
HELIX 12 12 ALA A 363 GLY A 374 1 12
HELIX 13 13 GLU A 376 SER A 383 1 8
HELIX 14 14 ASP A 407 LYS A 412 1 6
HELIX 15 15 ASP A 451 SER A 460 1 10
HELIX 16 16 GLY A 463 ALA A 473 1 11
HELIX 17 17 SER A 477 GLN A 488 1 12
HELIX 18 18 SER A 492 SER A 500 1 9
SHEET 1 A 6 VAL A 160 LEU A 165 0
SHEET 2 A 6 THR A 150 VAL A 157 -1 N ILE A 153 O VAL A 164
SHEET 3 A 6 ASP A 141 PHE A 147 -1 N PHE A 147 O THR A 150
SHEET 4 A 6 ARG A 221 MSE A 224 -1 O VAL A 222 N ILE A 144
SHEET 5 A 6 VAL A 207 MSE A 214 -1 N MSE A 214 O ARG A 221
SHEET 6 A 6 GLN A 194 SER A 199 -1 N ILE A 198 O VAL A 209
SHEET 1 B 6 VAL A 160 LEU A 165 0
SHEET 2 B 6 THR A 150 VAL A 157 -1 N ILE A 153 O VAL A 164
SHEET 3 B 6 ASP A 141 PHE A 147 -1 N PHE A 147 O THR A 150
SHEET 4 B 6 ARG A 221 MSE A 224 -1 O VAL A 222 N ILE A 144
SHEET 5 B 6 VAL A 207 MSE A 214 -1 N MSE A 214 O ARG A 221
SHEET 6 B 6 LEU A 227 ASP A 228 -1 O LEU A 227 N ASP A 208
SHEET 1 C 7 GLY A 303 GLN A 306 0
SHEET 2 C 7 ILE A 288 GLU A 292 1 N GLU A 292 O THR A 305
SHEET 3 C 7 VAL A 329 VAL A 332 1 O MSE A 331 N LEU A 289
SHEET 4 C 7 LEU A 353 LEU A 358 1 O LEU A 353 N VAL A 330
SHEET 5 C 7 GLY A 258 THR A 263 1 N ILE A 260 O VAL A 354
SHEET 6 C 7 LEU A 384 LEU A 396 1 O LEU A 388 N LEU A 261
SHEET 7 C 7 TYR A 438 LEU A 449 -1 O THR A 442 N VAL A 393
SHEET 1 D 2 GLU A 402 GLU A 405 0
SHEET 2 D 2 ILE A 423 ARG A 426 -1 O ARG A 426 N GLU A 402
LINK ZN ZN A 601 SG CYS A 397 1555 1555 2.31
LINK ZN ZN A 601 SG CYS A 400 1555 1555 2.33
LINK ZN ZN A 601 SG CYS A 430 1555 1555 2.34
LINK ZN ZN A 601 SG CYS A 433 1555 1555 2.33
LINK C ALA A 129 N MSE A 130 1555 1555 1.33
LINK C MSE A 130 N LEU A 131 1555 1555 1.33
LINK C VAL A 181 N MSE A 182 1555 1555 1.33
LINK C MSE A 182 N ALA A 183 1555 1555 1.33
LINK C THR A 213 N MSE A 214 1555 1555 1.33
LINK C MSE A 214 N PRO A 215 1555 1555 1.33
LINK C VAL A 223 N MSE A 224 1555 1555 1.33
LINK C MSE A 224 N ARG A 225 1555 1555 1.33
LINK C GLY A 240 N MSE A 241 1555 1555 1.33
LINK C MSE A 241 N THR A 242 1555 1555 1.33
LINK C ASP A 312 N MSE A 313 1555 1555 1.33
LINK C MSE A 313 N THR A 314 1555 1555 1.33
LINK C VAL A 330 N MSE A 331 1555 1555 1.33
LINK C MSE A 331 N VAL A 332 1555 1555 1.33
LINK C VAL A 354 N MSE A 355 1555 1555 1.33
LINK C MSE A 355 N SER A 356 1555 1555 1.33
LINK C ASP A 372 N MSE A 373 1555 1555 1.33
LINK C MSE A 373 N GLY A 374 1555 1555 1.33
LINK C ALA A 466 N MSE A 467 1555 1555 1.33
LINK C MSE A 467 N GLU A 468 1555 1555 1.33
LINK C VAL A 496 N MSE A 497 1555 1555 1.33
LINK C MSE A 497 N ARG A 498 1555 1555 1.33
CISPEP 1 ASP A 293 PRO A 294 0 -4.38
SITE 1 AC1 4 CYS A 397 CYS A 400 CYS A 430 CYS A 433
SITE 1 AC2 2 GLY A 269 LYS A 270
CRYST1 103.611 103.611 166.261 90.00 90.00 120.00 P 61 2 2 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 0.009651 0.005572 0.000000 0.00000
SCALE2 0.000000 0.011145 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006015 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
