HEADER OXIDOREDUCTASE 12-FEB-07 2JGD
TITLE E. COLI 2-OXOGLUTARATE DEHYDROGENASE (E1O)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ALPHA- KETOGLUTARATE DEHYDROGENASE;
COMPND 5 EC: 1.2.4.2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: ALPHA- KETOGLUTARATE DEHYDROGENASE;
COMPND 11 EC: 1.2.4.2;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 11 ORGANISM_TAXID: 83333;
SOURCE 12 STRAIN: K12;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS 2-OXOGLUTARATE DEHYDROGENASE, FLAVOPROTEIN, OXIDOREDUCTASE,
KEYWDS 2 THIAMINE DIPHOSPHATE, THIAMINE PYROPHOSPHATE, ADENOSINE
KEYWDS 3 MONOPHOSPHATE, E1O, KGDH, OGDH, GLYCOLYSIS, OXALOACETATE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.A.W.FRANK,A.J.PRICE,F.D.NORTHROP,R.N.PERHAM,B.F.LUISI
REVDAT 4 24-FEB-09 2JGD 1 VERSN
REVDAT 3 17-APR-07 2JGD 1 JRNL
REVDAT 2 03-APR-07 2JGD 1 JRNL
REVDAT 1 27-FEB-07 2JGD 0
JRNL AUTH R.A.W.FRANK,A.J.PRICE,F.D.NORTHROP,R.N.PERHAM,
JRNL AUTH 2 B.F.LUISI
JRNL TITL CRYSTAL STRUCTURE OF THE E1 COMPONENT OF THE
JRNL TITL 2 ESCHERICHIA COLI 2-OXOGLUTARATE DEHYDROGENASE
JRNL TITL 3 MULTIENZYME COMPLEX.
JRNL REF J.MOL.BIOL. V. 368 639 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17367808
JRNL DOI 10.1016/J.JMB.2007.01.080
REMARK 2
REMARK 2 RESOLUTION. 2.6 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.09
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 76341
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4041
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5422
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3080
REMARK 3 BIN FREE R VALUE SET COUNT : 290
REMARK 3 BIN FREE R VALUE : 0.3990
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12593
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 46
REMARK 3 SOLVENT ATOMS : 735
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : -0.01000
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): 0.376
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.276
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.900
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12931 ; 0.011 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17527 ; 1.079 ; 1.947
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1611 ; 9.894 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 618 ;36.348 ;23.738
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2086 ;19.587 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 93 ;21.838 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1906 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9959 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 6181 ; 0.259 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 8807 ; 0.333 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 723 ; 0.234 ; 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): 31 ; 0.300 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.224 ; 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): 8041 ; 8.388 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12864 ;10.148 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4890 ;15.484 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4659 ;16.373 ; 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 84 A 933 1
REMARK 3 1 B 84 B 933 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 6112 ; 0.48 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 6112 ; 2.13 ; 0.50
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 : 1.40
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 2JGD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-FEB-07.
REMARK 100 THE PDBE ID CODE IS EBI-31427.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.939272
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 80455
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 70.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 8.700
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 8.60
REMARK 200 R MERGE FOR SHELL (I) : 0.87000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: SELENIUM SITES WERE FOUND WITH MAD DATA IN SHELXD.
REMARK 200 PHASES WERE DETERMINED WITH SAD DATA IN PHASER
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SITTING DROP: 1UL 12% PEG 4000,
REMARK 280 50MM SOCIUM CITRATE PH5.6. 1UL 10MG/ML TE1O. RESERVOIR:
REMARK 280 1UL 12% PEG 4000, 50MM SOCIUM CITRATE PH5.6.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 125.90550
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 71.24650
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 71.24650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 62.95275
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 71.24650
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 71.24650
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 188.85825
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 71.24650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 71.24650
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 62.95275
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 71.24650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 71.24650
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 188.85825
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 125.90550
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 GLN A 2
REMARK 465 ASN A 3
REMARK 465 SER A 4
REMARK 465 ALA A 5
REMARK 465 LEU A 6
REMARK 465 LYS A 7
REMARK 465 ALA A 8
REMARK 465 TRP A 9
REMARK 465 LEU A 10
REMARK 465 ASP A 11
REMARK 465 SER A 12
REMARK 465 SER A 13
REMARK 465 TYR A 14
REMARK 465 LEU A 15
REMARK 465 SER A 16
REMARK 465 GLY A 17
REMARK 465 ALA A 18
REMARK 465 ASN A 19
REMARK 465 GLN A 20
REMARK 465 SER A 21
REMARK 465 TRP A 22
REMARK 465 ILE A 23
REMARK 465 GLU A 24
REMARK 465 GLN A 25
REMARK 465 LEU A 26
REMARK 465 TYR A 27
REMARK 465 GLU A 28
REMARK 465 ASP A 29
REMARK 465 PHE A 30
REMARK 465 LEU A 31
REMARK 465 THR A 32
REMARK 465 ASP A 33
REMARK 465 PRO A 34
REMARK 465 ASP A 35
REMARK 465 SER A 36
REMARK 465 VAL A 37
REMARK 465 ASP A 38
REMARK 465 ALA A 39
REMARK 465 ASN A 40
REMARK 465 TRP A 41
REMARK 465 ARG A 42
REMARK 465 SER A 43
REMARK 465 THR A 44
REMARK 465 PHE A 45
REMARK 465 GLN A 46
REMARK 465 GLN A 47
REMARK 465 LEU A 48
REMARK 465 PRO A 49
REMARK 465 GLY A 50
REMARK 465 THR A 51
REMARK 465 GLY A 52
REMARK 465 VAL A 53
REMARK 465 LYS A 54
REMARK 465 PRO A 55
REMARK 465 ASP A 56
REMARK 465 GLN A 57
REMARK 465 PHE A 58
REMARK 465 HIS A 59
REMARK 465 SER A 60
REMARK 465 GLN A 61
REMARK 465 THR A 62
REMARK 465 ARG A 63
REMARK 465 GLU A 64
REMARK 465 TYR A 65
REMARK 465 PHE A 66
REMARK 465 ARG A 67
REMARK 465 ARG A 68
REMARK 465 LEU A 69
REMARK 465 ALA A 70
REMARK 465 LYS A 71
REMARK 465 ASP A 72
REMARK 465 ALA A 73
REMARK 465 SER A 74
REMARK 465 ARG A 75
REMARK 465 TYR A 76
REMARK 465 SER A 77
REMARK 465 SER A 78
REMARK 465 THR A 79
REMARK 465 ILE A 80
REMARK 465 SER A 81
REMARK 465 ASP A 82
REMARK 465 PRO A 83
REMARK 465 LYS A 119
REMARK 465 VAL A 120
REMARK 465 ALA A 121
REMARK 465 ALA A 133
REMARK 465 SER A 146
REMARK 465 GLY A 147
REMARK 465 LYS A 148
REMARK 465 GLY A 191
REMARK 465 ALA A 224
REMARK 465 LYS A 225
REMARK 465 LYS A 287
REMARK 465 GLU A 288
REMARK 465 VAL A 392
REMARK 465 GLY A 393
REMARK 465 PHE A 394
REMARK 465 THR A 395
REMARK 465 THR A 396
REMARK 465 SER A 397
REMARK 465 ASN A 398
REMARK 465 PRO A 399
REMARK 465 LEU A 400
REMARK 465 ASP A 401
REMARK 465 ALA A 402
REMARK 465 ARG A 403
REMARK 465 SER A 404
REMARK 465 THR A 405
REMARK 465 PRO A 406
REMARK 465 GLY A 459
REMARK 465 HIS A 460
REMARK 465 ASN A 461
REMARK 465 GLU A 462
REMARK 465 ALA A 463
REMARK 465 ASP A 464
REMARK 465 GLU A 465
REMARK 465 PRO A 466
REMARK 465 SER A 467
REMARK 465 ALA A 468
REMARK 465 THR A 469
REMARK 465 MET B 1
REMARK 465 GLN B 2
REMARK 465 ASN B 3
REMARK 465 SER B 4
REMARK 465 ALA B 5
REMARK 465 LEU B 6
REMARK 465 LYS B 7
REMARK 465 ALA B 8
REMARK 465 TRP B 9
REMARK 465 LEU B 10
REMARK 465 ASP B 11
REMARK 465 SER B 12
REMARK 465 SER B 13
REMARK 465 TYR B 14
REMARK 465 LEU B 15
REMARK 465 SER B 16
REMARK 465 GLY B 17
REMARK 465 ALA B 18
REMARK 465 ASN B 19
REMARK 465 GLN B 20
REMARK 465 SER B 21
REMARK 465 TRP B 22
REMARK 465 ILE B 23
REMARK 465 GLU B 24
REMARK 465 GLN B 25
REMARK 465 LEU B 26
REMARK 465 TYR B 27
REMARK 465 GLU B 28
REMARK 465 ASP B 29
REMARK 465 PHE B 30
REMARK 465 LEU B 31
REMARK 465 THR B 32
REMARK 465 ASP B 33
REMARK 465 PRO B 34
REMARK 465 ASP B 35
REMARK 465 SER B 36
REMARK 465 VAL B 37
REMARK 465 ASP B 38
REMARK 465 ALA B 39
REMARK 465 ASN B 40
REMARK 465 TRP B 41
REMARK 465 ARG B 42
REMARK 465 SER B 43
REMARK 465 THR B 44
REMARK 465 PHE B 45
REMARK 465 GLN B 46
REMARK 465 GLN B 47
REMARK 465 LEU B 48
REMARK 465 PRO B 49
REMARK 465 GLY B 50
REMARK 465 THR B 51
REMARK 465 GLY B 52
REMARK 465 VAL B 53
REMARK 465 LYS B 54
REMARK 465 PRO B 55
REMARK 465 ASP B 56
REMARK 465 GLN B 57
REMARK 465 PHE B 58
REMARK 465 HIS B 59
REMARK 465 SER B 60
REMARK 465 GLN B 61
REMARK 465 THR B 62
REMARK 465 ARG B 63
REMARK 465 GLU B 64
REMARK 465 TYR B 65
REMARK 465 PHE B 66
REMARK 465 ARG B 67
REMARK 465 ARG B 68
REMARK 465 LEU B 69
REMARK 465 ALA B 70
REMARK 465 LYS B 71
REMARK 465 ASP B 72
REMARK 465 ALA B 73
REMARK 465 SER B 74
REMARK 465 ARG B 75
REMARK 465 TYR B 76
REMARK 465 SER B 77
REMARK 465 SER B 78
REMARK 465 THR B 79
REMARK 465 ILE B 80
REMARK 465 SER B 81
REMARK 465 ASP B 82
REMARK 465 PRO B 83
REMARK 465 ASP B 84
REMARK 465 GLN B 116
REMARK 465 GLN B 117
REMARK 465 ASP B 118
REMARK 465 GLY B 223
REMARK 465 ALA B 224
REMARK 465 LYS B 225
REMARK 465 LYS B 287
REMARK 465 GLU B 288
REMARK 465 HIS B 289
REMARK 465 LEU B 290
REMARK 465 VAL B 392
REMARK 465 GLY B 393
REMARK 465 PHE B 394
REMARK 465 THR B 395
REMARK 465 THR B 396
REMARK 465 SER B 397
REMARK 465 ASN B 398
REMARK 465 PRO B 399
REMARK 465 LEU B 400
REMARK 465 ASP B 401
REMARK 465 ALA B 402
REMARK 465 ARG B 403
REMARK 465 SER B 404
REMARK 465 THR B 405
REMARK 465 PRO B 406
REMARK 465 GLY B 459
REMARK 465 HIS B 460
REMARK 465 ASN B 461
REMARK 465 GLU B 462
REMARK 465 ALA B 463
REMARK 465 ASP B 464
REMARK 465 GLU B 465
REMARK 465 PRO B 466
REMARK 465 SER B 467
REMARK 465 ALA B 468
REMARK 465 THR B 469
REMARK 465 GLN B 470
REMARK 465 PRO B 471
REMARK 465 LEU B 472
REMARK 465 MET B 473
REMARK 465 VAL B 658
REMARK 465 LEU B 659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASP A 84 CG OD1 OD2
REMARK 470 TRP A 115 CG CD1 CD2 NE1 CE2 CE3 CZ2 CZ3 CH2
REMARK 470 GLN A 116 CG CD OE1 NE2
REMARK 470 ASP A 118 CG OD1 OD2
REMARK 470 ASP A 122 CG OD1 OD2
REMARK 470 LEU A 123 CG CD1 CD2
REMARK 470 GLU A 132 CD OE1 OE2
REMARK 470 GLU A 137 CD OE1 OE2
REMARK 470 GLU A 149 CG CD OE1 OE2
REMARK 470 LYS A 152 CD CE NZ
REMARK 470 GLU A 155 CD OE1 OE2
REMARK 470 GLU A 158 CG CD OE1 OE2
REMARK 470 ARG A 192 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 226 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 252 CD NE CZ NH1 NH2
REMARK 470 LYS A 274 CE NZ
REMARK 470 HIS A 289 CG ND1 CD2 CE1 NE2
REMARK 470 LEU A 290 CG CD1 CD2
REMARK 470 GLU A 343 CD OE1 OE2
REMARK 470 LYS A 374 CD CE NZ
REMARK 470 ARG A 376 CD NE CZ NH1 NH2
REMARK 470 GLN A 391 CG CD OE1 NE2
REMARK 470 LYS A 413 CD CE NZ
REMARK 470 ARG A 446 NH1 NH2
REMARK 470 GLN A 470 CG CD OE1 NE2
REMARK 470 LEU A 472 CG CD1 CD2
REMARK 470 LYS A 476 CD CE NZ
REMARK 470 LYS A 479 CG CD CE NZ
REMARK 470 GLN A 493 CD OE1 NE2
REMARK 470 LYS A 495 CD CE NZ
REMARK 470 GLU A 566 CD OE1 OE2
REMARK 470 ARG A 573 CD NE CZ NH1 NH2
REMARK 470 ASN A 635 CG OD1 ND2
REMARK 470 VAL A 658 CG1 CG2
REMARK 470 GLN A 685 O
REMARK 470 THR A 753 CG2
REMARK 470 GLU A 808 CG CD OE1 OE2
REMARK 470 LYS A 812 CG CD CE NZ
REMARK 470 LYS A 854 CE NZ
REMARK 470 GLN A 861 CD OE1 NE2
REMARK 470 LYS A 867 CD CE NZ
REMARK 470 GLU A 933 CG CD OE1 OE2
REMARK 470 LEU B 114 CG CD1 CD2
REMARK 470 TRP B 115 CG CD1 CD2 NE1 CE2 CE3 CZ2 CZ3 CH2
REMARK 470 LYS B 119 CG CD CE NZ
REMARK 470 GLN B 136 CD OE1 NE2
REMARK 470 LYS B 148 CE NZ
REMARK 470 GLN B 162 CG CD OE1 NE2
REMARK 470 GLU B 189 CG CD OE1 OE2
REMARK 470 ARG B 192 CD NE CZ NH1 NH2
REMARK 470 THR B 194 OG1 CG2
REMARK 470 ARG B 226 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 285 CD CE NZ
REMARK 470 ASP B 342 CG OD1 OD2
REMARK 470 ALA B 358 CB
REMARK 470 LYS B 374 CG CD CE NZ
REMARK 470 ARG B 376 CG CD NE CZ NH1 NH2
REMARK 470 TYR B 407 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TYR B 474 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN B 475 CG CD OE1 NE2
REMARK 470 LYS B 476 CG CD CE NZ
REMARK 470 LYS B 478 CD CE NZ
REMARK 470 GLN B 493 CD OE1 NE2
REMARK 470 LYS B 495 CG CD CE NZ
REMARK 470 GLU B 500 CD OE1 OE2
REMARK 470 GLU B 540 CD OE1 OE2
REMARK 470 LYS B 552 NZ
REMARK 470 LYS B 559 CE NZ
REMARK 470 GLU B 569 CD OE1 OE2
REMARK 470 GLN B 571 CD OE1 NE2
REMARK 470 ARG B 573 CD NE CZ NH1 NH2
REMARK 470 LYS B 576 CD CE NZ
REMARK 470 ALA B 579 CB
REMARK 470 GLU B 588 CD OE1 OE2
REMARK 470 SER B 634 OG
REMARK 470 ASN B 635 CG OD1 ND2
REMARK 470 THR B 753 CG2
REMARK 470 GLU B 808 CD OE1 OE2
REMARK 470 LYS B 812 CD CE NZ
REMARK 470 LYS B 815 CE NZ
REMARK 470 LYS B 834 CD CE NZ
REMARK 470 LYS B 854 CD CE NZ
REMARK 470 GLN B 857 CD OE1 NE2
REMARK 470 GLN B 861 CD OE1 NE2
REMARK 470 LYS B 867 CE NZ
REMARK 470 LYS B 920 CE NZ
REMARK 470 GLU B 933 CG CD OE1 OE2
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 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 123 -2.32 -57.66
REMARK 500 LEU A 130 76.27 63.06
REMARK 500 TYR A 172 2.71 -165.12
REMARK 500 PHE A 227 37.97 -91.31
REMARK 500 ALA A 259 -134.30 -120.81
REMARK 500 PHE A 301 143.86 -173.26
REMARK 500 GLU A 324 -0.06 98.68
REMARK 500 PRO A 344 62.81 -110.25
REMARK 500 SER A 373 0.41 -60.45
REMARK 500 ASN A 390 -72.80 -104.40
REMARK 500 CYS A 454 -156.35 -151.77
REMARK 500 PRO A 546 77.72 -66.54
REMARK 500 GLN A 571 155.48 -46.12
REMARK 500 ILE A 645 -62.08 -91.55
REMARK 500 SER A 657 170.77 -29.59
REMARK 500 LEU A 659 -155.19 36.97
REMARK 500 PHE A 700 -70.66 -124.59
REMARK 500 HIS A 729 34.55 -140.85
REMARK 500 SER A 730 -38.94 -137.35
REMARK 500 ALA A 742 151.02 179.70
REMARK 500 ARG A 783 22.24 -142.88
REMARK 500 ALA B 145 68.01 -103.11
REMARK 500 LYS B 148 110.97 -28.95
REMARK 500 TYR B 172 -19.94 -142.93
REMARK 500 ARG B 192 -56.33 -141.69
REMARK 500 ALA B 193 101.44 -160.17
REMARK 500 PHE B 227 66.72 -115.25
REMARK 500 ALA B 259 -135.36 -118.43
REMARK 500 VAL B 270 -51.61 -121.22
REMARK 500 GLU B 324 -7.98 91.40
REMARK 500 GLU B 343 74.13 -109.60
REMARK 500 PRO B 344 33.69 -69.55
REMARK 500 GLN B 416 48.78 77.40
REMARK 500 CYS B 518 135.72 -39.68
REMARK 500 PHE B 700 -69.88 -121.00
REMARK 500 SER B 730 -42.05 -134.94
REMARK 500 MET B 776 96.47 -67.28
REMARK 500 LYS B 779 -76.09 -110.96
REMARK 500 GLN B 886 -64.43 -22.11
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 PHE A 144 ALA A 145 -149.24
REMARK 500 GLU A 171 TYR A 172 -137.18
REMARK 500 ARG A 226 PHE A 227 124.54
REMARK 500 GLU A 230 GLY A 231 -43.09
REMARK 500 GLY A 231 GLY A 232 139.76
REMARK 500 LEU A 290 GLY A 291 145.47
REMARK 500 ASP A 342 GLU A 343 149.51
REMARK 500 MET A 414 VAL A 415 145.41
REMARK 500 SER A 657 VAL A 658 124.21
REMARK 500 GLY A 896 ALA A 897 -148.80
REMARK 500 PHE B 144 ALA B 145 -140.80
REMARK 500 ALA B 145 SER B 146 -146.51
REMARK 500 SER B 146 GLY B 147 -63.48
REMARK 500 GLY B 147 LYS B 148 115.67
REMARK 500 GLU B 189 SER B 190 -147.78
REMARK 500 SER B 190 GLY B 191 -114.38
REMARK 500 GLY B 191 ARG B 192 103.33
REMARK 500 ARG B 192 ALA B 193 -146.98
REMARK 500 PHE B 227 SER B 228 -149.47
REMARK 500 ARG B 376 GLY B 377 -71.98
REMARK 500 GLY B 377 TYR B 378 146.00
REMARK 500 TYR B 536 LEU B 537 -149.25
REMARK 500 GLY B 896 ALA B 897 -142.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 VAL A 334 23.9 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP A1934
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP B1934
DBREF 2JGD A 1 933 UNP P0AFG3 ODO1_ECOLI 1 933
DBREF 2JGD B 1 933 UNP P0AFG3 ODO1_ECOLI 1 933
SEQADV 2JGD HIS A 914 UNP P0AFG3 TYR 914 CONFLICT
SEQADV 2JGD ALA B 579 UNP P0AFG3 GLY 579 CONFLICT
SEQRES 1 A 933 MET GLN ASN SER ALA LEU LYS ALA TRP LEU ASP SER SER
SEQRES 2 A 933 TYR LEU SER GLY ALA ASN GLN SER TRP ILE GLU GLN LEU
SEQRES 3 A 933 TYR GLU ASP PHE LEU THR ASP PRO ASP SER VAL ASP ALA
SEQRES 4 A 933 ASN TRP ARG SER THR PHE GLN GLN LEU PRO GLY THR GLY
SEQRES 5 A 933 VAL LYS PRO ASP GLN PHE HIS SER GLN THR ARG GLU TYR
SEQRES 6 A 933 PHE ARG ARG LEU ALA LYS ASP ALA SER ARG TYR SER SER
SEQRES 7 A 933 THR ILE SER ASP PRO ASP THR ASN VAL LYS GLN VAL LYS
SEQRES 8 A 933 VAL LEU GLN LEU ILE ASN ALA TYR ARG PHE ARG GLY HIS
SEQRES 9 A 933 GLN HIS ALA ASN LEU ASP PRO LEU GLY LEU TRP GLN GLN
SEQRES 10 A 933 ASP LYS VAL ALA ASP LEU ASP PRO SER PHE HIS ASP LEU
SEQRES 11 A 933 THR GLU ALA ASP PHE GLN GLU THR PHE ASN VAL GLY SER
SEQRES 12 A 933 PHE ALA SER GLY LYS GLU THR MET LYS LEU GLY GLU LEU
SEQRES 13 A 933 LEU GLU ALA LEU LYS GLN THR TYR CYS GLY PRO ILE GLY
SEQRES 14 A 933 ALA GLU TYR MET HIS ILE THR SER THR GLU GLU LYS ARG
SEQRES 15 A 933 TRP ILE GLN GLN ARG ILE GLU SER GLY ARG ALA THR PHE
SEQRES 16 A 933 ASN SER GLU GLU LYS LYS ARG PHE LEU SER GLU LEU THR
SEQRES 17 A 933 ALA ALA GLU GLY LEU GLU ARG TYR LEU GLY ALA LYS PHE
SEQRES 18 A 933 PRO GLY ALA LYS ARG PHE SER LEU GLU GLY GLY ASP ALA
SEQRES 19 A 933 LEU ILE PRO MET LEU LYS GLU MET ILE ARG HIS ALA GLY
SEQRES 20 A 933 ASN SER GLY THR ARG GLU VAL VAL LEU GLY MET ALA HIS
SEQRES 21 A 933 ARG GLY ARG LEU ASN VAL LEU VAL ASN VAL LEU GLY LYS
SEQRES 22 A 933 LYS PRO GLN ASP LEU PHE ASP GLU PHE ALA GLY LYS HIS
SEQRES 23 A 933 LYS GLU HIS LEU GLY THR GLY ASP VAL LYS TYR HIS MET
SEQRES 24 A 933 GLY PHE SER SER ASP PHE GLN THR ASP GLY GLY LEU VAL
SEQRES 25 A 933 HIS LEU ALA LEU ALA PHE ASN PRO SER HIS LEU GLU ILE
SEQRES 26 A 933 VAL SER PRO VAL VAL ILE GLY SER VAL ARG ALA ARG LEU
SEQRES 27 A 933 ASP ARG LEU ASP GLU PRO SER SER ASN LYS VAL LEU PRO
SEQRES 28 A 933 ILE THR ILE HIS GLY ASP ALA ALA VAL THR GLY GLN GLY
SEQRES 29 A 933 VAL VAL GLN GLU THR LEU ASN MET SER LYS ALA ARG GLY
SEQRES 30 A 933 TYR GLU VAL GLY GLY THR VAL ARG ILE VAL ILE ASN ASN
SEQRES 31 A 933 GLN VAL GLY PHE THR THR SER ASN PRO LEU ASP ALA ARG
SEQRES 32 A 933 SER THR PRO TYR CYS THR ASP ILE GLY LYS MET VAL GLN
SEQRES 33 A 933 ALA PRO ILE PHE HIS VAL ASN ALA ASP ASP PRO GLU ALA
SEQRES 34 A 933 VAL ALA PHE VAL THR ARG LEU ALA LEU ASP PHE ARG ASN
SEQRES 35 A 933 THR PHE LYS ARG ASP VAL PHE ILE ASP LEU VAL CYS TYR
SEQRES 36 A 933 ARG ARG HIS GLY HIS ASN GLU ALA ASP GLU PRO SER ALA
SEQRES 37 A 933 THR GLN PRO LEU MET TYR GLN LYS ILE LYS LYS HIS PRO
SEQRES 38 A 933 THR PRO ARG LYS ILE TYR ALA ASP LYS LEU GLU GLN GLU
SEQRES 39 A 933 LYS VAL ALA THR LEU GLU ASP ALA THR GLU MET VAL ASN
SEQRES 40 A 933 LEU TYR ARG ASP ALA LEU ASP ALA GLY ASP CYS VAL VAL
SEQRES 41 A 933 ALA GLU TRP ARG PRO MET ASN MET HIS SER PHE THR TRP
SEQRES 42 A 933 SER PRO TYR LEU ASN HIS GLU TRP ASP GLU GLU TYR PRO
SEQRES 43 A 933 ASN LYS VAL GLU MET LYS ARG LEU GLN GLU LEU ALA LYS
SEQRES 44 A 933 ARG ILE SER THR VAL PRO GLU ALA VAL GLU MET GLN SER
SEQRES 45 A 933 ARG VAL ALA LYS ILE TYR GLY ASP ARG GLN ALA MET ALA
SEQRES 46 A 933 ALA GLY GLU LYS LEU PHE ASP TRP GLY GLY ALA GLU ASN
SEQRES 47 A 933 LEU ALA TYR ALA THR LEU VAL ASP GLU GLY ILE PRO VAL
SEQRES 48 A 933 ARG LEU SER GLY GLU ASP SER GLY ARG GLY THR PHE PHE
SEQRES 49 A 933 HIS ARG HIS ALA VAL ILE HIS ASN GLN SER ASN GLY SER
SEQRES 50 A 933 THR TYR THR PRO LEU GLN HIS ILE HIS ASN GLY GLN GLY
SEQRES 51 A 933 ALA PHE ARG VAL TRP ASP SER VAL LEU SER GLU GLU ALA
SEQRES 52 A 933 VAL LEU ALA PHE GLU TYR GLY TYR ALA THR ALA GLU PRO
SEQRES 53 A 933 ARG THR LEU THR ILE TRP GLU ALA GLN PHE GLY ASP PHE
SEQRES 54 A 933 ALA ASN GLY ALA GLN VAL VAL ILE ASP GLN PHE ILE SER
SEQRES 55 A 933 SER GLY GLU GLN LYS TRP GLY ARG MET CYS GLY LEU VAL
SEQRES 56 A 933 MET LEU LEU PRO HIS GLY TYR GLU GLY GLN GLY PRO GLU
SEQRES 57 A 933 HIS SER SER ALA ARG LEU GLU ARG TYR LEU GLN LEU CYS
SEQRES 58 A 933 ALA GLU GLN ASN MET GLN VAL CYS VAL PRO SER THR PRO
SEQRES 59 A 933 ALA GLN VAL TYR HIS MET LEU ARG ARG GLN ALA LEU ARG
SEQRES 60 A 933 GLY MET ARG ARG PRO LEU VAL VAL MET SER PRO LYS SER
SEQRES 61 A 933 LEU LEU ARG HIS PRO LEU ALA VAL SER SER LEU GLU GLU
SEQRES 62 A 933 LEU ALA ASN GLY THR PHE LEU PRO ALA ILE GLY GLU ILE
SEQRES 63 A 933 ASP GLU LEU ASP PRO LYS GLY VAL LYS ARG VAL VAL MET
SEQRES 64 A 933 CYS SER GLY LYS VAL TYR TYR ASP LEU LEU GLU GLN ARG
SEQRES 65 A 933 ARG LYS ASN ASN GLN HIS ASP VAL ALA ILE VAL ARG ILE
SEQRES 66 A 933 GLU GLN LEU TYR PRO PHE PRO HIS LYS ALA MET GLN GLU
SEQRES 67 A 933 VAL LEU GLN GLN PHE ALA HIS VAL LYS ASP PHE VAL TRP
SEQRES 68 A 933 CYS GLN GLU GLU PRO LEU ASN GLN GLY ALA TRP TYR CYS
SEQRES 69 A 933 SER GLN HIS HIS PHE ARG GLU VAL ILE PRO PHE GLY ALA
SEQRES 70 A 933 SER LEU ARG TYR ALA GLY ARG PRO ALA SER ALA SER PRO
SEQRES 71 A 933 ALA VAL GLY HIS MET SER VAL HIS GLN LYS GLN GLN GLN
SEQRES 72 A 933 ASP LEU VAL ASN ASP ALA LEU ASN VAL GLU
SEQRES 1 B 933 MET GLN ASN SER ALA LEU LYS ALA TRP LEU ASP SER SER
SEQRES 2 B 933 TYR LEU SER GLY ALA ASN GLN SER TRP ILE GLU GLN LEU
SEQRES 3 B 933 TYR GLU ASP PHE LEU THR ASP PRO ASP SER VAL ASP ALA
SEQRES 4 B 933 ASN TRP ARG SER THR PHE GLN GLN LEU PRO GLY THR GLY
SEQRES 5 B 933 VAL LYS PRO ASP GLN PHE HIS SER GLN THR ARG GLU TYR
SEQRES 6 B 933 PHE ARG ARG LEU ALA LYS ASP ALA SER ARG TYR SER SER
SEQRES 7 B 933 THR ILE SER ASP PRO ASP THR ASN VAL LYS GLN VAL LYS
SEQRES 8 B 933 VAL LEU GLN LEU ILE ASN ALA TYR ARG PHE ARG GLY HIS
SEQRES 9 B 933 GLN HIS ALA ASN LEU ASP PRO LEU GLY LEU TRP GLN GLN
SEQRES 10 B 933 ASP LYS VAL ALA ASP LEU ASP PRO SER PHE HIS ASP LEU
SEQRES 11 B 933 THR GLU ALA ASP PHE GLN GLU THR PHE ASN VAL GLY SER
SEQRES 12 B 933 PHE ALA SER GLY LYS GLU THR MET LYS LEU GLY GLU LEU
SEQRES 13 B 933 LEU GLU ALA LEU LYS GLN THR TYR CYS GLY PRO ILE GLY
SEQRES 14 B 933 ALA GLU TYR MET HIS ILE THR SER THR GLU GLU LYS ARG
SEQRES 15 B 933 TRP ILE GLN GLN ARG ILE GLU SER GLY ARG ALA THR PHE
SEQRES 16 B 933 ASN SER GLU GLU LYS LYS ARG PHE LEU SER GLU LEU THR
SEQRES 17 B 933 ALA ALA GLU GLY LEU GLU ARG TYR LEU GLY ALA LYS PHE
SEQRES 18 B 933 PRO GLY ALA LYS ARG PHE SER LEU GLU GLY GLY ASP ALA
SEQRES 19 B 933 LEU ILE PRO MET LEU LYS GLU MET ILE ARG HIS ALA GLY
SEQRES 20 B 933 ASN SER GLY THR ARG GLU VAL VAL LEU GLY MET ALA HIS
SEQRES 21 B 933 ARG GLY ARG LEU ASN VAL LEU VAL ASN VAL LEU GLY LYS
SEQRES 22 B 933 LYS PRO GLN ASP LEU PHE ASP GLU PHE ALA GLY LYS HIS
SEQRES 23 B 933 LYS GLU HIS LEU GLY THR GLY ASP VAL LYS TYR HIS MET
SEQRES 24 B 933 GLY PHE SER SER ASP PHE GLN THR ASP GLY GLY LEU VAL
SEQRES 25 B 933 HIS LEU ALA LEU ALA PHE ASN PRO SER HIS LEU GLU ILE
SEQRES 26 B 933 VAL SER PRO VAL VAL ILE GLY SER VAL ARG ALA ARG LEU
SEQRES 27 B 933 ASP ARG LEU ASP GLU PRO SER SER ASN LYS VAL LEU PRO
SEQRES 28 B 933 ILE THR ILE HIS GLY ASP ALA ALA VAL THR GLY GLN GLY
SEQRES 29 B 933 VAL VAL GLN GLU THR LEU ASN MET SER LYS ALA ARG GLY
SEQRES 30 B 933 TYR GLU VAL GLY GLY THR VAL ARG ILE VAL ILE ASN ASN
SEQRES 31 B 933 GLN VAL GLY PHE THR THR SER ASN PRO LEU ASP ALA ARG
SEQRES 32 B 933 SER THR PRO TYR CYS THR ASP ILE GLY LYS MET VAL GLN
SEQRES 33 B 933 ALA PRO ILE PHE HIS VAL ASN ALA ASP ASP PRO GLU ALA
SEQRES 34 B 933 VAL ALA PHE VAL THR ARG LEU ALA LEU ASP PHE ARG ASN
SEQRES 35 B 933 THR PHE LYS ARG ASP VAL PHE ILE ASP LEU VAL CYS TYR
SEQRES 36 B 933 ARG ARG HIS GLY HIS ASN GLU ALA ASP GLU PRO SER ALA
SEQRES 37 B 933 THR GLN PRO LEU MET TYR GLN LYS ILE LYS LYS HIS PRO
SEQRES 38 B 933 THR PRO ARG LYS ILE TYR ALA ASP LYS LEU GLU GLN GLU
SEQRES 39 B 933 LYS VAL ALA THR LEU GLU ASP ALA THR GLU MET VAL ASN
SEQRES 40 B 933 LEU TYR ARG ASP ALA LEU ASP ALA GLY ASP CYS VAL VAL
SEQRES 41 B 933 ALA GLU TRP ARG PRO MET ASN MET HIS SER PHE THR TRP
SEQRES 42 B 933 SER PRO TYR LEU ASN HIS GLU TRP ASP GLU GLU TYR PRO
SEQRES 43 B 933 ASN LYS VAL GLU MET LYS ARG LEU GLN GLU LEU ALA LYS
SEQRES 44 B 933 ARG ILE SER THR VAL PRO GLU ALA VAL GLU MET GLN SER
SEQRES 45 B 933 ARG VAL ALA LYS ILE TYR ALA ASP ARG GLN ALA MET ALA
SEQRES 46 B 933 ALA GLY GLU LYS LEU PHE ASP TRP GLY GLY ALA GLU ASN
SEQRES 47 B 933 LEU ALA TYR ALA THR LEU VAL ASP GLU GLY ILE PRO VAL
SEQRES 48 B 933 ARG LEU SER GLY GLU ASP SER GLY ARG GLY THR PHE PHE
SEQRES 49 B 933 HIS ARG HIS ALA VAL ILE HIS ASN GLN SER ASN GLY SER
SEQRES 50 B 933 THR TYR THR PRO LEU GLN HIS ILE HIS ASN GLY GLN GLY
SEQRES 51 B 933 ALA PHE ARG VAL TRP ASP SER VAL LEU SER GLU GLU ALA
SEQRES 52 B 933 VAL LEU ALA PHE GLU TYR GLY TYR ALA THR ALA GLU PRO
SEQRES 53 B 933 ARG THR LEU THR ILE TRP GLU ALA GLN PHE GLY ASP PHE
SEQRES 54 B 933 ALA ASN GLY ALA GLN VAL VAL ILE ASP GLN PHE ILE SER
SEQRES 55 B 933 SER GLY GLU GLN LYS TRP GLY ARG MET CYS GLY LEU VAL
SEQRES 56 B 933 MET LEU LEU PRO HIS GLY TYR GLU GLY GLN GLY PRO GLU
SEQRES 57 B 933 HIS SER SER ALA ARG LEU GLU ARG TYR LEU GLN LEU CYS
SEQRES 58 B 933 ALA GLU GLN ASN MET GLN VAL CYS VAL PRO SER THR PRO
SEQRES 59 B 933 ALA GLN VAL TYR HIS MET LEU ARG ARG GLN ALA LEU ARG
SEQRES 60 B 933 GLY MET ARG ARG PRO LEU VAL VAL MET SER PRO LYS SER
SEQRES 61 B 933 LEU LEU ARG HIS PRO LEU ALA VAL SER SER LEU GLU GLU
SEQRES 62 B 933 LEU ALA ASN GLY THR PHE LEU PRO ALA ILE GLY GLU ILE
SEQRES 63 B 933 ASP GLU LEU ASP PRO LYS GLY VAL LYS ARG VAL VAL MET
SEQRES 64 B 933 CYS SER GLY LYS VAL TYR TYR ASP LEU LEU GLU GLN ARG
SEQRES 65 B 933 ARG LYS ASN ASN GLN HIS ASP VAL ALA ILE VAL ARG ILE
SEQRES 66 B 933 GLU GLN LEU TYR PRO PHE PRO HIS LYS ALA MET GLN GLU
SEQRES 67 B 933 VAL LEU GLN GLN PHE ALA HIS VAL LYS ASP PHE VAL TRP
SEQRES 68 B 933 CYS GLN GLU GLU PRO LEU ASN GLN GLY ALA TRP TYR CYS
SEQRES 69 B 933 SER GLN HIS HIS PHE ARG GLU VAL ILE PRO PHE GLY ALA
SEQRES 70 B 933 SER LEU ARG TYR ALA GLY ARG PRO ALA SER ALA SER PRO
SEQRES 71 B 933 ALA VAL GLY TYR MET SER VAL HIS GLN LYS GLN GLN GLN
SEQRES 72 B 933 ASP LEU VAL ASN ASP ALA LEU ASN VAL GLU
HET AMP A1934 23
HET AMP B1934 23
HETNAM AMP ADENOSINE MONOPHOSPHATE
FORMUL 3 AMP 2(C10 H14 N5 O7 P)
FORMUL 5 HOH *735(H2 O1)
HELIX 1 1 ASP A 84 GLY A 103 1 20
HELIX 2 2 HIS A 104 ALA A 107 5 4
HELIX 3 3 PRO A 125 LEU A 130 5 6
HELIX 4 4 LEU A 153 GLY A 166 1 14
HELIX 5 5 SER A 177 GLU A 189 1 13
HELIX 6 6 ASN A 196 PHE A 221 1 26
HELIX 7 7 ALA A 234 ASN A 248 1 15
HELIX 8 8 GLY A 262 VAL A 270 1 9
HELIX 9 9 LYS A 274 ALA A 283 1 10
HELIX 10 10 VAL A 295 MET A 299 5 5
HELIX 11 11 ILE A 325 ASP A 339 1 15
HELIX 12 12 SER A 345 ASN A 347 5 3
HELIX 13 13 ASP A 357 GLN A 363 1 7
HELIX 14 14 GLY A 364 SER A 373 1 10
HELIX 15 15 TYR A 407 MET A 414 5 8
HELIX 16 16 ASP A 426 LYS A 445 1 20
HELIX 17 17 MET A 473 LYS A 479 1 7
HELIX 18 18 THR A 482 GLN A 493 1 12
HELIX 19 19 THR A 498 GLY A 516 1 19
HELIX 20 20 ASN A 527 PHE A 531 5 5
HELIX 21 21 TRP A 533 LEU A 537 5 5
HELIX 22 22 GLU A 550 ILE A 561 1 12
HELIX 23 23 GLN A 571 ALA A 586 1 16
HELIX 24 24 ASP A 592 ASP A 606 1 15
HELIX 25 25 THR A 640 HIS A 644 5 5
HELIX 26 26 SER A 660 GLU A 675 1 16
HELIX 27 27 PHE A 686 GLY A 692 5 7
HELIX 28 28 ALA A 693 PHE A 700 1 8
HELIX 29 29 SER A 703 GLY A 709 1 7
HELIX 30 30 ARG A 733 LEU A 740 1 8
HELIX 31 31 THR A 753 ARG A 767 1 15
HELIX 32 32 LYS A 779 HIS A 784 5 6
HELIX 33 33 SER A 790 GLY A 797 1 8
HELIX 34 34 ASP A 810 VAL A 814 5 5
HELIX 35 35 LYS A 823 ASN A 835 1 13
HELIX 36 36 PRO A 852 GLN A 861 1 10
HELIX 37 37 GLN A 862 ALA A 864 5 3
HELIX 38 38 ALA A 881 GLU A 891 1 11
HELIX 39 39 HIS A 914 ASN A 931 1 18
HELIX 40 40 THR B 85 GLY B 103 1 19
HELIX 41 41 HIS B 104 ALA B 107 5 4
HELIX 42 42 VAL B 120 ASP B 124 5 5
HELIX 43 43 ASP B 124 ASP B 129 5 6
HELIX 44 44 THR B 131 GLN B 136 5 6
HELIX 45 45 LEU B 153 CYS B 165 1 13
HELIX 46 46 SER B 177 GLU B 189 1 13
HELIX 47 47 ASN B 196 PHE B 221 1 26
HELIX 48 48 ALA B 234 ASN B 248 1 15
HELIX 49 49 GLY B 262 VAL B 270 1 9
HELIX 50 50 LYS B 274 ALA B 283 1 10
HELIX 51 51 VAL B 295 MET B 299 5 5
HELIX 52 52 ILE B 325 ARG B 340 1 16
HELIX 53 53 SER B 345 ASN B 347 5 3
HELIX 54 54 ASP B 357 GLN B 363 1 7
HELIX 55 55 GLY B 364 SER B 373 1 10
HELIX 56 56 THR B 409 MET B 414 5 6
HELIX 57 57 ASP B 426 LYS B 445 1 20
HELIX 58 58 TYR B 474 LYS B 479 1 6
HELIX 59 59 THR B 482 GLU B 494 1 13
HELIX 60 60 THR B 498 GLY B 516 1 19
HELIX 61 61 ASN B 527 PHE B 531 5 5
HELIX 62 62 TRP B 533 LEU B 537 5 5
HELIX 63 63 GLU B 550 ILE B 561 1 12
HELIX 64 64 GLN B 571 ALA B 586 1 16
HELIX 65 65 ASP B 592 GLU B 607 1 16
HELIX 66 66 THR B 640 HIS B 644 5 5
HELIX 67 67 SER B 660 GLU B 675 1 16
HELIX 68 68 PHE B 686 GLY B 692 5 7
HELIX 69 69 ALA B 693 PHE B 700 1 8
HELIX 70 70 SER B 703 GLY B 709 1 7
HELIX 71 71 ARG B 733 CYS B 741 1 9
HELIX 72 72 THR B 753 ARG B 767 1 15
HELIX 73 73 LYS B 779 HIS B 784 5 6
HELIX 74 74 SER B 790 GLY B 797 1 8
HELIX 75 75 ASP B 810 VAL B 814 5 5
HELIX 76 76 LYS B 823 ASN B 835 1 13
HELIX 77 77 PRO B 852 GLN B 861 1 10
HELIX 78 78 GLN B 862 ALA B 864 5 3
HELIX 79 79 ALA B 881 ILE B 893 1 13
HELIX 80 80 TYR B 914 ASN B 931 1 18
SHEET 1 AA 2 THR A 138 ASN A 140 0
SHEET 2 AA 2 THR A 150 LYS A 152 -1 O MET A 151 N PHE A 139
SHEET 1 AB 9 ILE A 168 GLU A 171 0
SHEET 2 AB 9 ILE A 419 ASN A 423 -1 O ILE A 419 N GLU A 171
SHEET 3 AB 9 VAL A 448 VAL A 453 1 O PHE A 449 N PHE A 420
SHEET 4 AB 9 VAL A 384 ASN A 389 1 O ARG A 385 N ILE A 450
SHEET 5 AB 9 VAL A 349 GLY A 356 1 O PRO A 351 N VAL A 384
SHEET 6 AB 9 GLU A 253 GLY A 257 1 O GLU A 253 N LEU A 350
SHEET 7 AB 9 GLY A 310 LEU A 316 1 O HIS A 313 N VAL A 254
SHEET 8 AB 9 PHE A 301 THR A 307 -1 O PHE A 301 N LEU A 316
SHEET 9 AB 9 TRP A 523 ARG A 524 -1 O ARG A 524 N ASP A 304
SHEET 1 AC 7 PHE A 652 TRP A 655 0
SHEET 2 AC 7 VAL A 611 GLY A 615 1 O VAL A 611 N ARG A 653
SHEET 3 AC 7 LEU A 679 GLU A 683 1 O LEU A 679 N ARG A 612
SHEET 4 AC 7 VAL A 715 PRO A 719 1 O VAL A 715 N TRP A 682
SHEET 5 AC 7 LEU A 773 SER A 777 1 O LEU A 773 N MET A 716
SHEET 6 AC 7 GLN A 747 CYS A 749 1 O GLN A 747 N VAL A 774
SHEET 7 AC 7 GLN A 847 TYR A 849 -1 N LEU A 848 O VAL A 748
SHEET 1 AD 2 ILE A 630 HIS A 631 0
SHEET 2 AD 2 THR A 638 TYR A 639 -1 O TYR A 639 N ILE A 630
SHEET 1 AE 5 ALA A 802 ILE A 803 0
SHEET 2 AE 5 VAL A 840 ILE A 845 -1 O ARG A 844 N ILE A 803
SHEET 3 AE 5 ARG A 816 CYS A 820 1 O ARG A 816 N ALA A 841
SHEET 4 AE 5 ASP A 868 PRO A 876 1 O ASP A 868 N VAL A 817
SHEET 5 AE 5 SER A 898 ARG A 904 1 O SER A 898 N PHE A 869
SHEET 1 BA 2 THR B 138 ASN B 140 0
SHEET 2 BA 2 THR B 150 LYS B 152 -1 O MET B 151 N PHE B 139
SHEET 1 BB 9 ILE B 168 GLU B 171 0
SHEET 2 BB 9 ILE B 419 ASN B 423 -1 O ILE B 419 N GLU B 171
SHEET 3 BB 9 VAL B 448 VAL B 453 1 O PHE B 449 N PHE B 420
SHEET 4 BB 9 VAL B 384 ASN B 389 1 O ARG B 385 N ILE B 450
SHEET 5 BB 9 VAL B 349 GLY B 356 1 O PRO B 351 N VAL B 384
SHEET 6 BB 9 GLU B 253 GLY B 257 1 O GLU B 253 N LEU B 350
SHEET 7 BB 9 GLY B 310 LEU B 316 1 O HIS B 313 N VAL B 254
SHEET 8 BB 9 PHE B 301 THR B 307 -1 O PHE B 301 N LEU B 316
SHEET 9 BB 9 TRP B 523 ARG B 524 -1 O ARG B 524 N ASP B 304
SHEET 1 BC 7 PHE B 652 ASP B 656 0
SHEET 2 BC 7 VAL B 611 GLY B 615 1 O VAL B 611 N ARG B 653
SHEET 3 BC 7 LEU B 679 GLU B 683 1 O LEU B 679 N ARG B 612
SHEET 4 BC 7 VAL B 715 PRO B 719 1 O VAL B 715 N TRP B 682
SHEET 5 BC 7 LEU B 773 SER B 777 1 O LEU B 773 N MET B 716
SHEET 6 BC 7 GLN B 747 CYS B 749 1 O GLN B 747 N VAL B 774
SHEET 7 BC 7 GLN B 847 TYR B 849 -1 N LEU B 848 O VAL B 748
SHEET 1 BD 2 ILE B 630 HIS B 631 0
SHEET 2 BD 2 THR B 638 TYR B 639 -1 O TYR B 639 N ILE B 630
SHEET 1 BE 5 ALA B 802 ILE B 803 0
SHEET 2 BE 5 VAL B 840 ILE B 845 -1 O ARG B 844 N ILE B 803
SHEET 3 BE 5 ARG B 816 CYS B 820 1 O ARG B 816 N ALA B 841
SHEET 4 BE 5 ASP B 868 PRO B 876 1 O ASP B 868 N VAL B 817
SHEET 5 BE 5 SER B 898 ARG B 904 1 O SER B 898 N PHE B 869
CISPEP 1 TYR A 849 PRO A 850 0 -19.03
CISPEP 2 TYR B 849 PRO B 850 0 -26.78
SITE 1 AC1 17 SER A 302 HIS A 313 ALA A 315 ARG A 337
SITE 2 AC1 17 MET A 526 SER A 530 PHE A 531 TRP A 533
SITE 3 AC1 17 THR A 673 GLY A 709 ARG A 710 MET A 711
SITE 4 AC1 17 HOH A2145 HOH A2146 HOH A2335 HOH A2336
SITE 5 AC1 17 HOH A2337
SITE 1 AC2 16 SER B 302 HIS B 313 ALA B 315 ARG B 337
SITE 2 AC2 16 SER B 530 PHE B 531 TRP B 533 THR B 673
SITE 3 AC2 16 GLY B 709 ARG B 710 MET B 711 HOH B2394
SITE 4 AC2 16 HOH B2395 HOH B2396 HOH B2397 HOH B2398
CRYST1 142.493 142.493 251.811 90.00 90.00 90.00 P 41 21 2 8
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 0.007018 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007018 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003971 0.00000
MTRIX1 1 0.790320 0.612290 -0.022060 15.62862 1
MTRIX2 1 0.612310 -0.790590 -0.006650 -44.72879 1
MTRIX3 1 -0.021510 -0.008250 -0.999730 50.09098 1
(ATOM LINES ARE NOT SHOWN.)
END
