HEADER TRANSFERASE 12-MAY-08 3D3U
TITLE CRYSTAL STRUCTURE OF 4-HYDROXYBUTYRATE COA-TRANSFERASE (ABFT-2) FROM
TITLE 2 PORPHYROMONAS GINGIVALIS. NORTHEAST STRUCTURAL GENOMICS CONSORTIUM
TITLE 3 TARGET PGR26
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 4-HYDROXYBUTYRATE COA-TRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: 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: ABFT-2, PG_1956;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21
KEYWDS ALPHA-BETA PROTEIN, STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG,
KEYWDS 3 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.FOROUHAR,H.NEELY,X.-Z.ZHANG,W.N.PRICE II,M.HUSSAIN,J.SEETHARAMAN,
AUTHOR 2 R.XIAO,K.CONOVER,K.CUNNINGHAM,L.-C.MA,C.K.HO,J.K.EVERETT,T.B.ACTON,
AUTHOR 3 G.T.MONTELIONE,J.F.HUNT,L.TONG,NORTHEAST STRUCTURAL GENOMICS
AUTHOR 4 CONSORTIUM (NESG)
REVDAT 5 24-JAN-18 3D3U 1 AUTHOR JRNL
REVDAT 4 25-OCT-17 3D3U 1 REMARK
REVDAT 3 13-JUL-11 3D3U 1 VERSN
REVDAT 2 24-FEB-09 3D3U 1 VERSN
REVDAT 1 15-JUL-08 3D3U 0
JRNL AUTH F.FOROUHAR,H.NEELY,X.-Z.ZHANG,W.N.PRICE II,M.HUSSAIN,
JRNL AUTH 2 J.SEETHARAMAN,R.XIAO,K.CONOVER,K.CUNNINGHAM,L.-C.MA,C.K.HO,
JRNL AUTH 3 J.K.EVERETT,T.B.ACTON,G.T.MONTELIONE,J.F.HUNT,L.TONG
JRNL TITL CRYSTAL STRUCTURE OF 4-HYDROXYBUTYRATE COA-TRANSFERASE
JRNL TITL 2 (ABFT-2) FROM PORPHYROMONAS GINGIVALIS.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0003
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.35
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 10089
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 505
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) : 648
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2340
REMARK 3 BIN FREE R VALUE SET COUNT : 34
REMARK 3 BIN FREE R VALUE : 0.3320
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3018
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 20
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 28.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.43000
REMARK 3 B22 (A**2) : -1.98000
REMARK 3 B33 (A**2) : 0.55000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.406
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.302
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 34.071
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.923
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.880
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3077 ; 0.033 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4157 ; 2.806 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 382 ; 7.975 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 141 ;40.745 ;23.688
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 534 ;25.220 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;16.766 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 465 ; 0.177 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2327 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1633 ; 0.299 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2105 ; 0.350 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 104 ; 0.198 ; 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): 17 ; 0.340 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.121 ; 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): 1973 ; 1.219 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3104 ; 2.075 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1229 ; 3.575 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1053 ; 5.599 ; 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 : 1
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 2 A 430
REMARK 3 ORIGIN FOR THE GROUP (A): 13.3542 5.1715 15.1827
REMARK 3 T TENSOR
REMARK 3 T11: -0.0329 T22: 0.0237
REMARK 3 T33: -0.0019 T12: 0.0121
REMARK 3 T13: 0.0016 T23: -0.0304
REMARK 3 L TENSOR
REMARK 3 L11: 0.6884 L22: 1.3709
REMARK 3 L33: 1.4346 L12: 0.3462
REMARK 3 L13: -0.1697 L23: -1.1791
REMARK 3 S TENSOR
REMARK 3 S11: -0.0297 S12: 0.0584 S13: -0.1483
REMARK 3 S21: -0.0810 S22: 0.0072 S23: -0.0954
REMARK 3 S31: 0.1341 S32: -0.0506 S33: 0.0225
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: THE FRIEDEL PAIRS WERE USED IN PHASING.
REMARK 3 PROGRAM CNS 1.2 HAS ALSO BEEN USED IN REFINEMENT
REMARK 4
REMARK 4 3D3U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAY-08.
REMARK 100 THE DEPOSITION ID IS D_1000047557.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-APR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97900
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21251
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 29.350
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.11200
REMARK 200 R SYM (I) : 0.09700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.35400
REMARK 200 R SYM FOR SHELL (I) : 0.32400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.250
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SNB, SOLVE, RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: THE STRUCTURE FACTOR FILE CONTAINS FRIEDEL PAIRS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 20 MM TRIS-HCL PH
REMARK 280 7.5, 100 MM NACL, 5 MM ACETYL-COA. RESERVOIR SOLUTION: 200 MM
REMARK 280 AMMONIUM CITRATE PH 5.0, 20% PEG 3350, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 27.34200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.75200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.63950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 46.75200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.34200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.63950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 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 MET A 1
REMARK 465 ASN A 81
REMARK 465 PHE A 82
REMARK 465 LEU A 83
REMARK 465 GLU A 84
REMARK 465 GLY A 85
REMARK 465 ASN A 86
REMARK 465 SER A 87
REMARK 465 ARG A 88
REMARK 465 PRO A 89
REMARK 465 ALA A 90
REMARK 465 SER A 91
REMARK 465 ARG A 92
REMARK 465 ASP A 93
REMARK 465 ARG A 94
REMARK 465 ARG A 95
REMARK 465 VAL A 96
REMARK 465 ASP A 97
REMARK 465 PHE A 98
REMARK 465 ILE A 99
REMARK 465 PRO A 100
REMARK 465 PRO A 190
REMARK 465 ALA A 191
REMARK 465 ALA A 323
REMARK 465 SER A 324
REMARK 465 GLU A 325
REMARK 465 SER A 326
REMARK 465 ILE A 327
REMARK 465 GLY A 328
REMARK 465 TYR A 329
REMARK 465 GLU A 330
REMARK 465 GLN A 331
REMARK 465 PHE A 332
REMARK 465 SER A 333
REMARK 465 GLY A 334
REMARK 465 SER A 335
REMARK 465 GLY A 336
REMARK 465 GLU A 375
REMARK 465 GLY A 376
REMARK 465 ALA A 377
REMARK 465 CYS A 378
REMARK 465 VAL A 379
REMARK 465 THR A 380
REMARK 465 GLU A 431
REMARK 465 LEU A 432
REMARK 465 GLU A 433
REMARK 465 HIS A 434
REMARK 465 HIS A 435
REMARK 465 HIS A 436
REMARK 465 HIS A 437
REMARK 465 HIS A 438
REMARK 465 HIS A 439
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 VAL A 11 CB VAL A 11 CG1 -0.137
REMARK 500 TYR A 61 CB TYR A 61 CG 0.121
REMARK 500 TYR A 61 CG TYR A 61 CD2 0.093
REMARK 500 TYR A 61 CG TYR A 61 CD1 0.083
REMARK 500 TYR A 61 CD1 TYR A 61 CE1 0.138
REMARK 500 TYR A 61 CE2 TYR A 61 CD2 0.117
REMARK 500 GLY A 63 N GLY A 63 CA 0.124
REMARK 500 ALA A 65 CA ALA A 65 CB 0.181
REMARK 500 PHE A 115 CE1 PHE A 115 CZ 0.128
REMARK 500 TYR A 141 CZ TYR A 141 CE2 -0.079
REMARK 500 GLU A 182 CG GLU A 182 CD 0.096
REMARK 500 GLU A 182 CD GLU A 182 OE1 0.069
REMARK 500 PRO A 189 N PRO A 189 CA 0.102
REMARK 500 LYS A 346 CB LYS A 346 CG 0.177
REMARK 500 MET A 355 CG MET A 355 SD 0.166
REMARK 500 PHE A 357 CZ PHE A 357 CE2 0.135
REMARK 500 GLU A 392 CD GLU A 392 OE1 0.088
REMARK 500 ARG A 399 CG ARG A 399 CD 0.177
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 LEU A 6 CB - CG - CD1 ANGL. DEV. = -13.4 DEGREES
REMARK 500 ASP A 15 CB - CG - OD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ASP A 20 CB - CG - OD2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 ARG A 46 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 HIS A 67 CB - CA - C ANGL. DEV. = -15.6 DEGREES
REMARK 500 GLU A 71 OE1 - CD - OE2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 CYS A 101 CA - CB - SG ANGL. DEV. = -13.0 DEGREES
REMARK 500 LEU A 109 CB - CG - CD2 ANGL. DEV. = -11.1 DEGREES
REMARK 500 ASP A 181 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 LEU A 188 CA - CB - CG ANGL. DEV. = 14.3 DEGREES
REMARK 500 ASP A 209 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 LEU A 225 CB - CG - CD2 ANGL. DEV. = -12.2 DEGREES
REMARK 500 ARG A 226 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ASP A 293 CB - CG - OD2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 LEU A 314 CB - CG - CD2 ANGL. DEV. = 10.9 DEGREES
REMARK 500 ARG A 343 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 MET A 355 CG - SD - CE ANGL. DEV. = 10.8 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 22 69.76 -112.00
REMARK 500 PRO A 24 143.42 -39.75
REMARK 500 ALA A 33 -118.71 81.17
REMARK 500 GLU A 52 -102.35 -104.61
REMARK 500 ASN A 53 69.59 -102.79
REMARK 500 HIS A 58 -171.64 -170.96
REMARK 500 MET A 59 -108.80 -138.45
REMARK 500 ASP A 64 67.34 -31.77
REMARK 500 ALA A 65 -80.72 -71.39
REMARK 500 PRO A 66 79.87 -41.27
REMARK 500 HIS A 67 -34.63 -152.47
REMARK 500 SER A 74 -6.54 79.98
REMARK 500 PHE A 103 -45.86 -29.44
REMARK 500 ARG A 111 22.99 -77.45
REMARK 500 GLN A 112 -6.14 -159.53
REMARK 500 PRO A 116 69.69 -67.38
REMARK 500 ASN A 128 -167.57 -111.67
REMARK 500 ASP A 140 -102.08 12.77
REMARK 500 GLU A 182 130.21 178.05
REMARK 500 ALA A 185 140.46 -32.02
REMARK 500 SER A 193 161.67 147.51
REMARK 500 ASP A 194 -91.37 -35.98
REMARK 500 HIS A 237 79.95 -152.60
REMARK 500 THR A 242 -160.08 -122.44
REMARK 500 ASN A 255 -7.77 -144.61
REMARK 500 LYS A 259 127.34 -29.82
REMARK 500 ASP A 293 21.65 -70.68
REMARK 500 TYR A 294 -59.37 -142.89
REMARK 500 LEU A 318 10.87 -60.11
REMARK 500 ASN A 384 41.74 -43.42
REMARK 500 GLU A 385 -70.69 -122.02
REMARK 500 GLU A 392 -19.69 -42.52
REMARK 500 LEU A 403 -52.94 -23.77
REMARK 500 ARG A 429 6.70 176.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: PGR26 RELATED DB: TARGETDB
DBREF 3D3U A 1 431 UNP Q7MTJ6 Q7MTJ6_PORGI 1 431
SEQADV 3D3U GLY A 192 UNP Q7MTJ6 ILE 192 EXPRESSION TAG
SEQADV 3D3U LEU A 432 UNP Q7MTJ6 EXPRESSION TAG
SEQADV 3D3U GLU A 433 UNP Q7MTJ6 EXPRESSION TAG
SEQADV 3D3U HIS A 434 UNP Q7MTJ6 EXPRESSION TAG
SEQADV 3D3U HIS A 435 UNP Q7MTJ6 EXPRESSION TAG
SEQADV 3D3U HIS A 436 UNP Q7MTJ6 EXPRESSION TAG
SEQADV 3D3U HIS A 437 UNP Q7MTJ6 EXPRESSION TAG
SEQADV 3D3U HIS A 438 UNP Q7MTJ6 EXPRESSION TAG
SEQADV 3D3U HIS A 439 UNP Q7MTJ6 EXPRESSION TAG
SEQRES 1 A 439 MET GLN TRP GLN GLU LEU TYR ARG GLN ARG VAL CYS SER
SEQRES 2 A 439 ALA ASP GLU ALA VAL VAL ASP SER LEU LYS PRO GLY THR
SEQRES 3 A 439 LYS VAL VAL PHE GLY HIS ALA ALA ALA ALA PRO VAL ARG
SEQRES 4 A 439 PHE SER GLN ALA MET TYR ARG GLN ARG GLU LYS LEU GLU
SEQRES 5 A 439 ASN ILE THR VAL PHE HIS MET LEU TYR PHE GLY ASP ALA
SEQRES 6 A 439 PRO HIS LEU ALA PRO GLU MET ARG SER HIS VAL HIS PRO
SEQRES 7 A 439 THR LEU ASN PHE LEU GLU GLY ASN SER ARG PRO ALA SER
SEQRES 8 A 439 ARG ASP ARG ARG VAL ASP PHE ILE PRO CYS HIS PHE HIS
SEQRES 9 A 439 GLU VAL PRO GLU LEU PHE ARG GLN GLY PHE PHE PRO LEU
SEQRES 10 A 439 ASP VAL ALA VAL VAL GLN VAL SER THR PRO ASN GLU GLU
SEQRES 11 A 439 GLY TYR CYS SER PHE GLY VAL SER CYS ASP TYR THR LYS
SEQRES 12 A 439 ALA ALA ALA GLU CYS ALA PRO VAL VAL VAL ALA GLU VAL
SEQRES 13 A 439 ASN LYS GLN MET PRO PHE ILE GLY GLY GLU ASN LEU ILE
SEQRES 14 A 439 HIS ILE SER LYS LEU THR HIS ILE ILE GLU VAL ASP GLU
SEQRES 15 A 439 PRO ILE ALA GLU VAL LEU PRO PRO ALA GLY SER ASP LEU
SEQRES 16 A 439 GLU LEU ARG ILE GLY GLN ASN CYS ALA SER LEU ILE LYS
SEQRES 17 A 439 ASP GLY ASP THR LEU GLN LEU GLY ILE GLY GLY ILE PRO
SEQRES 18 A 439 ASP ALA VAL LEU ARG ALA LEU GLU GLY HIS LYS ASP LEU
SEQRES 19 A 439 GLY ILE HIS THR GLU MET PHE THR ASP GLY VAL MET ARG
SEQRES 20 A 439 MET ILE ARG LYS GLY ILE ILE ASN GLY LYS LYS LYS THR
SEQRES 21 A 439 LEU HIS PRO GLU LYS VAL VAL THR SER LEU ILE PHE GLY
SEQRES 22 A 439 SER LYS GLU LEU TYR ASP PHE VAL ASN ASN ASN PRO VAL
SEQRES 23 A 439 ILE GLU CYS TYR PRO VAL ASP TYR ILE ASN ASN PRO ASP
SEQRES 24 A 439 VAL ILE GLY LYS ASN ASP ARG MET VAL SER ILE ASN SER
SEQRES 25 A 439 CYS LEU GLU MET ASP LEU MET GLY GLN ALA ALA SER GLU
SEQRES 26 A 439 SER ILE GLY TYR GLU GLN PHE SER GLY SER GLY GLY GLN
SEQRES 27 A 439 VAL ASP PHE LEU ARG GLY ALA LYS ARG SER LYS GLY GLY
SEQRES 28 A 439 ILE SER ILE MET ALA PHE PRO SER THR ALA LYS LYS GLY
SEQRES 29 A 439 THR GLU SER ARG ILE VAL PRO ILE LEU LYS GLU GLY ALA
SEQRES 30 A 439 CYS VAL THR THR GLY ARG ASN GLU VAL ASP TYR VAL VAL
SEQRES 31 A 439 THR GLU TYR GLY VAL ALA ARG LEU ARG GLY ALA THR LEU
SEQRES 32 A 439 ARG GLN ARG ALA GLU ALA LEU THR ALA ILE ALA HIS PRO
SEQRES 33 A 439 ASP PHE ARG PRO ALA LEU GLU GLU GLU ILE ARG ARG ARG
SEQRES 34 A 439 PHE GLU LEU GLU HIS HIS HIS HIS HIS HIS
FORMUL 2 HOH *20(H2 O)
HELIX 1 1 TRP A 3 VAL A 11 1 9
HELIX 2 2 SER A 13 LEU A 22 1 10
HELIX 3 3 HIS A 32 ALA A 36 5 5
HELIX 4 4 PRO A 37 GLN A 47 1 11
HELIX 5 5 ALA A 69 ARG A 73 5 5
HELIX 6 6 HIS A 102 HIS A 104 5 3
HELIX 7 7 GLU A 105 ARG A 111 1 7
HELIX 8 8 TYR A 141 ALA A 149 1 9
HELIX 9 9 SER A 172 LEU A 174 5 3
HELIX 10 10 SER A 193 SER A 205 1 13
HELIX 11 11 GLY A 218 ALA A 227 1 10
HELIX 12 12 THR A 242 LYS A 251 1 10
HELIX 13 13 SER A 274 ASN A 282 1 9
HELIX 14 14 PRO A 291 ASN A 296 1 6
HELIX 15 15 ASN A 297 ASN A 304 1 8
HELIX 16 16 GLY A 337 LYS A 346 1 10
HELIX 17 17 THR A 402 ALA A 414 1 13
HELIX 18 18 ASP A 417 ARG A 428 1 12
SHEET 1 A 6 VAL A 76 THR A 79 0
SHEET 2 A 6 ILE A 54 PHE A 57 1 N VAL A 56 O HIS A 77
SHEET 3 A 6 LYS A 27 PHE A 30 1 N VAL A 28 O THR A 55
SHEET 4 A 6 VAL A 119 SER A 125 1 O VAL A 121 N VAL A 29
SHEET 5 A 6 VAL A 151 ASN A 157 1 O ASN A 157 N VAL A 124
SHEET 6 A 6 HIS A 176 VAL A 180 1 O VAL A 180 N VAL A 156
SHEET 1 B 2 TYR A 132 SER A 134 0
SHEET 2 B 2 LEU A 168 HIS A 170 -1 O ILE A 169 N CYS A 133
SHEET 1 C 9 GLY A 164 GLY A 165 0
SHEET 2 C 9 ILE A 287 CYS A 289 1 O CYS A 289 N GLY A 164
SHEET 3 C 9 VAL A 266 THR A 268 1 N VAL A 266 O GLU A 288
SHEET 4 C 9 GLY A 235 HIS A 237 1 N ILE A 236 O VAL A 267
SHEET 5 C 9 THR A 212 LEU A 215 1 N LEU A 213 O HIS A 237
SHEET 6 C 9 MET A 307 ASN A 311 1 O ILE A 310 N GLN A 214
SHEET 7 C 9 ILE A 352 ALA A 356 1 O ILE A 354 N SER A 309
SHEET 8 C 9 TYR A 388 THR A 391 1 O VAL A 390 N MET A 355
SHEET 9 C 9 GLY A 394 ARG A 397 -1 O GLY A 394 N THR A 391
SHEET 1 D 2 MET A 316 ASP A 317 0
SHEET 2 D 2 ILE A 369 VAL A 370 1 O VAL A 370 N MET A 316
SHEET 1 E 2 THR A 360 ALA A 361 0
SHEET 2 E 2 GLU A 366 SER A 367 -1 O GLU A 366 N ALA A 361
LINK C ALA A 43 N MET A 44 1555 1555 1.32
LINK C MET A 44 N TYR A 45 1555 1555 1.33
LINK C HIS A 58 N MET A 59 1555 1555 1.34
LINK C MET A 59 N LEU A 60 1555 1555 1.33
LINK C GLU A 71 N MET A 72 1555 1555 1.33
LINK C MET A 72 N ARG A 73 1555 1555 1.34
LINK C GLN A 159 N MET A 160 1555 1555 1.34
LINK C MET A 160 N PRO A 161 1555 1555 1.33
LINK C GLU A 239 N MET A 240 1555 1555 1.33
LINK C MET A 240 N PHE A 241 1555 1555 1.29
LINK C VAL A 245 N MET A 246 1555 1555 1.35
LINK C MET A 246 N ARG A 247 1555 1555 1.30
LINK C ARG A 247 N MET A 248 1555 1555 1.32
LINK C MET A 248 N ILE A 249 1555 1555 1.33
LINK C ARG A 306 N MET A 307 1555 1555 1.31
LINK C MET A 307 N VAL A 308 1555 1555 1.34
LINK C GLU A 315 N MET A 316 1555 1555 1.32
LINK C MET A 316 N ASP A 317 1555 1555 1.33
LINK C LEU A 318 N MET A 319 1555 1555 1.34
LINK C MET A 319 N GLY A 320 1555 1555 1.32
LINK C ILE A 354 N MET A 355 1555 1555 1.35
LINK C MET A 355 N ALA A 356 1555 1555 1.31
CRYST1 54.684 87.279 93.504 90.00 90.00 90.00 P 21 21 21 4
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 0.018287 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011458 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010695 0.00000
(ATOM LINES ARE NOT SHOWN.)
END