HEADER OXIDOREDUCTASE 31-AUG-07 2R4J
TITLE CRYSTAL STRUCTURE OF ESCHERICHIA COLI SEMET SUBSTITUTED
TITLE 2 GLYCEROL-3-PHOSPHATE DEHYDROGENASE IN COMPLEX WITH DHAP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.1.99.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 GENE: GLPD, GLYD;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI
KEYWDS GLPD, CYTOPLASM, FAD, FLAVOPROTEIN, GLYCEROL METABOLISM,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.I.YEH,S.DU,U.CHINTE
REVDAT 2 24-FEB-09 2R4J 1 VERSN
REVDAT 1 03-JUN-08 2R4J 0
JRNL AUTH J.I.YEH,U.CHINTE,S.DU
JRNL TITL STRUCTURE OF GLYCEROL-3-PHOSPHATE DEHYDROGENASE,
JRNL TITL 2 AN ESSENTIAL MONOTOPIC MEMBRANE ENZYME INVOLVED IN
JRNL TITL 3 RESPIRATION AND METABOLISM.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 105 3280 2008
JRNL REFN ISSN 0027-8424
JRNL PMID 18296637
JRNL DOI 10.1073/PNAS.0712331105
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.96 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.96
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 77725
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) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4086
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) : 1.96
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.01
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2841
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2800
REMARK 3 BIN FREE R VALUE SET COUNT : 149
REMARK 3 BIN FREE R VALUE : 0.3310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7934
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 434
REMARK 3 SOLVENT ATOMS : 277
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.68000
REMARK 3 B22 (A**2) : 1.56000
REMARK 3 B33 (A**2) : -2.23000
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): 0.188
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.175
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.152
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.472
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8534 ; 0.024 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11492 ; 2.354 ; 1.996
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 989 ; 6.943 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 392 ;32.529 ;22.806
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1385 ;20.095 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 77 ;18.437 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1219 ; 0.161 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6343 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3920 ; 0.250 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5657 ; 0.327 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 447 ; 0.173 ; 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): 47 ; 0.198 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 10 ; 0.123 ; 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): 5049 ; 1.550 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7884 ; 2.305 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4068 ; 3.291 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3608 ; 4.923 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 5 A 494 4
REMARK 3 1 B 5 B 494 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 3920 ; 0.36 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 3920 ; 0.85 ; 2.00
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2R4J COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-DEC-07.
REMARK 100 THE RCSB ID CODE IS RCSB044415.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97928, 0.97947, 0.97181
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 87054
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.960
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.11300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.61400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M DI-AMMONIUM HYDROGEN
REMARK 280 PHOSPHATE, 0.1M BICINE, 12% W/V PEG 6000, PH 8.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 56.95800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 57.07100
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 96.79550
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 56.95800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 57.07100
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 96.79550
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 56.95800
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 57.07100
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 96.79550
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 56.95800
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 57.07100
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 96.79550
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 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 GLN A 495
REMARK 465 ARG A 496
REMARK 465 LEU A 497
REMARK 465 SER A 498
REMARK 465 LEU A 499
REMARK 465 ALA A 500
REMARK 465 SER A 501
REMARK 465 SER B 498
REMARK 465 LEU B 499
REMARK 465 ALA B 500
REMARK 465 SER B 501
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 2 -17.39 60.90
REMARK 500 GLN A 35 -96.34 -128.22
REMARK 500 ALA A 40 -115.40 -126.83
REMARK 500 GLU A 60 50.23 -94.23
REMARK 500 LYS A 113 111.22 44.73
REMARK 500 SER A 116 -45.55 -149.39
REMARK 500 PRO A 118 -133.42 -56.51
REMARK 500 GLU A 264 -32.11 -131.23
REMARK 500 ASP A 321 97.44 -68.02
REMARK 500 GLU A 341 -100.74 -112.99
REMARK 500 ASN A 342 47.29 -84.12
REMARK 500 LYS A 354 162.61 -46.91
REMARK 500 PRO A 371 -27.22 -39.62
REMARK 500 GLN A 374 -108.09 -78.76
REMARK 500 ALA A 379 150.50 -48.71
REMARK 500 TRP A 380 -1.60 -162.29
REMARK 500 GLU A 392 49.49 -68.79
REMARK 500 ASP A 397 36.96 -97.73
REMARK 500 SER A 423 -9.22 -58.73
REMARK 500 LYS B 4 86.46 81.50
REMARK 500 GLN B 35 -96.30 -125.75
REMARK 500 ALA B 40 -124.47 -126.91
REMARK 500 TYR B 59 91.09 38.08
REMARK 500 GLU B 60 55.29 -147.12
REMARK 500 LYS B 113 -92.47 0.32
REMARK 500 THR B 115 -45.88 -29.10
REMARK 500 SER B 116 -43.24 -134.10
REMARK 500 PRO B 118 -135.16 -64.34
REMARK 500 ARG B 169 27.81 46.05
REMARK 500 ASN B 179 31.38 74.93
REMARK 500 THR B 270 -155.08 -126.72
REMARK 500 GLU B 323 -169.89 63.57
REMARK 500 SER B 324 -71.56 156.48
REMARK 500 ASP B 325 -62.75 107.20
REMARK 500 PRO B 371 -29.20 -36.88
REMARK 500 GLN B 374 -94.40 -79.76
REMARK 500 ALA B 379 152.68 -24.65
REMARK 500 TRP B 380 -15.31 -169.22
REMARK 500 GLU B 392 78.07 -150.27
REMARK 500 ARG B 461 -31.90 -130.58
REMARK 500 GLN B 495 -76.53 -177.44
REMARK 500 ARG B 496 40.41 -63.65
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 BOG A 700
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 700
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 1949
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 1950
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 801
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1951
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 600
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 600
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 802
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 803
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 804
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 805
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 806
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1952
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 807
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 808
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1953
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1954
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1955
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1956
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 809
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1957
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 810
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 811
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1958
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1959
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 1960
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAM B 812
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 1961
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 813
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1962
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 814
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 1963
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1964
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1965
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 1966
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 815
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 1967
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 13P A 1968
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 13P B 816
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 817
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 818
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD B 819
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCN B 820
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCN B 821
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCN A 1969
DBREF 2R4J A 1 501 UNP P13035 GLPD_ECOLI 1 501
DBREF 2R4J B 1 501 UNP P13035 GLPD_ECOLI 1 501
SEQRES 1 A 501 MET GLU THR LYS ASP LEU ILE VAL ILE GLY GLY GLY ILE
SEQRES 2 A 501 ASN GLY ALA GLY ILE ALA ALA ASP ALA ALA GLY ARG GLY
SEQRES 3 A 501 LEU SER VAL LEU MSE LEU GLU ALA GLN ASP LEU ALA CYS
SEQRES 4 A 501 ALA THR SER SER ALA SER SER LYS LEU ILE HIS GLY GLY
SEQRES 5 A 501 LEU ARG TYR LEU GLU HIS TYR GLU PHE ARG LEU VAL SER
SEQRES 6 A 501 GLU ALA LEU ALA GLU ARG GLU VAL LEU LEU LYS MSE ALA
SEQRES 7 A 501 PRO HIS ILE ALA PHE PRO MSE ARG PHE ARG LEU PRO HIS
SEQRES 8 A 501 ARG PRO HIS LEU ARG PRO ALA TRP MET ILE ARG ILE GLY
SEQRES 9 A 501 LEU PHE MET TYR ASP HIS LEU GLY LYS ARG THR SER LEU
SEQRES 10 A 501 PRO GLY SER THR GLY LEU ARG PHE GLY ALA ASN SER VAL
SEQRES 11 A 501 LEU LYS PRO GLU ILE LYS ARG GLY PHE GLU TYR SER ASP
SEQRES 12 A 501 CYS TRP VAL ASP ASP ALA ARG LEU VAL LEU ALA ASN ALA
SEQRES 13 A 501 GLN MSE VAL VAL ARG LYS GLY GLY GLU VAL LEU THR ARG
SEQRES 14 A 501 THR ARG ALA THR SER ALA ARG ARG GLU ASN GLY LEU TRP
SEQRES 15 A 501 ILE VAL GLU ALA GLU ASP ILE ASP THR GLY LYS LYS TYR
SEQRES 16 A 501 SER TRP GLN ALA ARG GLY LEU VAL ASN ALA THR GLY PRO
SEQRES 17 A 501 TRP VAL LYS GLN PHE PHE ASP ASP GLY MSE HIS LEU PRO
SEQRES 18 A 501 SER PRO TYR GLY ILE ARG LEU ILE LYS GLY SER HIS ILE
SEQRES 19 A 501 VAL VAL PRO ARG VAL HIS THR GLN LYS GLN ALA TYR ILE
SEQRES 20 A 501 LEU GLN ASN GLU ASP LYS ARG ILE VAL PHE VAL ILE PRO
SEQRES 21 A 501 TRP MSE ASP GLU PHE SER ILE ILE GLY THR THR ASP VAL
SEQRES 22 A 501 GLU TYR LYS GLY ASP PRO LYS ALA VAL LYS ILE GLU GLU
SEQRES 23 A 501 SER GLU ILE ASN TYR LEU LEU ASN VAL TYR ASN THR HIS
SEQRES 24 A 501 PHE LYS LYS GLN LEU SER ARG ASP ASP ILE VAL TRP THR
SEQRES 25 A 501 TYR SER GLY VAL ARG PRO LEU CYS ASP ASP GLU SER ASP
SEQRES 26 A 501 SER PRO GLN ALA ILE THR ARG ASP TYR THR LEU ASP ILE
SEQRES 27 A 501 HIS ASP GLU ASN GLY LYS ALA PRO LEU LEU SER VAL PHE
SEQRES 28 A 501 GLY GLY LYS LEU THR THR TYR ARG LYS LEU ALA GLU HIS
SEQRES 29 A 501 ALA LEU GLU LYS LEU THR PRO TYR TYR GLN GLY ILE GLY
SEQRES 30 A 501 PRO ALA TRP THR LYS GLU SER VAL LEU PRO GLY GLY ALA
SEQRES 31 A 501 ILE GLU GLY ASP ARG ASP ASP TYR ALA ALA ARG LEU ARG
SEQRES 32 A 501 ARG ARG TYR PRO PHE LEU THR GLU SER LEU ALA ARG HIS
SEQRES 33 A 501 TYR ALA ARG THR TYR GLY SER ASN SER GLU LEU LEU LEU
SEQRES 34 A 501 GLY ASN ALA GLY THR VAL SER ASP LEU GLY GLU ASP PHE
SEQRES 35 A 501 GLY HIS GLU PHE TYR GLU ALA GLU LEU LYS TYR LEU VAL
SEQRES 36 A 501 ASP HIS GLU TRP VAL ARG ARG ALA ASP ASP ALA LEU TRP
SEQRES 37 A 501 ARG ARG THR LYS GLN GLY MSE TRP LEU ASN ALA ASP GLN
SEQRES 38 A 501 GLN SER ARG VAL SER GLN TRP LEU VAL GLU TYR THR GLN
SEQRES 39 A 501 GLN ARG LEU SER LEU ALA SER
SEQRES 1 B 501 MET GLU THR LYS ASP LEU ILE VAL ILE GLY GLY GLY ILE
SEQRES 2 B 501 ASN GLY ALA GLY ILE ALA ALA ASP ALA ALA GLY ARG GLY
SEQRES 3 B 501 LEU SER VAL LEU MSE LEU GLU ALA GLN ASP LEU ALA CYS
SEQRES 4 B 501 ALA THR SER SER ALA SER SER LYS LEU ILE HIS GLY GLY
SEQRES 5 B 501 LEU ARG TYR LEU GLU HIS TYR GLU PHE ARG LEU VAL SER
SEQRES 6 B 501 GLU ALA LEU ALA GLU ARG GLU VAL LEU LEU LYS MSE ALA
SEQRES 7 B 501 PRO HIS ILE ALA PHE PRO MSE ARG PHE ARG LEU PRO HIS
SEQRES 8 B 501 ARG PRO HIS LEU ARG PRO ALA TRP MET ILE ARG ILE GLY
SEQRES 9 B 501 LEU PHE MET TYR ASP HIS LEU GLY LYS ARG THR SER LEU
SEQRES 10 B 501 PRO GLY SER THR GLY LEU ARG PHE GLY ALA ASN SER VAL
SEQRES 11 B 501 LEU LYS PRO GLU ILE LYS ARG GLY PHE GLU TYR SER ASP
SEQRES 12 B 501 CYS TRP VAL ASP ASP ALA ARG LEU VAL LEU ALA ASN ALA
SEQRES 13 B 501 GLN MSE VAL VAL ARG LYS GLY GLY GLU VAL LEU THR ARG
SEQRES 14 B 501 THR ARG ALA THR SER ALA ARG ARG GLU ASN GLY LEU TRP
SEQRES 15 B 501 ILE VAL GLU ALA GLU ASP ILE ASP THR GLY LYS LYS TYR
SEQRES 16 B 501 SER TRP GLN ALA ARG GLY LEU VAL ASN ALA THR GLY PRO
SEQRES 17 B 501 TRP VAL LYS GLN PHE PHE ASP ASP GLY MSE HIS LEU PRO
SEQRES 18 B 501 SER PRO TYR GLY ILE ARG LEU ILE LYS GLY SER HIS ILE
SEQRES 19 B 501 VAL VAL PRO ARG VAL HIS THR GLN LYS GLN ALA TYR ILE
SEQRES 20 B 501 LEU GLN ASN GLU ASP LYS ARG ILE VAL PHE VAL ILE PRO
SEQRES 21 B 501 TRP MSE ASP GLU PHE SER ILE ILE GLY THR THR ASP VAL
SEQRES 22 B 501 GLU TYR LYS GLY ASP PRO LYS ALA VAL LYS ILE GLU GLU
SEQRES 23 B 501 SER GLU ILE ASN TYR LEU LEU ASN VAL TYR ASN THR HIS
SEQRES 24 B 501 PHE LYS LYS GLN LEU SER ARG ASP ASP ILE VAL TRP THR
SEQRES 25 B 501 TYR SER GLY VAL ARG PRO LEU CYS ASP ASP GLU SER ASP
SEQRES 26 B 501 SER PRO GLN ALA ILE THR ARG ASP TYR THR LEU ASP ILE
SEQRES 27 B 501 HIS ASP GLU ASN GLY LYS ALA PRO LEU LEU SER VAL PHE
SEQRES 28 B 501 GLY GLY LYS LEU THR THR TYR ARG LYS LEU ALA GLU HIS
SEQRES 29 B 501 ALA LEU GLU LYS LEU THR PRO TYR TYR GLN GLY ILE GLY
SEQRES 30 B 501 PRO ALA TRP THR LYS GLU SER VAL LEU PRO GLY GLY ALA
SEQRES 31 B 501 ILE GLU GLY ASP ARG ASP ASP TYR ALA ALA ARG LEU ARG
SEQRES 32 B 501 ARG ARG TYR PRO PHE LEU THR GLU SER LEU ALA ARG HIS
SEQRES 33 B 501 TYR ALA ARG THR TYR GLY SER ASN SER GLU LEU LEU LEU
SEQRES 34 B 501 GLY ASN ALA GLY THR VAL SER ASP LEU GLY GLU ASP PHE
SEQRES 35 B 501 GLY HIS GLU PHE TYR GLU ALA GLU LEU LYS TYR LEU VAL
SEQRES 36 B 501 ASP HIS GLU TRP VAL ARG ARG ALA ASP ASP ALA LEU TRP
SEQRES 37 B 501 ARG ARG THR LYS GLN GLY MSE TRP LEU ASN ALA ASP GLN
SEQRES 38 B 501 GLN SER ARG VAL SER GLN TRP LEU VAL GLU TYR THR GLN
SEQRES 39 B 501 GLN ARG LEU SER LEU ALA SER
MODRES 2R4J MSE A 31 MET SELENOMETHIONINE
MODRES 2R4J MSE A 77 MET SELENOMETHIONINE
MODRES 2R4J MSE A 85 MET SELENOMETHIONINE
MODRES 2R4J MSE A 158 MET SELENOMETHIONINE
MODRES 2R4J MSE A 218 MET SELENOMETHIONINE
MODRES 2R4J MSE A 262 MET SELENOMETHIONINE
MODRES 2R4J MSE A 475 MET SELENOMETHIONINE
MODRES 2R4J MSE B 31 MET SELENOMETHIONINE
MODRES 2R4J MSE B 77 MET SELENOMETHIONINE
MODRES 2R4J MSE B 85 MET SELENOMETHIONINE
MODRES 2R4J MSE B 158 MET SELENOMETHIONINE
MODRES 2R4J MSE B 218 MET SELENOMETHIONINE
MODRES 2R4J MSE B 262 MET SELENOMETHIONINE
MODRES 2R4J MSE B 475 MET SELENOMETHIONINE
HET MSE A 31 8
HET MSE A 77 8
HET MSE A 85 8
HET MSE A 158 8
HET MSE A 218 8
HET MSE A 262 8
HET MSE A 475 8
HET MSE B 31 8
HET MSE B 77 8
HET MSE B 85 8
HET MSE B 158 8
HET MSE B 218 8
HET MSE B 262 8
HET MSE B 475 8
HET BOG A 700 20
HET BOG A 800 20
HET BOG B 700 20
HET BOG B 800 20
HET BOG A1949 20
HET BOG A1950 20
HET PO4 B 801 5
HET PO4 A1951 5
HET FAD A 600 53
HET FAD B 600 53
HET EDO B 802 4
HET EDO B 803 4
HET EDO B 804 4
HET EDO B 805 4
HET EDO B 806 4
HET EDO A1952 4
HET EDO B 807 4
HET EDO B 808 4
HET EDO A1953 4
HET EDO A1954 4
HET EDO A1955 4
HET EDO A1956 4
HET EDO B 809 4
HET EDO A1957 4
HET EDO B 810 4
HET EDO B 811 4
HET EDO A1958 4
HET EDO A1959 4
HET IMD A1960 5
HET TAM B 812 11
HET IMD A1961 5
HET EDO B 813 4
HET EDO A1962 4
HET EDO B 814 4
HET IMD A1963 5
HET EDO A1964 4
HET EDO A1965 4
HET IMD A1966 5
HET EDO B 815 4
HET IMD A1967 5
HET 13P A1968 10
HET 13P B 816 10
HET EDO B 817 4
HET EDO B 818 4
HET IMD B 819 5
HET BCN B 820 11
HET BCN B 821 11
HET BCN A1969 11
HETNAM MSE SELENOMETHIONINE
HETNAM BOG B-OCTYLGLUCOSIDE
HETNAM PO4 PHOSPHATE ION
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM IMD IMIDAZOLE
HETNAM TAM TRIS(HYDROXYETHYL)AMINOMETHANE
HETNAM 13P 1,3-DIHYDROXYACETONEPHOSPHATE
HETNAM BCN BICINE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 14(C5 H11 N O2 SE)
FORMUL 3 BOG 6(C14 H28 O6)
FORMUL 9 PO4 2(O4 P 3-)
FORMUL 11 FAD 2(C27 H33 N9 O15 P2)
FORMUL 13 EDO 26(C2 H6 O2)
FORMUL 31 IMD 6(C3 H5 N2 1+)
FORMUL 32 TAM C7 H17 N O3
FORMUL 43 13P 2(C3 H7 O6 P)
FORMUL 48 BCN 3(C6 H13 N O4)
FORMUL 51 HOH *277(H2 O)
HELIX 1 1 GLY A 12 GLY A 24 1 13
HELIX 2 2 ALA A 40 ALA A 44 5 5
HELIX 3 3 GLY A 52 TYR A 59 5 8
HELIX 4 4 GLU A 60 ALA A 78 1 19
HELIX 5 5 PRO A 97 LEU A 111 1 15
HELIX 6 6 ASP A 147 LYS A 162 1 16
HELIX 7 7 THR A 206 PRO A 208 5 3
HELIX 8 8 TRP A 209 GLY A 217 1 9
HELIX 9 9 ASP A 278 VAL A 282 5 5
HELIX 10 10 GLU A 285 THR A 298 1 14
HELIX 11 11 SER A 305 ILE A 309 5 5
HELIX 12 12 SER A 326 ILE A 330 5 5
HELIX 13 13 THR A 357 THR A 370 1 14
HELIX 14 14 PRO A 371 TYR A 373 5 3
HELIX 15 15 TRP A 380 SER A 384 5 5
HELIX 16 16 ARG A 395 TYR A 406 1 12
HELIX 17 17 THR A 410 TYR A 421 1 12
HELIX 18 18 ASN A 424 GLY A 430 1 7
HELIX 19 19 THR A 434 GLY A 439 5 6
HELIX 20 20 TYR A 447 GLU A 458 1 12
HELIX 21 21 ARG A 462 ARG A 469 1 8
HELIX 22 22 LYS A 472 TRP A 476 5 5
HELIX 23 23 ASN A 478 THR A 493 1 16
HELIX 24 24 GLY B 12 GLY B 24 1 13
HELIX 25 25 ALA B 40 ALA B 44 5 5
HELIX 26 26 GLY B 52 TYR B 59 5 8
HELIX 27 27 GLU B 60 ALA B 78 1 19
HELIX 28 28 PRO B 97 LEU B 111 1 15
HELIX 29 29 ASP B 147 LYS B 162 1 16
HELIX 30 30 THR B 206 PRO B 208 5 3
HELIX 31 31 TRP B 209 GLY B 217 1 9
HELIX 32 32 ASP B 278 VAL B 282 5 5
HELIX 33 33 GLU B 285 PHE B 300 1 16
HELIX 34 34 SER B 305 ILE B 309 5 5
HELIX 35 35 SER B 326 ILE B 330 5 5
HELIX 36 36 THR B 357 THR B 370 1 14
HELIX 37 37 PRO B 371 TYR B 373 5 3
HELIX 38 38 TRP B 380 SER B 384 5 5
HELIX 39 39 ASP B 394 TYR B 406 1 13
HELIX 40 40 THR B 410 TYR B 421 1 12
HELIX 41 41 ASN B 424 GLY B 430 1 7
HELIX 42 42 VAL B 435 GLY B 439 5 5
HELIX 43 43 TYR B 447 GLU B 458 1 12
HELIX 44 44 ARG B 462 ARG B 469 1 8
HELIX 45 45 LYS B 472 TRP B 476 5 5
HELIX 46 46 ASN B 478 GLN B 494 1 17
SHEET 1 A 6 GLU A 165 LEU A 167 0
SHEET 2 A 6 VAL A 29 LEU A 32 1 N MSE A 31 O LEU A 167
SHEET 3 A 6 THR A 3 ILE A 9 1 N VAL A 8 O LEU A 32
SHEET 4 A 6 LYS A 194 ASN A 204 1 O VAL A 203 N ILE A 7
SHEET 5 A 6 LEU A 181 ASP A 188 -1 N TRP A 182 O ALA A 199
SHEET 6 A 6 THR A 170 GLU A 178 -1 N GLU A 178 O LEU A 181
SHEET 1 B 6 GLU A 165 LEU A 167 0
SHEET 2 B 6 VAL A 29 LEU A 32 1 N MSE A 31 O LEU A 167
SHEET 3 B 6 THR A 3 ILE A 9 1 N VAL A 8 O LEU A 32
SHEET 4 B 6 LYS A 194 ASN A 204 1 O VAL A 203 N ILE A 7
SHEET 5 B 6 LEU A 347 PHE A 351 1 O LEU A 348 N ASN A 204
SHEET 6 B 6 THR A 335 HIS A 339 -1 N THR A 335 O PHE A 351
SHEET 1 C 8 LEU A 48 ILE A 49 0
SHEET 2 C 8 ARG A 137 VAL A 146 -1 O CYS A 144 N ILE A 49
SHEET 3 C 8 ALA A 82 PRO A 90 -1 N LEU A 89 O PHE A 139
SHEET 4 C 8 ALA A 245 GLN A 249 1 O ALA A 245 N ARG A 88
SHEET 5 C 8 ILE A 255 TRP A 261 -1 O VAL A 256 N LEU A 248
SHEET 6 C 8 PHE A 265 GLY A 269 -1 O GLY A 269 N PHE A 257
SHEET 7 C 8 ILE A 226 PRO A 237 -1 N ILE A 234 O ILE A 268
SHEET 8 C 8 VAL A 273 GLU A 274 -1 O VAL A 273 N LYS A 230
SHEET 1 D 8 THR A 121 ARG A 124 0
SHEET 2 D 8 ARG A 137 VAL A 146 -1 O GLU A 140 N THR A 121
SHEET 3 D 8 ALA A 82 PRO A 90 -1 N LEU A 89 O PHE A 139
SHEET 4 D 8 ALA A 245 GLN A 249 1 O ALA A 245 N ARG A 88
SHEET 5 D 8 ILE A 255 TRP A 261 -1 O VAL A 256 N LEU A 248
SHEET 6 D 8 PHE A 265 GLY A 269 -1 O GLY A 269 N PHE A 257
SHEET 7 D 8 ILE A 226 PRO A 237 -1 N ILE A 234 O ILE A 268
SHEET 8 D 8 TRP A 311 CYS A 320 -1 O TRP A 311 N VAL A 235
SHEET 1 E 6 GLU B 165 LEU B 167 0
SHEET 2 E 6 VAL B 29 LEU B 32 1 N MSE B 31 O LEU B 167
SHEET 3 E 6 LEU B 6 ILE B 9 1 N VAL B 8 O LEU B 32
SHEET 4 E 6 GLY B 201 ASN B 204 1 O VAL B 203 N ILE B 7
SHEET 5 E 6 LYS B 344 PHE B 351 1 O LEU B 348 N ASN B 204
SHEET 6 E 6 THR B 335 GLU B 341 -1 N THR B 335 O PHE B 351
SHEET 1 F 8 LEU B 48 ILE B 49 0
SHEET 2 F 8 ARG B 137 VAL B 146 -1 O CYS B 144 N ILE B 49
SHEET 3 F 8 ALA B 82 PRO B 90 -1 N PHE B 87 O TYR B 141
SHEET 4 F 8 ALA B 245 GLN B 249 1 O ALA B 245 N ARG B 88
SHEET 5 F 8 ILE B 255 TRP B 261 -1 O VAL B 256 N LEU B 248
SHEET 6 F 8 PHE B 265 GLY B 269 -1 O ILE B 267 N ILE B 259
SHEET 7 F 8 ILE B 226 PRO B 237 -1 N ILE B 234 O ILE B 268
SHEET 8 F 8 VAL B 273 GLU B 274 -1 O VAL B 273 N LYS B 230
SHEET 1 G 8 THR B 121 ARG B 124 0
SHEET 2 G 8 ARG B 137 VAL B 146 -1 O GLU B 140 N THR B 121
SHEET 3 G 8 ALA B 82 PRO B 90 -1 N PHE B 87 O TYR B 141
SHEET 4 G 8 ALA B 245 GLN B 249 1 O ALA B 245 N ARG B 88
SHEET 5 G 8 ILE B 255 TRP B 261 -1 O VAL B 256 N LEU B 248
SHEET 6 G 8 PHE B 265 GLY B 269 -1 O ILE B 267 N ILE B 259
SHEET 7 G 8 ILE B 226 PRO B 237 -1 N ILE B 234 O ILE B 268
SHEET 8 G 8 TRP B 311 CYS B 320 -1 O TRP B 311 N VAL B 235
SHEET 1 H 3 THR B 170 GLU B 178 0
SHEET 2 H 3 LEU B 181 ASP B 188 -1 O LEU B 181 N GLU B 178
SHEET 3 H 3 LYS B 194 ALA B 199 -1 O ALA B 199 N TRP B 182
LINK C LEU A 30 N MSE A 31 1555 1555 1.33
LINK C MSE A 31 N LEU A 32 1555 1555 1.35
LINK C LYS A 76 N MSE A 77 1555 1555 1.32
LINK C MSE A 77 N ALA A 78 1555 1555 1.34
LINK C PRO A 84 N MSE A 85 1555 1555 1.33
LINK C MSE A 85 N ARG A 86 1555 1555 1.33
LINK C GLN A 157 N MSE A 158 1555 1555 1.31
LINK C MSE A 158 N VAL A 159 1555 1555 1.33
LINK C GLY A 217 N MSE A 218 1555 1555 1.33
LINK C MSE A 218 N HIS A 219 1555 1555 1.34
LINK C TRP A 261 N MSE A 262 1555 1555 1.32
LINK C MSE A 262 N ASP A 263 1555 1555 1.33
LINK C GLY A 474 N MSE A 475 1555 1555 1.32
LINK C MSE A 475 N TRP A 476 1555 1555 1.34
LINK C LEU B 30 N MSE B 31 1555 1555 1.32
LINK C MSE B 31 N LEU B 32 1555 1555 1.35
LINK C LYS B 76 N MSE B 77 1555 1555 1.33
LINK C MSE B 77 N ALA B 78 1555 1555 1.33
LINK C PRO B 84 N MSE B 85 1555 1555 1.34
LINK C MSE B 85 N ARG B 86 1555 1555 1.33
LINK C GLN B 157 N MSE B 158 1555 1555 1.32
LINK C MSE B 158 N VAL B 159 1555 1555 1.33
LINK C GLY B 217 N MSE B 218 1555 1555 1.32
LINK C MSE B 218 N HIS B 219 1555 1555 1.34
LINK C TRP B 261 N MSE B 262 1555 1555 1.33
LINK C MSE B 262 N ASP B 263 1555 1555 1.33
LINK C GLY B 474 N MSE B 475 1555 1555 1.32
LINK C MSE B 475 N TRP B 476 1555 1555 1.35
CISPEP 1 MET A 1 GLU A 2 0 20.42
CISPEP 2 GLY A 269 THR A 270 0 6.63
CISPEP 3 GLN A 374 GLY A 375 0 14.16
CISPEP 4 THR B 3 LYS B 4 0 20.04
CISPEP 5 LYS B 113 ARG B 114 0 -7.39
CISPEP 6 GLY B 269 THR B 270 0 -0.37
CISPEP 7 GLN B 374 GLY B 375 0 3.49
SITE 1 AC1 6 TRP A 99 ARG A 102 ARG A 137 BOG A1949
SITE 2 AC1 6 BOG A1950 TYR B 59
SITE 1 AC2 9 LEU A 53 ARG A 54 LEU A 56 GLU A 57
SITE 2 AC2 9 TYR A 59 PHE A 61 LEU A 89 ARG A 96
SITE 3 AC2 9 GLN A 249
SITE 1 AC3 4 TRP B 99 ARG B 102 ILE B 103 ARG B 137
SITE 1 AC4 12 LEU B 53 ARG B 54 LEU B 56 GLU B 57
SITE 2 AC4 12 TYR B 59 PHE B 61 ARG B 96 MET B 100
SITE 3 AC4 12 ILE B 101 GLY B 104 LEU B 105 ILE B 255
SITE 1 AC5 2 TRP A 99 BOG A 700
SITE 1 AC6 5 HIS A 91 PRO A 93 ALA A 98 ARG A 137
SITE 2 AC6 5 BOG A 700
SITE 1 AC7 5 ARG A 161 TYR B 398 ARG B 401 ARG B 405
SITE 2 AC7 5 HOH B 894
SITE 1 AC8 4 ILE A 183 SER A 196 TRP A 197 GLN A 198
SITE 1 AC9 31 ILE A 9 GLY A 12 ILE A 13 ASN A 14
SITE 2 AC9 31 LEU A 32 GLU A 33 ALA A 34 CYS A 39
SITE 3 AC9 31 THR A 41 SER A 42 ALA A 44 SER A 45
SITE 4 AC9 31 SER A 46 LYS A 47 LEU A 48 ALA A 172
SITE 5 AC9 31 THR A 206 GLY A 207 GLY A 231 THR A 270
SITE 6 AC9 31 ARG A 317 GLY A 353 LYS A 354 LEU A 355
SITE 7 AC9 31 THR A 356 EDO A1952 HOH A1972 HOH A1986
SITE 8 AC9 31 HOH A1988 HOH A2075 HOH A2076
SITE 1 BC1 33 ILE B 9 GLY B 10 GLY B 12 ILE B 13
SITE 2 BC1 33 ASN B 14 GLU B 33 ALA B 34 CYS B 39
SITE 3 BC1 33 ALA B 40 THR B 41 SER B 42 ALA B 44
SITE 4 BC1 33 SER B 45 SER B 46 LYS B 47 LEU B 48
SITE 5 BC1 33 ALA B 172 THR B 206 GLY B 207 PRO B 208
SITE 6 BC1 33 TRP B 209 GLY B 231 THR B 270 ARG B 317
SITE 7 BC1 33 GLY B 353 LYS B 354 LEU B 355 THR B 356
SITE 8 BC1 33 EDO B 804 HOH B 827 HOH B 831 HOH B 924
SITE 9 BC1 33 HOH B 948
SITE 1 BC2 5 ARG B 254 THR B 271 ASP B 272 HOH B 909
SITE 2 BC2 5 HOH B 919
SITE 1 BC3 5 LEU B 293 ASN B 294 ASN B 297 EDO B 817
SITE 2 BC3 5 HOH B 822
SITE 1 BC4 5 ALA B 34 ARG B 171 FAD B 600 HOH B 924
SITE 2 BC4 5 HOH B 937
SITE 1 BC5 2 TRP B 311 TRP B 468
SITE 1 BC6 5 SER B 43 TRP B 468 ARG B 469 HOH B 843
SITE 2 BC6 5 HOH B 958
SITE 1 BC7 2 ALA A 34 FAD A 600
SITE 1 BC8 6 MSE B 262 HIS B 416 LYS B 472 GLN B 473
SITE 2 BC8 6 EDO B 808 HOH B 853
SITE 1 BC9 4 HIS B 444 GLU B 445 GLN B 473 EDO B 807
SITE 1 CC1 5 SER A 43 TRP A 468 ARG A 469 EDO A1954
SITE 2 CC1 5 EDO A1965
SITE 1 CC2 2 TRP A 311 EDO A1953
SITE 1 CC3 3 ASN A 294 THR A 298 EDO B 817
SITE 1 CC4 6 ASN A 290 LEU A 293 ASN A 294 ASN B 294
SITE 2 CC4 6 HOH B 822 HOH B 856
SITE 1 CC5 2 ILE B 289 ARG B 306
SITE 1 CC6 7 MSE A 262 HIS A 416 LYS A 472 GLN A 473
SITE 2 CC6 7 TRP A 476 IMD A1960 HOH A1995
SITE 1 CC7 5 PRO B 208 GLN B 212 LEU B 228 PRO B 279
SITE 2 CC7 5 HOH B 838
SITE 1 CC8 6 VAL B 455 ASP B 456 HIS B 457 GLU B 458
SITE 2 CC8 6 TRP B 459 TAM B 812
SITE 1 CC9 6 THR A 41 PRO A 279 LYS A 280 GLY A 315
SITE 2 CC9 6 VAL A 316 HOH A2097
SITE 1 DC1 4 HIS A 457 IMD A1961 IMD A1963 ARG B 405
SITE 1 DC2 5 HIS A 416 HIS A 444 GLU A 445 GLN A 473
SITE 2 DC2 5 EDO A1957
SITE 1 DC3 6 ARG A 405 GLN B 157 VAL B 160 ARG B 161
SITE 2 DC3 6 HIS B 457 EDO B 811
SITE 1 DC4 4 ASN A 424 LEU A 427 EDO A1959 HOH A2058
SITE 1 DC5 7 ALA B 40 THR B 41 PRO B 279 LYS B 280
SITE 2 DC5 7 GLY B 315 VAL B 316 HOH B 869
SITE 1 DC6 2 ARG A 405 ARG B 161
SITE 1 DC7 2 MSE B 475 HOH B 896
SITE 1 DC8 6 VAL A 455 ASP A 456 HIS A 457 GLU A 458
SITE 2 DC8 6 TRP A 459 EDO A1959
SITE 1 DC9 1 PHE A 106
SITE 1 EC1 9 CYS A 39 ALA A 40 SER A 43 ALA A 44
SITE 2 EC1 9 TYR A 313 SER A 314 EDO A1953 HOH A2092
SITE 3 EC1 9 HOH A2097
SITE 1 EC2 2 PRO A 237 VAL A 310
SITE 1 EC3 4 ARG B 171 ALA B 172 GLY B 217 HOH B 937
SITE 1 EC4 4 PRO A 208 LEU A 228 PRO A 279 HOH A2002
SITE 1 EC5 9 ARG A 54 TYR A 55 ARG A 254 ILE A 255
SITE 2 EC5 9 THR A 270 ASP A 272 ARG A 317 ARG A 332
SITE 3 EC5 9 HOH A2100
SITE 1 EC6 8 ARG B 54 TYR B 55 ARG B 254 ILE B 255
SITE 2 EC6 8 THR B 270 ASP B 272 ARG B 317 ARG B 332
SITE 1 EC7 3 EDO A1955 GLN B 303 EDO B 803
SITE 1 EC8 1 GLU B 383
SITE 1 EC9 3 TRP B 488 GLU B 491 TYR B 492
SITE 1 FC1 7 GLU A 274 GLU A 285 SER A 287 ASP B 272
SITE 2 FC1 7 VAL B 273 GLU B 274 BCN B 821
SITE 1 FC2 7 ASP A 272 VAL A 273 SER A 287 GLU B 285
SITE 2 FC2 7 SER B 287 BCN B 820 HOH B 910
SITE 1 FC3 3 GLY A 26 LYS A 162 ARG B 404
CRYST1 113.916 114.142 193.591 90.00 90.00 90.00 I 2 2 2 16
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 0.008778 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008761 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005166 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
