HEADER OXIDOREDUCTASE 01-FEB-13 4J1Q
TITLE CRYSTAL STRUCTURE OF A KETOREDUCTASE DOMAIN FROM THE BACILLAENE
TITLE 2 ASSEMBLY LINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYKETIDE SYNTHASE PKSJ;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PKS;
COMPND 5 EC: 1.1.1.100;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 224308;
SOURCE 4 STRAIN: 168;
SOURCE 5 GENE: BSU17180, PKSJ, PKSJ (AMINO ACIDS 2669-3111), PKSK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS ROSSMANN FOLD, KETOREDUCTASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.ZHENG,A.T.KEATINGE-CLAY
REVDAT 5 28-FEB-24 4J1Q 1 REMARK SEQADV
REVDAT 4 03-SEP-14 4J1Q 1 JRNL
REVDAT 3 13-AUG-14 4J1Q 1 JRNL
REVDAT 2 26-MAR-14 4J1Q 1 JRNL
REVDAT 1 19-MAR-14 4J1Q 0
JRNL AUTH S.K.PIASECKI,J.ZHENG,A.J.AXELROD,M.E DETELICH,
JRNL AUTH 2 A.T.KEATINGE-CLAY
JRNL TITL STRUCTURAL AND FUNCTIONAL STUDIES OF A TRANS-ACYLTRANSFERASE
JRNL TITL 2 POLYKETIDE ASSEMBLY LINE ENZYME THAT CATALYZES
JRNL TITL 3 STEREOSELECTIVE ALPHA- AND BETA-KETOREDUCTION.
JRNL REF PROTEINS V. 82 2067 2014
JRNL REFN ISSN 0887-3585
JRNL PMID 24634061
JRNL DOI 10.1002/PROT.24561
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 17260
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) : 0.233
REMARK 3 R VALUE (WORKING SET) : 0.232
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 925
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) : 2.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.41
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1244
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.32
REMARK 3 BIN R VALUE (WORKING SET) : 0.3180
REMARK 3 BIN FREE R VALUE SET COUNT : 72
REMARK 3 BIN FREE R VALUE : 0.3590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3330
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 48.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 72.61
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.08000
REMARK 3 B22 (A**2) : 1.08000
REMARK 3 B33 (A**2) : -1.63000
REMARK 3 B12 (A**2) : 0.54000
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): 0.529
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.269
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.234
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.637
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3443 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4637 ; 1.091 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 414 ; 8.258 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 162 ;38.703 ;24.074
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 636 ;18.352 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;18.418 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 505 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2554 ; 0.012 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -1 A 424
REMARK 3 RESIDUE RANGE : A 501 A 501
REMARK 3 ORIGIN FOR THE GROUP (A): 12.8642 9.1642 107.2771
REMARK 3 T TENSOR
REMARK 3 T11: 0.3129 T22: 0.1784
REMARK 3 T33: 0.2699 T12: 0.1534
REMARK 3 T13: 0.0651 T23: 0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 0.2192 L22: 2.6511
REMARK 3 L33: 5.4313 L12: -0.6564
REMARK 3 L13: -0.5109 L23: -0.0578
REMARK 3 S TENSOR
REMARK 3 S11: -0.0293 S12: -0.1279 S13: 0.0282
REMARK 3 S21: 0.1927 S22: 0.5301 S23: -0.0591
REMARK 3 S31: -0.4025 S32: -0.0844 S33: -0.5008
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 USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4J1Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-FEB-13.
REMARK 100 THE DEPOSITION ID IS D_1000077485.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979468
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL, SI(111) LIQUID
REMARK 200 N2 COOLED
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18286
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 51.550
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 10.90
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.10
REMARK 200 R MERGE FOR SHELL (I) : 0.46400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, 25% PEG550 MME, PH 8.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
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
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 73.59733
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 147.19467
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 110.39600
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 183.99333
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 36.79867
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 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 -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 LEU A -7
REMARK 465 VAL A -6
REMARK 465 PRO A -5
REMARK 465 ARG A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 ARG A 16
REMARK 465 GLU A 17
REMARK 465 ASP A 18
REMARK 465 GLU A 19
REMARK 465 ASP A 20
REMARK 465 LEU A 168
REMARK 465 PRO A 169
REMARK 465 SER A 170
REMARK 465 ALA A 171
REMARK 465 SER A 425
REMARK 465 ALA A 426
REMARK 465 GLY A 427
REMARK 465 SER A 428
REMARK 465 LYS A 429
REMARK 465 ALA A 430
REMARK 465 LYS A 431
REMARK 465 ARG A 432
REMARK 465 ASN A 433
REMARK 465 ASP A 434
REMARK 465 GLN A 435
REMARK 465 ARG A 436
REMARK 465 LYS A 437
REMARK 465 ALA A 438
REMARK 465 ASP A 439
REMARK 465 GLN A 440
REMARK 465 ASP A 441
REMARK 465 GLN A 442
REMARK 465 GLY A 443
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ARG A 379 N THR A 383 1.97
REMARK 500 OG1 THR A 24 O ARG A 86 2.06
REMARK 500 OH TYR A 330 O2D NDP A 501 2.17
REMARK 500 O ALA A 228 OG SER A 231 2.18
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 GLN A 12 79.24 -155.91
REMARK 500 ARG A 145 79.96 -115.42
REMARK 500 VAL A 294 -67.37 -109.70
REMARK 500 LYS A 351 -1.05 85.77
REMARK 500 MET A 370 -121.66 60.99
REMARK 500 ALA A 374 -129.53 52.85
REMARK 500 ASP A 405 36.46 70.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASN A 54 GLU A 55 -148.12
REMARK 500 GLU A 367 GLY A 368 147.70
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 NDP A 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4J1S RELATED DB: PDB
DBREF 4J1Q A 1 443 UNP P40806 PKSJ_BACSU 2669 3111
SEQADV 4J1Q MET A -20 UNP P40806 EXPRESSION TAG
SEQADV 4J1Q GLY A -19 UNP P40806 EXPRESSION TAG
SEQADV 4J1Q SER A -18 UNP P40806 EXPRESSION TAG
SEQADV 4J1Q SER A -17 UNP P40806 EXPRESSION TAG
SEQADV 4J1Q HIS A -16 UNP P40806 EXPRESSION TAG
SEQADV 4J1Q HIS A -15 UNP P40806 EXPRESSION TAG
SEQADV 4J1Q HIS A -14 UNP P40806 EXPRESSION TAG
SEQADV 4J1Q HIS A -13 UNP P40806 EXPRESSION TAG
SEQADV 4J1Q HIS A -12 UNP P40806 EXPRESSION TAG
SEQADV 4J1Q HIS A -11 UNP P40806 EXPRESSION TAG
SEQADV 4J1Q SER A -10 UNP P40806 EXPRESSION TAG
SEQADV 4J1Q SER A -9 UNP P40806 EXPRESSION TAG
SEQADV 4J1Q GLY A -8 UNP P40806 EXPRESSION TAG
SEQADV 4J1Q LEU A -7 UNP P40806 EXPRESSION TAG
SEQADV 4J1Q VAL A -6 UNP P40806 EXPRESSION TAG
SEQADV 4J1Q PRO A -5 UNP P40806 EXPRESSION TAG
SEQADV 4J1Q ARG A -4 UNP P40806 EXPRESSION TAG
SEQADV 4J1Q GLY A -3 UNP P40806 EXPRESSION TAG
SEQADV 4J1Q SER A -2 UNP P40806 EXPRESSION TAG
SEQADV 4J1Q HIS A -1 UNP P40806 EXPRESSION TAG
SEQADV 4J1Q MET A 0 UNP P40806 EXPRESSION TAG
SEQRES 1 A 464 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 464 LEU VAL PRO ARG GLY SER HIS MET GLU ARG LEU MET LEU
SEQRES 3 A 464 GLU PRO VAL TRP GLU LYS GLN ASN GLU GLU ARG GLU ASP
SEQRES 4 A 464 GLU ASP LEU SER TYR THR GLU HIS ILE ILE VAL LEU PHE
SEQRES 5 A 464 GLU THR GLU ARG SER VAL THR ASP SER ILE ALA SER HIS
SEQRES 6 A 464 MET LYS ASP ALA ARG VAL ILE THR LEU ASN GLU ALA VAL
SEQRES 7 A 464 GLY HIS ILE ALA GLU ARG TYR GLN CYS TYR MET GLN ASN
SEQRES 8 A 464 ILE PHE GLU LEU LEU GLN SER LYS VAL ARG LYS LEU SER
SEQRES 9 A 464 ALA GLY ARG ILE ILE ILE GLN ALA ILE VAL PRO LEU GLU
SEQRES 10 A 464 LYS GLU LYS GLN LEU PHE ALA GLY VAL SER GLY LEU PHE
SEQRES 11 A 464 LYS THR ALA GLU ILE GLU PHE SER LYS LEU THR ALA GLN
SEQRES 12 A 464 VAL ILE GLU ILE GLU LYS PRO GLU GLU MET ILE ASP LEU
SEQRES 13 A 464 HIS LEU LYS LEU LYS ASP ASP SER ARG ARG PRO PHE ASP
SEQRES 14 A 464 LYS GLN ILE ARG TYR GLU ALA GLY TYR ARG PHE VAL LYS
SEQRES 15 A 464 GLY TRP ARG GLU MET VAL LEU PRO SER ALA ASP THR LEU
SEQRES 16 A 464 HIS MET PRO TRP ARG ASP GLU GLY VAL TYR LEU ILE THR
SEQRES 17 A 464 GLY GLY ALA GLY SER LEU GLY LEU LEU PHE ALA LYS GLU
SEQRES 18 A 464 ILE ALA ASN ARG THR GLY ARG SER THR ILE VAL LEU THR
SEQRES 19 A 464 GLY ARG SER VAL LEU SER GLU ASP LYS GLU ASN GLU LEU
SEQRES 20 A 464 GLU ALA LEU ARG SER ILE GLY ALA GLU VAL VAL TYR ARG
SEQRES 21 A 464 GLU ALA ASP VAL SER ASP GLN HIS ALA VAL ARG HIS LEU
SEQRES 22 A 464 LEU GLU GLU ILE LYS GLU ARG TYR GLY THR LEU ASN GLY
SEQRES 23 A 464 ILE ILE HIS GLY ALA GLY SER SER LYS ASP ARG PHE ILE
SEQRES 24 A 464 ILE HIS LYS THR ASN GLU GLU PHE GLN GLU VAL LEU GLN
SEQRES 25 A 464 PRO LYS VAL SER GLY LEU LEU HIS VAL ASP GLU CYS SER
SEQRES 26 A 464 LYS ASP PHE PRO LEU ASP PHE PHE ILE PHE PHE SER SER
SEQRES 27 A 464 VAL SER GLY CYS LEU GLY ASN ALA GLY GLN ALA ASP TYR
SEQRES 28 A 464 ALA ALA ALA ASN SER PHE MET ASP ALA PHE ALA GLU TYR
SEQRES 29 A 464 ARG ARG SER LEU ALA ALA SER LYS LYS ARG PHE GLY SER
SEQRES 30 A 464 THR ILE SER PHE ASN TRP PRO LEU TRP GLU GLU GLY GLY
SEQRES 31 A 464 MET GLN VAL GLY ALA GLU ASP GLU LYS ARG MET LEU LYS
SEQRES 32 A 464 THR THR GLY MET VAL PRO MET PRO THR ASP SER GLY LEU
SEQRES 33 A 464 LYS ALA PHE TYR GLN GLY ILE VAL SER ASP LYS PRO GLN
SEQRES 34 A 464 VAL PHE VAL MET GLU GLY GLN LEU GLN LYS MET LYS GLN
SEQRES 35 A 464 LYS LEU LEU SER ALA GLY SER LYS ALA LYS ARG ASN ASP
SEQRES 36 A 464 GLN ARG LYS ALA ASP GLN ASP GLN GLY
HET NDP A 501 48
HETNAM NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NDP PHOSPHATE
FORMUL 2 NDP C21 H30 N7 O17 P3
HELIX 1 1 GLU A 34 MET A 45 1 12
HELIX 2 2 HIS A 59 LYS A 78 1 20
HELIX 3 3 LYS A 78 GLY A 85 1 8
HELIX 4 4 GLU A 98 ALA A 103 5 6
HELIX 5 5 GLY A 104 PHE A 116 1 13
HELIX 6 6 ASP A 134 ARG A 144 1 11
HELIX 7 7 GLY A 191 GLY A 206 1 16
HELIX 8 8 SER A 219 ILE A 232 1 14
HELIX 9 9 ASP A 245 TYR A 260 1 16
HELIX 10 10 THR A 282 GLN A 291 1 10
HELIX 11 11 VAL A 294 SER A 304 1 11
HELIX 12 12 VAL A 318 GLY A 323 1 6
HELIX 13 13 GLN A 327 SER A 350 1 24
HELIX 14 14 GLU A 375 GLY A 385 1 11
HELIX 15 15 PRO A 390 ASP A 405 1 16
HELIX 16 16 GLN A 415 LEU A 424 1 10
SHEET 1 A14 ARG A 49 LEU A 53 0
SHEET 2 A14 GLU A 25 PHE A 31 1 N ILE A 28 O ILE A 51
SHEET 3 A14 ILE A 87 PRO A 94 1 O ILE A 88 N ILE A 27
SHEET 4 A14 LEU A 119 ILE A 126 1 O ILE A 126 N VAL A 93
SHEET 5 A14 GLN A 150 GLU A 154 1 O TYR A 153 N GLU A 125
SHEET 6 A14 TYR A 157 GLU A 165 -1 O PHE A 159 N ARG A 152
SHEET 7 A14 GLU A 1 GLU A 10 -1 N VAL A 8 O GLY A 162
SHEET 8 A14 GLN A 408 GLY A 414 -1 O PHE A 410 N LEU A 5
SHEET 9 A14 SER A 356 TRP A 362 1 N ASN A 361 O VAL A 409
SHEET 10 A14 PHE A 311 SER A 317 1 N PHE A 314 O ILE A 358
SHEET 11 A14 GLY A 265 HIS A 268 1 N ILE A 266 O ILE A 313
SHEET 12 A14 VAL A 183 THR A 187 1 N LEU A 185 O ILE A 267
SHEET 13 A14 THR A 209 THR A 213 1 O THR A 209 N TYR A 184
SHEET 14 A14 GLU A 235 TYR A 238 1 O GLU A 235 N ILE A 210
SITE 1 AC1 23 GLY A 188 GLY A 191 SER A 192 LEU A 193
SITE 2 AC1 23 GLY A 214 ARG A 215 SER A 216 ALA A 241
SITE 3 AC1 23 ASP A 242 VAL A 243 GLY A 269 ALA A 270
SITE 4 AC1 23 GLY A 271 LYS A 293 PHE A 315 SER A 316
SITE 5 AC1 23 TYR A 330 TRP A 362 PRO A 363 LEU A 364
SITE 6 AC1 23 TRP A 365 GLY A 369 MET A 370
CRYST1 59.529 59.529 220.792 90.00 90.00 120.00 P 61 6
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 0.016799 0.009699 0.000000 0.00000
SCALE2 0.000000 0.019397 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004529 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
