HEADER OXIDOREDUCTASE/INHIBITOR 26-FEB-19 6O3I
TITLE CRYSTAL STRUCTURE OF HUMAN IDO1 BOUND TO NAVOXIMOD (NLG-919)
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 DIOXYGENASE, TRYPTOPHAN, IDO, TDO, OXIDOREDUCTASE-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.F.HARRIS,A.OH
REVDAT 2 07-AUG-19 6O3I 1 JRNL
REVDAT 1 17-JUL-19 6O3I 0
JRNL AUTH S.KUMAR,J.P.WALDO,F.A.JAIPURI,A.MARCINOWICZ,C.VAN ALLEN,
JRNL AUTH 2 J.ADAMS,T.KESHARWANI,X.ZHANG,R.METZ,A.J.OH,S.F.HARRIS,
JRNL AUTH 3 M.R.MAUTINO
JRNL TITL DISCOVERY OF CLINICAL CANDIDATE
JRNL TITL 2 (1R,4R)-4-((R)-2-((S)-6-FLUORO-5H-IMIDAZO[5,
JRNL TITL 3 1-A]ISOINDOL-5-YL)-1-HYDROXYETHYL)CYCLOHEXAN-1-OL
JRNL TITL 4 (NAVOXIMOD), A POTENT AND SELECTIVE INHIBITOR OF INDOLEAMINE
JRNL TITL 5 2,3-DIOXYGENASE 1.
JRNL REF J.MED.CHEM. V. 62 6705 2019
JRNL REFN ISSN 0022-2623
JRNL PMID 31264862
JRNL DOI 10.1021/ACS.JMEDCHEM.9B00662
REMARK 2
REMARK 2 RESOLUTION. 2.69 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.5
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 74.17
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 28331
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) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 1452
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 14
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.69
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.79
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.30
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2935
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2671
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2788
REMARK 3 BIN R VALUE (WORKING SET) : 0.2622
REMARK 3 BIN FREE R VALUE : 0.3626
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.01
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 147
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5957
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 132
REMARK 3 SOLVENT ATOMS : 91
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 82.95
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 74.28
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 17.27680
REMARK 3 B22 (A**2) : 0.26520
REMARK 3 B33 (A**2) : -17.54200
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.413
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.761
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.326
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.764
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.331
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.926
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.883
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 6258 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 8514 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2148 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 143 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 934 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 6258 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 768 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 7334 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.04
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.38
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.20
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6O3I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-19.
REMARK 100 THE DEPOSITION ID IS D_1000239947.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-FEB-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.2.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28655
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.680
REMARK 200 RESOLUTION RANGE LOW (A) : 85.060
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.68
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : 0.63100
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: FOURIER SYNTHESIS
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 (%): 53.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS TRIS PROPANE PH 6.5, 20% PEG
REMARK 280 3350, 0.2 M POTASSIUM THIOCYANATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 42.53100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.11850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.11200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.11850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.53100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.11200
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 GLY A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 GLY A 0
REMARK 465 SER A 1
REMARK 465 ALA A 2
REMARK 465 HIS A 3
REMARK 465 ALA A 4
REMARK 465 MET A 5
REMARK 465 GLU A 6
REMARK 465 ASN A 7
REMARK 465 SER A 8
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 THR A 379
REMARK 465 GLU A 402
REMARK 465 GLY A 403
REMARK 465 ASN A 404
REMARK 465 SER A 405
REMARK 465 MET B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 GLY B -7
REMARK 465 GLU B -6
REMARK 465 ASN B -5
REMARK 465 LEU B -4
REMARK 465 TYR B -3
REMARK 465 PHE B -2
REMARK 465 GLN B -1
REMARK 465 GLY B 0
REMARK 465 SER B 1
REMARK 465 ALA B 2
REMARK 465 HIS B 3
REMARK 465 ALA B 4
REMARK 465 MET B 5
REMARK 465 GLU B 6
REMARK 465 ASN B 7
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 GLU B 402
REMARK 465 GLY B 403
REMARK 465 ASN B 404
REMARK 465 SER B 405
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 THR A 10 -30.68 -163.87
REMARK 500 ILE A 11 71.29 54.40
REMARK 500 LYS A 13 -79.85 -68.59
REMARK 500 ASN A 27 76.84 45.06
REMARK 500 LYS A 61 34.12 -96.12
REMARK 500 ASP A 98 95.78 -68.71
REMARK 500 ASN A 133 52.58 -102.74
REMARK 500 VAL A 229 -74.44 -115.29
REMARK 500 LEU A 243 63.01 -155.68
REMARK 500 GLN A 280 54.82 -62.20
REMARK 500 ILE A 354 -58.27 -129.15
REMARK 500 TRP B 9 -23.32 71.22
REMARK 500 THR B 10 63.25 -101.47
REMARK 500 ASN B 27 75.88 46.17
REMARK 500 ASP B 98 96.30 -68.70
REMARK 500 VAL B 130 -71.05 -117.34
REMARK 500 ASN B 133 52.52 -102.43
REMARK 500 VAL B 229 -77.05 -115.52
REMARK 500 LEU B 243 62.95 -155.39
REMARK 500 ILE B 354 -60.48 -125.43
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 88.4
REMARK 620 3 HEM A 501 NB 93.4 89.6
REMARK 620 4 HEM A 501 NC 98.8 172.6 88.5
REMARK 620 5 HEM A 501 ND 89.5 89.2 176.8 92.3
REMARK 620 6 LKP A 502 N10 175.4 90.0 82.3 82.7 94.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 346 NE2
REMARK 620 2 HEM B 501 NA 89.1
REMARK 620 3 HEM B 501 NB 85.1 90.5
REMARK 620 4 HEM B 501 NC 86.9 175.9 88.1
REMARK 620 5 HEM B 501 ND 84.6 91.5 169.5 89.1
REMARK 620 6 LKP B 502 N10 172.6 94.3 88.3 89.5 101.8
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 LKP A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LKP B 502
DBREF 6O3I A 2 403 UNP P14902 I23O1_HUMAN 2 403
DBREF 6O3I B 2 403 UNP P14902 I23O1_HUMAN 2 403
SEQADV 6O3I MET A -14 UNP P14902 INITIATING METHIONINE
SEQADV 6O3I HIS A -13 UNP P14902 EXPRESSION TAG
SEQADV 6O3I HIS A -12 UNP P14902 EXPRESSION TAG
SEQADV 6O3I HIS A -11 UNP P14902 EXPRESSION TAG
SEQADV 6O3I HIS A -10 UNP P14902 EXPRESSION TAG
SEQADV 6O3I HIS A -9 UNP P14902 EXPRESSION TAG
SEQADV 6O3I HIS A -8 UNP P14902 EXPRESSION TAG
SEQADV 6O3I GLY A -7 UNP P14902 EXPRESSION TAG
SEQADV 6O3I GLU A -6 UNP P14902 EXPRESSION TAG
SEQADV 6O3I ASN A -5 UNP P14902 EXPRESSION TAG
SEQADV 6O3I LEU A -4 UNP P14902 EXPRESSION TAG
SEQADV 6O3I TYR A -3 UNP P14902 EXPRESSION TAG
SEQADV 6O3I PHE A -2 UNP P14902 EXPRESSION TAG
SEQADV 6O3I GLN A -1 UNP P14902 EXPRESSION TAG
SEQADV 6O3I GLY A 0 UNP P14902 EXPRESSION TAG
SEQADV 6O3I SER A 1 UNP P14902 EXPRESSION TAG
SEQADV 6O3I ASN A 404 UNP P14902 EXPRESSION TAG
SEQADV 6O3I SER A 405 UNP P14902 EXPRESSION TAG
SEQADV 6O3I MET B -14 UNP P14902 INITIATING METHIONINE
SEQADV 6O3I HIS B -13 UNP P14902 EXPRESSION TAG
SEQADV 6O3I HIS B -12 UNP P14902 EXPRESSION TAG
SEQADV 6O3I HIS B -11 UNP P14902 EXPRESSION TAG
SEQADV 6O3I HIS B -10 UNP P14902 EXPRESSION TAG
SEQADV 6O3I HIS B -9 UNP P14902 EXPRESSION TAG
SEQADV 6O3I HIS B -8 UNP P14902 EXPRESSION TAG
SEQADV 6O3I GLY B -7 UNP P14902 EXPRESSION TAG
SEQADV 6O3I GLU B -6 UNP P14902 EXPRESSION TAG
SEQADV 6O3I ASN B -5 UNP P14902 EXPRESSION TAG
SEQADV 6O3I LEU B -4 UNP P14902 EXPRESSION TAG
SEQADV 6O3I TYR B -3 UNP P14902 EXPRESSION TAG
SEQADV 6O3I PHE B -2 UNP P14902 EXPRESSION TAG
SEQADV 6O3I GLN B -1 UNP P14902 EXPRESSION TAG
SEQADV 6O3I GLY B 0 UNP P14902 EXPRESSION TAG
SEQADV 6O3I SER B 1 UNP P14902 EXPRESSION TAG
SEQADV 6O3I ASN B 404 UNP P14902 EXPRESSION TAG
SEQADV 6O3I SER B 405 UNP P14902 EXPRESSION TAG
SEQRES 1 A 420 MET HIS HIS HIS HIS HIS HIS GLY GLU ASN LEU TYR PHE
SEQRES 2 A 420 GLN GLY SER ALA HIS ALA MET GLU ASN SER TRP THR ILE
SEQRES 3 A 420 SER LYS GLU TYR HIS ILE ASP GLU GLU VAL GLY PHE ALA
SEQRES 4 A 420 LEU PRO ASN PRO GLN GLU ASN LEU PRO ASP PHE TYR ASN
SEQRES 5 A 420 ASP TRP MET PHE ILE ALA LYS HIS LEU PRO ASP LEU ILE
SEQRES 6 A 420 GLU SER GLY GLN LEU ARG GLU ARG VAL GLU LYS LEU ASN
SEQRES 7 A 420 MET LEU SER ILE ASP HIS LEU THR ASP HIS LYS SER GLN
SEQRES 8 A 420 ARG LEU ALA ARG LEU VAL LEU GLY CYS ILE THR MET ALA
SEQRES 9 A 420 TYR VAL TRP GLY LYS GLY HIS GLY ASP VAL ARG LYS VAL
SEQRES 10 A 420 LEU PRO ARG ASN ILE ALA VAL PRO TYR CYS GLN LEU SER
SEQRES 11 A 420 LYS LYS LEU GLU LEU PRO PRO ILE LEU VAL TYR ALA ASP
SEQRES 12 A 420 CYS VAL LEU ALA ASN TRP LYS LYS LYS ASP PRO ASN LYS
SEQRES 13 A 420 PRO LEU THR TYR GLU ASN MET ASP VAL LEU PHE SER PHE
SEQRES 14 A 420 ARG ASP GLY ASP CYS SER LYS GLY PHE PHE LEU VAL SER
SEQRES 15 A 420 LEU LEU VAL GLU ILE ALA ALA ALA SER ALA ILE LYS VAL
SEQRES 16 A 420 ILE PRO THR VAL PHE LYS ALA MET GLN MET GLN GLU ARG
SEQRES 17 A 420 ASP THR LEU LEU LYS ALA LEU LEU GLU ILE ALA SER CYS
SEQRES 18 A 420 LEU GLU LYS ALA LEU GLN VAL PHE HIS GLN ILE HIS ASP
SEQRES 19 A 420 HIS VAL ASN PRO LYS ALA PHE PHE SER VAL LEU ARG ILE
SEQRES 20 A 420 TYR LEU SER GLY TRP LYS GLY ASN PRO GLN LEU SER ASP
SEQRES 21 A 420 GLY LEU VAL TYR GLU GLY PHE TRP GLU ASP PRO LYS GLU
SEQRES 22 A 420 PHE ALA GLY GLY SER ALA GLY GLN SER SER VAL PHE GLN
SEQRES 23 A 420 CYS PHE ASP VAL LEU LEU GLY ILE GLN GLN THR ALA GLY
SEQRES 24 A 420 GLY GLY HIS ALA ALA GLN PHE LEU GLN ASP MET ARG ARG
SEQRES 25 A 420 TYR MET PRO PRO ALA HIS ARG ASN PHE LEU CYS SER LEU
SEQRES 26 A 420 GLU SER ASN PRO SER VAL ARG GLU PHE VAL LEU SER LYS
SEQRES 27 A 420 GLY ASP ALA GLY LEU ARG GLU ALA TYR ASP ALA CYS VAL
SEQRES 28 A 420 LYS ALA LEU VAL SER LEU ARG SER TYR HIS LEU GLN ILE
SEQRES 29 A 420 VAL THR LYS TYR ILE LEU ILE PRO ALA SER GLN GLN PRO
SEQRES 30 A 420 LYS GLU ASN LYS THR SER GLU ASP PRO SER LYS LEU GLU
SEQRES 31 A 420 ALA LYS GLY THR GLY GLY THR ASP LEU MET ASN PHE LEU
SEQRES 32 A 420 LYS THR VAL ARG SER THR THR GLU LYS SER LEU LEU LYS
SEQRES 33 A 420 GLU GLY ASN SER
SEQRES 1 B 420 MET HIS HIS HIS HIS HIS HIS GLY GLU ASN LEU TYR PHE
SEQRES 2 B 420 GLN GLY SER ALA HIS ALA MET GLU ASN SER TRP THR ILE
SEQRES 3 B 420 SER LYS GLU TYR HIS ILE ASP GLU GLU VAL GLY PHE ALA
SEQRES 4 B 420 LEU PRO ASN PRO GLN GLU ASN LEU PRO ASP PHE TYR ASN
SEQRES 5 B 420 ASP TRP MET PHE ILE ALA LYS HIS LEU PRO ASP LEU ILE
SEQRES 6 B 420 GLU SER GLY GLN LEU ARG GLU ARG VAL GLU LYS LEU ASN
SEQRES 7 B 420 MET LEU SER ILE ASP HIS LEU THR ASP HIS LYS SER GLN
SEQRES 8 B 420 ARG LEU ALA ARG LEU VAL LEU GLY CYS ILE THR MET ALA
SEQRES 9 B 420 TYR VAL TRP GLY LYS GLY HIS GLY ASP VAL ARG LYS VAL
SEQRES 10 B 420 LEU PRO ARG ASN ILE ALA VAL PRO TYR CYS GLN LEU SER
SEQRES 11 B 420 LYS LYS LEU GLU LEU PRO PRO ILE LEU VAL TYR ALA ASP
SEQRES 12 B 420 CYS VAL LEU ALA ASN TRP LYS LYS LYS ASP PRO ASN LYS
SEQRES 13 B 420 PRO LEU THR TYR GLU ASN MET ASP VAL LEU PHE SER PHE
SEQRES 14 B 420 ARG ASP GLY ASP CYS SER LYS GLY PHE PHE LEU VAL SER
SEQRES 15 B 420 LEU LEU VAL GLU ILE ALA ALA ALA SER ALA ILE LYS VAL
SEQRES 16 B 420 ILE PRO THR VAL PHE LYS ALA MET GLN MET GLN GLU ARG
SEQRES 17 B 420 ASP THR LEU LEU LYS ALA LEU LEU GLU ILE ALA SER CYS
SEQRES 18 B 420 LEU GLU LYS ALA LEU GLN VAL PHE HIS GLN ILE HIS ASP
SEQRES 19 B 420 HIS VAL ASN PRO LYS ALA PHE PHE SER VAL LEU ARG ILE
SEQRES 20 B 420 TYR LEU SER GLY TRP LYS GLY ASN PRO GLN LEU SER ASP
SEQRES 21 B 420 GLY LEU VAL TYR GLU GLY PHE TRP GLU ASP PRO LYS GLU
SEQRES 22 B 420 PHE ALA GLY GLY SER ALA GLY GLN SER SER VAL PHE GLN
SEQRES 23 B 420 CYS PHE ASP VAL LEU LEU GLY ILE GLN GLN THR ALA GLY
SEQRES 24 B 420 GLY GLY HIS ALA ALA GLN PHE LEU GLN ASP MET ARG ARG
SEQRES 25 B 420 TYR MET PRO PRO ALA HIS ARG ASN PHE LEU CYS SER LEU
SEQRES 26 B 420 GLU SER ASN PRO SER VAL ARG GLU PHE VAL LEU SER LYS
SEQRES 27 B 420 GLY ASP ALA GLY LEU ARG GLU ALA TYR ASP ALA CYS VAL
SEQRES 28 B 420 LYS ALA LEU VAL SER LEU ARG SER TYR HIS LEU GLN ILE
SEQRES 29 B 420 VAL THR LYS TYR ILE LEU ILE PRO ALA SER GLN GLN PRO
SEQRES 30 B 420 LYS GLU ASN LYS THR SER GLU ASP PRO SER LYS LEU GLU
SEQRES 31 B 420 ALA LYS GLY THR GLY GLY THR ASP LEU MET ASN PHE LEU
SEQRES 32 B 420 LYS THR VAL ARG SER THR THR GLU LYS SER LEU LEU LYS
SEQRES 33 B 420 GLU GLY ASN SER
HET HEM A 501 43
HET LKP A 502 27
HET HEM B 501 43
HET LKP B 502 27
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM LKP TRANS-4-{(1R)-2-[(5S)-6-FLUORO-5H-IMIDAZO[5,1-
HETNAM 2 LKP A]ISOINDOL-5-YL]-1-HYDROXYETHYL}CYCLOHEXAN-1-OL
HETSYN HEM HEME
HETSYN LKP NAVOXIMOD
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 LKP 2(C18 H21 F N2 O2)
FORMUL 7 HOH *91(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 SER A 52 1 8
HELIX 4 AA4 GLN A 54 LYS A 61 1 8
HELIX 5 AA5 SER A 66 LEU A 70 5 5
HELIX 6 AA6 ASP A 72 GLY A 93 1 22
HELIX 7 AA7 PRO A 104 LEU A 118 1 15
HELIX 8 AA8 VAL A 125 VAL A 130 1 6
HELIX 9 AA9 THR A 144 GLU A 146 5 3
HELIX 10 AB1 CYS A 159 LYS A 179 1 21
HELIX 11 AB2 VAL A 180 MET A 190 1 11
HELIX 12 AB3 GLU A 192 HIS A 215 1 24
HELIX 13 AB4 GLN A 216 VAL A 221 1 6
HELIX 14 AB5 ASN A 222 VAL A 229 1 8
HELIX 15 AB6 VAL A 229 LEU A 234 1 6
HELIX 16 AB7 ASN A 240 SER A 244 5 5
HELIX 17 AB8 SER A 263 GLN A 266 5 4
HELIX 18 AB9 SER A 267 LEU A 277 1 11
HELIX 19 AC1 GLY A 286 ARG A 296 1 11
HELIX 20 AC2 ARG A 297 MET A 299 5 3
HELIX 21 AC3 PRO A 300 SER A 312 1 13
HELIX 22 AC4 SER A 315 LYS A 323 1 9
HELIX 23 AC5 ASP A 325 ILE A 354 1 30
HELIX 24 AC6 ILE A 354 GLN A 360 1 7
HELIX 25 AC7 GLY A 381 SER A 398 1 18
HELIX 26 AC8 ILE B 11 HIS B 16 1 6
HELIX 27 AC9 PRO B 33 PHE B 35 5 3
HELIX 28 AD1 TYR B 36 HIS B 45 1 10
HELIX 29 AD2 HIS B 45 SER B 52 1 8
HELIX 30 AD3 GLN B 54 LYS B 61 1 8
HELIX 31 AD4 SER B 66 LEU B 70 5 5
HELIX 32 AD5 ASP B 72 GLY B 93 1 22
HELIX 33 AD6 PRO B 104 LEU B 118 1 15
HELIX 34 AD7 VAL B 125 VAL B 130 1 6
HELIX 35 AD8 THR B 144 GLU B 146 5 3
HELIX 36 AD9 CYS B 159 LYS B 179 1 21
HELIX 37 AE1 VAL B 180 MET B 190 1 11
HELIX 38 AE2 GLU B 192 PHE B 214 1 23
HELIX 39 AE3 GLN B 216 VAL B 221 1 6
HELIX 40 AE4 ASN B 222 VAL B 229 1 8
HELIX 41 AE5 VAL B 229 SER B 235 1 7
HELIX 42 AE6 ASN B 240 SER B 244 5 5
HELIX 43 AE7 SER B 263 GLN B 266 5 4
HELIX 44 AE8 SER B 267 LEU B 277 1 11
HELIX 45 AE9 GLY B 286 ARG B 296 1 11
HELIX 46 AF1 ARG B 297 MET B 299 5 3
HELIX 47 AF2 PRO B 300 SER B 312 1 13
HELIX 48 AF3 SER B 315 LYS B 323 1 9
HELIX 49 AF4 ASP B 325 ILE B 354 1 30
HELIX 50 AF5 ILE B 354 GLN B 360 1 7
HELIX 51 AF6 GLY B 381 LYS B 397 1 17
SHEET 1 AA1 2 VAL A 102 LEU A 103 0
SHEET 2 AA1 2 VAL A 248 TYR A 249 1 O VAL A 248 N LEU A 103
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 2.05
LINK NE2 HIS A 346 FE HEM A 501 1555 1555 2.06
LINK NE2 HIS B 346 FE HEM B 501 1555 1555 2.23
LINK FE HEM A 501 N10 LKP A 502 1555 1555 2.13
LINK FE HEM B 501 N10 LKP B 502 1555 1555 1.95
SITE 1 AC1 20 PHE A 163 VAL A 170 PHE A 214 ILE A 217
SITE 2 AC1 20 PHE A 226 SER A 263 ALA A 264 PHE A 270
SITE 3 AC1 20 ARG A 343 HIS A 346 ILE A 349 VAL A 350
SITE 4 AC1 20 TYR A 353 ILE A 354 PHE A 387 LEU A 388
SITE 5 AC1 20 VAL A 391 LKP A 502 HOH A 612 HOH A 622
SITE 1 AC2 11 CYS A 129 VAL A 130 PHE A 163 PHE A 164
SITE 2 AC2 11 SER A 167 ARG A 231 LEU A 234 SER A 235
SITE 3 AC2 11 GLY A 262 ALA A 264 HEM A 501
SITE 1 AC3 22 TYR B 126 PHE B 163 SER B 167 VAL B 170
SITE 2 AC3 22 PHE B 214 ILE B 217 PHE B 226 SER B 263
SITE 3 AC3 22 ALA B 264 PHE B 270 PHE B 291 ARG B 343
SITE 4 AC3 22 HIS B 346 ILE B 349 VAL B 350 TYR B 353
SITE 5 AC3 22 ILE B 354 PHE B 387 LEU B 388 VAL B 391
SITE 6 AC3 22 LKP B 502 HOH B 611
SITE 1 AC4 9 CYS B 129 VAL B 130 PHE B 163 ARG B 231
SITE 2 AC4 9 SER B 235 GLY B 262 SER B 263 ALA B 264
SITE 3 AC4 9 HEM B 501
CRYST1 85.062 90.224 130.237 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 0.011756 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011084 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007678 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
