HEADER OXIDOREDUCTASE 08-JUL-97 1AOM
TITLE SUBSTRATE AND PRODUCT BOUND TO CYTOCHROME CD1 NITRITE
TITLE 2 REDUCTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRITE REDUCTASE;
COMPND 3 CHAIN: A, B
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PARACOCCUS PANTOTROPHUS;
SOURCE 3 ORGANISM_TAXID: 82367;
SOURCE 4 CELLULAR_LOCATION: PERIPLASM
KEYWDS OXIDOREDUCTASE, ENZYME, NITRITE REDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.A.WILLIAMS,V.FULOP
REVDAT 3 24-FEB-09 1AOM 1 VERSN
REVDAT 2 30-SEP-03 1AOM 1 DBREF
REVDAT 1 04-FEB-98 1AOM 0
JRNL AUTH P.A.WILLIAMS,V.FULOP,E.F.GARMAN,N.F.SAUNDERS,
JRNL AUTH 2 S.J.FERGUSON,J.HAJDU
JRNL TITL HAEM-LIGAND SWITCHING DURING CATALYSIS IN CRYSTALS
JRNL TITL 2 OF A NITROGEN-CYCLE ENZYME.
JRNL REF NATURE V. 389 406 1997
JRNL REFN ISSN 0028-0836
JRNL PMID 9311786
JRNL DOI 10.1038/38775
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.2
REMARK 3 NUMBER OF REFLECTIONS : 98949
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : NULL
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : NULL
REMARK 3 SOLVENT ATOMS : 1078
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : CONSTRAINTS
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1AOM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-95
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX9.5
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.88
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 98949
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.15500
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.8
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.3 M AMMONIUM SULFATE 50MM
REMARK 280 POTASSIUM PHOSPHATE PH 7.0 CRYSTALS WERE REDUCED USING 16MM
REMARK 280 SODIUM DITHIONITE. CRYSTAL 1 SOAKED IN NITRITE.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 30.30000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 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 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 GLN A 1
REMARK 465 GLU A 2
REMARK 465 GLN A 3
REMARK 465 VAL A 4
REMARK 465 ALA A 5
REMARK 465 PRO A 6
REMARK 465 PRO A 7
REMARK 465 LYS A 8
REMARK 465 ASP A 9
REMARK 465 PRO A 10
REMARK 465 ALA A 11
REMARK 465 ALA A 12
REMARK 465 ALA A 13
REMARK 465 LEU A 14
REMARK 465 GLU A 15
REMARK 465 ASP A 16
REMARK 465 HIS A 17
REMARK 465 LYS A 18
REMARK 465 THR A 19
REMARK 465 ARG A 20
REMARK 465 THR A 21
REMARK 465 ASP A 22
REMARK 465 ASN A 23
REMARK 465 ARG A 24
REMARK 465 TYR A 25
REMARK 465 GLU A 26
REMARK 465 PRO A 27
REMARK 465 SER A 28
REMARK 465 LEU A 29
REMARK 465 ASP A 30
REMARK 465 ASN A 31
REMARK 465 LEU A 32
REMARK 465 ALA A 33
REMARK 465 GLN A 34
REMARK 465 GLN A 35
REMARK 465 ASP A 36
REMARK 465 VAL A 37
REMARK 465 ALA A 38
REMARK 465 ALA A 39
REMARK 465 PRO A 40
REMARK 465 GLY A 41
REMARK 465 ALA A 42
REMARK 465 PRO A 43
REMARK 465 GLU A 44
REMARK 465 GLY A 45
REMARK 465 VAL A 46
REMARK 465 THR A 47
REMARK 465 ALA A 48
REMARK 465 LEU A 49
REMARK 465 SER A 50
REMARK 465 ASP A 51
REMARK 465 ALA A 52
REMARK 465 GLN A 53
REMARK 465 TYR A 54
REMARK 465 ASN A 55
REMARK 465 GLU A 56
REMARK 465 ALA A 57
REMARK 465 ASN A 58
REMARK 465 LYS A 59
REMARK 465 ILE A 60
REMARK 465 TYR A 61
REMARK 465 PHE A 62
REMARK 465 GLU A 63
REMARK 465 ARG A 64
REMARK 465 CYS A 65
REMARK 465 ALA A 66
REMARK 465 GLY A 67
REMARK 465 CYS A 68
REMARK 465 HIS A 69
REMARK 465 GLY A 70
REMARK 465 VAL A 71
REMARK 465 LEU A 72
REMARK 465 ARG A 73
REMARK 465 LYS A 74
REMARK 465 GLY A 75
REMARK 465 ALA A 76
REMARK 465 THR A 77
REMARK 465 GLY A 78
REMARK 465 LYS A 79
REMARK 465 ALA A 80
REMARK 465 LEU A 81
REMARK 465 THR A 82
REMARK 465 PRO A 83
REMARK 465 ASP A 84
REMARK 465 LEU A 85
REMARK 465 THR A 86
REMARK 465 ARG A 87
REMARK 465 ASP A 88
REMARK 465 LEU A 89
REMARK 465 GLY A 90
REMARK 465 PHE A 91
REMARK 465 ASP A 92
REMARK 465 TYR A 93
REMARK 465 LEU A 94
REMARK 465 GLN A 95
REMARK 465 SER A 96
REMARK 465 PHE A 97
REMARK 465 ILE A 98
REMARK 465 THR A 99
REMARK 465 TYR A 100
REMARK 465 ALA A 101
REMARK 465 SER A 102
REMARK 465 PRO A 103
REMARK 465 ALA A 104
REMARK 465 GLY A 105
REMARK 465 MET A 106
REMARK 465 PRO A 107
REMARK 465 ASN A 108
REMARK 465 TRP A 109
REMARK 465 GLY A 110
REMARK 465 THR A 111
REMARK 465 SER A 112
REMARK 465 GLY A 113
REMARK 465 GLU A 114
REMARK 465 LEU A 115
REMARK 465 SER A 116
REMARK 465 ALA A 117
REMARK 465 GLU A 118
REMARK 465 GLN A 119
REMARK 465 VAL A 120
REMARK 465 ASP A 121
REMARK 465 LEU A 122
REMARK 465 MET A 123
REMARK 465 ALA A 124
REMARK 465 ASN A 125
REMARK 465 TYR A 126
REMARK 465 LEU A 127
REMARK 465 LEU A 128
REMARK 465 GLN B 1
REMARK 465 GLU B 2
REMARK 465 GLN B 3
REMARK 465 VAL B 4
REMARK 465 ALA B 5
REMARK 465 PRO B 6
REMARK 465 PRO B 7
REMARK 465 LYS B 8
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 ARG A 299 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (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,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ALA A 360 N - CA - C ANGL. DEV. = -17.6 DEGREES
REMARK 500 GLY A 390 N - CA - C ANGL. DEV. = -17.0 DEGREES
REMARK 500 ALA B 360 N - CA - C ANGL. DEV. = -17.5 DEGREES
REMARK 500 GLY B 390 N - CA - C ANGL. DEV. = -16.4 DEGREES
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 LEU A 173 77.92 -108.92
REMARK 500 ARG A 174 -73.55 -35.26
REMARK 500 GLU A 297 59.04 -141.83
REMARK 500 ALA A 301 -127.00 -102.63
REMARK 500 LYS A 317 -74.96 -50.18
REMARK 500 ASN A 332 78.96 -108.69
REMARK 500 ALA A 340 -103.52 -123.49
REMARK 500 PHE A 343 31.06 74.34
REMARK 500 HIS A 345 -95.67 -129.49
REMARK 500 THR A 386 67.10 61.90
REMARK 500 ALA A 437 -142.68 -114.91
REMARK 500 ALA A 458 42.92 -147.18
REMARK 500 GLN A 507 104.47 54.46
REMARK 500 THR A 554 -100.30 -128.85
REMARK 500 LEU B 29 59.06 -91.92
REMARK 500 ALA B 76 -101.44 -137.44
REMARK 500 ALA B 101 175.80 86.39
REMARK 500 TRP B 109 -27.30 -174.27
REMARK 500 LEU B 173 77.18 -107.93
REMARK 500 ARG B 174 -78.54 -32.53
REMARK 500 ALA B 301 -126.29 -102.29
REMARK 500 LYS B 317 -74.31 -52.01
REMARK 500 ASN B 332 75.52 -111.63
REMARK 500 ALA B 340 -102.05 -124.39
REMARK 500 PHE B 343 33.30 73.07
REMARK 500 HIS B 345 -93.09 -131.81
REMARK 500 THR B 386 72.17 60.36
REMARK 500 ALA B 437 -143.21 -113.80
REMARK 500 ALA B 458 48.59 -151.34
REMARK 500 GLN B 507 104.44 55.84
REMARK 500 THR B 554 -99.16 -127.97
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 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 745 DISTANCE = 6.59 ANGSTROMS
REMARK 525 HOH B 773 DISTANCE = 10.65 ANGSTROMS
REMARK 525 HOH B 797 DISTANCE = 7.68 ANGSTROMS
REMARK 525 HOH B 811 DISTANCE = 6.97 ANGSTROMS
REMARK 525 HOH A 877 DISTANCE = 9.98 ANGSTROMS
REMARK 525 HOH A 885 DISTANCE = 10.03 ANGSTROMS
REMARK 525 HOH B 908 DISTANCE = 7.52 ANGSTROMS
REMARK 525 HOH A 909 DISTANCE = 13.21 ANGSTROMS
REMARK 525 HOH B 954 DISTANCE = 5.09 ANGSTROMS
REMARK 525 HOH B 982 DISTANCE = 5.47 ANGSTROMS
REMARK 525 HOH A1019 DISTANCE = 7.58 ANGSTROMS
REMARK 525 HOH B1027 DISTANCE = 8.84 ANGSTROMS
REMARK 525 HOH A1038 DISTANCE = 5.03 ANGSTROMS
REMARK 525 HOH B1044 DISTANCE = 7.84 ANGSTROMS
REMARK 525 HOH A1085 DISTANCE = 6.78 ANGSTROMS
REMARK 525 HOH A1099 DISTANCE = 7.33 ANGSTROMS
REMARK 525 HOH A1104 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH B1107 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH B1178 DISTANCE = 8.07 ANGSTROMS
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 DHE A 602 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 200 NE2
REMARK 620 2 2NO A 603 N 178.3
REMARK 620 3 2NO A 603 O1 160.0 21.6
REMARK 620 4 2NO A 603 O2 155.9 22.4 44.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 17 NE2
REMARK 620 2 HIS B 69 NE2 178.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 DHE B 602 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 200 NE2
REMARK 620 2 NO B 603 N 178.2
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DHE A 602
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2NO A 603
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 601
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DHE B 602
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO B 603
DBREF 1AOM A 1 567 UNP P72181 NIRS_PARPN 30 596
DBREF 1AOM B 1 567 UNP P72181 NIRS_PARPN 30 596
SEQADV 1AOM MET A 160 UNP P72181 GLU 189 CONFLICT
SEQADV 1AOM SER A 185 UNP P72181 THR 214 CONFLICT
SEQADV 1AOM THR A 191 UNP P72181 SER 220 CONFLICT
SEQADV 1AOM ASN A 331 UNP P72181 ASP 360 CONFLICT
SEQADV 1AOM MET B 160 UNP P72181 GLU 189 CONFLICT
SEQADV 1AOM SER B 185 UNP P72181 THR 214 CONFLICT
SEQADV 1AOM THR B 191 UNP P72181 SER 220 CONFLICT
SEQADV 1AOM ASN B 331 UNP P72181 ASP 360 CONFLICT
SEQRES 1 A 567 GLN GLU GLN VAL ALA PRO PRO LYS ASP PRO ALA ALA ALA
SEQRES 2 A 567 LEU GLU ASP HIS LYS THR ARG THR ASP ASN ARG TYR GLU
SEQRES 3 A 567 PRO SER LEU ASP ASN LEU ALA GLN GLN ASP VAL ALA ALA
SEQRES 4 A 567 PRO GLY ALA PRO GLU GLY VAL THR ALA LEU SER ASP ALA
SEQRES 5 A 567 GLN TYR ASN GLU ALA ASN LYS ILE TYR PHE GLU ARG CYS
SEQRES 6 A 567 ALA GLY CYS HIS GLY VAL LEU ARG LYS GLY ALA THR GLY
SEQRES 7 A 567 LYS ALA LEU THR PRO ASP LEU THR ARG ASP LEU GLY PHE
SEQRES 8 A 567 ASP TYR LEU GLN SER PHE ILE THR TYR ALA SER PRO ALA
SEQRES 9 A 567 GLY MET PRO ASN TRP GLY THR SER GLY GLU LEU SER ALA
SEQRES 10 A 567 GLU GLN VAL ASP LEU MET ALA ASN TYR LEU LEU LEU ASP
SEQRES 11 A 567 PRO ALA ALA PRO PRO GLU PHE GLY MET LYS GLU MET ARG
SEQRES 12 A 567 GLU SER TRP LYS VAL HIS VAL ALA PRO GLU ASP ARG PRO
SEQRES 13 A 567 THR GLN GLN MET ASN ASP TRP ASP LEU GLU ASN LEU PHE
SEQRES 14 A 567 SER VAL THR LEU ARG ASP ALA GLY GLN ILE ALA LEU ILE
SEQRES 15 A 567 ASP GLY SER THR TYR GLU ILE LYS THR VAL LEU ASP THR
SEQRES 16 A 567 GLY TYR ALA VAL HIS ILE SER ARG LEU SER ALA SER GLY
SEQRES 17 A 567 ARG TYR LEU PHE VAL ILE GLY ARG ASP GLY LYS VAL ASN
SEQRES 18 A 567 MET ILE ASP LEU TRP MET LYS GLU PRO THR THR VAL ALA
SEQRES 19 A 567 GLU ILE LYS ILE GLY SER GLU ALA ARG SER ILE GLU THR
SEQRES 20 A 567 SER LYS MET GLU GLY TRP GLU ASP LYS TYR ALA ILE ALA
SEQRES 21 A 567 GLY ALA TYR TRP PRO PRO GLN TYR VAL ILE MET ASP GLY
SEQRES 22 A 567 GLU THR LEU GLU PRO LYS LYS ILE GLN SER THR ARG GLY
SEQRES 23 A 567 MET THR TYR ASP GLU GLN GLU TYR HIS PRO GLU PRO ARG
SEQRES 24 A 567 VAL ALA ALA ILE LEU ALA SER HIS TYR ARG PRO GLU PHE
SEQRES 25 A 567 ILE VAL ASN VAL LYS GLU THR GLY LYS ILE LEU LEU VAL
SEQRES 26 A 567 ASP TYR THR ASP LEU ASN ASN LEU LYS THR THR GLU ILE
SEQRES 27 A 567 SER ALA GLU ARG PHE LEU HIS ASP GLY GLY LEU ASP GLY
SEQRES 28 A 567 SER HIS ARG TYR PHE ILE THR ALA ALA ASN ALA ARG ASN
SEQRES 29 A 567 LYS LEU VAL VAL ILE ASP THR LYS GLU GLY LYS LEU VAL
SEQRES 30 A 567 ALA ILE GLU ASP THR GLY GLY GLN THR PRO HIS PRO GLY
SEQRES 31 A 567 ARG GLY ALA ASN PHE VAL HIS PRO THR PHE GLY PRO VAL
SEQRES 32 A 567 TRP ALA THR SER HIS MET GLY ASP ASP SER VAL ALA LEU
SEQRES 33 A 567 ILE GLY THR ASP PRO GLU GLY HIS PRO ASP ASN ALA TRP
SEQRES 34 A 567 LYS ILE LEU ASP SER PHE PRO ALA LEU GLY GLY GLY SER
SEQRES 35 A 567 LEU PHE ILE LYS THR HIS PRO ASN SER GLN TYR LEU TYR
SEQRES 36 A 567 VAL ASP ALA THR LEU ASN PRO GLU ALA GLU ILE SER GLY
SEQRES 37 A 567 SER VAL ALA VAL PHE ASP ILE LYS ALA MET THR GLY ASP
SEQRES 38 A 567 GLY SER ASP PRO GLU PHE LYS THR LEU PRO ILE ALA GLU
SEQRES 39 A 567 TRP ALA GLY ILE THR GLU GLY GLN PRO ARG VAL VAL GLN
SEQRES 40 A 567 GLY GLU PHE ASN LYS ASP GLY THR GLU VAL TRP PHE SER
SEQRES 41 A 567 VAL TRP ASN GLY LYS ASP GLN GLU SER ALA LEU VAL VAL
SEQRES 42 A 567 VAL ASP ASP LYS THR LEU GLU LEU LYS HIS VAL ILE LYS
SEQRES 43 A 567 ASP GLU ARG LEU VAL THR PRO THR GLY LYS PHE ASN VAL
SEQRES 44 A 567 TYR ASN THR MET THR ASP THR TYR
SEQRES 1 B 567 GLN GLU GLN VAL ALA PRO PRO LYS ASP PRO ALA ALA ALA
SEQRES 2 B 567 LEU GLU ASP HIS LYS THR ARG THR ASP ASN ARG TYR GLU
SEQRES 3 B 567 PRO SER LEU ASP ASN LEU ALA GLN GLN ASP VAL ALA ALA
SEQRES 4 B 567 PRO GLY ALA PRO GLU GLY VAL THR ALA LEU SER ASP ALA
SEQRES 5 B 567 GLN TYR ASN GLU ALA ASN LYS ILE TYR PHE GLU ARG CYS
SEQRES 6 B 567 ALA GLY CYS HIS GLY VAL LEU ARG LYS GLY ALA THR GLY
SEQRES 7 B 567 LYS ALA LEU THR PRO ASP LEU THR ARG ASP LEU GLY PHE
SEQRES 8 B 567 ASP TYR LEU GLN SER PHE ILE THR TYR ALA SER PRO ALA
SEQRES 9 B 567 GLY MET PRO ASN TRP GLY THR SER GLY GLU LEU SER ALA
SEQRES 10 B 567 GLU GLN VAL ASP LEU MET ALA ASN TYR LEU LEU LEU ASP
SEQRES 11 B 567 PRO ALA ALA PRO PRO GLU PHE GLY MET LYS GLU MET ARG
SEQRES 12 B 567 GLU SER TRP LYS VAL HIS VAL ALA PRO GLU ASP ARG PRO
SEQRES 13 B 567 THR GLN GLN MET ASN ASP TRP ASP LEU GLU ASN LEU PHE
SEQRES 14 B 567 SER VAL THR LEU ARG ASP ALA GLY GLN ILE ALA LEU ILE
SEQRES 15 B 567 ASP GLY SER THR TYR GLU ILE LYS THR VAL LEU ASP THR
SEQRES 16 B 567 GLY TYR ALA VAL HIS ILE SER ARG LEU SER ALA SER GLY
SEQRES 17 B 567 ARG TYR LEU PHE VAL ILE GLY ARG ASP GLY LYS VAL ASN
SEQRES 18 B 567 MET ILE ASP LEU TRP MET LYS GLU PRO THR THR VAL ALA
SEQRES 19 B 567 GLU ILE LYS ILE GLY SER GLU ALA ARG SER ILE GLU THR
SEQRES 20 B 567 SER LYS MET GLU GLY TRP GLU ASP LYS TYR ALA ILE ALA
SEQRES 21 B 567 GLY ALA TYR TRP PRO PRO GLN TYR VAL ILE MET ASP GLY
SEQRES 22 B 567 GLU THR LEU GLU PRO LYS LYS ILE GLN SER THR ARG GLY
SEQRES 23 B 567 MET THR TYR ASP GLU GLN GLU TYR HIS PRO GLU PRO ARG
SEQRES 24 B 567 VAL ALA ALA ILE LEU ALA SER HIS TYR ARG PRO GLU PHE
SEQRES 25 B 567 ILE VAL ASN VAL LYS GLU THR GLY LYS ILE LEU LEU VAL
SEQRES 26 B 567 ASP TYR THR ASP LEU ASN ASN LEU LYS THR THR GLU ILE
SEQRES 27 B 567 SER ALA GLU ARG PHE LEU HIS ASP GLY GLY LEU ASP GLY
SEQRES 28 B 567 SER HIS ARG TYR PHE ILE THR ALA ALA ASN ALA ARG ASN
SEQRES 29 B 567 LYS LEU VAL VAL ILE ASP THR LYS GLU GLY LYS LEU VAL
SEQRES 30 B 567 ALA ILE GLU ASP THR GLY GLY GLN THR PRO HIS PRO GLY
SEQRES 31 B 567 ARG GLY ALA ASN PHE VAL HIS PRO THR PHE GLY PRO VAL
SEQRES 32 B 567 TRP ALA THR SER HIS MET GLY ASP ASP SER VAL ALA LEU
SEQRES 33 B 567 ILE GLY THR ASP PRO GLU GLY HIS PRO ASP ASN ALA TRP
SEQRES 34 B 567 LYS ILE LEU ASP SER PHE PRO ALA LEU GLY GLY GLY SER
SEQRES 35 B 567 LEU PHE ILE LYS THR HIS PRO ASN SER GLN TYR LEU TYR
SEQRES 36 B 567 VAL ASP ALA THR LEU ASN PRO GLU ALA GLU ILE SER GLY
SEQRES 37 B 567 SER VAL ALA VAL PHE ASP ILE LYS ALA MET THR GLY ASP
SEQRES 38 B 567 GLY SER ASP PRO GLU PHE LYS THR LEU PRO ILE ALA GLU
SEQRES 39 B 567 TRP ALA GLY ILE THR GLU GLY GLN PRO ARG VAL VAL GLN
SEQRES 40 B 567 GLY GLU PHE ASN LYS ASP GLY THR GLU VAL TRP PHE SER
SEQRES 41 B 567 VAL TRP ASN GLY LYS ASP GLN GLU SER ALA LEU VAL VAL
SEQRES 42 B 567 VAL ASP ASP LYS THR LEU GLU LEU LYS HIS VAL ILE LYS
SEQRES 43 B 567 ASP GLU ARG LEU VAL THR PRO THR GLY LYS PHE ASN VAL
SEQRES 44 B 567 TYR ASN THR MET THR ASP THR TYR
HET DHE A 602 49
HET 2NO A 603 3
HET HEM B 601 43
HET DHE B 602 49
HET NO B 603 2
HETNAM DHE HEME D
HETNAM 2NO NITROGEN DIOXIDE
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM NO NITRIC OXIDE
HETSYN HEM HEME
HETSYN NO NITROGEN MONOXIDE
FORMUL 3 DHE 2(C34 H32 FE N4 O10)
FORMUL 4 2NO N O2
FORMUL 5 HEM C34 H32 FE N4 O4
FORMUL 7 NO N O
FORMUL 8 HOH *1078(H2 O)
HELIX 1 1 MET A 139 SER A 145 1 7
HELIX 2 2 PRO A 152 ASP A 154 5 3
HELIX 3 3 LEU A 165 ASN A 167 5 3
HELIX 4 4 ARG A 174 ALA A 176 5 3
HELIX 5 5 ASN A 361 ARG A 363 5 3
HELIX 6 6 ALA A 464 SER A 467 1 4
HELIX 7 7 ILE A 475 ALA A 477 5 3
HELIX 8 8 ILE A 492 ALA A 496 1 5
HELIX 9 9 VAL A 559 MET A 563 1 5
HELIX 10 10 PRO B 10 ASP B 16 5 7
HELIX 11 11 THR B 21 ASN B 23 5 3
HELIX 12 12 LEU B 32 GLN B 34 5 3
HELIX 13 13 ASP B 51 ARG B 64 1 14
HELIX 14 14 ALA B 66 HIS B 69 1 4
HELIX 15 15 PRO B 83 LEU B 89 1 7
HELIX 16 16 PHE B 91 TYR B 100 1 10
HELIX 17 17 ALA B 117 LEU B 128 1 12
HELIX 18 18 MET B 139 SER B 145 1 7
HELIX 19 19 PRO B 152 ASP B 154 5 3
HELIX 20 20 LEU B 165 ASN B 167 5 3
HELIX 21 21 ARG B 174 ALA B 176 5 3
HELIX 22 22 ASN B 361 ARG B 363 5 3
HELIX 23 23 PRO B 425 ASN B 427 5 3
HELIX 24 24 ALA B 464 SER B 467 1 4
HELIX 25 25 ILE B 475 ALA B 477 5 3
HELIX 26 26 ILE B 492 ALA B 496 1 5
HELIX 27 27 VAL B 559 MET B 563 1 5
SHEET 1 A 4 LYS A 556 ASN A 558 0
SHEET 2 A 4 LEU A 168 LEU A 173 -1 N SER A 170 O PHE A 557
SHEET 3 A 4 GLN A 178 ASP A 183 -1 N ILE A 182 O PHE A 169
SHEET 4 A 4 ILE A 189 ASP A 194 -1 N LEU A 193 O ILE A 179
SHEET 1 B 4 VAL A 199 LEU A 204 0
SHEET 2 B 4 TYR A 210 GLY A 215 -1 N ILE A 214 O HIS A 200
SHEET 3 B 4 LYS A 219 ASP A 224 -1 N ILE A 223 O LEU A 211
SHEET 4 B 4 THR A 232 LYS A 237 -1 N ILE A 236 O VAL A 220
SHEET 1 C 4 SER A 244 THR A 247 0
SHEET 2 C 4 TYR A 257 ALA A 262 -1 N GLY A 261 O SER A 244
SHEET 3 C 4 GLN A 267 ASP A 272 -1 N MET A 271 O ALA A 258
SHEET 4 C 4 PRO A 278 SER A 283 -1 N GLN A 282 O TYR A 268
SHEET 1 D 4 ILE A 303 ALA A 305 0
SHEET 2 D 4 GLU A 311 VAL A 316 -1 N ILE A 313 O LEU A 304
SHEET 3 D 4 LYS A 321 ASP A 326 -1 N VAL A 325 O PHE A 312
SHEET 4 D 4 THR A 335 SER A 339 -1 N ILE A 338 O ILE A 322
SHEET 1 E 4 GLY A 347 LEU A 349 0
SHEET 2 E 4 TYR A 355 ALA A 360 -1 N ILE A 357 O GLY A 348
SHEET 3 E 4 LYS A 365 ASP A 370 -1 N ILE A 369 O PHE A 356
SHEET 4 E 4 LYS A 375 ASP A 381 -1 N GLU A 380 O LEU A 366
SHEET 1 F 4 ALA A 393 HIS A 397 0
SHEET 2 F 4 GLY A 401 SER A 407 -1 N ALA A 405 O ALA A 393
SHEET 3 F 4 SER A 413 GLY A 418 -1 N ILE A 417 O TRP A 404
SHEET 4 F 4 ILE A 431 PRO A 436 -1 N PHE A 435 O VAL A 414
SHEET 1 G 3 TYR A 453 ASP A 457 0
SHEET 2 G 3 VAL A 470 ASP A 474 -1 N PHE A 473 O LEU A 454
SHEET 3 G 3 PHE A 487 LEU A 490 -1 N LEU A 490 O VAL A 470
SHEET 1 H 4 ARG A 504 VAL A 506 0
SHEET 2 H 4 GLU A 516 TRP A 522 -1 N TRP A 522 O ARG A 504
SHEET 3 H 4 ALA A 530 ASP A 535 -1 N VAL A 534 O VAL A 517
SHEET 4 H 4 GLU A 540 ILE A 545 -1 N ILE A 545 O LEU A 531
SHEET 1 I 4 LYS B 556 ASN B 558 0
SHEET 2 I 4 PHE B 169 LEU B 173 -1 N SER B 170 O PHE B 557
SHEET 3 I 4 GLN B 178 ILE B 182 -1 N ILE B 182 O PHE B 169
SHEET 4 I 4 ILE B 189 ASP B 194 -1 N LEU B 193 O ILE B 179
SHEET 1 J 4 VAL B 199 LEU B 204 0
SHEET 2 J 4 TYR B 210 GLY B 215 -1 N ILE B 214 O HIS B 200
SHEET 3 J 4 LYS B 219 ASP B 224 -1 N ILE B 223 O LEU B 211
SHEET 4 J 4 THR B 232 LYS B 237 -1 N ILE B 236 O VAL B 220
SHEET 1 K 4 SER B 244 THR B 247 0
SHEET 2 K 4 TYR B 257 ALA B 262 -1 N GLY B 261 O SER B 244
SHEET 3 K 4 GLN B 267 ASP B 272 -1 N MET B 271 O ALA B 258
SHEET 4 K 4 PRO B 278 SER B 283 -1 N GLN B 282 O TYR B 268
SHEET 1 L 4 ILE B 303 ALA B 305 0
SHEET 2 L 4 GLU B 311 VAL B 316 -1 N ILE B 313 O LEU B 304
SHEET 3 L 4 LYS B 321 ASP B 326 -1 N VAL B 325 O PHE B 312
SHEET 4 L 4 THR B 335 SER B 339 -1 N ILE B 338 O ILE B 322
SHEET 1 M 4 GLY B 347 LEU B 349 0
SHEET 2 M 4 TYR B 355 ALA B 360 -1 N ILE B 357 O GLY B 348
SHEET 3 M 4 LYS B 365 ASP B 370 -1 N ILE B 369 O PHE B 356
SHEET 4 M 4 LYS B 375 ASP B 381 -1 N GLU B 380 O LEU B 366
SHEET 1 N 4 ALA B 393 HIS B 397 0
SHEET 2 N 4 GLY B 401 SER B 407 -1 N ALA B 405 O ALA B 393
SHEET 3 N 4 SER B 413 GLY B 418 -1 N ILE B 417 O TRP B 404
SHEET 4 N 4 ILE B 431 PRO B 436 -1 N PHE B 435 O VAL B 414
SHEET 1 O 3 TYR B 453 VAL B 456 0
SHEET 2 O 3 VAL B 470 ASP B 474 -1 N PHE B 473 O LEU B 454
SHEET 3 O 3 PHE B 487 LEU B 490 -1 N LEU B 490 O VAL B 470
SHEET 1 P 4 ARG B 504 VAL B 506 0
SHEET 2 P 4 GLU B 516 TRP B 522 -1 N TRP B 522 O ARG B 504
SHEET 3 P 4 ALA B 530 ASP B 535 -1 N VAL B 534 O VAL B 517
SHEET 4 P 4 GLU B 540 ILE B 545 -1 N ILE B 545 O LEU B 531
LINK FE DHE A 602 NE2 HIS A 200 1555 1555 1.96
LINK FE DHE A 602 N 2NO A 603 1555 1555 2.00
LINK FE HEM B 601 NE2 HIS B 17 1555 1555 1.99
LINK FE HEM B 601 NE2 HIS B 69 1555 1555 2.00
LINK CAB HEM B 601 SG CYS B 65 1555 1555 1.79
LINK CAC HEM B 601 SG CYS B 68 1555 1555 1.81
LINK FE DHE B 602 NE2 HIS B 200 1555 1555 2.00
LINK FE DHE B 602 N NO B 603 1555 1555 1.99
LINK FE DHE A 602 O1 2NO A 603 1555 1555 2.81
LINK FE DHE A 602 O2 2NO A 603 1555 1555 2.79
CISPEP 1 TRP A 264 PRO A 265 0 -0.33
CISPEP 2 TRP B 264 PRO B 265 0 -0.63
SITE 1 AC1 26 ARG A 174 HIS A 200 ILE A 201 ARG A 203
SITE 2 AC1 26 ARG A 216 ARG A 243 SER A 244 ILE A 245
SITE 3 AC1 26 TYR A 263 ALA A 301 ALA A 302 ILE A 303
SITE 4 AC1 26 HIS A 345 ARG A 391 PHE A 444 GLN A 507
SITE 5 AC1 26 GLY A 555 PHE A 557 2NO A 603 HOH A 613
SITE 6 AC1 26 HOH A 621 HOH A 639 HOH A 642 HOH A 707
SITE 7 AC1 26 HOH A 790 HOH A 804
SITE 1 AC2 4 HIS A 345 HIS A 388 PHE A 444 DHE A 602
SITE 1 AC3 16 ASP B 16 HIS B 17 ASN B 23 ARG B 64
SITE 2 AC3 16 CYS B 65 CYS B 68 HIS B 69 GLY B 78
SITE 3 AC3 16 LYS B 79 LEU B 81 LEU B 89 TYR B 93
SITE 4 AC3 16 LEU B 94 PHE B 97 SER B 102 HOH B1141
SITE 1 AC4 32 TYR B 25 PRO B 27 SER B 28 MET B 106
SITE 2 AC4 32 TRP B 109 ARG B 174 HIS B 200 ILE B 201
SITE 3 AC4 32 ARG B 203 ARG B 216 ARG B 243 SER B 244
SITE 4 AC4 32 ILE B 245 TYR B 263 ALA B 302 ILE B 303
SITE 5 AC4 32 HIS B 345 ARG B 391 PHE B 444 GLN B 507
SITE 6 AC4 32 TRP B 522 THR B 554 GLY B 555 PHE B 557
SITE 7 AC4 32 NO B 603 HOH B 621 HOH B 629 HOH B 632
SITE 8 AC4 32 HOH B 633 HOH B 814 HOH B 888 HOH B 912
SITE 1 AC5 4 TYR B 25 HIS B 388 PHE B 444 DHE B 602
CRYST1 106.700 60.600 100.100 90.00 112.30 90.00 P 1 21 1 4
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 0.009372 0.000000 0.003844 0.00000
SCALE2 0.000000 0.016502 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010798 0.00000
MTRIX1 1 0.716984 0.550397 0.427781 -27.69604 1
MTRIX2 1 0.545203 -0.825157 0.147884 4.48448 1
MTRIX3 1 0.434382 0.127197 -0.891703 107.20798 1
(ATOM LINES ARE NOT SHOWN.)
END
