HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 16-MAR-09 3GN3
TITLE CRYSTAL STRUCTURE OF A PUTATIVE PROTEIN-DISULFIDE ISOMERASE FROM
TITLE 2 PSEUDOMONAS SYRINGAE TO 2.5A RESOLUTION.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE PROTEIN-DISULFIDE ISOMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS SYRINGAE PV. TOMATO;
SOURCE 3 ORGANISM_TAXID: 323;
SOURCE 4 STRAIN: PV. TOMATO DC3000;
SOURCE 5 GENE: PSPTO4780, PSPTO_4780;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG19
KEYWDS DISULFIDE, ISOMERASE, PSEUDOMONAS, MCSG, PSI, STRUCTURAL GENOMICS,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.J.STEIN,G.CHHOR,L.FREEMAN,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (MCSG)
REVDAT 3 21-FEB-24 3GN3 1 REMARK
REVDAT 2 13-JUL-11 3GN3 1 VERSN
REVDAT 1 31-MAR-09 3GN3 0
JRNL AUTH A.J.STEIN,G.CHHOR,L.FREEMAN,A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF A PUTATIVE PROTEIN-DISULFIDE ISOMERASE
JRNL TITL 2 FROM PSEUDOMONAS SYRINGAE TO 2.5A RESOLUTION.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0054
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 26297
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) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1393
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) : 2.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1890
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.16
REMARK 3 BIN R VALUE (WORKING SET) : 0.3060
REMARK 3 BIN FREE R VALUE SET COUNT : 89
REMARK 3 BIN FREE R VALUE : 0.3340
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2762
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 17
REMARK 3 SOLVENT ATOMS : 93
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.19000
REMARK 3 B22 (A**2) : 0.19000
REMARK 3 B33 (A**2) : -0.28000
REMARK 3 B12 (A**2) : 0.09000
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): 0.231
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.199
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.141
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.494
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2852 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3870 ; 1.352 ; 1.935
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 356 ; 5.956 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 128 ;37.289 ;23.594
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 442 ;17.312 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;19.194 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 416 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2192 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1780 ; 0.533 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2850 ; 1.063 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1072 ; 1.853 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1020 ; 3.096 ; 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 : 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 3GN3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAR-09.
REMARK 100 THE DEPOSITION ID IS D_1000052066.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-MAR-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97974
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM Q215R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27721
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.14200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.0000
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) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.74600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000, MLPHARE, SHELX, DM
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.5, 2M AMMONIUM
REMARK 280 SULFATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
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 38.63133
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 77.26267
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 57.94700
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 96.57833
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 19.31567
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 38.63133
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 77.26267
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 96.57833
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 57.94700
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 19.31567
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: ASYMMETRIC UNIT IS A DIMER
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -89.0 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 350 BIOMT1 2 0.500000 -0.866025 0.000000 75.98400
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 131.60815
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -19.31567
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 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 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
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 GLU A 74 CG CD OE1 OE2
REMARK 470 GLU A 97 CG CD OE1 OE2
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 ASP A 4 27.27 -140.51
REMARK 500 HIS A 10 18.16 -143.33
REMARK 500 PHE A 31 1.18 -62.55
REMARK 500 LEU A 73 170.54 -57.16
REMARK 500 ALA A 100 -46.14 -136.94
REMARK 500 HIS A 150 -61.20 -135.62
REMARK 500 SER B 3 8.12 -57.87
REMARK 500 LEU B 6 60.08 -119.86
REMARK 500 HIS B 10 15.14 -149.33
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 180
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 181
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 180
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC61705 RELATED DB: TARGETDB
DBREF 3GN3 A 1 179 UNP Q87W03 Q87W03_PSESM 1 179
DBREF 3GN3 B 1 179 UNP Q87W03 Q87W03_PSESM 1 179
SEQADV 3GN3 SER A -2 UNP Q87W03 EXPRESSION TAG
SEQADV 3GN3 ASN A -1 UNP Q87W03 EXPRESSION TAG
SEQADV 3GN3 ALA A 0 UNP Q87W03 EXPRESSION TAG
SEQADV 3GN3 SER B -2 UNP Q87W03 EXPRESSION TAG
SEQADV 3GN3 ASN B -1 UNP Q87W03 EXPRESSION TAG
SEQADV 3GN3 ALA B 0 UNP Q87W03 EXPRESSION TAG
SEQRES 1 A 182 SER ASN ALA MET HIS SER ASP ALA LEU SER TRP GLY HIS
SEQRES 2 A 182 GLY PRO ARG LEU PHE GLU VAL PHE LEU GLU PRO THR CYS
SEQRES 3 A 182 PRO PHE SER VAL LYS ALA PHE PHE LYS LEU ASP ASP LEU
SEQRES 4 A 182 LEU ALA GLN ALA GLY GLU ASP ASN VAL THR VAL ARG ILE
SEQRES 5 A 182 ARG LEU GLN SER GLN PRO TRP HIS MET PHE SER GLY VAL
SEQRES 6 A 182 ILE VAL ARG CYS ILE LEU ALA ALA ALA THR LEU GLU GLY
SEQRES 7 A 182 GLY LYS GLU SER ALA LYS ALA VAL MET THR ALA VAL ALA
SEQRES 8 A 182 SER HIS ARG GLU GLU PHE GLU PHE GLU HIS HIS ALA GLY
SEQRES 9 A 182 GLY PRO ASN LEU ASP ALA THR PRO ASN ASP ILE ILE ALA
SEQRES 10 A 182 ARG ILE GLU ARG TYR SER GLY LEU ALA LEU ALA GLU ALA
SEQRES 11 A 182 PHE ALA ASN PRO GLU LEU GLU HIS ALA VAL LYS TRP HIS
SEQRES 12 A 182 THR LYS TYR ALA ARG GLN ASN GLY ILE HIS VAL SER PRO
SEQRES 13 A 182 THR PHE MET ILE ASN GLY LEU VAL GLN PRO GLY MET SER
SEQRES 14 A 182 SER GLY ASP PRO VAL SER LYS TRP VAL SER ASP ILE GLY
SEQRES 1 B 182 SER ASN ALA MET HIS SER ASP ALA LEU SER TRP GLY HIS
SEQRES 2 B 182 GLY PRO ARG LEU PHE GLU VAL PHE LEU GLU PRO THR CYS
SEQRES 3 B 182 PRO PHE SER VAL LYS ALA PHE PHE LYS LEU ASP ASP LEU
SEQRES 4 B 182 LEU ALA GLN ALA GLY GLU ASP ASN VAL THR VAL ARG ILE
SEQRES 5 B 182 ARG LEU GLN SER GLN PRO TRP HIS MET PHE SER GLY VAL
SEQRES 6 B 182 ILE VAL ARG CYS ILE LEU ALA ALA ALA THR LEU GLU GLY
SEQRES 7 B 182 GLY LYS GLU SER ALA LYS ALA VAL MET THR ALA VAL ALA
SEQRES 8 B 182 SER HIS ARG GLU GLU PHE GLU PHE GLU HIS HIS ALA GLY
SEQRES 9 B 182 GLY PRO ASN LEU ASP ALA THR PRO ASN ASP ILE ILE ALA
SEQRES 10 B 182 ARG ILE GLU ARG TYR SER GLY LEU ALA LEU ALA GLU ALA
SEQRES 11 B 182 PHE ALA ASN PRO GLU LEU GLU HIS ALA VAL LYS TRP HIS
SEQRES 12 B 182 THR LYS TYR ALA ARG GLN ASN GLY ILE HIS VAL SER PRO
SEQRES 13 B 182 THR PHE MET ILE ASN GLY LEU VAL GLN PRO GLY MET SER
SEQRES 14 B 182 SER GLY ASP PRO VAL SER LYS TRP VAL SER ASP ILE GLY
HET SO4 A 180 5
HET GOL A 181 6
HET GOL B 180 6
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 SO4 O4 S 2-
FORMUL 4 GOL 2(C3 H8 O3)
FORMUL 6 HOH *93(H2 O)
HELIX 1 1 MET A 1 ALA A 5 5 5
HELIX 2 2 CYS A 23 PHE A 31 1 9
HELIX 3 3 LYS A 32 GLY A 41 1 10
HELIX 4 4 PHE A 59 ALA A 71 1 13
HELIX 5 5 GLY A 75 HIS A 90 1 16
HELIX 6 6 ARG A 91 GLU A 95 5 5
HELIX 7 7 PHE A 96 ALA A 100 5 5
HELIX 8 8 GLY A 102 ALA A 107 5 6
HELIX 9 9 THR A 108 GLY A 121 1 14
HELIX 10 10 LEU A 124 ASN A 130 1 7
HELIX 11 11 LEU A 133 GLY A 148 1 16
HELIX 12 12 PRO A 170 GLY A 179 1 10
HELIX 13 13 CYS B 23 PHE B 31 1 9
HELIX 14 14 LYS B 32 GLY B 41 1 10
HELIX 15 15 PHE B 59 ALA B 71 1 13
HELIX 16 16 GLY B 76 HIS B 90 1 15
HELIX 17 17 ARG B 91 GLU B 95 5 5
HELIX 18 18 PHE B 96 ALA B 100 5 5
HELIX 19 19 GLY B 102 ALA B 107 5 6
HELIX 20 20 THR B 108 GLY B 121 1 14
HELIX 21 21 LEU B 124 ALA B 129 1 6
HELIX 22 22 ASN B 130 GLU B 132 5 3
HELIX 23 23 LEU B 133 ASN B 147 1 15
HELIX 24 24 PRO B 170 GLY B 179 1 10
SHEET 1 A 5 SER A 7 GLY A 9 0
SHEET 2 A 5 VAL A 45 LEU A 51 -1 O VAL A 47 N TRP A 8
SHEET 3 A 5 ARG A 13 LEU A 19 1 N PHE A 15 O THR A 46
SHEET 4 A 5 THR A 154 ILE A 157 -1 O MET A 156 N GLU A 16
SHEET 5 A 5 LEU A 160 VAL A 161 -1 O LEU A 160 N ILE A 157
SHEET 1 B 5 SER B 7 GLY B 9 0
SHEET 2 B 5 VAL B 45 LEU B 51 -1 O VAL B 47 N TRP B 8
SHEET 3 B 5 ARG B 13 LEU B 19 1 N VAL B 17 O ARG B 50
SHEET 4 B 5 THR B 154 ILE B 157 -1 O MET B 156 N GLU B 16
SHEET 5 B 5 LEU B 160 VAL B 161 -1 O LEU B 160 N ILE B 157
CISPEP 1 SER A 152 PRO A 153 0 -1.94
CISPEP 2 SER B 152 PRO B 153 0 -5.23
SITE 1 AC1 5 PHE A 25 PRO A 153 SER A 166 SER A 167
SITE 2 AC1 5 HOH A 215
SITE 1 AC2 6 GLY A 148 ILE A 149 HIS A 150 VAL A 151
SITE 2 AC2 6 THR A 154 HOH A 199
SITE 1 AC3 5 ILE B 149 HIS B 150 VAL B 151 THR B 154
SITE 2 AC3 5 HOH B 205
CRYST1 151.968 151.968 115.894 90.00 90.00 120.00 P 61 2 2 24
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 0.006580 0.003799 0.000000 0.00000
SCALE2 0.000000 0.007598 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008629 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
