HEADER OXIDOREDUCTASE 15-AUG-07 2QYT
TITLE CRYSTAL STRUCTURE OF 2-DEHYDROPANTOATE 2-REDUCTASE FROM PORPHYROMONAS
TITLE 2 GINGIVALIS W83
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-DEHYDROPANTOATE 2-REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PORPHYROMONAS GINGIVALIS;
SOURCE 3 ORGANISM_TAXID: 242619;
SOURCE 4 STRAIN: W83;
SOURCE 5 ATCC: BAA-308;
SOURCE 6 GENE: PANE, PG_2205;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS APC81190, 2-DEHYDROPANTOATE 2-REDUCTASE, PORPHYROMONAS GINGIVALIS
KEYWDS 2 W83, STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE,
KEYWDS 3 MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.TAN,R.WU,S.MOY,A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL GENOMICS
AUTHOR 2 (MCSG)
REVDAT 3 13-JUL-11 2QYT 1 VERSN
REVDAT 2 24-FEB-09 2QYT 1 VERSN
REVDAT 1 04-SEP-07 2QYT 0
JRNL AUTH K.TAN,R.WU,S.MOY,A.JOACHIMIAK
JRNL TITL THE CRYSTAL STRUCTURE OF 2-DEHYDROPANTOATE 2-REDUCTASE FROM
JRNL TITL 2 PORPHYROMONAS GINGIVALIS W83.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 16055
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 866
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) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 823
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 68.29
REMARK 3 BIN R VALUE (WORKING SET) : 0.2130
REMARK 3 BIN FREE R VALUE SET COUNT : 45
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2241
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 147
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 24.83
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.94000
REMARK 3 B22 (A**2) : -0.94000
REMARK 3 B33 (A**2) : 1.87000
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): 0.274
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.231
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.152
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.355
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.899
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2357 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3193 ; 1.748 ; 2.000
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 295 ; 6.688 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 100 ;32.654 ;22.700
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 409 ;19.520 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;19.216 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 360 ; 0.117 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1741 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1176 ; 0.232 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1598 ; 0.309 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 137 ; 0.175 ; 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): 64 ; 0.257 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.165 ; 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): 1489 ; 0.966 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2324 ; 1.486 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 991 ; 2.196 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 864 ; 3.288 ; 4.500
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 189
REMARK 3 ORIGIN FOR THE GROUP (A): 40.8870 21.3250 35.7410
REMARK 3 T TENSOR
REMARK 3 T11: -0.1434 T22: -0.1499
REMARK 3 T33: -0.3167 T12: -0.0149
REMARK 3 T13: 0.0009 T23: -0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 2.6513 L22: 1.0355
REMARK 3 L33: 1.9008 L12: -0.6739
REMARK 3 L13: -1.1241 L23: -0.0517
REMARK 3 S TENSOR
REMARK 3 S11: -0.0029 S12: 0.0292 S13: 0.0289
REMARK 3 S21: 0.0518 S22: 0.0498 S23: 0.0844
REMARK 3 S31: -0.1504 S32: -0.0694 S33: -0.0469
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 190 A 260
REMARK 3 RESIDUE RANGE : A 281 A 310
REMARK 3 ORIGIN FOR THE GROUP (A): 25.0250 21.8310 12.7870
REMARK 3 T TENSOR
REMARK 3 T11: 0.0350 T22: 0.3585
REMARK 3 T33: 0.0052 T12: -0.0660
REMARK 3 T13: 0.0129 T23: 0.0664
REMARK 3 L TENSOR
REMARK 3 L11: 6.3784 L22: 7.0298
REMARK 3 L33: 16.7711 L12: 2.4181
REMARK 3 L13: 8.1315 L23: 5.6380
REMARK 3 S TENSOR
REMARK 3 S11: -0.0658 S12: 0.1653 S13: -0.4713
REMARK 3 S21: -0.3506 S22: 0.0614 S23: 0.4173
REMARK 3 S31: -0.0611 S32: -0.6691 S33: 0.0045
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 2QYT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-AUG-07.
REMARK 100 THE RCSB ID CODE IS RCSB044215.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97925, 0.97938
REMARK 200 MONOCHROMATOR : SI 111 CRYSTAL
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16966
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 62.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.13200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 67.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.47500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: MLPHARE, HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULFATE, 0.1M MES, 30%
REMARK 280 PEG MME5000, PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 289K
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 49.13000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.78850
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.78850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 24.56500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.78850
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.78850
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 73.69500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.78850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.78850
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 24.56500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.78850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.78850
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 73.69500
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 49.13000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE PROGRAM GENERATED ASSEMBLY
REMARK 300 INFORMATION FOR THE STRUCTURE IN THIS ENTRY.
REMARK 300 AUTHORS STATE THAT THE BIOLOGICAL UNIT OF THIS
REMARK 300 PROTEIN IS EXPERIMENTALLY UNKNOWN.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MSE A 1
REMARK 465 ASN A 2
REMARK 465 GLN A 3
REMARK 465 PRO A 261
REMARK 465 PRO A 262
REMARK 465 GLU A 263
REMARK 465 SER A 264
REMARK 465 THR A 265
REMARK 465 SER A 266
REMARK 465 SER A 267
REMARK 465 MSE A 268
REMARK 465 HIS A 269
REMARK 465 SER A 270
REMARK 465 ASP A 271
REMARK 465 PHE A 272
REMARK 465 LEU A 273
REMARK 465 GLN A 274
REMARK 465 GLY A 275
REMARK 465 GLY A 276
REMARK 465 SER A 277
REMARK 465 THR A 278
REMARK 465 GLU A 279
REMARK 465 VAL A 280
REMARK 465 ARG A 311
REMARK 465 THR A 312
REMARK 465 ALA A 313
REMARK 465 ASN A 314
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 292 CD GLU A 292 OE2 0.086
REMARK 500
REMARK 500 REMARK: NULL
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 50 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 50 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 67 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 PRO A 246 C - N - CA ANGL. DEV. = 10.9 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 LEU A 13 52.87 -110.72
REMARK 500 ASP A 32 79.00 -102.10
REMARK 500 ASP A 118 33.44 -146.74
REMARK 500 SER A 140 79.65 -108.39
REMARK 500 GLN A 244 -89.91 -115.25
REMARK 500 VAL A 245 93.40 64.30
REMARK 500 PRO A 246 -152.22 -19.73
REMARK 500 THR A 284 -58.40 -124.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ARG A 295 24.3 L L OUTSIDE RANGE
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 315
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 316
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 317
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 318
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 319
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 320
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 322
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 323
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 324
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC81190 RELATED DB: TARGETDB
DBREF 2QYT A 1 314 UNP Q7MT04 Q7MT04_PORGI 1 314
SEQADV 2QYT SER A -2 UNP Q7MT04 EXPRESSION TAG
SEQADV 2QYT ASN A -1 UNP Q7MT04 EXPRESSION TAG
SEQADV 2QYT ALA A 0 UNP Q7MT04 EXPRESSION TAG
SEQRES 1 A 317 SER ASN ALA MSE ASN GLN GLN PRO ILE LYS ILE ALA VAL
SEQRES 2 A 317 PHE GLY LEU GLY GLY VAL GLY GLY TYR TYR GLY ALA MSE
SEQRES 3 A 317 LEU ALA LEU ARG ALA ALA ALA THR ASP GLY LEU LEU GLU
SEQRES 4 A 317 VAL SER TRP ILE ALA ARG GLY ALA HIS LEU GLU ALA ILE
SEQRES 5 A 317 ARG ALA ALA GLY GLY LEU ARG VAL VAL THR PRO SER ARG
SEQRES 6 A 317 ASP PHE LEU ALA ARG PRO THR CYS VAL THR ASP ASN PRO
SEQRES 7 A 317 ALA GLU VAL GLY THR VAL ASP TYR ILE LEU PHE CYS THR
SEQRES 8 A 317 LYS ASP TYR ASP MSE GLU ARG GLY VAL ALA GLU ILE ARG
SEQRES 9 A 317 PRO MSE ILE GLY GLN ASN THR LYS ILE LEU PRO LEU LEU
SEQRES 10 A 317 ASN GLY ALA ASP ILE ALA GLU ARG MSE ARG THR TYR LEU
SEQRES 11 A 317 PRO ASP THR VAL VAL TRP LYS GLY CYS VAL TYR ILE SER
SEQRES 12 A 317 ALA ARG LYS SER ALA PRO GLY LEU ILE THR LEU GLU ALA
SEQRES 13 A 317 ASP ARG GLU LEU PHE TYR PHE GLY SER GLY LEU PRO GLU
SEQRES 14 A 317 GLN THR ASP ASP GLU VAL ARG LEU ALA GLU LEU LEU THR
SEQRES 15 A 317 ALA ALA GLY ILE ARG ALA TYR ASN PRO THR ASP ILE ASP
SEQRES 16 A 317 TRP TYR ILE MSE LYS LYS PHE MSE MSE ILE SER VAL THR
SEQRES 17 A 317 ALA THR ALA THR ALA TYR PHE ASP LYS PRO ILE GLY SER
SEQRES 18 A 317 ILE LEU THR GLU HIS GLU PRO GLU LEU LEU SER LEU LEU
SEQRES 19 A 317 GLU GLU VAL ALA GLU LEU PHE ARG ALA LYS TYR GLY GLN
SEQRES 20 A 317 VAL PRO ASP ASP VAL VAL GLN GLN LEU LEU ASP LYS GLN
SEQRES 21 A 317 ARG LYS MSE PRO PRO GLU SER THR SER SER MSE HIS SER
SEQRES 22 A 317 ASP PHE LEU GLN GLY GLY SER THR GLU VAL GLU THR LEU
SEQRES 23 A 317 THR GLY TYR VAL VAL ARG GLU ALA GLU ALA LEU ARG VAL
SEQRES 24 A 317 ASP LEU PRO MSE TYR LYS ARG MSE TYR ARG GLU LEU VAL
SEQRES 25 A 317 SER ARG THR ALA ASN
MODRES 2QYT MSE A 23 MET SELENOMETHIONINE
MODRES 2QYT MSE A 93 MET SELENOMETHIONINE
MODRES 2QYT MSE A 103 MET SELENOMETHIONINE
MODRES 2QYT MSE A 123 MET SELENOMETHIONINE
MODRES 2QYT MSE A 196 MET SELENOMETHIONINE
MODRES 2QYT MSE A 200 MET SELENOMETHIONINE
MODRES 2QYT MSE A 201 MET SELENOMETHIONINE
MODRES 2QYT MSE A 260 MET SELENOMETHIONINE
MODRES 2QYT MSE A 300 MET SELENOMETHIONINE
MODRES 2QYT MSE A 304 MET SELENOMETHIONINE
HET MSE A 23 8
HET MSE A 93 8
HET MSE A 103 8
HET MSE A 123 8
HET MSE A 196 13
HET MSE A 200 8
HET MSE A 201 13
HET MSE A 260 8
HET MSE A 300 8
HET MSE A 304 8
HET SO4 A 315 5
HET SO4 A 316 5
HET SO4 A 317 5
HET SO4 A 318 5
HET SO4 A 319 5
HET EDO A 320 4
HET EDO A 321 4
HET EDO A 322 4
HET EDO A 323 4
HET EDO A 324 4
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 10(C5 H11 N O2 SE)
FORMUL 2 SO4 5(O4 S 2-)
FORMUL 7 EDO 5(C2 H6 O2)
FORMUL 12 HOH *147(H2 O)
HELIX 1 1 GLY A 14 THR A 31 1 18
HELIX 2 2 ARG A 42 GLY A 53 1 12
HELIX 3 3 ASN A 74 GLY A 79 1 6
HELIX 4 4 ASP A 92 ARG A 101 1 10
HELIX 5 5 ASP A 118 ARG A 124 1 7
HELIX 6 6 THR A 168 ALA A 181 1 14
HELIX 7 7 ASP A 190 ASP A 213 1 24
HELIX 8 8 PRO A 215 HIS A 223 1 9
HELIX 9 9 HIS A 223 TYR A 242 1 20
HELIX 10 10 ASP A 248 MSE A 260 1 13
HELIX 11 11 THR A 284 LEU A 294 1 11
HELIX 12 12 LEU A 298 GLU A 307 1 10
SHEET 1 A 5 CYS A 70 THR A 72 0
SHEET 2 A 5 LEU A 35 ILE A 40 1 N TRP A 39 O THR A 72
SHEET 3 A 5 ILE A 6 PHE A 11 1 N VAL A 10 O ILE A 40
SHEET 4 A 5 VAL A 81 PHE A 86 1 O LEU A 85 N ALA A 9
SHEET 5 A 5 ILE A 104 PRO A 112 1 O LEU A 111 N ILE A 84
SHEET 1 B 4 ASP A 63 ALA A 66 0
SHEET 2 B 4 LEU A 55 VAL A 58 -1 N LEU A 55 O ALA A 66
SHEET 3 B 4 LEU A 148 LEU A 151 1 O ILE A 149 N ARG A 56
SHEET 4 B 4 ALA A 141 ALA A 145 -1 N ARG A 142 O THR A 150
SHEET 1 C 3 LYS A 134 TYR A 138 0
SHEET 2 C 3 LEU A 157 GLY A 161 -1 O GLY A 161 N LYS A 134
SHEET 3 C 3 ALA A 185 TYR A 186 1 O TYR A 186 N PHE A 158
LINK C ALA A 22 N MSE A 23 1555 1555 1.33
LINK C MSE A 23 N LEU A 24 1555 1555 1.33
LINK C ASP A 92 N MSE A 93 1555 1555 1.33
LINK C MSE A 93 N GLU A 94 1555 1555 1.33
LINK C PRO A 102 N MSE A 103 1555 1555 1.33
LINK C MSE A 103 N ILE A 104 1555 1555 1.33
LINK C ARG A 122 N MSE A 123 1555 1555 1.33
LINK C MSE A 123 N ARG A 124 1555 1555 1.33
LINK C ILE A 195 N MSE A 196 1555 1555 1.33
LINK C MSE A 196 N LYS A 197 1555 1555 1.33
LINK C PHE A 199 N MSE A 200 1555 1555 1.33
LINK C MSE A 200 N MSE A 201 1555 1555 1.34
LINK C MSE A 201 N ILE A 202 1555 1555 1.33
LINK C LYS A 259 N MSE A 260 1555 1555 1.35
LINK C PRO A 299 N MSE A 300 1555 1555 1.33
LINK C MSE A 300 N TYR A 301 1555 1555 1.34
LINK C ARG A 303 N MSE A 304 1555 1555 1.33
LINK C MSE A 304 N TYR A 305 1555 1555 1.33
SITE 1 AC1 9 GLY A 15 LYS A 89 ALA A 141 ARG A 142
SITE 2 AC1 9 LYS A 143 SO4 A 318 EDO A 320 HOH A 443
SITE 3 AC1 9 HOH A 444
SITE 1 AC2 8 LEU A 13 ALA A 41 ARG A 42 HIS A 45
SITE 2 AC2 8 LYS A 143 SO4 A 318 HOH A 365 HOH A 393
SITE 1 AC3 6 ASP A 32 GLU A 281 THR A 282 GLY A 285
SITE 2 AC3 6 ARG A 289 TYR A 305
SITE 1 AC4 10 GLY A 12 LEU A 13 GLY A 14 CYS A 87
SITE 2 AC4 10 THR A 88 ASP A 90 SO4 A 315 SO4 A 316
SITE 3 AC4 10 EDO A 320 HOH A 443
SITE 1 AC5 4 TYR A 186 ASN A 187 EDO A 324 HOH A 459
SITE 1 AC6 8 GLY A 12 GLY A 14 GLY A 15 VAL A 16
SITE 2 AC6 8 GLY A 17 CYS A 87 SO4 A 315 SO4 A 318
SITE 1 AC7 4 THR A 80 GLY A 105 GLN A 106 THR A 130
SITE 1 AC8 3 ALA A 293 ARG A 295 HOH A 440
SITE 1 AC9 6 TYR A 19 ARG A 62 ASP A 154 GLU A 156
SITE 2 AC9 6 ARG A 184 HOH A 471
SITE 1 BC1 5 TYR A 186 ASN A 187 PRO A 188 TYR A 194
SITE 2 BC1 5 SO4 A 319
CRYST1 79.577 79.577 98.260 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 0.012566 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012566 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010177 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
