HEADER OXIDOREDUCTASE 30-AUG-07 2R45
TITLE CRYSTAL STRUCTURE OF ESCHERICHIA COLI GLYCEROL-3-PHOSPHATE
TITLE 2 DEHYDROGENASE IN COMPLEX WITH 2-PHOSPHO-D-GLYCERIC ACID
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;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GLPD, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.I.YEH,S.DU,U.CHINTE
REVDAT 2 24-FEB-09 2R45 1 VERSN
REVDAT 1 15-APR-08 2R45 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. 2.30 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 54271
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2754
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3122
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.76
REMARK 3 BIN R VALUE (WORKING SET) : 0.2400
REMARK 3 BIN FREE R VALUE SET COUNT : 171
REMARK 3 BIN FREE R VALUE : 0.3530
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7924
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 398
REMARK 3 SOLVENT ATOMS : 305
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.76000
REMARK 3 B22 (A**2) : 0.77000
REMARK 3 B33 (A**2) : -1.53000
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): 0.314
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.259
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.181
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.337
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.908
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8340 ; 0.028 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11315 ; 2.747 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 999 ;10.074 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 394 ;32.724 ;22.792
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1400 ;21.924 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 78 ;20.119 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1204 ; 0.206 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6350 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4307 ; 0.293 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5421 ; 0.322 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 546 ; 0.239 ; 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): 37 ; 0.201 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.371 ; 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): 5153 ; 1.328 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7967 ; 2.143 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3823 ; 3.272 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3348 ; 4.952 ; 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 495 4
REMARK 3 1 B 5 B 495 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 3929 ; 0.480 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 3929 ; 0.970 ; 2.000
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 2R45 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-08.
REMARK 100 THE RCSB ID CODE IS RCSB044401.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-APR-07
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 : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9803
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-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55038
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
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 (%) : 98.5
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.50500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.29
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 TAPS, 12% W/V PEG 6000, PH 8.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 56.87200
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 56.95400
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 96.53450
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 56.87200
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 56.95400
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 96.53450
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 56.87200
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 56.95400
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 96.53450
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 56.87200
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 56.95400
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 96.53450
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 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 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 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 ARG B 496
REMARK 465 LEU B 497
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 -45.59 40.48
REMARK 500 GLN A 35 -95.20 -126.48
REMARK 500 ALA A 40 -116.93 -114.89
REMARK 500 ALA A 78 58.19 -140.25
REMARK 500 THR A 115 -84.43 -78.52
REMARK 500 ASP A 143 -179.31 -171.93
REMARK 500 ASP A 190 -61.06 -101.00
REMARK 500 THR A 191 -71.85 -70.01
REMARK 500 ASP A 263 -1.80 63.94
REMARK 500 ASP A 321 91.87 -58.62
REMARK 500 GLU A 323 20.85 48.75
REMARK 500 PRO A 371 -35.34 -30.98
REMARK 500 GLN A 374 -132.28 24.40
REMARK 500 TRP A 380 -10.53 -154.28
REMARK 500 GLU A 392 94.40 11.73
REMARK 500 ASP A 394 -62.61 89.41
REMARK 500 ASP A 396 -22.78 130.48
REMARK 500 THR A 420 -66.40 -96.87
REMARK 500 SER A 423 -9.89 -47.45
REMARK 500 TRP A 459 19.41 58.94
REMARK 500 GLN A 494 -81.49 -51.65
REMARK 500 GLN B 35 -102.42 -122.24
REMARK 500 ALA B 38 17.74 55.16
REMARK 500 ALA B 40 -119.42 -122.31
REMARK 500 SER B 116 -26.23 -142.66
REMARK 500 SER B 120 131.98 106.15
REMARK 500 SER B 129 -179.38 -67.16
REMARK 500 ASP B 143 -169.95 -166.92
REMARK 500 ASN B 179 32.67 76.53
REMARK 500 ARG B 238 117.80 -30.89
REMARK 500 ASP B 263 -5.30 57.74
REMARK 500 ASP B 321 85.00 -60.47
REMARK 500 ASP B 325 -62.10 120.83
REMARK 500 LYS B 354 159.03 -48.46
REMARK 500 PRO B 371 -27.50 -34.08
REMARK 500 TRP B 380 -12.50 -158.48
REMARK 500 GLU B 392 89.55 8.20
REMARK 500 ASP B 394 177.77 64.57
REMARK 500 ARG B 395 -11.30 69.28
REMARK 500 ASP B 396 -63.39 -168.50
REMARK 500 THR B 420 -66.58 -106.53
REMARK 500 ARG B 469 -62.05 -120.22
REMARK 500 THR B 493 -64.08 -93.67
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 TYR A 373 GLN A 374 149.81
REMARK 500 ILE A 391 GLU A 392 -147.54
REMARK 500 ASP A 394 ARG A 395 -147.80
REMARK 500 ILE B 391 GLU B 392 -148.70
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 BOG B 800
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 A 900
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 900
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 PO4 A 1951
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 901
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 902
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1952
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 903
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1953
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 904
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1954
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1955
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 600
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 600
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 905
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 1956
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 906
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 907
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 908
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1957
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 1958
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1959
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1960
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1961
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 909
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1962
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 910
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1963
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD B 912
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T3A B 7066
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T3A A 7066
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 7067
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 7067
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2PG B 700
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2PG A 700
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2R46 RELATED DB: PDB
REMARK 900 SAME PROTEIN IN COMPLEX WITH 2-PHOSPHOPYRUVIC ACID
DBREF 2R45 A 1 501 UNP P13035 GLPD_ECOLI 1 501
DBREF 2R45 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 800 20
HET BOG A 900 20
HET BOG A1949 20
HET BOG A1950 20
HET BOG B 800 20
HET BOG B 900 20
HET PO4 A1951 5
HET PO4 A1952 5
HET PO4 A1953 5
HET PO4 A1954 5
HET PO4 A1955 5
HET PO4 B 901 5
HET PO4 B 902 5
HET PO4 B 903 5
HET PO4 B 904 5
HET FAD A 600 53
HET IMD A1956 5
HET EDO A1957 4
HET IMD A1958 5
HET EDO A1959 4
HET EDO A1960 4
HET EDO A1961 4
HET EDO A1962 4
HET EDO A1963 4
HET T3A A7066 15
HET EDO A7067 4
HET 2PG A 700 11
HET FAD B 600 53
HET EDO B 905 4
HET EDO B 906 4
HET EDO B 907 4
HET EDO B 908 4
HET EDO B 909 4
HET EDO B 910 4
HET EDO B 911 4
HET IMD B 912 5
HET T3A B7066 15
HET EDO B7067 4
HET 2PG B 700 11
HETNAM BOG B-OCTYLGLUCOSIDE
HETNAM PO4 PHOSPHATE ION
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM IMD IMIDAZOLE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM T3A N-(TRIS(HYDROXYMETHYL)METHYL)-3-AMINOPROPANESULFONIC
HETNAM 2 T3A ACID
HETNAM 2PG 2-PHOSPHOGLYCERIC ACID
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 BOG 6(C14 H28 O6)
FORMUL 9 PO4 9(O4 P 3-)
FORMUL 18 FAD 2(C27 H33 N9 O15 P2)
FORMUL 19 IMD 3(C3 H5 N2 1+)
FORMUL 20 EDO 15(C2 H6 O2)
FORMUL 27 T3A 2(C7 H17 N O6 S)
FORMUL 29 2PG 2(C3 H7 O7 P)
FORMUL 42 HOH *305(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 GLU A 285 PHE A 300 1 16
HELIX 10 10 SER A 305 ILE A 309 5 5
HELIX 11 11 SER A 326 ILE A 330 5 5
HELIX 12 12 LYS A 354 THR A 356 5 3
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 ASP A 396 TYR A 406 1 11
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 GLN A 494 1 17
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 LEU B 56 5 5
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 GLU B 285 PHE B 300 1 16
HELIX 33 33 SER B 305 ILE B 309 5 5
HELIX 34 34 SER B 326 ILE B 330 5 5
HELIX 35 35 THR B 357 LEU B 369 1 13
HELIX 36 36 THR B 370 TYR B 373 5 4
HELIX 37 37 TRP B 380 SER B 384 5 5
HELIX 38 38 ASP B 396 TYR B 406 1 11
HELIX 39 39 THR B 410 TYR B 421 1 12
HELIX 40 40 ASN B 424 GLY B 430 1 7
HELIX 41 41 THR B 434 GLY B 439 5 6
HELIX 42 42 TYR B 447 TRP B 459 1 13
HELIX 43 43 ARG B 462 ARG B 469 1 8
HELIX 44 44 LYS B 472 TRP B 476 5 5
HELIX 45 45 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 VAL A 29 O GLU A 165
SHEET 3 A 6 LEU A 6 ILE A 9 1 N VAL A 8 O LEU A 32
SHEET 4 A 6 LEU A 202 ASN A 204 1 O VAL A 203 N ILE A 7
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 THR A 335 O PHE A 351
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 MET A 85 O ASP A 143
SHEET 4 B 8 ALA A 245 GLN A 249 1 O ALA A 245 N ARG A 88
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 PHE A 265 N TRP A 261
SHEET 7 B 8 ILE A 226 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 MET A 85 O ASP A 143
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 PHE A 265 N TRP A 261
SHEET 7 C 8 ILE A 226 PRO A 237 -1 N ILE A 234 O ILE A 268
SHEET 8 C 8 TRP A 311 CYS A 320 -1 O LEU A 319 N ARG A 227
SHEET 1 D 3 THR A 170 GLU A 178 0
SHEET 2 D 3 LEU A 181 ASP A 188 -1 O GLU A 185 N THR A 173
SHEET 3 D 3 LYS A 194 ALA A 199 -1 O ALA A 199 N TRP A 182
SHEET 1 E 6 GLU B 165 LEU B 167 0
SHEET 2 E 6 VAL B 29 LEU B 32 1 N MET B 31 O GLU B 165
SHEET 3 E 6 LEU B 6 ILE B 9 1 N VAL B 8 O LEU B 32
SHEET 4 E 6 LEU B 202 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 LEU B 202
SHEET 6 E 6 THR B 335 GLU B 341 -1 N ASP B 337 O SER B 349
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 PHE B 265 N TRP B 261
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 TYR B 275 -1 O TYR B 275 N LEU B 228
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 PHE B 265 N TRP B 261
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 GLU B 185 N THR B 173
SHEET 3 H 3 LYS B 194 ALA B 199 -1 O ALA B 199 N TRP B 182
CISPEP 1 MET A 1 GLU A 2 0 22.48
CISPEP 2 GLY A 269 THR A 270 0 2.35
CISPEP 3 GLN A 374 GLY A 375 0 18.09
CISPEP 4 GLN A 494 GLN A 495 0 -20.43
CISPEP 5 LYS B 113 ARG B 114 0 -4.95
CISPEP 6 GLY B 269 THR B 270 0 9.07
SITE 1 AC1 3 TRP B 99 ARG B 102 ARG B 137
SITE 1 AC2 4 TRP A 99 ARG A 102 ARG A 137 TYR B 59
SITE 1 AC3 9 LEU A 53 ARG A 54 LEU A 56 GLU A 57
SITE 2 AC3 9 LEU A 89 ARG A 96 MET A 100 ILE A 101
SITE 3 AC3 9 GLY A 104
SITE 1 AC4 7 LEU B 53 ARG B 54 LEU B 56 GLU B 57
SITE 2 AC4 7 ARG B 96 ILE B 101 LEU B 105
SITE 1 AC5 5 HIS A 91 PRO A 93 ALA A 98 ARG A 137
SITE 2 AC5 5 ASP B 322
SITE 1 AC6 2 TRP A 468 GLY A 474
SITE 1 AC7 4 ARG A 161 TYR B 398 ARG B 401 ARG B 405
SITE 1 AC8 5 PRO B 208 GLN B 212 LEU B 228 GLY B 277
SITE 2 AC8 5 PRO B 279
SITE 1 AC9 3 ARG A 462 ALA A 463 ASP A 464
SITE 1 BC1 3 ARG B 462 ALA B 463 ASP B 464
SITE 1 BC2 3 ARG A 92 PRO A 93 HIS A 94
SITE 1 BC3 3 ARG B 92 PRO B 93 HIS B 94
SITE 1 BC4 4 TYR A 398 ARG A 401 ARG A 405 ARG B 161
SITE 1 BC5 5 PRO A 208 GLN A 212 LEU A 228 GLY A 277
SITE 2 BC5 5 PRO A 279
SITE 1 BC6 30 ILE A 9 GLY A 10 GLY A 11 GLY A 12
SITE 2 BC6 30 ILE A 13 ASN A 14 GLU A 33 ALA A 34
SITE 3 BC6 30 CYS A 39 ALA A 40 THR A 41 SER A 42
SITE 4 BC6 30 ALA A 44 SER A 45 SER A 46 LYS A 47
SITE 5 BC6 30 LEU A 48 ALA A 172 THR A 206 GLY A 207
SITE 6 BC6 30 PRO A 208 TRP A 209 PHE A 213 GLY A 231
SITE 7 BC6 30 THR A 270 ARG A 317 GLY A 353 LYS A 354
SITE 8 BC6 30 LEU A 355 THR A 356
SITE 1 BC7 31 ILE B 9 GLY B 10 GLY B 12 ILE B 13
SITE 2 BC7 31 ASN B 14 LEU B 32 GLU B 33 ALA B 34
SITE 3 BC7 31 CYS B 39 ALA B 40 THR B 41 SER B 42
SITE 4 BC7 31 ALA B 44 SER B 45 SER B 46 LYS B 47
SITE 5 BC7 31 LEU B 48 HIS B 50 ARG B 171 ALA B 172
SITE 6 BC7 31 THR B 206 GLY B 207 PRO B 208 GLY B 231
SITE 7 BC7 31 HIS B 233 THR B 270 ARG B 317 GLY B 353
SITE 8 BC7 31 LYS B 354 LEU B 355 THR B 356
SITE 1 BC8 3 ARG B 254 THR B 271 ASP B 272
SITE 1 BC9 4 HIS A 80 PHE A 83 ASP A 394 ARG A 419
SITE 1 CC1 3 ALA B 34 ARG B 171 TRP B 209
SITE 1 CC2 2 TRP B 311 TRP B 468
SITE 1 CC3 4 SER B 43 TRP B 311 TRP B 468 ARG B 469
SITE 1 CC4 3 ALA A 34 ARG A 171 TRP A 209
SITE 1 CC5 4 HIS A 416 HIS A 444 GLU A 445 GLN A 473
SITE 1 CC6 3 SER A 43 TRP A 311 ARG A 469
SITE 1 CC7 1 TRP A 311
SITE 1 CC8 3 ASN A 294 SER B 305 ARG B 306
SITE 1 CC9 5 SER B 412 HIS B 416 HIS B 444 GLU B 445
SITE 2 CC9 5 GLN B 473
SITE 1 DC1 4 ARG A 254 THR A 271 ASP A 272 SER B 287
SITE 1 DC2 2 LYS B 162 SER B 384
SITE 1 DC3 3 ARG A 161 TRP A 380 SER A 384
SITE 1 DC4 3 TRP B 488 GLU B 491 TYR B 492
SITE 1 DC5 5 GLN B 157 ASP B 456 HIS B 457 GLU B 458
SITE 2 DC5 5 TRP B 459
SITE 1 DC6 6 GLN A 157 ASP A 456 HIS A 457 GLU A 458
SITE 2 DC6 6 TRP A 459 ARG B 405
SITE 1 DC7 4 GLN A 157 ARG A 161 ASN A 424 GLU B 426
SITE 1 DC8 5 ARG A 405 GLN B 157 ARG B 161 PRO B 387
SITE 2 DC8 5 ASN B 424
SITE 1 DC9 10 ARG B 54 TYR B 55 ARG B 254 ILE B 255
SITE 2 DC9 10 PHE B 257 THR B 270 ASP B 272 ARG B 317
SITE 3 DC9 10 ARG B 332 LYS B 354
SITE 1 EC1 8 ARG A 54 TYR A 55 ARG A 254 ILE A 255
SITE 2 EC1 8 PHE A 257 THR A 270 ARG A 317 ARG A 332
CRYST1 113.744 113.908 193.069 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 0.008792 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008779 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005179 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
