HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 09-OCT-18 6MQ6
TITLE MAPPING THE BINDING TRAJECTORY OF A SUICIDE INHIBITOR IN HUMAN
TITLE 2 INDOLEAMINE 2,3-DIOXYGENASE 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INDOLEAMINE 2,3-DIOXYGENASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: IDO-1,INDOLEAMINE-PYRROLE 2,3-DIOXYGENASE;
COMPND 5 EC: 1.13.11.52;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: IDO1, IDO, INDO;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS INDOLEAMINE 2, 3-DIOXYGENASE, HEME-CONTAINING ENZYME, BMS-986205,
KEYWDS 2 STRUCTURE-BASED DESIGN, HIDO1-SELECTIVE INHIBITOR, OXIDOREDUCTASE-
KEYWDS 3 OXIDOREDUCTASE INHIBITOR COMPLEX, OXYGEN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR K.N.PHAM,S.R.YEH
REVDAT 4 11-OCT-23 6MQ6 1 REMARK
REVDAT 3 27-NOV-19 6MQ6 1 REMARK
REVDAT 2 21-NOV-18 6MQ6 1 JRNL
REVDAT 1 07-NOV-18 6MQ6 0
JRNL AUTH K.N.PHAM,S.R.YEH
JRNL TITL MAPPING THE BINDING TRAJECTORY OF A SUICIDE INHIBITOR IN
JRNL TITL 2 HUMAN INDOLEAMINE 2,3-DIOXYGENASE 1.
JRNL REF J. AM. CHEM. SOC. V. 140 14538 2018
JRNL REFN ESSN 1520-5126
JRNL PMID 30347977
JRNL DOI 10.1021/JACS.8B07994
REMARK 2
REMARK 2 RESOLUTION. 3.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0230
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 19862
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) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1094
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) : 3.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.13
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1416
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2950
REMARK 3 BIN FREE R VALUE SET COUNT : 77
REMARK 3 BIN FREE R VALUE : 0.3010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5858
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 108
REMARK 3 SOLVENT ATOMS : 148
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 110.5
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.70000
REMARK 3 B22 (A**2) : -0.28000
REMARK 3 B33 (A**2) : 3.98000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.395
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.350
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.839
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6107 ; 0.001 ; 0.014
REMARK 3 BOND LENGTHS OTHERS (A): 5609 ; 0.000 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8266 ; 0.520 ; 1.669
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13123 ; 0.698 ; 1.653
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 733 ; 8.008 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 301 ;35.108 ;22.625
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1059 ;19.238 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;18.256 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 758 ; 0.026 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6744 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1151 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2944 ; 5.401 ;11.287
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2945 ; 5.400 ;11.287
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3673 ; 8.630 ;16.925
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3674 ; 8.629 ;16.927
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3163 ; 4.535 ;11.659
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3163 ; 4.534 ;11.659
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4594 ; 7.552 ;17.338
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 7234 ;11.850 ;11.890
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 7234 ;11.850 ;11.890
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6MQ6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1000237384.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAR-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 10.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97931
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL DIAMOND(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21005
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.050
REMARK 200 RESOLUTION RANGE LOW (A) : 29.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.10000
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) : 3.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.50
REMARK 200 R MERGE FOR SHELL (I) : 0.97800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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: PDB ENTRY 5WN8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM THIOSULFATE, 100 MM
REMARK 280 CAPS, PH 10.0, 200 MM SODIUM CHLORIDE, 20% W/V PEG8000,
REMARK 280 MICROBATCH, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 42.66350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.96550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.20350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.96550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.66350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.20350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 MET A 11
REMARK 465 SER A 12
REMARK 465 LYS A 13
REMARK 465 GLN A 361
REMARK 465 PRO A 362
REMARK 465 LYS A 363
REMARK 465 GLU A 364
REMARK 465 ASN A 365
REMARK 465 LYS A 366
REMARK 465 THR A 367
REMARK 465 SER A 368
REMARK 465 GLU A 369
REMARK 465 ASP A 370
REMARK 465 PRO A 371
REMARK 465 SER A 372
REMARK 465 LYS A 373
REMARK 465 LEU A 374
REMARK 465 GLU A 375
REMARK 465 ALA A 376
REMARK 465 LYS A 377
REMARK 465 GLY A 378
REMARK 465 GLY A 403
REMARK 465 LYS A 404
REMARK 465 GLY A 405
REMARK 465 GLU A 406
REMARK 465 LEU A 407
REMARK 465 ASN A 408
REMARK 465 SER A 409
REMARK 465 LYS A 410
REMARK 465 LEU A 411
REMARK 465 GLU A 412
REMARK 465 GLY A 413
REMARK 465 LYS A 414
REMARK 465 PRO A 415
REMARK 465 ILE A 416
REMARK 465 PRO A 417
REMARK 465 ASN A 418
REMARK 465 PRO A 419
REMARK 465 LEU A 420
REMARK 465 LEU A 421
REMARK 465 GLY A 422
REMARK 465 LEU A 423
REMARK 465 ASP A 424
REMARK 465 SER A 425
REMARK 465 THR A 426
REMARK 465 ARG A 427
REMARK 465 THR A 428
REMARK 465 GLY A 429
REMARK 465 HIS A 430
REMARK 465 HIS A 431
REMARK 465 HIS A 432
REMARK 465 HIS A 433
REMARK 465 HIS A 434
REMARK 465 HIS A 435
REMARK 465 MET B 11
REMARK 465 SER B 12
REMARK 465 SER B 359
REMARK 465 GLN B 360
REMARK 465 GLN B 361
REMARK 465 PRO B 362
REMARK 465 LYS B 363
REMARK 465 GLU B 364
REMARK 465 ASN B 365
REMARK 465 LYS B 366
REMARK 465 THR B 367
REMARK 465 SER B 368
REMARK 465 GLU B 369
REMARK 465 ASP B 370
REMARK 465 PRO B 371
REMARK 465 SER B 372
REMARK 465 LYS B 373
REMARK 465 LEU B 374
REMARK 465 GLU B 375
REMARK 465 ALA B 376
REMARK 465 LYS B 377
REMARK 465 GLY B 378
REMARK 465 THR B 379
REMARK 465 GLY B 380
REMARK 465 GLY B 381
REMARK 465 THR B 382
REMARK 465 GLY B 403
REMARK 465 LYS B 404
REMARK 465 GLY B 405
REMARK 465 GLU B 406
REMARK 465 LEU B 407
REMARK 465 ASN B 408
REMARK 465 SER B 409
REMARK 465 LYS B 410
REMARK 465 LEU B 411
REMARK 465 GLU B 412
REMARK 465 GLY B 413
REMARK 465 LYS B 414
REMARK 465 PRO B 415
REMARK 465 ILE B 416
REMARK 465 PRO B 417
REMARK 465 ASN B 418
REMARK 465 PRO B 419
REMARK 465 LEU B 420
REMARK 465 LEU B 421
REMARK 465 GLY B 422
REMARK 465 LEU B 423
REMARK 465 ASP B 424
REMARK 465 SER B 425
REMARK 465 THR B 426
REMARK 465 ARG B 427
REMARK 465 THR B 428
REMARK 465 GLY B 429
REMARK 465 HIS B 430
REMARK 465 HIS B 431
REMARK 465 HIS B 432
REMARK 465 HIS B 433
REMARK 465 HIS B 434
REMARK 465 HIS B 435
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 OG SER B 66 OD1 ASP B 68 2.03
REMARK 500 NE2 HIS B 346 C1 GOL B 505 2.14
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 PRO A 33 171.14 -58.37
REMARK 500 TYR A 36 61.98 -114.74
REMARK 500 MET A 64 69.50 -66.96
REMARK 500 VAL A 130 -57.59 -137.07
REMARK 500 LYS A 135 133.07 -174.99
REMARK 500 PRO A 139 4.33 -60.35
REMARK 500 PRO A 142 169.13 -44.09
REMARK 500 VAL A 229 -64.12 -97.57
REMARK 500 PRO A 300 150.13 -49.24
REMARK 500 ILE A 354 -56.07 -141.24
REMARK 500 ASN B 27 77.69 41.99
REMARK 500 PRO B 104 148.54 -33.88
REMARK 500 ASN B 133 53.87 -111.46
REMARK 500 ASN B 140 51.89 -93.50
REMARK 500 VAL B 229 -87.67 -106.41
REMARK 500 PHE B 252 -54.81 -126.68
REMARK 500 ILE B 354 -60.00 -129.28
REMARK 500 PRO B 357 -10.15 -49.29
REMARK 500 LEU B 400 -88.82 -114.12
REMARK 500 LYS B 401 -12.00 78.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 100 0.09 SIDE CHAIN
REMARK 500 ARG B 77 0.08 SIDE CHAIN
REMARK 500 ARG B 105 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 346 NE2
REMARK 620 2 HEM A 501 NA 91.3
REMARK 620 3 HEM A 501 NB 89.7 87.7
REMARK 620 4 HEM A 501 NC 87.2 173.8 86.2
REMARK 620 5 HEM A 501 ND 90.2 94.0 178.2 92.0
REMARK 620 6 HOH A 610 O 164.9 81.6 76.8 98.4 103.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H7P B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 505
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6DPQ RELATED DB: PDB
REMARK 900 HUMAN INDOLEAMINE 2,3-DIOXYGENASE 1 COMPLEXED WITH BMS
REMARK 900 RELATED ID: 6DPR RELATED DB: PDB
REMARK 900 HUMAN INDOLEAMINE 2,3-DIOXYGENASE 1 COMPLEXED WITH BMS
REMARK 900 RELATED ID: 5WN8 RELATED DB: PDB
REMARK 900 HUMAN INDOLEAMINE 2,3-DIOXYGENASE 1
REMARK 900 RELATED ID: 5WMV RELATED DB: PDB
REMARK 900 HUMAN INDOLEAMINE 2,3-DIOXYGENASE 1
REMARK 900 RELATED ID: 5WMX RELATED DB: PDB
REMARK 900 HUMAN INDOLEAMINE 2,3-DIOXYGENASE 1
DBREF 6MQ6 A 12 403 UNP P14902 I23O1_HUMAN 12 403
DBREF 6MQ6 B 12 403 UNP P14902 I23O1_HUMAN 12 403
SEQADV 6MQ6 MET A 11 UNP P14902 INITIATING METHIONINE
SEQADV 6MQ6 LYS A 404 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 GLY A 405 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 GLU A 406 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 LEU A 407 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 ASN A 408 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 SER A 409 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 LYS A 410 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 LEU A 411 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 GLU A 412 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 GLY A 413 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 LYS A 414 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 PRO A 415 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 ILE A 416 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 PRO A 417 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 ASN A 418 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 PRO A 419 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 LEU A 420 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 LEU A 421 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 GLY A 422 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 LEU A 423 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 ASP A 424 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 SER A 425 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 THR A 426 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 ARG A 427 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 THR A 428 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 GLY A 429 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 HIS A 430 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 HIS A 431 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 HIS A 432 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 HIS A 433 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 HIS A 434 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 HIS A 435 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 MET B 11 UNP P14902 INITIATING METHIONINE
SEQADV 6MQ6 LYS B 404 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 GLY B 405 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 GLU B 406 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 LEU B 407 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 ASN B 408 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 SER B 409 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 LYS B 410 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 LEU B 411 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 GLU B 412 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 GLY B 413 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 LYS B 414 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 PRO B 415 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 ILE B 416 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 PRO B 417 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 ASN B 418 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 PRO B 419 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 LEU B 420 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 LEU B 421 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 GLY B 422 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 LEU B 423 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 ASP B 424 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 SER B 425 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 THR B 426 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 ARG B 427 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 THR B 428 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 GLY B 429 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 HIS B 430 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 HIS B 431 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 HIS B 432 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 HIS B 433 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 HIS B 434 UNP P14902 EXPRESSION TAG
SEQADV 6MQ6 HIS B 435 UNP P14902 EXPRESSION TAG
SEQRES 1 A 425 MET SER LYS GLU TYR HIS ILE ASP GLU GLU VAL GLY PHE
SEQRES 2 A 425 ALA LEU PRO ASN PRO GLN GLU ASN LEU PRO ASP PHE TYR
SEQRES 3 A 425 ASN ASP TRP MET PHE ILE ALA LYS HIS LEU PRO ASP LEU
SEQRES 4 A 425 ILE GLU SER GLY GLN LEU ARG GLU ARG VAL GLU LYS LEU
SEQRES 5 A 425 ASN MET LEU SER ILE ASP HIS LEU THR ASP HIS LYS SER
SEQRES 6 A 425 GLN ARG LEU ALA ARG LEU VAL LEU GLY CYS ILE THR MET
SEQRES 7 A 425 ALA TYR VAL TRP GLY LYS GLY HIS GLY ASP VAL ARG LYS
SEQRES 8 A 425 VAL LEU PRO ARG ASN ILE ALA VAL PRO TYR CYS GLN LEU
SEQRES 9 A 425 SER LYS LYS LEU GLU LEU PRO PRO ILE LEU VAL TYR ALA
SEQRES 10 A 425 ASP CYS VAL LEU ALA ASN TRP LYS LYS LYS ASP PRO ASN
SEQRES 11 A 425 LYS PRO LEU THR TYR GLU ASN MET ASP VAL LEU PHE SER
SEQRES 12 A 425 PHE ARG ASP GLY ASP CYS SER LYS GLY PHE PHE LEU VAL
SEQRES 13 A 425 SER LEU LEU VAL GLU ILE ALA ALA ALA SER ALA ILE LYS
SEQRES 14 A 425 VAL ILE PRO THR VAL PHE LYS ALA MET GLN MET GLN GLU
SEQRES 15 A 425 ARG ASP THR LEU LEU LYS ALA LEU LEU GLU ILE ALA SER
SEQRES 16 A 425 CYS LEU GLU LYS ALA LEU GLN VAL PHE HIS GLN ILE HIS
SEQRES 17 A 425 ASP HIS VAL ASN PRO LYS ALA PHE PHE SER VAL LEU ARG
SEQRES 18 A 425 ILE TYR LEU SER GLY TRP LYS GLY ASN PRO GLN LEU SER
SEQRES 19 A 425 ASP GLY LEU VAL TYR GLU GLY PHE TRP GLU ASP PRO LYS
SEQRES 20 A 425 GLU PHE ALA GLY GLY SER ALA GLY GLN SER SER VAL PHE
SEQRES 21 A 425 GLN CYS PHE ASP VAL LEU LEU GLY ILE GLN GLN THR ALA
SEQRES 22 A 425 GLY GLY GLY HIS ALA ALA GLN PHE LEU GLN ASP MET ARG
SEQRES 23 A 425 ARG TYR MET PRO PRO ALA HIS ARG ASN PHE LEU CYS SER
SEQRES 24 A 425 LEU GLU SER ASN PRO SER VAL ARG GLU PHE VAL LEU SER
SEQRES 25 A 425 LYS GLY ASP ALA GLY LEU ARG GLU ALA TYR ASP ALA CYS
SEQRES 26 A 425 VAL LYS ALA LEU VAL SER LEU ARG SER TYR HIS LEU GLN
SEQRES 27 A 425 ILE VAL THR LYS TYR ILE LEU ILE PRO ALA SER GLN GLN
SEQRES 28 A 425 PRO LYS GLU ASN LYS THR SER GLU ASP PRO SER LYS LEU
SEQRES 29 A 425 GLU ALA LYS GLY THR GLY GLY THR ASP LEU MET ASN PHE
SEQRES 30 A 425 LEU LYS THR VAL ARG SER THR THR GLU LYS SER LEU LEU
SEQRES 31 A 425 LYS GLU GLY LYS GLY GLU LEU ASN SER LYS LEU GLU GLY
SEQRES 32 A 425 LYS PRO ILE PRO ASN PRO LEU LEU GLY LEU ASP SER THR
SEQRES 33 A 425 ARG THR GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 B 425 MET SER LYS GLU TYR HIS ILE ASP GLU GLU VAL GLY PHE
SEQRES 2 B 425 ALA LEU PRO ASN PRO GLN GLU ASN LEU PRO ASP PHE TYR
SEQRES 3 B 425 ASN ASP TRP MET PHE ILE ALA LYS HIS LEU PRO ASP LEU
SEQRES 4 B 425 ILE GLU SER GLY GLN LEU ARG GLU ARG VAL GLU LYS LEU
SEQRES 5 B 425 ASN MET LEU SER ILE ASP HIS LEU THR ASP HIS LYS SER
SEQRES 6 B 425 GLN ARG LEU ALA ARG LEU VAL LEU GLY CYS ILE THR MET
SEQRES 7 B 425 ALA TYR VAL TRP GLY LYS GLY HIS GLY ASP VAL ARG LYS
SEQRES 8 B 425 VAL LEU PRO ARG ASN ILE ALA VAL PRO TYR CYS GLN LEU
SEQRES 9 B 425 SER LYS LYS LEU GLU LEU PRO PRO ILE LEU VAL TYR ALA
SEQRES 10 B 425 ASP CYS VAL LEU ALA ASN TRP LYS LYS LYS ASP PRO ASN
SEQRES 11 B 425 LYS PRO LEU THR TYR GLU ASN MET ASP VAL LEU PHE SER
SEQRES 12 B 425 PHE ARG ASP GLY ASP CYS SER LYS GLY PHE PHE LEU VAL
SEQRES 13 B 425 SER LEU LEU VAL GLU ILE ALA ALA ALA SER ALA ILE LYS
SEQRES 14 B 425 VAL ILE PRO THR VAL PHE LYS ALA MET GLN MET GLN GLU
SEQRES 15 B 425 ARG ASP THR LEU LEU LYS ALA LEU LEU GLU ILE ALA SER
SEQRES 16 B 425 CYS LEU GLU LYS ALA LEU GLN VAL PHE HIS GLN ILE HIS
SEQRES 17 B 425 ASP HIS VAL ASN PRO LYS ALA PHE PHE SER VAL LEU ARG
SEQRES 18 B 425 ILE TYR LEU SER GLY TRP LYS GLY ASN PRO GLN LEU SER
SEQRES 19 B 425 ASP GLY LEU VAL TYR GLU GLY PHE TRP GLU ASP PRO LYS
SEQRES 20 B 425 GLU PHE ALA GLY GLY SER ALA GLY GLN SER SER VAL PHE
SEQRES 21 B 425 GLN CYS PHE ASP VAL LEU LEU GLY ILE GLN GLN THR ALA
SEQRES 22 B 425 GLY GLY GLY HIS ALA ALA GLN PHE LEU GLN ASP MET ARG
SEQRES 23 B 425 ARG TYR MET PRO PRO ALA HIS ARG ASN PHE LEU CYS SER
SEQRES 24 B 425 LEU GLU SER ASN PRO SER VAL ARG GLU PHE VAL LEU SER
SEQRES 25 B 425 LYS GLY ASP ALA GLY LEU ARG GLU ALA TYR ASP ALA CYS
SEQRES 26 B 425 VAL LYS ALA LEU VAL SER LEU ARG SER TYR HIS LEU GLN
SEQRES 27 B 425 ILE VAL THR LYS TYR ILE LEU ILE PRO ALA SER GLN GLN
SEQRES 28 B 425 PRO LYS GLU ASN LYS THR SER GLU ASP PRO SER LYS LEU
SEQRES 29 B 425 GLU ALA LYS GLY THR GLY GLY THR ASP LEU MET ASN PHE
SEQRES 30 B 425 LEU LYS THR VAL ARG SER THR THR GLU LYS SER LEU LEU
SEQRES 31 B 425 LYS GLU GLY LYS GLY GLU LEU ASN SER LYS LEU GLU GLY
SEQRES 32 B 425 LYS PRO ILE PRO ASN PRO LEU LEU GLY LEU ASP SER THR
SEQRES 33 B 425 ARG THR GLY HIS HIS HIS HIS HIS HIS
HET HEM A 501 43
HET GOL A 502 6
HET GOL A 503 6
HET H7P B 501 29
HET GOL B 502 6
HET GOL B 503 6
HET GOL B 504 6
HET GOL B 505 6
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM GOL GLYCEROL
HETNAM H7P (2R)-N-(4-CHLOROPHENYL)-2-[CIS-4-(6-FLUOROQUINOLIN-4-
HETNAM 2 H7P YL)CYCLOHEXYL]PROPANAMIDE
HETSYN HEM HEME
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 HEM C34 H32 FE N4 O4
FORMUL 4 GOL 6(C3 H8 O3)
FORMUL 6 H7P C24 H24 CL F N2 O
FORMUL 11 HOH *148(H2 O)
HELIX 1 AA1 PRO A 33 PHE A 35 5 3
HELIX 2 AA2 TYR A 36 HIS A 45 1 10
HELIX 3 AA3 HIS A 45 GLY A 53 1 9
HELIX 4 AA4 LEU A 55 LYS A 61 1 7
HELIX 5 AA5 ASP A 72 GLY A 93 1 22
HELIX 6 AA6 PRO A 104 LEU A 118 1 15
HELIX 7 AA7 VAL A 125 VAL A 130 1 6
HELIX 8 AA8 THR A 144 GLU A 146 5 3
HELIX 9 AA9 CYS A 159 LYS A 179 1 21
HELIX 10 AB1 VAL A 180 MET A 190 1 11
HELIX 11 AB2 GLU A 192 HIS A 215 1 24
HELIX 12 AB3 GLN A 216 VAL A 221 1 6
HELIX 13 AB4 ASN A 222 VAL A 229 1 8
HELIX 14 AB5 VAL A 229 LEU A 234 1 6
HELIX 15 AB6 ASN A 240 SER A 244 5 5
HELIX 16 AB7 SER A 263 SER A 267 5 5
HELIX 17 AB8 SER A 268 LEU A 277 1 10
HELIX 18 AB9 GLY A 286 MET A 295 1 10
HELIX 19 AC1 ARG A 296 MET A 299 5 4
HELIX 20 AC2 PRO A 300 ASN A 313 1 14
HELIX 21 AC3 SER A 315 LYS A 323 1 9
HELIX 22 AC4 ASP A 325 ILE A 354 1 30
HELIX 23 AC5 ILE A 356 GLN A 360 5 5
HELIX 24 AC6 GLY A 380 LYS A 397 1 18
HELIX 25 AC7 PRO B 33 PHE B 35 5 3
HELIX 26 AC8 TYR B 36 HIS B 45 1 10
HELIX 27 AC9 HIS B 45 SER B 52 1 8
HELIX 28 AD1 GLN B 54 LYS B 61 1 8
HELIX 29 AD2 SER B 66 LEU B 70 5 5
HELIX 30 AD3 ASP B 72 GLY B 93 1 22
HELIX 31 AD4 PRO B 104 LEU B 118 1 15
HELIX 32 AD5 VAL B 125 VAL B 130 1 6
HELIX 33 AD6 THR B 144 GLU B 146 5 3
HELIX 34 AD7 CYS B 159 LYS B 179 1 21
HELIX 35 AD8 VAL B 180 MET B 190 1 11
HELIX 36 AD9 GLU B 192 HIS B 215 1 24
HELIX 37 AE1 GLN B 216 VAL B 221 1 6
HELIX 38 AE2 ASN B 222 VAL B 229 1 8
HELIX 39 AE3 VAL B 229 LEU B 234 1 6
HELIX 40 AE4 ASN B 240 SER B 244 5 5
HELIX 41 AE5 SER B 263 GLN B 266 5 4
HELIX 42 AE6 SER B 267 LEU B 277 1 11
HELIX 43 AE7 GLY B 286 ARG B 296 1 11
HELIX 44 AE8 ARG B 297 MET B 299 5 3
HELIX 45 AE9 PRO B 300 SER B 312 1 13
HELIX 46 AF1 SER B 315 SER B 322 1 8
HELIX 47 AF2 ASP B 325 ILE B 354 1 30
HELIX 48 AF3 LEU B 384 LYS B 397 1 14
SHEET 1 AA1 3 VAL A 102 LEU A 103 0
SHEET 2 AA1 3 LEU A 247 TYR A 249 1 O VAL A 248 N LEU A 103
SHEET 3 AA1 3 PRO A 256 LYS A 257 -1 O LYS A 257 N LEU A 247
SHEET 1 AA2 2 LYS A 135 LYS A 136 0
SHEET 2 AA2 2 MET A 148 ASP A 149 -1 O ASP A 149 N LYS A 135
SHEET 1 AA3 2 VAL B 102 LEU B 103 0
SHEET 2 AA3 2 VAL B 248 TYR B 249 1 O VAL B 248 N LEU B 103
SHEET 1 AA4 2 LYS B 135 LYS B 136 0
SHEET 2 AA4 2 MET B 148 ASP B 149 -1 O ASP B 149 N LYS B 135
SSBOND 1 CYS A 308 CYS B 308 1555 1555 2.03
LINK NE2 HIS A 346 FE HEM A 501 1555 1555 2.04
LINK FE HEM A 501 O HOH A 610 1555 1555 2.29
SITE 1 AC1 19 SER A 167 VAL A 170 PHE A 214 SER A 263
SITE 2 AC1 19 ALA A 264 GLY A 265 PHE A 270 PHE A 291
SITE 3 AC1 19 LEU A 292 ARG A 343 HIS A 346 ILE A 349
SITE 4 AC1 19 VAL A 350 TYR A 353 LEU A 384 GOL A 502
SITE 5 AC1 19 HOH A 610 HOH A 620 HOH A 625
SITE 1 AC2 3 SER A 263 ILE A 354 HEM A 501
SITE 1 AC3 3 PRO A 182 SER A 309 ASN A 313
SITE 1 AC4 14 TYR B 126 VAL B 130 PHE B 163 SER B 167
SITE 2 AC4 14 VAL B 170 PHE B 214 GLY B 262 SER B 263
SITE 3 AC4 14 ALA B 264 VAL B 269 PHE B 270 ARG B 343
SITE 4 AC4 14 GOL B 505 HOH B 623
SITE 1 AC5 5 ARG B 231 LEU B 234 GLY B 262 SER B 263
SITE 2 AC5 5 GOL B 505
SITE 1 AC6 3 PHE B 306 ASN B 313 HOH B 648
SITE 1 AC7 5 GLY B 53 ARG B 56 ASP B 98 HOH B 613
SITE 2 AC7 5 HOH B 641
SITE 1 AC8 7 ALA B 264 HIS B 346 H7P B 501 GOL B 502
SITE 2 AC8 7 HOH B 622 HOH B 623 HOH B 628
CRYST1 85.327 96.407 129.931 90.00 90.00 90.00 P 21 21 21 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 0.011720 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010373 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007696 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
