spacer
spacer

PDBsum entry 3rgp

Go to PDB code: 
Top Page protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
3rgp
Jmol
Contents
Protein chains
499 a.a.
Ligands
HEM-_NO ×4
Waters ×2020
HEADER    OXIDOREDUCTASE                          08-APR-11   3RGP
TITLE     STRUCTURAL AND KINETIC ANALYSIS OF THE BEEF LIVER CATALASE COMPLEXED
TITLE    2 WITH NITRIC OXIDE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CATALASE;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 FRAGMENT: UNP RESIDUES 4-502;
COMPND   5 EC: 1.11.1.6
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE   3 ORGANISM_COMMON: BOVINE,COW,DOMESTIC CATTLE,DOMESTIC COW;
SOURCE   4 ORGANISM_TAXID: 9913
KEYWDS    HEME PROTEIN, 6TH COORDINATION SITE AS A BINDING POCKET,
KEYWDS   2 OXIDOREDUCATASE, BINDING OF NITRIC OXIDE, NITROSYLATION,
KEYWDS   3 OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    N.PURWAR,M SCHMIDT
REVDAT   4   29-OCT-14 3RGP    1       AUTHOR
REVDAT   3   04-APR-12 3RGP    1       JRNL   VERSN
REVDAT   2   25-MAY-11 3RGP    1       JRNL
REVDAT   1   11-MAY-11 3RGP    0
JRNL        AUTH   N.PURWAR,J.M.MCGARRY,J.KOSTERA,A.A.PACHECO,M.SCHMIDT
JRNL        TITL   INTERACTION OF NITRIC OXIDE WITH CATALASE: STRUCTURAL AND
JRNL        TITL 2 KINETIC ANALYSIS.
JRNL        REF    BIOCHEMISTRY                  V.  50  4491 2011
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   21524057
JRNL        DOI    10.1021/BI200130R
REMARK   2
REMARK   2 RESOLUTION.    1.88 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.3
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.88
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.30
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 4853841.740
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.0
REMARK   3   NUMBER OF REFLECTIONS             : 205859
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 SET) : 0.180
REMARK   3   FREE R VALUE                     : 0.214
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900
REMARK   3   FREE R VALUE TEST SET COUNT      : 10125
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.002
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.88
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.00
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.50
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 31410
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2500
REMARK   3   BIN FREE R VALUE                    : 0.2840
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1638
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.007
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 16068
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 180
REMARK   3   SOLVENT ATOMS            : 2020
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 16.10
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.80
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -3.43000
REMARK   3    B22 (A**2) : -2.87000
REMARK   3    B33 (A**2) : 6.30000
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) : 0.20
REMARK   3   ESD FROM SIGMAA              (A) : 0.20
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 4.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.24
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.25
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : 1.300
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.200
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.960
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.750 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.370 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.930 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.690 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.42
REMARK   3   BSOL        : 63.29
REMARK   3
REMARK   3  NCS MODEL : NONE
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  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : HEME_NAD.PARAM
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  4  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : HEME_NAD.TOP
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK   4
REMARK   4 3RGP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-11.
REMARK 100 THE RCSB ID CODE IS RCSB064909.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 17-JUL-09
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.7
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 14-BM-C
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9
REMARK 200  MONOCHROMATOR                  : BENT GE(111) MONOCHROMATOR
REMARK 200  OPTICS                         : BENT CONICAL SI-MIRROR (RH
REMARK 200                                   COATED) BENT GE(111) MONOCHROMATOR
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 205959
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.880
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.301
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 5.100
REMARK 200  R MERGE                    (I) : 0.09100
REMARK 200  R SYM                      (I) : 0.09100
REMARK 200   FOR THE DATA SET  : 11.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.88
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.32900
REMARK 200  R SYM FOR SHELL            (I) : 0.09100
REMARK 200   FOR SHELL         : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY CODE 4BLC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 59.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1. 45-60MM MG FORMATE MIXED WITH 12-13
REMARK 280  MG/ML PROTEIN CONTAINING 1-5 WT% OF NH4OH. 2. CRYSTALS THEN
REMARK 280  SOAKED OVERNIGHT IN 80 MM MG-FORMATE SOLUTION, PH 6.7, 3. FINALLY
REMARK 280  SOAKED IN 80 MM MG FORMATE AND 150 MM BIS-TRIS & 10-100MM DEANO,
REMARK 280  PH 6.5 , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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       43.05500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      114.01000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       69.97000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      114.01000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       43.05500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       69.97000
REMARK 290   SMTRY3   4  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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 49140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -298.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D
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 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   O    HOH A  1146     O    HOH A  1597              1.88
REMARK 500   O    HOH B   970     O    HOH B  1735              1.89
REMARK 500   NZ   LYS B    37     O    HOH B   511              1.91
REMARK 500   O    HOH A  1449     O    HOH A  1458              1.95
REMARK 500   O    HOH A   644     O    HOH B  2025              1.96
REMARK 500   O    HOH A  1744     O    HOH B  1604              1.97
REMARK 500   O    HOH D   924     O    HOH D  1836              1.97
REMARK 500   O    HOH C  1296     O    HOH C  1395              1.99
REMARK 500   O    HOH C   611     O    HOH C   774              1.99
REMARK 500   O    HOH B  1429     O    HOH B  1946              2.00
REMARK 500   O    HOH B  1023     O    HOH B  1569              2.00
REMARK 500   O    HOH B  1064     O    HOH B  1722              2.01
REMARK 500   O    HOH D  1803     O    HOH D  1939              2.01
REMARK 500   O    HOH A  1224     O    HOH A  1362              2.01
REMARK 500   O    HOH A  1004     O    HOH A  1449              2.05
REMARK 500   O    HOH A   701     O    HOH A  1683              2.05
REMARK 500   N    GLY D   120     O    HOH D   638              2.08
REMARK 500   O    HOH C   561     O    HOH C  1949              2.08
REMARK 500   O    HOH D   975     O    HOH D  1480              2.09
REMARK 500   O    HOH D  1085     O    HOH D  1316              2.09
REMARK 500   O    HOH C  1099     O    HOH C  1369              2.09
REMARK 500   O    HOH D  1312     O    HOH D  1869              2.11
REMARK 500   O    HOH C   620     O    HOH C  1189              2.11
REMARK 500   O    HOH D  1284     O    HOH D  1368              2.12
REMARK 500   O    HOH A  1217     O    HOH A  1784              2.13
REMARK 500   OE1  GLU D   227     O    HOH D  1359              2.14
REMARK 500   O    HOH A  1350     O    HOH A  1508              2.14
REMARK 500   O    HOH D  1911     O    HOH D  1944              2.14
REMARK 500   O    HOH C  1247     O    HOH C  1537              2.16
REMARK 500   O    HOH C  1263     O    HOH C  1610              2.16
REMARK 500   O    HOH C   783     O    HOH C  1764              2.16
REMARK 500   O    HOH A  1506     O    HOH A  2004              2.17
REMARK 500   O    HOH D  1197     O    HOH D  1361              2.17
REMARK 500   O    HOH D  1197     O    HOH D  1377              2.18
REMARK 500   NH1  ARG C   262     O    HOH C   986              2.18
REMARK 500   O    HOH B   855     O    HOH C  1586              2.18
REMARK 500   O    HOH C  1398     O    HOH C  1724              2.19
REMARK 500   N    GLY A   120     O    HOH D   638              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH C   666     O    HOH C   774     3555     2.07
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    ARG A   4     -161.57   -115.75
REMARK 500    ALA A  19     -131.34     26.15
REMARK 500    ASP A 127      159.54    173.54
REMARK 500    ASP A 139       35.47    -98.41
REMARK 500    LYS A 168     -147.08   -100.53
REMARK 500    SER A 216      -64.15     68.39
REMARK 500    ASP A 256       83.65   -153.23
REMARK 500    ASP A 347      111.86    -38.96
REMARK 500    ASN A 384     -162.06   -163.94
REMARK 500    ASP A 388     -145.56     65.05
REMARK 500    MET A 394     -135.00     45.05
REMARK 500    ASP A 437       99.96     44.14
REMARK 500    ARG B   4     -162.76   -127.51
REMARK 500    ALA B  19     -126.04     34.11
REMARK 500    ASP B 127      156.68    174.95
REMARK 500    ASP B 139       32.85    -96.80
REMARK 500    LYS B 168     -147.98    -92.69
REMARK 500    SER B 216      -63.08     69.63
REMARK 500    VAL B 312      -55.70   -124.29
REMARK 500    ASN B 384     -159.75   -161.11
REMARK 500    ASP B 388     -145.17     61.92
REMARK 500    MET B 394     -135.15     61.72
REMARK 500    ASN B 500       12.92    -67.86
REMARK 500    ARG C   4     -166.27   -111.88
REMARK 500    ALA C  20       20.57     84.10
REMARK 500    ASP C 127      154.29    172.78
REMARK 500    ASP C 139       31.30    -99.63
REMARK 500    LYS C 168     -146.51   -100.78
REMARK 500    PRO C 189       -9.71    -59.22
REMARK 500    SER C 216      -62.02     72.10
REMARK 500    VAL C 312      -51.92   -127.17
REMARK 500    ASN C 384     -159.97   -158.76
REMARK 500    ASP C 388     -143.43     61.93
REMARK 500    MET C 394     -150.94     50.25
REMARK 500    ASP C 437       98.09     45.75
REMARK 500    ALA D  19     -141.28     60.25
REMARK 500    VAL D 115      -59.41   -120.67
REMARK 500    ASP D 127      156.77    178.27
REMARK 500    LYS D 168     -148.55   -102.61
REMARK 500    HIS D 210       44.49   -109.67
REMARK 500    SER D 216      -60.48     69.27
REMARK 500    ASP D 256       82.36   -151.74
REMARK 500    ASN D 272       59.88    -90.10
REMARK 500    ASP D 347      115.69    -37.37
REMARK 500    TYR D 378       -4.80    -59.91
REMARK 500    ASN D 384     -161.77   -160.32
REMARK 500    ASP D 388     -143.92     63.48
REMARK 500    MET D 394     -135.85     52.53
REMARK 500    HIS D 413     -119.02    -26.80
REMARK 500    GLN D 414       74.42    133.54
REMARK 500
REMARK 500 THIS ENTRY HAS      53 RAMACHANDRAN OUTLIERS.
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 A1350        DISTANCE =  6.09 ANGSTROMS
REMARK 525    HOH A1774        DISTANCE =  6.59 ANGSTROMS
REMARK 525    HOH A1922        DISTANCE =  5.08 ANGSTROMS
REMARK 525    HOH B1454        DISTANCE =  6.14 ANGSTROMS
REMARK 525    HOH B1797        DISTANCE =  5.12 ANGSTROMS
REMARK 525    HOH B1947        DISTANCE =  5.53 ANGSTROMS
REMARK 525    HOH B1979        DISTANCE =  5.81 ANGSTROMS
REMARK 525    HOH C1349        DISTANCE =  5.60 ANGSTROMS
REMARK 525    HOH C1468        DISTANCE =  6.65 ANGSTROMS
REMARK 525    HOH C1539        DISTANCE =  5.89 ANGSTROMS
REMARK 525    HOH C1589        DISTANCE =  6.65 ANGSTROMS
REMARK 525    HOH C1671        DISTANCE =  5.13 ANGSTROMS
REMARK 525    HOH C1839        DISTANCE =  5.48 ANGSTROMS
REMARK 525    HOH C1967        DISTANCE =  5.24 ANGSTROMS
REMARK 525    HOH D1088        DISTANCE =  5.02 ANGSTROMS
REMARK 525    HOH D1455        DISTANCE =  5.72 ANGSTROMS
REMARK 525    HOH D1723        DISTANCE =  6.79 ANGSTROMS
REMARK 525    HOH D1971        DISTANCE =  5.30 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                             HEM C   1  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR C 357   OH
REMARK 620 2 HEM C   1   NA   91.5
REMARK 620 3 HEM C   1   NB   90.9  89.8
REMARK 620 4 HEM C   1   NC   89.8 178.5  89.5
REMARK 620 5 HEM C   1   ND   87.5  91.1 178.2  89.5
REMARK 620 6  NO C 502   N   169.9  98.5  90.6  80.2  90.8
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM D   1  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR D 357   OH
REMARK 620 2 HEM D   1   NA   94.2
REMARK 620 3 HEM D   1   NB   89.0  90.1
REMARK 620 4 HEM D   1   NC   89.2 176.6  89.9
REMARK 620 5 HEM D   1   ND   89.6  90.1 178.6  89.9
REMARK 620 6  NO D 502   N   170.1  93.8  96.7  82.8  84.7
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM B   1  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 357   OH
REMARK 620 2 HEM B   1   NA   94.1
REMARK 620 3 HEM B   1   NB   87.4  91.1
REMARK 620 4 HEM B   1   NC   85.8 178.6  90.4
REMARK 620 5 HEM B   1   ND   88.9  90.0 176.2  88.5
REMARK 620 6  NO B 502   N   166.4  99.1  95.3  80.9  88.2
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM A   1  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 357   OH
REMARK 620 2 HEM A   1   NA   94.3
REMARK 620 3 HEM A   1   NB   86.2  91.7
REMARK 620 4 HEM A   1   NC   88.0 177.0  90.4
REMARK 620 5 HEM A   1   ND   91.1  89.2 177.2  88.8
REMARK 620 6  NO A 502   N   169.4  96.2  95.3  81.5  87.2
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 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO D 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3RE8   RELATED DB: PDB
REMARK 900 RELATED ID: 3RGS   RELATED DB: PDB
DBREF  3RGP A    3   501  UNP    P00432   CATA_BOVIN       4    502
DBREF  3RGP B    3   501  UNP    P00432   CATA_BOVIN       4    502
DBREF  3RGP C    3   501  UNP    P00432   CATA_BOVIN       4    502
DBREF  3RGP D    3   501  UNP    P00432   CATA_BOVIN       4    502
SEQRES   1 A  499  ASN ARG ASP PRO ALA SER ASP GLN MET LYS HIS TRP LYS
SEQRES   2 A  499  GLU GLN ARG ALA ALA GLN LYS PRO ASP VAL LEU THR THR
SEQRES   3 A  499  GLY GLY GLY ASN PRO VAL GLY ASP LYS LEU ASN SER LEU
SEQRES   4 A  499  THR VAL GLY PRO ARG GLY PRO LEU LEU VAL GLN ASP VAL
SEQRES   5 A  499  VAL PHE THR ASP GLU MET ALA HIS PHE ASP ARG GLU ARG
SEQRES   6 A  499  ILE PRO GLU ARG VAL VAL HIS ALA LYS GLY ALA GLY ALA
SEQRES   7 A  499  PHE GLY TYR PHE GLU VAL THR HIS ASP ILE THR ARG TYR
SEQRES   8 A  499  SER LYS ALA LYS VAL PHE GLU HIS ILE GLY LYS ARG THR
SEQRES   9 A  499  PRO ILE ALA VAL ARG PHE SER THR VAL ALA GLY GLU SER
SEQRES  10 A  499  GLY SER ALA ASP THR VAL ARG ASP PRO ARG GLY PHE ALA
SEQRES  11 A  499  VAL LYS PHE TYR THR GLU ASP GLY ASN TRP ASP LEU VAL
SEQRES  12 A  499  GLY ASN ASN THR PRO ILE PHE PHE ILE ARG ASP ALA LEU
SEQRES  13 A  499  LEU PHE PRO SER PHE ILE HIS SER GLN LYS ARG ASN PRO
SEQRES  14 A  499  GLN THR HIS LEU LYS ASP PRO ASP MET VAL TRP ASP PHE
SEQRES  15 A  499  TRP SER LEU ARG PRO GLU SER LEU HIS GLN VAL SER PHE
SEQRES  16 A  499  LEU PHE SER ASP ARG GLY ILE PRO ASP GLY HIS ARG HIS
SEQRES  17 A  499  MET ASN GLY TYR GLY SER HIS THR PHE LYS LEU VAL ASN
SEQRES  18 A  499  ALA ASN GLY GLU ALA VAL TYR CYS LYS PHE HIS TYR LYS
SEQRES  19 A  499  THR ASP GLN GLY ILE LYS ASN LEU SER VAL GLU ASP ALA
SEQRES  20 A  499  ALA ARG LEU ALA HIS GLU ASP PRO ASP TYR GLY LEU ARG
SEQRES  21 A  499  ASP LEU PHE ASN ALA ILE ALA THR GLY ASN TYR PRO SER
SEQRES  22 A  499  TRP THR LEU TYR ILE GLN VAL MET THR PHE SER GLU ALA
SEQRES  23 A  499  GLU ILE PHE PRO PHE ASN PRO PHE ASP LEU THR LYS VAL
SEQRES  24 A  499  TRP PRO HIS GLY ASP TYR PRO LEU ILE PRO VAL GLY LYS
SEQRES  25 A  499  LEU VAL LEU ASN ARG ASN PRO VAL ASN TYR PHE ALA GLU
SEQRES  26 A  499  VAL GLU GLN LEU ALA PHE ASP PRO SER ASN MET PRO PRO
SEQRES  27 A  499  GLY ILE GLU PRO SER PRO ASP LYS MET LEU GLN GLY ARG
SEQRES  28 A  499  LEU PHE ALA TYR PRO ASP THR HIS ARG HIS ARG LEU GLY
SEQRES  29 A  499  PRO ASN TYR LEU GLN ILE PRO VAL ASN CYS PRO TYR ARG
SEQRES  30 A  499  ALA ARG VAL ALA ASN TYR GLN ARG ASP GLY PRO MET CYS
SEQRES  31 A  499  MET MET ASP ASN GLN GLY GLY ALA PRO ASN TYR TYR PRO
SEQRES  32 A  499  ASN SER PHE SER ALA PRO GLU HIS GLN PRO SER ALA LEU
SEQRES  33 A  499  GLU HIS ARG THR HIS PHE SER GLY ASP VAL GLN ARG PHE
SEQRES  34 A  499  ASN SER ALA ASN ASP ASP ASN VAL THR GLN VAL ARG THR
SEQRES  35 A  499  PHE TYR LEU LYS VAL LEU ASN GLU GLU GLN ARG LYS ARG
SEQRES  36 A  499  LEU CYS GLU ASN ILE ALA GLY HIS LEU LYS ASP ALA GLN
SEQRES  37 A  499  LEU PHE ILE GLN LYS LYS ALA VAL LYS ASN PHE SER ASP
SEQRES  38 A  499  VAL HIS PRO GLU TYR GLY SER ARG ILE GLN ALA LEU LEU
SEQRES  39 A  499  ASP LYS TYR ASN GLU
SEQRES   1 B  499  ASN ARG ASP PRO ALA SER ASP GLN MET LYS HIS TRP LYS
SEQRES   2 B  499  GLU GLN ARG ALA ALA GLN LYS PRO ASP VAL LEU THR THR
SEQRES   3 B  499  GLY GLY GLY ASN PRO VAL GLY ASP LYS LEU ASN SER LEU
SEQRES   4 B  499  THR VAL GLY PRO ARG GLY PRO LEU LEU VAL GLN ASP VAL
SEQRES   5 B  499  VAL PHE THR ASP GLU MET ALA HIS PHE ASP ARG GLU ARG
SEQRES   6 B  499  ILE PRO GLU ARG VAL VAL HIS ALA LYS GLY ALA GLY ALA
SEQRES   7 B  499  PHE GLY TYR PHE GLU VAL THR HIS ASP ILE THR ARG TYR
SEQRES   8 B  499  SER LYS ALA LYS VAL PHE GLU HIS ILE GLY LYS ARG THR
SEQRES   9 B  499  PRO ILE ALA VAL ARG PHE SER THR VAL ALA GLY GLU SER
SEQRES  10 B  499  GLY SER ALA ASP THR VAL ARG ASP PRO ARG GLY PHE ALA
SEQRES  11 B  499  VAL LYS PHE TYR THR GLU ASP GLY ASN TRP ASP LEU VAL
SEQRES  12 B  499  GLY ASN ASN THR PRO ILE PHE PHE ILE ARG ASP ALA LEU
SEQRES  13 B  499  LEU PHE PRO SER PHE ILE HIS SER GLN LYS ARG ASN PRO
SEQRES  14 B  499  GLN THR HIS LEU LYS ASP PRO ASP MET VAL TRP ASP PHE
SEQRES  15 B  499  TRP SER LEU ARG PRO GLU SER LEU HIS GLN VAL SER PHE
SEQRES  16 B  499  LEU PHE SER ASP ARG GLY ILE PRO ASP GLY HIS ARG HIS
SEQRES  17 B  499  MET ASN GLY TYR GLY SER HIS THR PHE LYS LEU VAL ASN
SEQRES  18 B  499  ALA ASN GLY GLU ALA VAL TYR CYS LYS PHE HIS TYR LYS
SEQRES  19 B  499  THR ASP GLN GLY ILE LYS ASN LEU SER VAL GLU ASP ALA
SEQRES  20 B  499  ALA ARG LEU ALA HIS GLU ASP PRO ASP TYR GLY LEU ARG
SEQRES  21 B  499  ASP LEU PHE ASN ALA ILE ALA THR GLY ASN TYR PRO SER
SEQRES  22 B  499  TRP THR LEU TYR ILE GLN VAL MET THR PHE SER GLU ALA
SEQRES  23 B  499  GLU ILE PHE PRO PHE ASN PRO PHE ASP LEU THR LYS VAL
SEQRES  24 B  499  TRP PRO HIS GLY ASP TYR PRO LEU ILE PRO VAL GLY LYS
SEQRES  25 B  499  LEU VAL LEU ASN ARG ASN PRO VAL ASN TYR PHE ALA GLU
SEQRES  26 B  499  VAL GLU GLN LEU ALA PHE ASP PRO SER ASN MET PRO PRO
SEQRES  27 B  499  GLY ILE GLU PRO SER PRO ASP LYS MET LEU GLN GLY ARG
SEQRES  28 B  499  LEU PHE ALA TYR PRO ASP THR HIS ARG HIS ARG LEU GLY
SEQRES  29 B  499  PRO ASN TYR LEU GLN ILE PRO VAL ASN CYS PRO TYR ARG
SEQRES  30 B  499  ALA ARG VAL ALA ASN TYR GLN ARG ASP GLY PRO MET CYS
SEQRES  31 B  499  MET MET ASP ASN GLN GLY GLY ALA PRO ASN TYR TYR PRO
SEQRES  32 B  499  ASN SER PHE SER ALA PRO GLU HIS GLN PRO SER ALA LEU
SEQRES  33 B  499  GLU HIS ARG THR HIS PHE SER GLY ASP VAL GLN ARG PHE
SEQRES  34 B  499  ASN SER ALA ASN ASP ASP ASN VAL THR GLN VAL ARG THR
SEQRES  35 B  499  PHE TYR LEU LYS VAL LEU ASN GLU GLU GLN ARG LYS ARG
SEQRES  36 B  499  LEU CYS GLU ASN ILE ALA GLY HIS LEU LYS ASP ALA GLN
SEQRES  37 B  499  LEU PHE ILE GLN LYS LYS ALA VAL LYS ASN PHE SER ASP
SEQRES  38 B  499  VAL HIS PRO GLU TYR GLY SER ARG ILE GLN ALA LEU LEU
SEQRES  39 B  499  ASP LYS TYR ASN GLU
SEQRES   1 C  499  ASN ARG ASP PRO ALA SER ASP GLN MET LYS HIS TRP LYS
SEQRES   2 C  499  GLU GLN ARG ALA ALA GLN LYS PRO ASP VAL LEU THR THR
SEQRES   3 C  499  GLY GLY GLY ASN PRO VAL GLY ASP LYS LEU ASN SER LEU
SEQRES   4 C  499  THR VAL GLY PRO ARG GLY PRO LEU LEU VAL GLN ASP VAL
SEQRES   5 C  499  VAL PHE THR ASP GLU MET ALA HIS PHE ASP ARG GLU ARG
SEQRES   6 C  499  ILE PRO GLU ARG VAL VAL HIS ALA LYS GLY ALA GLY ALA
SEQRES   7 C  499  PHE GLY TYR PHE GLU VAL THR HIS ASP ILE THR ARG TYR
SEQRES   8 C  499  SER LYS ALA LYS VAL PHE GLU HIS ILE GLY LYS ARG THR
SEQRES   9 C  499  PRO ILE ALA VAL ARG PHE SER THR VAL ALA GLY GLU SER
SEQRES  10 C  499  GLY SER ALA ASP THR VAL ARG ASP PRO ARG GLY PHE ALA
SEQRES  11 C  499  VAL LYS PHE TYR THR GLU ASP GLY ASN TRP ASP LEU VAL
SEQRES  12 C  499  GLY ASN ASN THR PRO ILE PHE PHE ILE ARG ASP ALA LEU
SEQRES  13 C  499  LEU PHE PRO SER PHE ILE HIS SER GLN LYS ARG ASN PRO
SEQRES  14 C  499  GLN THR HIS LEU LYS ASP PRO ASP MET VAL TRP ASP PHE
SEQRES  15 C  499  TRP SER LEU ARG PRO GLU SER LEU HIS GLN VAL SER PHE
SEQRES  16 C  499  LEU PHE SER ASP ARG GLY ILE PRO ASP GLY HIS ARG HIS
SEQRES  17 C  499  MET ASN GLY TYR GLY SER HIS THR PHE LYS LEU VAL ASN
SEQRES  18 C  499  ALA ASN GLY GLU ALA VAL TYR CYS LYS PHE HIS TYR LYS
SEQRES  19 C  499  THR ASP GLN GLY ILE LYS ASN LEU SER VAL GLU ASP ALA
SEQRES  20 C  499  ALA ARG LEU ALA HIS GLU ASP PRO ASP TYR GLY LEU ARG
SEQRES  21 C  499  ASP LEU PHE ASN ALA ILE ALA THR GLY ASN TYR PRO SER
SEQRES  22 C  499  TRP THR LEU TYR ILE GLN VAL MET THR PHE SER GLU ALA
SEQRES  23 C  499  GLU ILE PHE PRO PHE ASN PRO PHE ASP LEU THR LYS VAL
SEQRES  24 C  499  TRP PRO HIS GLY ASP TYR PRO LEU ILE PRO VAL GLY LYS
SEQRES  25 C  499  LEU VAL LEU ASN ARG ASN PRO VAL ASN TYR PHE ALA GLU
SEQRES  26 C  499  VAL GLU GLN LEU ALA PHE ASP PRO SER ASN MET PRO PRO
SEQRES  27 C  499  GLY ILE GLU PRO SER PRO ASP LYS MET LEU GLN GLY ARG
SEQRES  28 C  499  LEU PHE ALA TYR PRO ASP THR HIS ARG HIS ARG LEU GLY
SEQRES  29 C  499  PRO ASN TYR LEU GLN ILE PRO VAL ASN CYS PRO TYR ARG
SEQRES  30 C  499  ALA ARG VAL ALA ASN TYR GLN ARG ASP GLY PRO MET CYS
SEQRES  31 C  499  MET MET ASP ASN GLN GLY GLY ALA PRO ASN TYR TYR PRO
SEQRES  32 C  499  ASN SER PHE SER ALA PRO GLU HIS GLN PRO SER ALA LEU
SEQRES  33 C  499  GLU HIS ARG THR HIS PHE SER GLY ASP VAL GLN ARG PHE
SEQRES  34 C  499  ASN SER ALA ASN ASP ASP ASN VAL THR GLN VAL ARG THR
SEQRES  35 C  499  PHE TYR LEU LYS VAL LEU ASN GLU GLU GLN ARG LYS ARG
SEQRES  36 C  499  LEU CYS GLU ASN ILE ALA GLY HIS LEU LYS ASP ALA GLN
SEQRES  37 C  499  LEU PHE ILE GLN LYS LYS ALA VAL LYS ASN PHE SER ASP
SEQRES  38 C  499  VAL HIS PRO GLU TYR GLY SER ARG ILE GLN ALA LEU LEU
SEQRES  39 C  499  ASP LYS TYR ASN GLU
SEQRES   1 D  499  ASN ARG ASP PRO ALA SER ASP GLN MET LYS HIS TRP LYS
SEQRES   2 D  499  GLU GLN ARG ALA ALA GLN LYS PRO ASP VAL LEU THR THR
SEQRES   3 D  499  GLY GLY GLY ASN PRO VAL GLY ASP LYS LEU ASN SER LEU
SEQRES   4 D  499  THR VAL GLY PRO ARG GLY PRO LEU LEU VAL GLN ASP VAL
SEQRES   5 D  499  VAL PHE THR ASP GLU MET ALA HIS PHE ASP ARG GLU ARG
SEQRES   6 D  499  ILE PRO GLU ARG VAL VAL HIS ALA LYS GLY ALA GLY ALA
SEQRES   7 D  499  PHE GLY TYR PHE GLU VAL THR HIS ASP ILE THR ARG TYR
SEQRES   8 D  499  SER LYS ALA LYS VAL PHE GLU HIS ILE GLY LYS ARG THR
SEQRES   9 D  499  PRO ILE ALA VAL ARG PHE SER THR VAL ALA GLY GLU SER
SEQRES  10 D  499  GLY SER ALA ASP THR VAL ARG ASP PRO ARG GLY PHE ALA
SEQRES  11 D  499  VAL LYS PHE TYR THR GLU ASP GLY ASN TRP ASP LEU VAL
SEQRES  12 D  499  GLY ASN ASN THR PRO ILE PHE PHE ILE ARG ASP ALA LEU
SEQRES  13 D  499  LEU PHE PRO SER PHE ILE HIS SER GLN LYS ARG ASN PRO
SEQRES  14 D  499  GLN THR HIS LEU LYS ASP PRO ASP MET VAL TRP ASP PHE
SEQRES  15 D  499  TRP SER LEU ARG PRO GLU SER LEU HIS GLN VAL SER PHE
SEQRES  16 D  499  LEU PHE SER ASP ARG GLY ILE PRO ASP GLY HIS ARG HIS
SEQRES  17 D  499  MET ASN GLY TYR GLY SER HIS THR PHE LYS LEU VAL ASN
SEQRES  18 D  499  ALA ASN GLY GLU ALA VAL TYR CYS LYS PHE HIS TYR LYS
SEQRES  19 D  499  THR ASP GLN GLY ILE LYS ASN LEU SER VAL GLU ASP ALA
SEQRES  20 D  499  ALA ARG LEU ALA HIS GLU ASP PRO ASP TYR GLY LEU ARG
SEQRES  21 D  499  ASP LEU PHE ASN ALA ILE ALA THR GLY ASN TYR PRO SER
SEQRES  22 D  499  TRP THR LEU TYR ILE GLN VAL MET THR PHE SER GLU ALA
SEQRES  23 D  499  GLU ILE PHE PRO PHE ASN PRO PHE ASP LEU THR LYS VAL
SEQRES  24 D  499  TRP PRO HIS GLY ASP TYR PRO LEU ILE PRO VAL GLY LYS
SEQRES  25 D  499  LEU VAL LEU ASN ARG ASN PRO VAL ASN TYR PHE ALA GLU
SEQRES  26 D  499  VAL GLU GLN LEU ALA PHE ASP PRO SER ASN MET PRO PRO
SEQRES  27 D  499  GLY ILE GLU PRO SER PRO ASP LYS MET LEU GLN GLY ARG
SEQRES  28 D  499  LEU PHE ALA TYR PRO ASP THR HIS ARG HIS ARG LEU GLY
SEQRES  29 D  499  PRO ASN TYR LEU GLN ILE PRO VAL ASN CYS PRO TYR ARG
SEQRES  30 D  499  ALA ARG VAL ALA ASN TYR GLN ARG ASP GLY PRO MET CYS
SEQRES  31 D  499  MET MET ASP ASN GLN GLY GLY ALA PRO ASN TYR TYR PRO
SEQRES  32 D  499  ASN SER PHE SER ALA PRO GLU HIS GLN PRO SER ALA LEU
SEQRES  33 D  499  GLU HIS ARG THR HIS PHE SER GLY ASP VAL GLN ARG PHE
SEQRES  34 D  499  ASN SER ALA ASN ASP ASP ASN VAL THR GLN VAL ARG THR
SEQRES  35 D  499  PHE TYR LEU LYS VAL LEU ASN GLU GLU GLN ARG LYS ARG
SEQRES  36 D  499  LEU CYS GLU ASN ILE ALA GLY HIS LEU LYS ASP ALA GLN
SEQRES  37 D  499  LEU PHE ILE GLN LYS LYS ALA VAL LYS ASN PHE SER ASP
SEQRES  38 D  499  VAL HIS PRO GLU TYR GLY SER ARG ILE GLN ALA LEU LEU
SEQRES  39 D  499  ASP LYS TYR ASN GLU
HET    HEM  A   1      43
HET     NO  A 502       2
HET    HEM  B   1      43
HET     NO  B 502       2
HET    HEM  C   1      43
HET     NO  C 502       2
HET    HEM  D   1      43
HET     NO  D 502       2
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM      NO NITRIC OXIDE
HETSYN     HEM HEME
HETSYN      NO NITROGEN MONOXIDE
FORMUL   5  HEM    4(C34 H32 FE N4 O4)
FORMUL   6   NO    4(N O)
FORMUL  13  HOH   *2020(H2 O)
HELIX    1   1 ASP A    9  ARG A   18  1                                  10
HELIX    2   2 ASP A   53  ASP A   64  1                                  12
HELIX    3   3 ALA A   96  GLU A  100  5                                   5
HELIX    4   4 ASP A  156  LEU A  158  5                                   3
HELIX    5   5 LEU A  159  LYS A  168  1                                  10
HELIX    6   6 ASP A  177  ARG A  188  1                                  12
HELIX    7   7 SER A  191  PHE A  199  1                                   9
HELIX    8   8 SER A  200  ILE A  204  5                                   5
HELIX    9   9 SER A  245  ASP A  256  1                                  12
HELIX   10  10 ASP A  258  THR A  270  1                                  13
HELIX   11  11 THR A  284  PHE A  291  1                                   8
HELIX   12  12 ASN A  323  VAL A  328  1                                   6
HELIX   13  13 ASP A  347  LEU A  365  1                                  19
HELIX   14  14 ASN A  368  CYS A  376  5                                   9
HELIX   15  15 GLN A  414  LEU A  418  5                                   5
HELIX   16  16 VAL A  439  LYS A  448  1                                  10
HELIX   17  17 ASN A  451  LYS A  467  1                                  17
HELIX   18  18 GLN A  470  HIS A  485  1                                  16
HELIX   19  19 HIS A  485  ASN A  500  1                                  16
HELIX   20  20 ASP B    9  GLN B   17  1                                   9
HELIX   21  21 ASP B   53  ASP B   64  1                                  12
HELIX   22  22 ALA B   96  GLU B  100  5                                   5
HELIX   23  23 ASP B  156  LEU B  158  5                                   3
HELIX   24  24 LEU B  159  LYS B  168  1                                  10
HELIX   25  25 ASP B  177  ARG B  188  1                                  12
HELIX   26  26 SER B  191  PHE B  199  1                                   9
HELIX   27  27 SER B  200  ILE B  204  5                                   5
HELIX   28  28 SER B  245  ASP B  256  1                                  12
HELIX   29  29 ASP B  258  THR B  270  1                                  13
HELIX   30  30 THR B  284  PHE B  291  1                                   8
HELIX   31  31 ASN B  323  VAL B  328  1                                   6
HELIX   32  32 ASP B  347  LEU B  365  1                                  19
HELIX   33  33 ASN B  368  CYS B  376  5                                   9
HELIX   34  34 GLN B  414  LEU B  418  5                                   5
HELIX   35  35 VAL B  439  LYS B  448  1                                  10
HELIX   36  36 ASN B  451  LYS B  467  1                                  17
HELIX   37  37 GLN B  470  HIS B  485  1                                  16
HELIX   38  38 HIS B  485  ASN B  500  1                                  16
HELIX   39  39 ASP C    9  GLN C   17  1                                   9
HELIX   40  40 ASP C   53  ASP C   64  1                                  12
HELIX   41  41 ALA C   96  GLU C  100  5                                   5
HELIX   42  42 ASP C  156  LEU C  158  5                                   3
HELIX   43  43 LEU C  159  LYS C  168  1                                  10
HELIX   44  44 ASP C  177  ARG C  188  1                                  12
HELIX   45  45 SER C  191  PHE C  199  1                                   9
HELIX   46  46 SER C  200  ILE C  204  5                                   5
HELIX   47  47 SER C  245  ASP C  256  1                                  12
HELIX   48  48 ASP C  258  THR C  270  1                                  13
HELIX   49  49 THR C  284  PHE C  291  1                                   8
HELIX   50  50 ASN C  323  VAL C  328  1                                   6
HELIX   51  51 ASP C  347  LEU C  365  1                                  19
HELIX   52  52 ASN C  368  CYS C  376  5                                   9
HELIX   53  53 GLN C  414  LEU C  418  5                                   5
HELIX   54  54 VAL C  439  LYS C  448  1                                  10
HELIX   55  55 ASN C  451  LYS C  467  1                                  17
HELIX   56  56 GLN C  470  HIS C  485  1                                  16
HELIX   57  57 HIS C  485  ASN C  500  1                                  16
HELIX   58  58 ASP D    9  ARG D   18  1                                  10
HELIX   59  59 ASP D   53  ASP D   64  1                                  12
HELIX   60  60 ALA D   96  GLU D  100  5                                   5
HELIX   61  61 ASP D  156  LEU D  158  5                                   3
HELIX   62  62 LEU D  159  LYS D  168  1                                  10
HELIX   63  63 ASP D  177  ARG D  188  1                                  12
HELIX   64  64 SER D  191  PHE D  199  1                                   9
HELIX   65  65 SER D  200  ILE D  204  5                                   5
HELIX   66  66 SER D  245  ASP D  256  1                                  12
HELIX   67  67 ASP D  258  THR D  270  1                                  13
HELIX   68  68 THR D  284  GLU D  289  1                                   6
HELIX   69  69 ASN D  323  VAL D  328  1                                   6
HELIX   70  70 ASP D  347  LEU D  365  1                                  19
HELIX   71  71 ASN D  368  CYS D  376  5                                   9
HELIX   72  72 GLN D  414  LEU D  418  5                                   5
HELIX   73  73 VAL D  439  LYS D  448  1                                  10
HELIX   74  74 ASN D  451  LYS D  467  1                                  17
HELIX   75  75 GLN D  470  HIS D  485  1                                  16
HELIX   76  76 HIS D  485  ASN D  500  1                                  16
SHEET    1   A 3 LEU A  41  VAL A  43  0
SHEET    2   A 3 GLY D 426  ARG D 430 -1  O  GLN D 429   N  THR A  42
SHEET    3   A 3 THR C 422  PHE C 424 -1  N  THR C 422   O  VAL D 428
SHEET    1   B11 ILE A 342  PRO A 344  0
SHEET    2   B11 PHE A 219  VAL A 222 -1  N  LYS A 220   O  GLU A 343
SHEET    3   B11 ALA A 228  THR A 237 -1  O  VAL A 229   N  LEU A 221
SHEET    4   B11 SER A 275  MET A 283 -1  O  TYR A 279   N  HIS A 234
SHEET    5   B11 ILE A 310  ARG A 319 -1  O  LEU A 315   N  TRP A 276
SHEET    6   B11 GLY A  77  VAL A  86 -1  N  PHE A  81   O  ARG A 319
SHEET    7   B11 ARG A 105  SER A 113 -1  O  PHE A 112   N  ALA A  78
SHEET    8   B11 GLY A 130  THR A 137 -1  O  LYS A 134   N  ALA A 109
SHEET    9   B11 GLY A 140  ASN A 147 -1  O  TRP A 142   N  PHE A 135
SHEET   10   B11 GLY A 213  TYR A 214 -1  O  TYR A 214   N  ASN A 147
SHEET   11   B11 ALA A 228  THR A 237 -1  O  TYR A 235   N  GLY A 213
SHEET    1   C 4 LEU C  41  VAL C  43  0
SHEET    2   C 4 HIS B 423  ARG B 430 -1  N  GLN B 429   O  THR C  42
SHEET    3   C 4 HIS A 423  GLN A 429 -1  N  PHE A 424   O  GLY B 426
SHEET    4   C 4 THR D  42  VAL D  43 -1  O  THR D  42   N  GLN A 429
SHEET    1   D 3 LEU B  41  VAL B  43  0
SHEET    2   D 3 ASP C 427  ARG C 430 -1  O  GLN C 429   N  THR B  42
SHEET    3   D 3 THR D 422  HIS D 423 -1  O  THR D 422   N  VAL C 428
SHEET    1   E11 ILE B 342  PRO B 344  0
SHEET    2   E11 PHE B 219  VAL B 222 -1  N  LYS B 220   O  GLU B 343
SHEET    3   E11 ALA B 228  THR B 237 -1  O  CYS B 231   N  PHE B 219
SHEET    4   E11 SER B 275  MET B 283 -1  O  TYR B 279   N  HIS B 234
SHEET    5   E11 ILE B 310  ARG B 319 -1  O  LEU B 315   N  TRP B 276
SHEET    6   E11 GLY B  77  VAL B  86 -1  N  PHE B  81   O  ARG B 319
SHEET    7   E11 ARG B 105  SER B 113 -1  O  PHE B 112   N  ALA B  78
SHEET    8   E11 GLY B 130  THR B 137 -1  O  LYS B 134   N  ALA B 109
SHEET    9   E11 GLY B 140  ASN B 147 -1  O  GLY B 146   N  PHE B 131
SHEET   10   E11 GLY B 213  TYR B 214 -1  O  TYR B 214   N  ASN B 147
SHEET   11   E11 ALA B 228  THR B 237 -1  O  TYR B 235   N  GLY B 213
SHEET    1   F11 ILE C 342  PRO C 344  0
SHEET    2   F11 PHE C 219  VAL C 222 -1  N  LYS C 220   O  GLU C 343
SHEET    3   F11 ALA C 228  THR C 237 -1  O  VAL C 229   N  LEU C 221
SHEET    4   F11 SER C 275  MET C 283 -1  O  TYR C 279   N  HIS C 234
SHEET    5   F11 ILE C 310  ARG C 319 -1  O  ILE C 310   N  ILE C 280
SHEET    6   F11 GLY C  77  VAL C  86 -1  N  PHE C  81   O  ARG C 319
SHEET    7   F11 ARG C 105  SER C 113 -1  O  PHE C 112   N  ALA C  78
SHEET    8   F11 GLY C 130  THR C 137 -1  O  LYS C 134   N  ALA C 109
SHEET    9   F11 GLY C 140  ASN C 147 -1  O  LEU C 144   N  VAL C 133
SHEET   10   F11 GLY C 213  TYR C 214 -1  O  TYR C 214   N  ASN C 147
SHEET   11   F11 ALA C 228  THR C 237 -1  O  TYR C 235   N  GLY C 213
SHEET    1   G11 ILE D 342  PRO D 344  0
SHEET    2   G11 PHE D 219  VAL D 222 -1  N  LYS D 220   O  GLU D 343
SHEET    3   G11 ALA D 228  THR D 237 -1  O  CYS D 231   N  PHE D 219
SHEET    4   G11 SER D 275  MET D 283 -1  O  TYR D 279   N  HIS D 234
SHEET    5   G11 ILE D 310  ARG D 319 -1  O  LEU D 315   N  TRP D 276
SHEET    6   G11 GLY D  77  VAL D  86 -1  N  PHE D  81   O  ARG D 319
SHEET    7   G11 ARG D 105  SER D 113 -1  O  PHE D 112   N  ALA D  78
SHEET    8   G11 GLY D 130  THR D 137 -1  O  LYS D 134   N  ALA D 109
SHEET    9   G11 GLY D 140  ASN D 147 -1  O  TRP D 142   N  PHE D 135
SHEET   10   G11 GLY D 213  TYR D 214 -1  O  TYR D 214   N  ASN D 147
SHEET   11   G11 ALA D 228  THR D 237 -1  O  TYR D 235   N  GLY D 213
LINK         OH  TYR C 357                FE   HEM C   1     1555   1555  1.95
LINK         OH  TYR D 357                FE   HEM D   1     1555   1555  1.97
LINK         OH  TYR B 357                FE   HEM B   1     1555   1555  1.99
LINK         OH  TYR A 357                FE   HEM A   1     1555   1555  2.01
LINK        FE   HEM C   1                 N    NO C 502     1555   1555  1.73
LINK        FE   HEM B   1                 N    NO B 502     1555   1555  1.74
LINK        FE   HEM D   1                 N    NO D 502     1555   1555  1.75
LINK        FE   HEM A   1                 N    NO A 502     1555   1555  1.80
CISPEP   1 TYR A  404    PRO A  405          0        -0.03
CISPEP   2 TYR B  404    PRO B  405          0         0.08
CISPEP   3 TYR C  404    PRO C  405          0         0.26
CISPEP   4 TYR D  404    PRO D  405          0        -0.02
SITE     1 AC1 27 ARG A  71  VAL A  72  VAL A  73  HIS A  74
SITE     2 AC1 27 ARG A 111  GLY A 130  VAL A 145  GLY A 146
SITE     3 AC1 27 ASN A 147  PHE A 152  ALA A 157  PHE A 160
SITE     4 AC1 27 GLY A 215  SER A 216  PHE A 333  MET A 349
SITE     5 AC1 27 ARG A 353  TYR A 357  THR A 360  HIS A 361
SITE     6 AC1 27 ARG A 364   NO A 502  HOH A 504  HOH A 523
SITE     7 AC1 27 HOH A 548  MET D  60  ASP D  64
SITE     1 AC2  4 HEM A   1  HIS A  74  PHE A 160  HOH A 864
SITE     1 AC3 29 ARG B  71  VAL B  72  VAL B  73  HIS B  74
SITE     2 AC3 29 ARG B 111  GLY B 130  VAL B 145  GLY B 146
SITE     3 AC3 29 ASN B 147  ALA B 157  PHE B 160  GLY B 215
SITE     4 AC3 29 SER B 216  LEU B 298  PHE B 333  MET B 349
SITE     5 AC3 29 ARG B 353  TYR B 357  THR B 360  HIS B 361
SITE     6 AC3 29 ARG B 364   NO B 502  HOH B 508  HOH B 533
SITE     7 AC3 29 HOH B 556  HOH B 977  HOH B1360  MET C  60
SITE     8 AC3 29 ASP C  64
SITE     1 AC4  5 HEM B   1  VAL B  73  HIS B  74  PHE B 160
SITE     2 AC4  5 HOH B 977
SITE     1 AC5 28 MET B  60  ASP B  64  ARG C  71  VAL C  72
SITE     2 AC5 28 VAL C  73  HIS C  74  ARG C 111  GLY C 130
SITE     3 AC5 28 VAL C 145  GLY C 146  ASN C 147  ALA C 157
SITE     4 AC5 28 PHE C 160  GLY C 215  SER C 216  LEU C 298
SITE     5 AC5 28 PHE C 333  MET C 349  ARG C 353  ALA C 356
SITE     6 AC5 28 TYR C 357  THR C 360  HIS C 361  ARG C 364
SITE     7 AC5 28  NO C 502  HOH C 519  HOH C 543  HOH C 574
SITE     1 AC6  5 HEM C   1  HIS C  74  PHE C 160  TYR C 357
SITE     2 AC6  5 HOH C1185
SITE     1 AC7 27 MET A  60  ASP A  64  ARG D  71  VAL D  72
SITE     2 AC7 27 VAL D  73  HIS D  74  ARG D 111  GLY D 130
SITE     3 AC7 27 VAL D 145  GLY D 146  ASN D 147  ALA D 157
SITE     4 AC7 27 PHE D 160  GLY D 215  SER D 216  PHE D 333
SITE     5 AC7 27 MET D 349  ARG D 353  ALA D 356  TYR D 357
SITE     6 AC7 27 THR D 360  HIS D 361  ARG D 364   NO D 502
SITE     7 AC7 27 HOH D 504  HOH D 529  HOH D 595
SITE     1 AC8  5 HEM D   1  HIS D  74  PHE D 160  TYR D 357
SITE     2 AC8  5 HOH D 727
CRYST1   86.110  139.940  228.020  90.00  90.00  90.00 P 21 21 21   16
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.011613  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007146  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004386        0.00000
      
PROCHECK
Go to PROCHECK summary
 References

 

spacer

spacer