HEADER OXIDOREDUCTASE 19-JUN-07 2QCU
TITLE CRYSTAL STRUCTURE OF GLYCEROL-3-PHOSPHATE DEHYDROGENASE
TITLE 2 FROM ESCHERICHIA COLI
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 ORGANISM_TAXID: 562;
SOURCE 4 GENE: GLPD, GLYD;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GLYCEROL-3-PHOSHATE DEHYDROGENASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.I.YEH,U.CHINTE,S.DU
REVDAT 2 24-FEB-09 2QCU 1 VERSN
REVDAT 1 15-APR-08 2QCU 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. 1.75 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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 118338
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6272
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) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.79
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8482
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.04
REMARK 3 BIN R VALUE (WORKING SET) : 0.2620
REMARK 3 BIN FREE R VALUE SET COUNT : 420
REMARK 3 BIN FREE R VALUE : 0.3360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7997
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 419
REMARK 3 SOLVENT ATOMS : 476
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.65
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : -0.03000
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): 0.119
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.117
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.076
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.320
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8582 ; 0.011 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11552 ; 1.740 ; 1.995
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 998 ;14.085 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 393 ;32.356 ;22.774
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1395 ;18.183 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 78 ;17.041 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1233 ; 0.251 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6340 ; 0.019 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4272 ; 0.253 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5733 ; 0.326 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 552 ; 0.167 ; 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): 53 ; 0.288 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.250 ; 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): 5079 ; 2.108 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7970 ; 3.034 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4042 ; 4.344 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3582 ; 6.223 ; 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 499 2
REMARK 3 1 B 5 B 499 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1980 ; 0.08 ; 0.05
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1982 ; 0.56 ; 0.50
REMARK 3 TIGHT THERMAL 1 A (A**2): 1980 ; 0.28 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1982 ; 1.19 ; 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 2QCU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUN-07.
REMARK 100 THE RCSB ID CODE IS RCSB043437.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL; NULL
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : SLS; APS
REMARK 200 BEAMLINE : X10SA; 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9803; 0.97928, 0.97947,
REMARK 200 0.97181
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD;
REMARK 200 MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 136571
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
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 (%) : 99.4
REMARK 200 DATA REDUNDANCY : 9.000
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.71200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE, PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M DI-AMMONIUM HYDROGEN
REMARK 280 PHOSPHATE, 0.1 M TRIS-HCL PH 8.5, 12 % W/V PEG MME 550, 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 56.89550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 57.04850
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 96.40050
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 56.89550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 57.04850
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 96.40050
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 56.89550
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 57.04850
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 96.40050
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 56.89550
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 57.04850
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 96.40050
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 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 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 MET A 1
REMARK 465 GLU A 2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LEU A 37 C
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 HOH B 1036 O HOH B 1037 2.19
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 35 -94.41 -125.12
REMARK 500 ALA A 40 -116.15 -117.23
REMARK 500 ALA A 78 58.80 -144.50
REMARK 500 LYS A 113 16.52 99.57
REMARK 500 ARG A 114 141.27 -23.80
REMARK 500 SER A 116 -17.58 -152.97
REMARK 500 SER A 120 131.50 124.70
REMARK 500 ASP A 143 -157.02 -149.76
REMARK 500 ALA A 205 51.91 -110.94
REMARK 500 LYS A 253 -1.83 81.38
REMARK 500 ASP A 263 -14.21 64.60
REMARK 500 LEU A 319 116.81 43.05
REMARK 500 TRP A 380 -22.45 -153.82
REMARK 500 ILE A 391 -140.43 -109.33
REMARK 500 GLU A 392 58.76 -174.17
REMARK 500 ASP A 396 17.43 132.25
REMARK 500 THR A 420 -65.62 -109.60
REMARK 500 TRP A 459 18.09 58.76
REMARK 500 LEU A 497 -47.60 -161.49
REMARK 500 LEU A 499 -83.25 -115.06
REMARK 500 GLU B 2 -0.53 -163.83
REMARK 500 GLN B 35 -94.21 -126.08
REMARK 500 ALA B 40 -121.82 -114.86
REMARK 500 HIS B 50 -61.73 -109.96
REMARK 500 ALA B 78 58.39 -147.71
REMARK 500 LYS B 113 -59.37 128.79
REMARK 500 ARG B 114 124.97 54.03
REMARK 500 SER B 116 -18.91 -149.60
REMARK 500 ASP B 143 -159.89 -151.31
REMARK 500 ALA B 205 51.44 -107.13
REMARK 500 ILE B 226 109.74 55.70
REMARK 500 LYS B 253 -1.46 77.29
REMARK 500 ASP B 263 -12.43 64.07
REMARK 500 THR B 270 -147.05 -126.46
REMARK 500 LEU B 319 119.78 37.56
REMARK 500 ILE B 376 -109.04 -52.26
REMARK 500 ALA B 379 157.55 -34.24
REMARK 500 TRP B 380 -21.13 -158.31
REMARK 500 ILE B 391 -101.12 -122.15
REMARK 500 GLU B 392 86.60 136.12
REMARK 500 ASP B 394 -66.68 114.62
REMARK 500 LEU B 497 -70.35 -161.87
REMARK 500 ALA B 500 161.11 172.44
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 ARG A 496 LEU A 497 116.49
REMARK 500 LEU A 497 SER A 498 146.84
REMARK 500 SER A 498 LEU A 499 -124.81
REMARK 500 LEU A 499 ALA A 500 -132.25
REMARK 500 ARG B 496 LEU B 497 133.65
REMARK 500 LEU B 497 SER B 498 146.20
REMARK 500 SER B 498 LEU B 499 -139.55
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 701
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 801
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 700
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 802
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 803
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 801
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 802
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 804
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 803
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 600
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 600
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAM A 805
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 806
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 807
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 808
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 809
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 810
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 811
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 812
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 813
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 814
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 815
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 816
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 817
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 818
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 819
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 820
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 821
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 822
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAM A 823
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 804
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 805
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 806
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 807
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 808
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 809
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAM B 810
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 811
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 812
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 813
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 814
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 816
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 817
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 819
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 820
DBREF 2QCU A 1 501 UNP P13035 GLPD_ECOLI 1 501
DBREF 2QCU 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 MET 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 MET ALA
SEQRES 7 A 501 PRO HIS ILE ALA PHE PRO MET 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 MET 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 MET 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 MET 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 MET 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 MET 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 MET ALA
SEQRES 7 B 501 PRO HIS ILE ALA PHE PRO MET 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 MET 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 MET 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 MET 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 MET 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
HET BOG A 700 20
HET BOG A 701 20
HET BOG A 800 20
HET BOG A 801 20
HET BOG B 700 20
HET BOG B 800 20
HET SO4 A 802 5
HET SO4 A 803 5
HET SO4 B 801 5
HET SO4 B 802 5
HET PO4 A 804 5
HET PO4 B 803 5
HET FAD A 600 53
HET FAD B 600 53
HET TAM A 805 11
HET EDO A 806 4
HET IMD A 807 5
HET EDO A 808 4
HET EDO A 809 4
HET EDO A 810 4
HET EDO A 811 4
HET EDO A 812 4
HET EDO A 813 4
HET EDO A 814 4
HET EDO A 815 4
HET EDO A 816 4
HET EDO A 817 4
HET EDO A 818 4
HET EDO A 819 4
HET EDO A 820 4
HET IMD A 821 5
HET EDO A 822 4
HET TAM A 823 11
HET EDO B 804 4
HET EDO B 805 4
HET EDO B 806 4
HET EDO B 807 4
HET EDO B 808 4
HET EDO B 809 4
HET TAM B 810 11
HET EDO B 811 4
HET EDO B 812 4
HET EDO B 813 4
HET EDO B 814 4
HET EDO B 815 4
HET EDO B 816 4
HET EDO B 817 4
HET EDO B 819 4
HET EDO B 820 4
HETNAM BOG B-OCTYLGLUCOSIDE
HETNAM SO4 SULFATE ION
HETNAM PO4 PHOSPHATE ION
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM TAM TRIS(HYDROXYETHYL)AMINOMETHANE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM IMD IMIDAZOLE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 BOG 6(C14 H28 O6)
FORMUL 9 SO4 4(O4 S 2-)
FORMUL 13 PO4 2(O4 P 3-)
FORMUL 15 FAD 2(C27 H33 N9 O15 P2)
FORMUL 17 TAM 3(C7 H17 N O3)
FORMUL 18 EDO 30(C2 H6 O2)
FORMUL 19 IMD 2(C3 H5 N2 1+)
FORMUL 52 HOH *476(H2 O)
HELIX 1 1 GLY A 12 ARG A 25 1 14
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 HIS A 110 1 14
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 PHE A 300 1 16
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 LYS A 354 THR A 356 5 3
HELIX 14 14 THR A 357 THR A 370 1 14
HELIX 15 15 PRO A 371 TYR A 373 5 3
HELIX 16 16 TRP A 380 SER A 384 5 5
HELIX 17 17 ASP A 397 TYR A 406 1 10
HELIX 18 18 THR A 410 TYR A 421 1 12
HELIX 19 19 ASN A 424 GLY A 430 1 7
HELIX 20 20 THR A 434 GLY A 439 5 6
HELIX 21 21 TYR A 447 GLU A 458 1 12
HELIX 22 22 ARG A 462 ARG A 469 1 8
HELIX 23 23 LYS A 472 TRP A 476 5 5
HELIX 24 24 ASN A 478 GLN A 495 1 18
HELIX 25 25 GLY B 12 ARG B 25 1 14
HELIX 26 26 ALA B 40 ALA B 44 5 5
HELIX 27 27 GLY B 52 TYR B 59 5 8
HELIX 28 28 GLU B 60 ALA B 78 1 19
HELIX 29 29 PRO B 97 HIS B 110 1 14
HELIX 30 30 ASP B 147 LYS B 162 1 16
HELIX 31 31 THR B 206 PRO B 208 5 3
HELIX 32 32 TRP B 209 GLY B 217 1 9
HELIX 33 33 ASP B 278 VAL B 282 5 5
HELIX 34 34 GLU B 285 PHE B 300 1 16
HELIX 35 35 SER B 305 ILE B 309 5 5
HELIX 36 36 SER B 326 ILE B 330 5 5
HELIX 37 37 THR B 357 THR B 370 1 14
HELIX 38 38 PRO B 371 TYR B 373 5 3
HELIX 39 39 TRP B 380 SER B 384 5 5
HELIX 40 40 ASP B 397 TYR B 406 1 10
HELIX 41 41 THR B 410 TYR B 421 1 12
HELIX 42 42 ASN B 424 GLY B 430 1 7
HELIX 43 43 THR B 434 GLY B 439 5 6
HELIX 44 44 TYR B 447 GLU B 458 1 12
HELIX 45 45 ARG B 462 ARG B 469 1 8
HELIX 46 46 LYS B 472 TRP B 476 5 5
HELIX 47 47 ASN B 478 GLN B 495 1 18
SHEET 1 A 6 GLU A 165 LEU A 167 0
SHEET 2 A 6 VAL A 29 LEU A 32 1 N MET A 31 O GLU A 165
SHEET 3 A 6 LEU A 6 ILE A 9 1 N VAL A 8 O LEU A 30
SHEET 4 A 6 LEU A 202 ASN A 204 1 O VAL A 203 N ILE A 9
SHEET 5 A 6 LYS A 344 PHE A 351 1 O LEU A 348 N ASN A 204
SHEET 6 A 6 THR A 335 GLU A 341 -1 N HIS A 339 O LEU A 347
SHEET 1 B 8 LEU A 48 ILE A 49 0
SHEET 2 B 8 ARG A 137 VAL A 146 -1 O CYS A 144 N ILE A 49
SHEET 3 B 8 ALA A 82 PRO A 90 -1 N PHE A 87 O TYR A 141
SHEET 4 B 8 ALA A 245 GLN A 249 1 O ALA A 245 N ARG A 86
SHEET 5 B 8 ILE A 255 TRP A 261 -1 O VAL A 256 N LEU A 248
SHEET 6 B 8 PHE A 265 GLY A 269 -1 O GLY A 269 N PHE A 257
SHEET 7 B 8 ILE A 229 PRO A 237 -1 N ILE A 234 O ILE A 268
SHEET 8 B 8 VAL A 273 GLU A 274 -1 O VAL A 273 N LYS A 230
SHEET 1 C 8 THR A 121 ARG A 124 0
SHEET 2 C 8 ARG A 137 VAL A 146 -1 O GLU A 140 N THR A 121
SHEET 3 C 8 ALA A 82 PRO A 90 -1 N PHE A 87 O TYR A 141
SHEET 4 C 8 ALA A 245 GLN A 249 1 O ALA A 245 N ARG A 86
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 229 PRO A 237 -1 N ILE A 234 O ILE A 268
SHEET 8 C 8 TRP A 311 ARG A 317 -1 O TRP A 311 N VAL A 235
SHEET 1 D 3 THR A 170 GLU A 178 0
SHEET 2 D 3 LEU A 181 ASP A 188 -1 O LEU A 181 N GLU A 178
SHEET 3 D 3 LYS A 194 ALA A 199 -1 O TRP A 197 N VAL A 184
SHEET 1 E 4 THR B 3 LYS B 4 0
SHEET 2 E 4 LYS B 194 ALA B 199 1 O GLN B 198 N LYS B 4
SHEET 3 E 4 LEU B 181 ASP B 188 -1 N TRP B 182 O ALA B 199
SHEET 4 E 4 THR B 170 GLU B 178 -1 N GLU B 178 O LEU B 181
SHEET 1 F 6 GLU B 165 LEU B 167 0
SHEET 2 F 6 VAL B 29 LEU B 32 1 N MET B 31 O GLU B 165
SHEET 3 F 6 LEU B 6 ILE B 9 1 N VAL B 8 O LEU B 30
SHEET 4 F 6 LEU B 202 ASN B 204 1 O VAL B 203 N ILE B 9
SHEET 5 F 6 LYS B 344 PHE B 351 1 O LEU B 348 N ASN B 204
SHEET 6 F 6 THR B 335 GLU B 341 -1 N THR B 335 O PHE B 351
SHEET 1 G 8 LEU B 48 ILE B 49 0
SHEET 2 G 8 ARG B 137 VAL B 146 -1 O CYS B 144 N ILE B 49
SHEET 3 G 8 ALA B 82 PRO B 90 -1 N LEU B 89 O PHE B 139
SHEET 4 G 8 ALA B 245 GLN B 249 1 O ALA B 245 N ARG B 86
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 GLY B 269 N PHE B 257
SHEET 7 G 8 ILE B 229 PRO B 237 -1 N ILE B 234 O ILE B 268
SHEET 8 G 8 VAL B 273 GLU B 274 -1 O VAL B 273 N LYS B 230
SHEET 1 H 8 THR B 121 ARG B 124 0
SHEET 2 H 8 ARG B 137 VAL B 146 -1 O GLU B 140 N THR B 121
SHEET 3 H 8 ALA B 82 PRO B 90 -1 N LEU B 89 O PHE B 139
SHEET 4 H 8 ALA B 245 GLN B 249 1 O ALA B 245 N ARG B 86
SHEET 5 H 8 ILE B 255 TRP B 261 -1 O VAL B 256 N LEU B 248
SHEET 6 H 8 PHE B 265 GLY B 269 -1 O GLY B 269 N PHE B 257
SHEET 7 H 8 ILE B 229 PRO B 237 -1 N ILE B 234 O ILE B 268
SHEET 8 H 8 TRP B 311 ARG B 317 -1 O TRP B 311 N VAL B 235
CISPEP 1 GLY A 269 THR A 270 0 26.14
CISPEP 2 ARG A 395 ASP A 396 0 -1.63
CISPEP 3 ASP A 396 ASP A 397 0 -1.27
CISPEP 4 GLY B 269 THR B 270 0 0.93
CISPEP 5 ASP B 396 ASP B 397 0 1.32
SITE 1 AC1 1 TRP A 99
SITE 1 AC2 4 TRP A 99 ARG A 102 ARG A 137 BOG A 800
SITE 1 AC3 7 HIS A 91 PRO A 93 PRO A 97 ALA A 98
SITE 2 AC3 7 GLU A 134 LYS A 136 BOG A 701
SITE 1 AC4 9 LEU A 53 ARG A 54 LEU A 56 GLU A 57
SITE 2 AC4 9 TYR A 59 ARG A 96 ILE A 101 GLY A 104
SITE 3 AC4 9 MET A 107
SITE 1 AC5 6 ALA B 98 TRP B 99 ILE B 103 ARG B 137
SITE 2 AC5 6 BOG B 800 EDO B 820
SITE 1 AC6 6 TYR A 59 ARG A 62 ARG B 102 THR B 121
SITE 2 AC6 6 GLY B 122 BOG B 700
SITE 1 AC7 5 VAL A 310 TRP A 311 TRP A 468 GLY A 474
SITE 2 AC7 5 MET A 475
SITE 1 AC8 5 HIS A 80 PHE A 83 ASP A 394 ARG A 419
SITE 2 AC8 5 HOH A1031
SITE 1 AC9 4 VAL B 310 TRP B 468 GLY B 474 MET B 475
SITE 1 BC1 7 ARG A 161 HOH A 942 TYR B 398 ARG B 401
SITE 2 BC1 7 LEU B 402 ARG B 405 GLU B 426
SITE 1 BC2 9 ARG A 54 TYR A 55 ARG A 317 ARG A 332
SITE 2 BC2 9 LYS A 354 HOH A 897 HOH A 973 HOH A 989
SITE 3 BC2 9 HOH A1057
SITE 1 BC3 9 ARG B 54 TYR B 55 ARG B 317 ARG B 332
SITE 2 BC3 9 HOH B 908 HOH B 922 HOH B 943 HOH B1005
SITE 3 BC3 9 HOH B1038
SITE 1 BC4 34 ILE A 9 GLY A 10 GLY A 11 GLY A 12
SITE 2 BC4 34 ILE A 13 ASN A 14 GLU A 33 ALA A 34
SITE 3 BC4 34 CYS A 39 ALA A 40 THR A 41 SER A 42
SITE 4 BC4 34 ALA A 44 SER A 45 SER A 46 LYS A 47
SITE 5 BC4 34 LEU A 48 HIS A 50 ALA A 172 THR A 206
SITE 6 BC4 34 GLY A 207 PRO A 208 PHE A 213 GLY A 231
SITE 7 BC4 34 THR A 270 ARG A 317 GLY A 353 LYS A 354
SITE 8 BC4 34 LEU A 355 THR A 356 EDO A 806 HOH A 824
SITE 9 BC4 34 HOH A 825 HOH A1052
SITE 1 BC5 32 ILE B 9 GLY B 10 GLY B 12 ILE B 13
SITE 2 BC5 32 ASN B 14 LEU B 32 GLU B 33 ALA B 34
SITE 3 BC5 32 CYS B 39 ALA B 40 THR B 41 SER B 42
SITE 4 BC5 32 ALA B 44 SER B 45 SER B 46 LYS B 47
SITE 5 BC5 32 LEU B 48 HIS B 50 ALA B 172 THR B 206
SITE 6 BC5 32 GLY B 207 PRO B 208 GLY B 231 ARG B 317
SITE 7 BC5 32 GLY B 353 LYS B 354 LEU B 355 THR B 356
SITE 8 BC5 32 EDO B 806 HOH B 821 HOH B 822 HOH B1050
SITE 1 BC6 8 ALA A 23 GLY A 24 LYS A 162 HOH A 942
SITE 2 BC6 8 HOH A1056 ARG B 401 ARG B 404 HOH B 971
SITE 1 BC7 4 ALA A 34 ARG A 171 LYS A 280 FAD A 600
SITE 1 BC8 4 HIS A 444 GLU A 445 GLN A 473 EDO A 811
SITE 1 BC9 8 SER A 43 TRP A 311 TRP A 468 EDO A 812
SITE 2 BC9 8 HOH A 826 HOH A 832 HOH A1034 HOH A1035
SITE 1 CC1 5 GLN A 303 EDO A 815 HOH A 964 HOH A1039
SITE 2 CC1 5 EDO B 805
SITE 1 CC2 2 ARG A 306 ILE A 309
SITE 1 CC3 7 HIS A 416 THR A 471 LYS A 472 GLN A 473
SITE 2 CC3 7 TRP A 476 IMD A 807 HOH A 872
SITE 1 CC4 3 TRP A 311 TRP A 468 EDO A 808
SITE 1 CC5 1 GLU A 448
SITE 1 CC6 2 GLU A 440 ASP A 441
SITE 1 CC7 5 ASN A 294 ASN A 297 THR A 298 EDO A 809
SITE 2 CC7 5 HOH A 928
SITE 1 CC8 5 ASN A 294 HOH A 947 SER B 305 ARG B 306
SITE 2 CC8 5 HOH B 839
SITE 1 CC9 4 ARG A 254 THR A 271 ASP A 272 TAM A 823
SITE 1 DC1 8 ALA A 40 THR A 41 PRO A 279 LYS A 280
SITE 2 DC1 8 VAL A 282 GLY A 315 VAL A 316 HOH A1043
SITE 1 DC2 4 ARG A 404 ALA B 23 GLY B 24 HOH B1025
SITE 1 DC3 4 ASP A 397 ARG A 404 HOH A 939 HOH A 969
SITE 1 DC4 7 GLN A 157 ASN A 424 LEU A 427 TYR A 453
SITE 2 DC4 7 EDO A 822 HOH A1066 HOH B 957
SITE 1 DC5 6 GLN A 157 HIS A 457 TRP A 459 IMD A 821
SITE 2 DC5 6 HOH A1063 ARG B 405
SITE 1 DC6 10 ASP A 272 VAL A 273 GLU A 274 GLU A 285
SITE 2 DC6 10 SER A 287 GLU A 288 EDO A 817 GLU B 285
SITE 3 DC6 10 SER B 287 HOH B 924
SITE 1 DC7 3 ARG B 254 THR B 271 ASP B 272
SITE 1 DC8 5 EDO A 809 LEU B 293 ASN B 294 ASN B 297
SITE 2 DC8 5 HOH B 860
SITE 1 DC9 4 ALA B 34 TRP B 209 LYS B 280 FAD B 600
SITE 1 EC1 3 TRP B 311 TRP B 468 EDO B 811
SITE 1 EC2 4 MET B 262 EDO B 817 HOH B1030 HOH B1033
SITE 1 EC3 2 ILE B 289 ARG B 306
SITE 1 EC4 9 ARG A 405 GLU A 426 GLN B 157 VAL B 160
SITE 2 EC4 9 ARG B 161 PRO B 387 ASN B 424 HIS B 457
SITE 3 EC4 9 HOH B1054
SITE 1 EC5 7 SER B 43 ALA B 44 TRP B 311 TRP B 468
SITE 2 EC5 7 EDO B 807 HOH B 830 HOH B 833
SITE 1 EC6 7 ARG B 88 ARG B 124 PHE B 125 SER B 129
SITE 2 EC6 7 VAL B 130 GLN B 242 HOH B1000
SITE 1 EC7 4 PRO B 208 GLN B 212 LEU B 228 PRO B 279
SITE 1 EC8 5 VAL B 455 ASP B 456 HIS B 457 GLU B 458
SITE 2 EC8 5 TRP B 459
SITE 1 EC9 1 ILE B 101
SITE 1 FC1 5 HIS B 416 EDO B 808 EDO B 819 HOH B 826
SITE 2 FC1 5 HOH B1028
SITE 1 FC2 5 HIS B 444 GLU B 445 GLN B 473 EDO B 817
SITE 2 FC2 5 HOH B 866
SITE 1 FC3 5 HIS B 91 PRO B 93 PRO B 97 ALA B 98
SITE 2 FC3 5 BOG B 700
CRYST1 113.791 114.097 192.801 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 0.008788 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008764 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005187 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
