HEADER OXIDOREDUCTASE 15-NOV-84 8CAT
TITLE THE NADPH BINDING SITE ON BEEF LIVER CATALASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATALASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.11.1.6;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS OXIDOREDUCTASE, H2O2 ACCEPTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR M.R.N.MURTHY,T.J.REID III,A.SICIGNANO,N.TANAKA,I.FITA,M.G.ROSSMANN
REVDAT 12 27-SEP-23 8CAT 1 REMARK SCALE MTRIX ATOM
REVDAT 11 01-NOV-17 8CAT 1 REMARK
REVDAT 10 21-NOV-12 8CAT 1 REMARK
REVDAT 9 05-OCT-11 8CAT 1 REMARK HEADER AUTHOR
REVDAT 8 13-JUL-11 8CAT 1 VERSN
REVDAT 7 24-FEB-09 8CAT 1 VERSN
REVDAT 6 16-APR-88 8CAT 1 AUTHOR
REVDAT 5 24-OCT-86 8CAT 1 REMARK
REVDAT 4 25-APR-86 8CAT 1 REMARK
REVDAT 3 29-OCT-85 8CAT 1 REMARK
REVDAT 2 12-JUL-85 8CAT 1 JRNL
REVDAT 1 01-APR-85 8CAT 0
SPRSDE 01-APR-85 8CAT 3CAT
JRNL AUTH I.FITA,M.G.ROSSMANN
JRNL TITL THE NADPH BINDING SITE ON BEEF LIVER CATALASE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 82 1604 1985
JRNL REFN ISSN 0027-8424
JRNL PMID 3856839
JRNL DOI 10.1073/PNAS.82.6.1604
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH I.FITA,A.M.SILVA,M.R.N.MURTHY,M.G.ROSSMANN
REMARK 1 TITL THE REFINED STRUCTURE OF BEEF LIVER CATALASE AT 2.5
REMARK 1 TITL 2 ANGSTROMS RESOLUTION
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.B V. 42 497 1986
REMARK 1 REFN ISSN 0108-7681
REMARK 1 REFERENCE 2
REMARK 1 AUTH W.R.MELIK-ADAMYAN,V.V.BARYNIN,A.A.VAGIN,V.V.BORISOV,
REMARK 1 AUTH 2 B.K.VAINSHTEIN,I.FITA,M.R.N.MURTHY,M.G.ROSSMANN
REMARK 1 TITL COMPARISON OF BEEF LIVER AND PENICILLIUM VITALE CATALASES
REMARK 1 REF J.MOL.BIOL. V. 188 63 1986
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 3
REMARK 1 AUTH I.FITA,M.G.ROSSMANN
REMARK 1 TITL THE ACTIVE CENTER OF CATALASE
REMARK 1 REF J.MOL.BIOL. V. 185 21 1985
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 4
REMARK 1 AUTH M.R.N.MURTHY,T.J.REID III,A.SICIGNANO,N.TANAKA,M.G.ROSSMANN
REMARK 1 TITL STRUCTURE OF BEEF LIVER CATALASE
REMARK 1 REF J.MOL.BIOL. V. 152 465 1981
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 5
REMARK 1 AUTH M.R.N.MURTHY,T.J.REID III,A.SICIGNANO,N.TANAKA,M.G.ROSSMANN
REMARK 1 TITL THE STRUCTURE OF BEEF LIVER CATALASE
REMARK 1 REF KRISTALLOGRAFIYA V. 26 1017 1981
REMARK 1 REFN ISSN 0023-4761
REMARK 1 REFERENCE 6
REMARK 1 AUTH M.R.N.MURTHY,T.J.REID III,A.SICIGNANO,N.TANAKA,M.G.ROSSMANN
REMARK 1 TITL THE STRUCTURE OF BEEF LIVER CATALASE
REMARK 1 REF SOV.PHYS.CRYSTALLOGR.(ENGL. V. 26 577 1981
REMARK 1 REF 2 TRANSL.)
REMARK 1 REFN ISSN 0038-5638
REMARK 1 REFERENCE 7
REMARK 1 AUTH T.J.REID III,M.R.N.MURTHY,A.SICIGNANO,N.TANAKA,W.D.L.MUSICK,
REMARK 1 AUTH 2 M.G.ROSSMANN
REMARK 1 TITL STRUCTURE AND HEME ENVIRONMENT OF BEEF LIVER CATALASE AT 2.5
REMARK 1 TITL 2 ANGSTROMS RESOLUTION
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 78 4767 1981
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 8
REMARK 1 AUTH W.EVENTOFF,N.TANAKA,M.G.ROSSMANN
REMARK 1 TITL CRYSTALLINE BOVINE LIVER CATALASE
REMARK 1 REF J.MOL.BIOL. V. 103 799 1976
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 9
REMARK 1 AUTH W.EVENTOFF,G.V.GURSKAYA
REMARK 1 TITL THE MOLECULAR SYMMETRY OF BOVINE LIVER CATALASE
REMARK 1 REF J.MOL.BIOL. V. 93 55 1975
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
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) : 0.191
REMARK 3 FREE R VALUE : NULL
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 : 8016
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 182
REMARK 3 SOLVENT ATOMS : 98
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) : 0.290
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 : NULL
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 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8CAT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000179964.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.13333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 34.56667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 34.56667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 69.13333
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 300 REMARK: TRANSLATION IS REQUIRED TO OBTAIN THE TETRAMER BECAUSE THE
REMARK 300 COORDINATES ARE NOT PRESENTED IN STANDARD FRAME.
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 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 350 BIOMT1 2 0.418202 0.818829 0.393083 -126.55513
REMARK 350 BIOMT2 2 0.818937 -0.527169 0.226985 140.74365
REMARK 350 BIOMT3 2 0.393142 0.226989 -0.891033 163.41545
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 ALA A 1
REMARK 465 ASP A 2
REMARK 465 GLU A 501
REMARK 465 GLU A 502
REMARK 465 LYS A 503
REMARK 465 PRO A 504
REMARK 465 LYS A 505
REMARK 465 ASN A 506
REMARK 465 ALA B 1
REMARK 465 ASP B 2
REMARK 465 GLU B 501
REMARK 465 GLU B 502
REMARK 465 LYS B 503
REMARK 465 PRO B 504
REMARK 465 LYS B 505
REMARK 465 ASN B 506
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 NH2 ARG A 155 ND2 ASN A 438 2.05
REMARK 500 O GLY A 77 OH TYR A 324 2.06
REMARK 500 O HIS B 74 NH2 ARG B 111 2.11
REMARK 500 OD1 ASP A 238 NZ LYS A 314 2.13
REMARK 500 NH2 ARG B 155 ND2 ASN B 438 2.13
REMARK 500 O PRO A 321 NE2 GLN B 172 2.17
REMARK 500 OH TYR A 385 O PRO A 411 2.18
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 OE2 GLU A 419 NH1 ARG B 430 6556 1.78
REMARK 500 NE2 GLN A 10 O HOH A 541 6556 1.86
REMARK 500 OD1 ASP A 183 OG SER B 407 6556 2.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 59 CD GLU A 59 OE1 0.068
REMARK 500 ARG A 67 CD ARG A 67 NE -0.116
REMARK 500 SER A 166 CB SER A 166 OG 0.084
REMARK 500 PRO A 171 CD PRO A 171 N 0.084
REMARK 500 GLU A 343 N GLU A 343 CA 0.130
REMARK 500 ARG A 364 NE ARG A 364 CZ 0.079
REMARK 500 GLU B 100 CD GLU B 100 OE2 -0.070
REMARK 500 SER B 119 CB SER B 119 OG -0.082
REMARK 500 ASN B 294 N ASN B 294 CA 0.122
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 4 CD - NE - CZ ANGL. DEV. = 8.6 DEGREES
REMARK 500 ARG A 4 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP A 9 CB - CG - OD1 ANGL. DEV. = 9.4 DEGREES
REMARK 500 GLN A 10 CB - CG - CD ANGL. DEV. = 18.3 DEGREES
REMARK 500 GLU A 16 OE1 - CD - OE2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 THR A 28 CA - C - N ANGL. DEV. = 13.5 DEGREES
REMARK 500 ARG A 46 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 LEU A 49 CA - CB - CG ANGL. DEV. = 15.1 DEGREES
REMARK 500 ASP A 53 CB - CG - OD2 ANGL. DEV. = -8.2 DEGREES
REMARK 500 ARG A 65 CD - NE - CZ ANGL. DEV. = 16.3 DEGREES
REMARK 500 ARG A 65 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 67 CA - CB - CG ANGL. DEV. = 17.0 DEGREES
REMARK 500 ARG A 67 CG - CD - NE ANGL. DEV. = 15.4 DEGREES
REMARK 500 ARG A 67 CD - NE - CZ ANGL. DEV. = 36.2 DEGREES
REMARK 500 ARG A 71 CD - NE - CZ ANGL. DEV. = 8.5 DEGREES
REMARK 500 ARG A 71 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ALA A 80 CB - CA - C ANGL. DEV. = 11.0 DEGREES
REMARK 500 ASP A 89 CB - CG - OD1 ANGL. DEV. = -8.5 DEGREES
REMARK 500 ARG A 92 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 TYR A 93 CB - CG - CD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 TYR A 93 CB - CG - CD1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG A 111 N - CA - CB ANGL. DEV. = 11.9 DEGREES
REMARK 500 ARG A 111 NE - CZ - NH1 ANGL. DEV. = 8.4 DEGREES
REMARK 500 ARG A 111 NE - CZ - NH2 ANGL. DEV. = -10.1 DEGREES
REMARK 500 ALA A 122 CB - CA - C ANGL. DEV. = 10.2 DEGREES
REMARK 500 ASP A 123 CB - CG - OD1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG A 126 CA - CB - CG ANGL. DEV. = 13.3 DEGREES
REMARK 500 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 LYS A 134 CD - CE - NZ ANGL. DEV. = -14.9 DEGREES
REMARK 500 ASP A 143 CB - CG - OD2 ANGL. DEV. = -9.0 DEGREES
REMARK 500 ASP A 143 O - C - N ANGL. DEV. = 9.9 DEGREES
REMARK 500 ARG A 155 CD - NE - CZ ANGL. DEV. = -13.1 DEGREES
REMARK 500 ARG A 155 NE - CZ - NH1 ANGL. DEV. = -7.9 DEGREES
REMARK 500 ARG A 155 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 LEU A 159 CA - CB - CG ANGL. DEV. = 17.9 DEGREES
REMARK 500 ARG A 169 NE - CZ - NH1 ANGL. DEV. = 8.7 DEGREES
REMARK 500 ARG A 169 NE - CZ - NH2 ANGL. DEV. = -9.8 DEGREES
REMARK 500 GLN A 172 CA - CB - CG ANGL. DEV. = -13.7 DEGREES
REMARK 500 ASP A 177 N - CA - CB ANGL. DEV. = -10.8 DEGREES
REMARK 500 ASP A 179 CA - CB - CG ANGL. DEV. = 17.4 DEGREES
REMARK 500 ASP A 179 CB - CG - OD2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ARG A 188 CD - NE - CZ ANGL. DEV. = -9.8 DEGREES
REMARK 500 ARG A 188 NE - CZ - NH1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG A 188 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP A 201 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ARG A 209 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 LEU A 221 O - C - N ANGL. DEV. = 11.1 DEGREES
REMARK 500 ASP A 238 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 GLU A 247 CG - CD - OE1 ANGL. DEV. = 12.9 DEGREES
REMARK 500 ASP A 248 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 248 ANGLE DEVIATIONS.
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 GLN A 21 -150.08 -80.26
REMARK 500 LYS A 22 94.62 81.67
REMARK 500 PRO A 23 157.27 -49.52
REMARK 500 VAL A 54 12.29 -57.64
REMARK 500 ASP A 64 -9.89 -49.70
REMARK 500 HIS A 74 21.14 81.35
REMARK 500 THR A 87 -14.13 -141.93
REMARK 500 THR A 91 -7.92 -58.86
REMARK 500 VAL A 98 -35.68 -38.04
REMARK 500 GLU A 100 -2.40 -55.65
REMARK 500 HIS A 101 113.90 170.66
REMARK 500 ILE A 102 131.64 -34.56
REMARK 500 SER A 121 -179.23 -63.77
REMARK 500 ASP A 127 150.81 175.75
REMARK 500 PRO A 128 -179.23 -52.76
REMARK 500 PHE A 131 80.72 -158.94
REMARK 500 LYS A 168 -142.84 -93.30
REMARK 500 PHE A 184 -70.98 -37.96
REMARK 500 SER A 216 -60.97 74.00
REMARK 500 LYS A 242 117.31 154.92
REMARK 500 SER A 245 160.96 -46.00
REMARK 500 ASP A 256 74.46 -150.60
REMARK 500 ALA A 267 -105.19 -20.59
REMARK 500 ILE A 268 -42.02 -24.80
REMARK 500 TYR A 273 109.27 -56.04
REMARK 500 PRO A 292 -1.57 -56.17
REMARK 500 PRO A 308 152.74 -47.00
REMARK 500 ASN A 318 20.19 -141.10
REMARK 500 PRO A 340 113.66 -25.93
REMARK 500 GLU A 343 143.10 178.17
REMARK 500 ASP A 347 114.38 -37.75
REMARK 500 PHE A 355 -60.75 -90.54
REMARK 500 HIS A 363 -68.45 -97.86
REMARK 500 PRO A 373 -77.18 1.69
REMARK 500 ASN A 384 -157.02 -154.40
REMARK 500 ASP A 388 -142.28 61.82
REMARK 500 MET A 394 -162.05 -79.95
REMARK 500 PRO A 401 128.68 -33.30
REMARK 500 SER A 407 31.97 -91.54
REMARK 500 PHE A 408 25.84 -141.36
REMARK 500 PRO A 411 155.79 -42.88
REMARK 500 SER A 433 -0.12 -141.13
REMARK 500 ASP A 436 177.07 -55.47
REMARK 500 VAL A 439 -44.36 -130.85
REMARK 500 THR A 440 -85.29 -25.36
REMARK 500 ASN A 451 -140.26 -62.74
REMARK 500 HIS A 485 127.60 171.99
REMARK 500 GLN B 21 -138.44 -83.35
REMARK 500 LYS B 22 92.62 78.12
REMARK 500 ASP B 53 57.04 -67.63
REMARK 500
REMARK 500 THIS ENTRY HAS 84 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 71 0.14 SIDE CHAIN
REMARK 500 ARG A 353 0.16 SIDE CHAIN
REMARK 500 ARG A 362 0.12 SIDE CHAIN
REMARK 500 ARG A 430 0.12 SIDE CHAIN
REMARK 500 ARG B 105 0.13 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ILE B 310 -10.57
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 507 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 357 OH
REMARK 620 2 HEM A 507 NA 76.3
REMARK 620 3 HEM A 507 NB 98.9 90.1
REMARK 620 4 HEM A 507 NC 95.9 170.1 85.1
REMARK 620 5 HEM A 507 ND 79.8 89.1 178.6 95.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 507 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 357 OH
REMARK 620 2 HEM B 507 NA 86.2
REMARK 620 3 HEM B 507 NB 99.6 89.9
REMARK 620 4 HEM B 507 NC 97.0 174.8 85.6
REMARK 620 5 HEM B 507 ND 82.0 91.0 178.2 93.5
REMARK 620 N 1 2 3 4
REMARK 700
REMARK 700 SHEET
REMARK 700 THE NINE-STRANDED SHEETS S1A AND S1B DESCRIBED BELOW ARE
REMARK 700 ACTUALLY EIGHT-STRANDED BETA BARRELS. THIS IS DENOTED BY
REMARK 700 THE FIRST STRAND RECURRING AS THE LAST STRAND.
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 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP B 508
DBREF 8CAT A 1 506 UNP P00432 CATA_BOVIN 1 506
DBREF 8CAT B 1 506 UNP P00432 CATA_BOVIN 1 506
SEQRES 1 A 506 ALA ASP ASN ARG ASP PRO ALA SER ASP GLN MET LYS HIS
SEQRES 2 A 506 TRP LYS GLU GLN ARG ALA ALA GLN LYS PRO ASP VAL LEU
SEQRES 3 A 506 THR THR GLY GLY GLY ASN PRO VAL GLY ASP LYS LEU ASN
SEQRES 4 A 506 SER LEU THR VAL GLY PRO ARG GLY PRO LEU LEU VAL GLN
SEQRES 5 A 506 ASP VAL VAL PHE THR ASP GLU MET ALA HIS PHE ASP ARG
SEQRES 6 A 506 GLU ARG ILE PRO GLU ARG VAL VAL HIS ALA LYS GLY ALA
SEQRES 7 A 506 GLY ALA PHE GLY TYR PHE GLU VAL THR HIS ASP ILE THR
SEQRES 8 A 506 ARG TYR SER LYS ALA LYS VAL PHE GLU HIS ILE GLY LYS
SEQRES 9 A 506 ARG THR PRO ILE ALA VAL ARG PHE SER THR VAL ALA GLY
SEQRES 10 A 506 GLU SER GLY SER ALA ASP THR VAL ARG ASP PRO ARG GLY
SEQRES 11 A 506 PHE ALA VAL LYS PHE TYR THR GLU ASP GLY ASN TRP ASP
SEQRES 12 A 506 LEU VAL GLY ASN ASN THR PRO ILE PHE PHE ILE ARG ASP
SEQRES 13 A 506 ALA LEU LEU PHE PRO SER PHE ILE HIS SER GLN LYS ARG
SEQRES 14 A 506 ASN PRO GLN THR HIS LEU LYS ASP PRO ASP MET VAL TRP
SEQRES 15 A 506 ASP PHE TRP SER LEU ARG PRO GLU SER LEU HIS GLN VAL
SEQRES 16 A 506 SER PHE LEU PHE SER ASP ARG GLY ILE PRO ASP GLY HIS
SEQRES 17 A 506 ARG HIS MET ASP GLY TYR GLY SER HIS THR PHE LYS LEU
SEQRES 18 A 506 VAL ASN ALA ASP GLY GLU ALA VAL TYR CYS LYS PHE HIS
SEQRES 19 A 506 TYR LYS THR ASP GLN GLY ILE LYS ASN LEU SER VAL GLU
SEQRES 20 A 506 ASP ALA ALA ARG LEU ALA HIS GLU ASP PRO ASP TYR GLY
SEQRES 21 A 506 LEU ARG ASP LEU PHE ASN ALA ILE ALA THR GLY ASN TYR
SEQRES 22 A 506 PRO SER TRP THR LEU TYR ILE GLN VAL MET THR PHE SER
SEQRES 23 A 506 GLU ALA GLU ILE PHE PRO PHE ASN PRO PHE ASP LEU THR
SEQRES 24 A 506 LYS VAL TRP PRO HIS GLY ASP TYR PRO LEU ILE PRO VAL
SEQRES 25 A 506 GLY LYS LEU VAL LEU ASN ARG ASN PRO VAL ASN TYR PHE
SEQRES 26 A 506 ALA GLU VAL GLU GLN LEU ALA PHE ASP PRO SER ASN MET
SEQRES 27 A 506 PRO PRO GLY ILE GLU PRO SER PRO ASP LYS MET LEU GLN
SEQRES 28 A 506 GLY ARG LEU PHE ALA TYR PRO ASP THR HIS ARG HIS ARG
SEQRES 29 A 506 LEU GLY PRO ASN TYR LEU GLN ILE PRO VAL ASN CYS PRO
SEQRES 30 A 506 TYR ARG ALA ARG VAL ALA ASN TYR GLN ARG ASP GLY PRO
SEQRES 31 A 506 MET CYS MET MET ASP ASN GLN GLY GLY ALA PRO ASN TYR
SEQRES 32 A 506 TYR PRO ASN SER PHE SER ALA PRO GLU HIS GLN PRO SER
SEQRES 33 A 506 ALA LEU GLU HIS ARG THR HIS PHE SER GLY ASP VAL GLN
SEQRES 34 A 506 ARG PHE ASN SER ALA ASN ASP ASP ASN VAL THR GLN VAL
SEQRES 35 A 506 ARG THR PHE TYR LEU LYS VAL LEU ASN GLU GLU GLN ARG
SEQRES 36 A 506 LYS ARG LEU CYS GLU ASN ILE ALA GLY HIS LEU LYS ASP
SEQRES 37 A 506 ALA GLN LEU PHE ILE GLN LYS LYS ALA VAL LYS ASN PHE
SEQRES 38 A 506 SER ASP VAL HIS PRO GLU TYR GLY SER ARG ILE GLN ALA
SEQRES 39 A 506 LEU LEU ASP LYS TYR ASN GLU GLU LYS PRO LYS ASN
SEQRES 1 B 506 ALA ASP ASN ARG ASP PRO ALA SER ASP GLN MET LYS HIS
SEQRES 2 B 506 TRP LYS GLU GLN ARG ALA ALA GLN LYS PRO ASP VAL LEU
SEQRES 3 B 506 THR THR GLY GLY GLY ASN PRO VAL GLY ASP LYS LEU ASN
SEQRES 4 B 506 SER LEU THR VAL GLY PRO ARG GLY PRO LEU LEU VAL GLN
SEQRES 5 B 506 ASP VAL VAL PHE THR ASP GLU MET ALA HIS PHE ASP ARG
SEQRES 6 B 506 GLU ARG ILE PRO GLU ARG VAL VAL HIS ALA LYS GLY ALA
SEQRES 7 B 506 GLY ALA PHE GLY TYR PHE GLU VAL THR HIS ASP ILE THR
SEQRES 8 B 506 ARG TYR SER LYS ALA LYS VAL PHE GLU HIS ILE GLY LYS
SEQRES 9 B 506 ARG THR PRO ILE ALA VAL ARG PHE SER THR VAL ALA GLY
SEQRES 10 B 506 GLU SER GLY SER ALA ASP THR VAL ARG ASP PRO ARG GLY
SEQRES 11 B 506 PHE ALA VAL LYS PHE TYR THR GLU ASP GLY ASN TRP ASP
SEQRES 12 B 506 LEU VAL GLY ASN ASN THR PRO ILE PHE PHE ILE ARG ASP
SEQRES 13 B 506 ALA LEU LEU PHE PRO SER PHE ILE HIS SER GLN LYS ARG
SEQRES 14 B 506 ASN PRO GLN THR HIS LEU LYS ASP PRO ASP MET VAL TRP
SEQRES 15 B 506 ASP PHE TRP SER LEU ARG PRO GLU SER LEU HIS GLN VAL
SEQRES 16 B 506 SER PHE LEU PHE SER ASP ARG GLY ILE PRO ASP GLY HIS
SEQRES 17 B 506 ARG HIS MET ASP GLY TYR GLY SER HIS THR PHE LYS LEU
SEQRES 18 B 506 VAL ASN ALA ASP GLY GLU ALA VAL TYR CYS LYS PHE HIS
SEQRES 19 B 506 TYR LYS THR ASP GLN GLY ILE LYS ASN LEU SER VAL GLU
SEQRES 20 B 506 ASP ALA ALA ARG LEU ALA HIS GLU ASP PRO ASP TYR GLY
SEQRES 21 B 506 LEU ARG ASP LEU PHE ASN ALA ILE ALA THR GLY ASN TYR
SEQRES 22 B 506 PRO SER TRP THR LEU TYR ILE GLN VAL MET THR PHE SER
SEQRES 23 B 506 GLU ALA GLU ILE PHE PRO PHE ASN PRO PHE ASP LEU THR
SEQRES 24 B 506 LYS VAL TRP PRO HIS GLY ASP TYR PRO LEU ILE PRO VAL
SEQRES 25 B 506 GLY LYS LEU VAL LEU ASN ARG ASN PRO VAL ASN TYR PHE
SEQRES 26 B 506 ALA GLU VAL GLU GLN LEU ALA PHE ASP PRO SER ASN MET
SEQRES 27 B 506 PRO PRO GLY ILE GLU PRO SER PRO ASP LYS MET LEU GLN
SEQRES 28 B 506 GLY ARG LEU PHE ALA TYR PRO ASP THR HIS ARG HIS ARG
SEQRES 29 B 506 LEU GLY PRO ASN TYR LEU GLN ILE PRO VAL ASN CYS PRO
SEQRES 30 B 506 TYR ARG ALA ARG VAL ALA ASN TYR GLN ARG ASP GLY PRO
SEQRES 31 B 506 MET CYS MET MET ASP ASN GLN GLY GLY ALA PRO ASN TYR
SEQRES 32 B 506 TYR PRO ASN SER PHE SER ALA PRO GLU HIS GLN PRO SER
SEQRES 33 B 506 ALA LEU GLU HIS ARG THR HIS PHE SER GLY ASP VAL GLN
SEQRES 34 B 506 ARG PHE ASN SER ALA ASN ASP ASP ASN VAL THR GLN VAL
SEQRES 35 B 506 ARG THR PHE TYR LEU LYS VAL LEU ASN GLU GLU GLN ARG
SEQRES 36 B 506 LYS ARG LEU CYS GLU ASN ILE ALA GLY HIS LEU LYS ASP
SEQRES 37 B 506 ALA GLN LEU PHE ILE GLN LYS LYS ALA VAL LYS ASN PHE
SEQRES 38 B 506 SER ASP VAL HIS PRO GLU TYR GLY SER ARG ILE GLN ALA
SEQRES 39 B 506 LEU LEU ASP LYS TYR ASN GLU GLU LYS PRO LYS ASN
HET HEM A 507 43
HET NDP A 508 48
HET HEM B 507 43
HET NDP B 508 48
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NDP PHOSPHATE
HETSYN HEM HEME
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 NDP 2(C21 H30 N7 O17 P3)
FORMUL 7 HOH *98(H2 O)
HELIX 1 H1A ASP A 9 ALA A 19 1 11
HELIX 2 H2A ASP A 53 ARG A 67 1 15
HELIX 3 H3A ASP A 156 LYS A 168 1 13
HELIX 4 H4A ASP A 177 ARG A 188 1 12
HELIX 5 H5A PRO A 189 SER A 200 1 12
HELIX 6 H6A SER A 245 ASP A 256 1 12
HELIX 7 H7A ASP A 258 ASN A 272 1 15
HELIX 8 H8A ASN A 323 GLU A 329 1 7
HELIX 9 H9A ASP A 347 GLY A 366 1 20
HELIX 10 10A ASP A 437 LEU A 447 1 11
HELIX 11 11A ASN A 451 LYS A 467 1 17
HELIX 12 12A GLN A 470 ASP A 483 1 14
HELIX 13 13A HIS A 485 ASN A 500 1 16
HELIX 14 H1B ASP B 9 ALA B 19 1 11
HELIX 15 H2B ASP B 53 ARG B 67 1 15
HELIX 16 H3B ASP B 156 LYS B 168 1 13
HELIX 17 H4B ASP B 177 ARG B 188 1 12
HELIX 18 H5B PRO B 189 SER B 200 1 12
HELIX 19 H6B SER B 245 ASP B 256 1 12
HELIX 20 H7B ASP B 258 ASN B 272 1 15
HELIX 21 H8B ASN B 323 GLU B 329 1 7
HELIX 22 H9B ASP B 347 GLY B 366 1 20
HELIX 23 10B ASP B 437 LEU B 447 1 11
HELIX 24 11B ASN B 451 LYS B 467 1 17
HELIX 25 12B GLN B 470 ASP B 483 1 14
HELIX 26 13B HIS B 485 ASN B 500 1 16
SHEET 1 S1A 9 LYS A 76 VAL A 86 0
SHEET 2 S1A 9 LYS A 104 THR A 114 -1 N ILE A 108 O GLY A 82
SHEET 3 S1A 9 ARG A 129 PHE A 135 -1 N ALA A 132 O ARG A 111
SHEET 4 S1A 9 TRP A 142 ASN A 148 -1 N LEU A 144 O VAL A 133
SHEET 5 S1A 9 GLY A 213 ASN A 223 -1 N SER A 216 O VAL A 145
SHEET 6 S1A 9 GLY A 226 GLN A 239 -1 N TYR A 230 O PHE A 219
SHEET 7 S1A 9 PRO A 274 MET A 283 -1 N TYR A 279 O TYR A 235
SHEET 8 S1A 9 GLY A 313 LEU A 317 -1 N LEU A 315 O TRP A 276
SHEET 9 S1A 9 LYS A 76 VAL A 86 -1 N GLU A 85 O LYS A 314
SHEET 1 S1B 9 LYS B 76 VAL B 86 0
SHEET 2 S1B 9 LYS B 104 THR B 114 -1 N ILE B 108 O GLY B 82
SHEET 3 S1B 9 ARG B 129 PHE B 135 -1 N ALA B 132 O ARG B 111
SHEET 4 S1B 9 TRP B 142 ASN B 148 -1 N LEU B 144 O VAL B 133
SHEET 5 S1B 9 GLY B 213 ASN B 223 -1 N SER B 216 O VAL B 145
SHEET 6 S1B 9 GLY B 226 GLN B 239 -1 N TYR B 230 O PHE B 219
SHEET 7 S1B 9 PRO B 274 MET B 283 -1 N TYR B 279 O TYR B 235
SHEET 8 S1B 9 GLY B 313 LEU B 317 -1 N LEU B 315 O TRP B 276
SHEET 9 S1B 9 LYS B 76 VAL B 86 -1 N GLU B 85 O LYS B 314
LINK OH TYR A 357 FE HEM A 507 1555 1555 1.90
LINK OH TYR B 357 FE HEM B 507 1555 1555 1.89
CISPEP 1 TYR A 404 PRO A 405 0 2.39
CISPEP 2 TYR B 404 PRO B 405 0 5.87
SITE 1 AC1 23 ARG A 71 VAL A 72 VAL A 73 HIS A 74
SITE 2 AC1 23 ARG A 111 GLY A 130 VAL A 145 GLY A 146
SITE 3 AC1 23 ASN A 147 ALA A 157 PHE A 160 SER A 216
SITE 4 AC1 23 LEU A 298 PHE A 333 ARG A 353 ALA A 356
SITE 5 AC1 23 TYR A 357 THR A 360 HIS A 361 ARG A 364
SITE 6 AC1 23 HOH A 509 HOH A 511 ASP B 64
SITE 1 AC2 15 HIS A 193 PHE A 197 SER A 200 ARG A 202
SITE 2 AC2 15 LYS A 236 ILE A 241 VAL A 301 TRP A 302
SITE 3 AC2 15 PRO A 303 HIS A 304 GLN A 441 THR A 444
SITE 4 AC2 15 PHE A 445 VAL A 449 HOH A 512
SITE 1 AC3 23 ASP A 64 ARG B 71 VAL B 72 VAL B 73
SITE 2 AC3 23 HIS B 74 ARG B 111 GLY B 130 VAL B 145
SITE 3 AC3 23 GLY B 146 ASN B 147 ALA B 157 PHE B 160
SITE 4 AC3 23 GLY B 215 PHE B 333 MET B 349 ARG B 353
SITE 5 AC3 23 ALA B 356 TYR B 357 THR B 360 HIS B 361
SITE 6 AC3 23 ARG B 364 HOH B 518 HOH B 520
SITE 1 AC4 15 HIS B 193 PHE B 197 SER B 200 ARG B 202
SITE 2 AC4 15 HIS B 234 LYS B 236 ILE B 241 VAL B 301
SITE 3 AC4 15 TRP B 302 PRO B 303 HIS B 304 GLN B 441
SITE 4 AC4 15 PHE B 445 VAL B 449 HOH B 521
CRYST1 142.000 142.000 103.700 90.00 90.00 120.00 P 32 2 1 12
ORIGX1 0.842103 0.486206 0.233405 -20.17144
ORIGX2 -0.500073 0.866014 -0.000017 -92.58507
ORIGX3 -0.202151 -0.116716 0.972359 -84.02731
SCALE1 0.007042 0.004066 0.000000 0.00000
SCALE2 0.000000 0.008132 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009643 0.00000
MTRIX1 1 -0.918275 0.047185 -0.393099 -58.61394 1
MTRIX2 1 0.047184 -0.972758 -0.226956 179.97282 1
MTRIX3 1 -0.393142 -0.226989 0.891033 9.41719 1
(ATOM LINES ARE NOT SHOWN.)
END