HEADER OXIDOREDUCTASE 02-MAR-04 1SJ2
TITLE CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS CATALASE-PEROXIDASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEROXIDASE/CATALASE T;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CATALASE-PEROXIDASE T;
COMPND 5 EC: 1.11.1.6;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: KATG, RV1908C, MT1959, MTCY180.10;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: UM255;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTRC99A
KEYWDS HOMODIMER, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.BERTRAND,N.A.J.EADY,J.N.JONES,J.BODIGUEL,JESMIN,J.M.NAGY,E.L.RAVEN,
AUTHOR 2 B.JAMART-GREGOIRE,K.A.BROWN
REVDAT 5 23-AUG-23 1SJ2 1 REMARK SEQADV LINK
REVDAT 4 13-JUL-11 1SJ2 1 VERSN
REVDAT 3 24-FEB-09 1SJ2 1 VERSN
REVDAT 2 14-SEP-04 1SJ2 1 JRNL
REVDAT 1 20-JUL-04 1SJ2 0
JRNL AUTH T.BERTRAND,N.A.J.EADY,J.N.JONES,JESMIN,J.M.NAGY,
JRNL AUTH 2 B.JAMART-GREGOIRE,E.L.RAVEN,K.A.BROWN
JRNL TITL CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS
JRNL TITL 2 CATALASE-PEROXIDASE.
JRNL REF J.BIOL.CHEM. V. 279 38991 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15231843
JRNL DOI 10.1074/JBC.M402382200
REMARK 2
REMARK 2 RESOLUTION. 2.41 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 2.41
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.3
REMARK 3 NUMBER OF REFLECTIONS : 61822
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) : 0.211
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 6260
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
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) : 2.41
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.52
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6712
REMARK 3 BIN R VALUE (WORKING SET) : 0.3700
REMARK 3 BIN FREE R VALUE : 0.3960
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 715
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11058
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 122
REMARK 3 SOLVENT ATOMS : 703
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -19.35000
REMARK 3 B22 (A**2) : -19.35000
REMARK 3 B33 (A**2) : 38.70000
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) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.54
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.39
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.60
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.400
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : CNS BULK SOLVENT MODEL USED
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 41.40
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 1SJ2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1000021747.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-NOV-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.488
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61822
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.410
REMARK 200 RESOLUTION RANGE LOW (A) : 23.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.15900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.41
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.39100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1MWV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, SODIUM ACETATE, PH 4.6,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 75.16500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 75.16500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 77.14050
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 75.16500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 75.16500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 77.14050
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 75.16500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 75.16500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 77.14050
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 75.16500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 75.16500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 77.14050
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 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 300 REMARK: THE ASYMMETRIC UNIT CONTAINS TWO MOLECULES BUT TO ACTUALLY
REMARK 300 REGENERATE THE BIOLOGICAL DIMER ONE SHOULD APPLY THE FOLLOWING
REMARK 300 TRANSFORMATION : -Y, -X, -Z
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -99.0 KCAL/MOL
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 MET A -2
REMARK 465 GLU A -1
REMARK 465 PHE A 0
REMARK 465 VAL A 1
REMARK 465 PRO A 2
REMARK 465 GLU A 3
REMARK 465 GLN A 4
REMARK 465 HIS A 5
REMARK 465 PRO A 6
REMARK 465 PRO A 7
REMARK 465 ILE A 8
REMARK 465 THR A 9
REMARK 465 GLU A 10
REMARK 465 THR A 11
REMARK 465 THR A 12
REMARK 465 THR A 13
REMARK 465 GLY A 14
REMARK 465 ALA A 15
REMARK 465 ALA A 16
REMARK 465 SER A 17
REMARK 465 ASN A 18
REMARK 465 GLY A 19
REMARK 465 CYS A 20
REMARK 465 PRO A 21
REMARK 465 VAL A 22
REMARK 465 VAL A 23
REMARK 465 MET B -2
REMARK 465 GLU B -1
REMARK 465 PHE B 0
REMARK 465 VAL B 1
REMARK 465 PRO B 2
REMARK 465 GLU B 3
REMARK 465 GLN B 4
REMARK 465 HIS B 5
REMARK 465 PRO B 6
REMARK 465 PRO B 7
REMARK 465 ILE B 8
REMARK 465 THR B 9
REMARK 465 GLU B 10
REMARK 465 THR B 11
REMARK 465 THR B 12
REMARK 465 THR B 13
REMARK 465 GLY B 14
REMARK 465 ALA B 15
REMARK 465 ALA B 16
REMARK 465 SER B 17
REMARK 465 ASN B 18
REMARK 465 GLY B 19
REMARK 465 CYS B 20
REMARK 465 PRO B 21
REMARK 465 VAL B 22
REMARK 465 VAL B 23
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 ILE B 228 N TYR B 229 1.12
REMARK 500 O ILE B 228 CA TYR B 229 1.46
REMARK 500 CH2 TRP A 107 CE1 TYR A 229 1.50
REMARK 500 CE2 TYR B 229 SD MET B 255 1.60
REMARK 500 CH2 TRP B 107 CE1 TYR B 229 1.60
REMARK 500 CE2 TYR A 229 SD MET A 255 1.73
REMARK 500 O HOH A 1545 O HOH B 2353 2.18
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 ILE A 228 C TYR A 229 N -0.283
REMARK 500 TYR A 229 C VAL A 230 N -0.275
REMARK 500 ILE B 228 C TYR B 229 N -0.425
REMARK 500 TYR B 229 C VAL B 230 N -0.292
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 PRO A 40 C - N - CA ANGL. DEV. = 10.0 DEGREES
REMARK 500 ILE A 228 O - C - N ANGL. DEV. = -10.7 DEGREES
REMARK 500 PRO B 40 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 ILE B 228 O - C - N ANGL. DEV. = -61.3 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 ASN A 35 -55.22 -8.32
REMARK 500 HIS A 49 47.86 -148.17
REMARK 500 TRP A 91 73.06 -179.40
REMARK 500 TYR A 95 23.45 42.86
REMARK 500 HIS A 97 106.65 -164.79
REMARK 500 SER A 140 -24.90 73.00
REMARK 500 GLU A 208 29.57 -143.23
REMARK 500 LEU A 220 144.55 -36.00
REMARK 500 TYR A 229 -73.42 -142.19
REMARK 500 ASN A 236 19.99 53.42
REMARK 500 PRO A 239 22.09 -57.58
REMARK 500 THR A 314 -75.01 -124.92
REMARK 500 THR A 363 -25.20 -154.30
REMARK 500 PHE A 368 -69.47 -132.35
REMARK 500 SER A 486 -77.53 -58.87
REMARK 500 ASP A 509 99.50 7.30
REMARK 500 ASP A 511 -55.11 -4.45
REMARK 500 ASP A 513 -50.33 -169.12
REMARK 500 PRO A 533 -134.07 -58.92
REMARK 500 ASN A 562 102.93 -55.07
REMARK 500 ASP A 592 89.96 -160.66
REMARK 500 GLU A 651 5.99 60.00
REMARK 500 ALA A 673 -122.40 -79.22
REMARK 500 ASP A 675 -157.29 -95.80
REMARK 500 ASP A 682 -150.28 -103.16
REMARK 500 HIS B 25 -52.85 -156.19
REMARK 500 GLU B 31 -128.22 -113.75
REMARK 500 LYS B 46 -8.43 -59.34
REMARK 500 TRP B 91 77.84 -177.30
REMARK 500 SER B 140 -19.33 75.25
REMARK 500 LEU B 205 -1.96 71.78
REMARK 500 GLU B 208 32.15 -141.14
REMARK 500 PRO B 219 35.52 -97.05
REMARK 500 TYR B 229 -78.31 179.48
REMARK 500 PRO B 239 36.51 -60.90
REMARK 500 THR B 314 -66.73 -124.94
REMARK 500 ASP B 357 12.46 53.63
REMARK 500 ARG B 373 -97.53 -104.23
REMARK 500 SER B 374 143.09 170.92
REMARK 500 SER B 465 -71.21 -42.09
REMARK 500 ARG B 496 3.15 -64.65
REMARK 500 GLN B 500 -82.13 -22.65
REMARK 500 PRO B 501 -71.25 -35.84
REMARK 500 ASP B 509 82.16 38.14
REMARK 500 ASP B 511 79.29 -60.34
REMARK 500 ALA B 532 64.58 162.84
REMARK 500 PRO B 533 -116.59 -45.03
REMARK 500 ASN B 535 -2.82 71.38
REMARK 500 ALA B 558 25.35 -62.94
REMARK 500 ALA B 559 30.95 -157.38
REMARK 500
REMARK 500 THIS ENTRY HAS 56 RAMACHANDRAN OUTLIERS.
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 A 228 -17.55
REMARK 500 ILE B 228 -65.80
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 A1500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 270 NE2
REMARK 620 2 HEM A1500 NA 92.3
REMARK 620 3 HEM A1500 NB 84.2 88.4
REMARK 620 4 HEM A1500 NC 89.9 177.1 89.9
REMARK 620 5 HEM A1500 ND 96.4 89.8 178.2 91.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B1500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 270 NE2
REMARK 620 2 HEM B1500 NA 88.5
REMARK 620 3 HEM B1500 NB 83.5 88.2
REMARK 620 4 HEM B1500 NC 93.9 176.7 89.8
REMARK 620 5 HEM B1500 ND 96.7 89.9 178.1 92.0
REMARK 620 N 1 2 3 4
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 1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1194
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1195
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1196
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 2194
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 2195
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 2196
DBREF 1SJ2 A 2 740 UNP Q08129 CATA_MYCTU 2 740
DBREF 1SJ2 B 2 740 UNP Q08129 CATA_MYCTU 2 740
SEQADV 1SJ2 MET A -2 UNP Q08129 INITIATING METHIONINE
SEQADV 1SJ2 GLU A -1 UNP Q08129 CLONING ARTIFACT
SEQADV 1SJ2 PHE A 0 UNP Q08129 CLONING ARTIFACT
SEQADV 1SJ2 VAL A 1 UNP Q08129 CLONING ARTIFACT
SEQADV 1SJ2 MET B -2 UNP Q08129 INITIATING METHIONINE
SEQADV 1SJ2 GLU B -1 UNP Q08129 CLONING ARTIFACT
SEQADV 1SJ2 PHE B 0 UNP Q08129 CLONING ARTIFACT
SEQADV 1SJ2 VAL B 1 UNP Q08129 CLONING ARTIFACT
SEQRES 1 A 743 MET GLU PHE VAL PRO GLU GLN HIS PRO PRO ILE THR GLU
SEQRES 2 A 743 THR THR THR GLY ALA ALA SER ASN GLY CYS PRO VAL VAL
SEQRES 3 A 743 GLY HIS MET LYS TYR PRO VAL GLU GLY GLY GLY ASN GLN
SEQRES 4 A 743 ASP TRP TRP PRO ASN ARG LEU ASN LEU LYS VAL LEU HIS
SEQRES 5 A 743 GLN ASN PRO ALA VAL ALA ASP PRO MET GLY ALA ALA PHE
SEQRES 6 A 743 ASP TYR ALA ALA GLU VAL ALA THR ILE ASP VAL ASP ALA
SEQRES 7 A 743 LEU THR ARG ASP ILE GLU GLU VAL MET THR THR SER GLN
SEQRES 8 A 743 PRO TRP TRP PRO ALA ASP TYR GLY HIS TYR GLY PRO LEU
SEQRES 9 A 743 PHE ILE ARG MET ALA TRP HIS ALA ALA GLY THR TYR ARG
SEQRES 10 A 743 ILE HIS ASP GLY ARG GLY GLY ALA GLY GLY GLY MET GLN
SEQRES 11 A 743 ARG PHE ALA PRO LEU ASN SER TRP PRO ASP ASN ALA SER
SEQRES 12 A 743 LEU ASP LYS ALA ARG ARG LEU LEU TRP PRO VAL LYS LYS
SEQRES 13 A 743 LYS TYR GLY LYS LYS LEU SER TRP ALA ASP LEU ILE VAL
SEQRES 14 A 743 PHE ALA GLY ASN CYS ALA LEU GLU SER MET GLY PHE LYS
SEQRES 15 A 743 THR PHE GLY PHE GLY PHE GLY ARG VAL ASP GLN TRP GLU
SEQRES 16 A 743 PRO ASP GLU VAL TYR TRP GLY LYS GLU ALA THR TRP LEU
SEQRES 17 A 743 GLY ASP GLU ARG TYR SER GLY LYS ARG ASP LEU GLU ASN
SEQRES 18 A 743 PRO LEU ALA ALA VAL GLN MET GLY LEU ILE TYR VAL ASN
SEQRES 19 A 743 PRO GLU GLY PRO ASN GLY ASN PRO ASP PRO MET ALA ALA
SEQRES 20 A 743 ALA VAL ASP ILE ARG GLU THR PHE ARG ARG MET ALA MET
SEQRES 21 A 743 ASN ASP VAL GLU THR ALA ALA LEU ILE VAL GLY GLY HIS
SEQRES 22 A 743 THR PHE GLY LYS THR HIS GLY ALA GLY PRO ALA ASP LEU
SEQRES 23 A 743 VAL GLY PRO GLU PRO GLU ALA ALA PRO LEU GLU GLN MET
SEQRES 24 A 743 GLY LEU GLY TRP LYS SER SER TYR GLY THR GLY THR GLY
SEQRES 25 A 743 LYS ASP ALA ILE THR SER GLY ILE GLU VAL VAL TRP THR
SEQRES 26 A 743 ASN THR PRO THR LYS TRP ASP ASN SER PHE LEU GLU ILE
SEQRES 27 A 743 LEU TYR GLY TYR GLU TRP GLU LEU THR LYS SER PRO ALA
SEQRES 28 A 743 GLY ALA TRP GLN TYR THR ALA LYS ASP GLY ALA GLY ALA
SEQRES 29 A 743 GLY THR ILE PRO ASP PRO PHE GLY GLY PRO GLY ARG SER
SEQRES 30 A 743 PRO THR MET LEU ALA THR ASP LEU SER LEU ARG VAL ASP
SEQRES 31 A 743 PRO ILE TYR GLU ARG ILE THR ARG ARG TRP LEU GLU HIS
SEQRES 32 A 743 PRO GLU GLU LEU ALA ASP GLU PHE ALA LYS ALA TRP TYR
SEQRES 33 A 743 LYS LEU ILE HIS ARG ASP MET GLY PRO VAL ALA ARG TYR
SEQRES 34 A 743 LEU GLY PRO LEU VAL PRO LYS GLN THR LEU LEU TRP GLN
SEQRES 35 A 743 ASP PRO VAL PRO ALA VAL SER HIS ASP LEU VAL GLY GLU
SEQRES 36 A 743 ALA GLU ILE ALA SER LEU LYS SER GLN ILE ARG ALA SER
SEQRES 37 A 743 GLY LEU THR VAL SER GLN LEU VAL SER THR ALA TRP ALA
SEQRES 38 A 743 ALA ALA SER SER PHE ARG GLY SER ASP LYS ARG GLY GLY
SEQRES 39 A 743 ALA ASN GLY GLY ARG ILE ARG LEU GLN PRO GLN VAL GLY
SEQRES 40 A 743 TRP GLU VAL ASN ASP PRO ASP GLY ASP LEU ARG LYS VAL
SEQRES 41 A 743 ILE ARG THR LEU GLU GLU ILE GLN GLU SER PHE ASN SER
SEQRES 42 A 743 ALA ALA PRO GLY ASN ILE LYS VAL SER PHE ALA ASP LEU
SEQRES 43 A 743 VAL VAL LEU GLY GLY CYS ALA ALA ILE GLU LYS ALA ALA
SEQRES 44 A 743 LYS ALA ALA GLY HIS ASN ILE THR VAL PRO PHE THR PRO
SEQRES 45 A 743 GLY ARG THR ASP ALA SER GLN GLU GLN THR ASP VAL GLU
SEQRES 46 A 743 SER PHE ALA VAL LEU GLU PRO LYS ALA ASP GLY PHE ARG
SEQRES 47 A 743 ASN TYR LEU GLY LYS GLY ASN PRO LEU PRO ALA GLU TYR
SEQRES 48 A 743 MET LEU LEU ASP LYS ALA ASN LEU LEU THR LEU SER ALA
SEQRES 49 A 743 PRO GLU MET THR VAL LEU VAL GLY GLY LEU ARG VAL LEU
SEQRES 50 A 743 GLY ALA ASN TYR LYS ARG LEU PRO LEU GLY VAL PHE THR
SEQRES 51 A 743 GLU ALA SER GLU SER LEU THR ASN ASP PHE PHE VAL ASN
SEQRES 52 A 743 LEU LEU ASP MET GLY ILE THR TRP GLU PRO SER PRO ALA
SEQRES 53 A 743 ASP ASP GLY THR TYR GLN GLY LYS ASP GLY SER GLY LYS
SEQRES 54 A 743 VAL LYS TRP THR GLY SER ARG VAL ASP LEU VAL PHE GLY
SEQRES 55 A 743 SER ASN SER GLU LEU ARG ALA LEU VAL GLU VAL TYR GLY
SEQRES 56 A 743 ALA ASP ASP ALA GLN PRO LYS PHE VAL GLN ASP PHE VAL
SEQRES 57 A 743 ALA ALA TRP ASP LYS VAL MET ASN LEU ASP ARG PHE ASP
SEQRES 58 A 743 VAL ARG
SEQRES 1 B 743 MET GLU PHE VAL PRO GLU GLN HIS PRO PRO ILE THR GLU
SEQRES 2 B 743 THR THR THR GLY ALA ALA SER ASN GLY CYS PRO VAL VAL
SEQRES 3 B 743 GLY HIS MET LYS TYR PRO VAL GLU GLY GLY GLY ASN GLN
SEQRES 4 B 743 ASP TRP TRP PRO ASN ARG LEU ASN LEU LYS VAL LEU HIS
SEQRES 5 B 743 GLN ASN PRO ALA VAL ALA ASP PRO MET GLY ALA ALA PHE
SEQRES 6 B 743 ASP TYR ALA ALA GLU VAL ALA THR ILE ASP VAL ASP ALA
SEQRES 7 B 743 LEU THR ARG ASP ILE GLU GLU VAL MET THR THR SER GLN
SEQRES 8 B 743 PRO TRP TRP PRO ALA ASP TYR GLY HIS TYR GLY PRO LEU
SEQRES 9 B 743 PHE ILE ARG MET ALA TRP HIS ALA ALA GLY THR TYR ARG
SEQRES 10 B 743 ILE HIS ASP GLY ARG GLY GLY ALA GLY GLY GLY MET GLN
SEQRES 11 B 743 ARG PHE ALA PRO LEU ASN SER TRP PRO ASP ASN ALA SER
SEQRES 12 B 743 LEU ASP LYS ALA ARG ARG LEU LEU TRP PRO VAL LYS LYS
SEQRES 13 B 743 LYS TYR GLY LYS LYS LEU SER TRP ALA ASP LEU ILE VAL
SEQRES 14 B 743 PHE ALA GLY ASN CYS ALA LEU GLU SER MET GLY PHE LYS
SEQRES 15 B 743 THR PHE GLY PHE GLY PHE GLY ARG VAL ASP GLN TRP GLU
SEQRES 16 B 743 PRO ASP GLU VAL TYR TRP GLY LYS GLU ALA THR TRP LEU
SEQRES 17 B 743 GLY ASP GLU ARG TYR SER GLY LYS ARG ASP LEU GLU ASN
SEQRES 18 B 743 PRO LEU ALA ALA VAL GLN MET GLY LEU ILE TYR VAL ASN
SEQRES 19 B 743 PRO GLU GLY PRO ASN GLY ASN PRO ASP PRO MET ALA ALA
SEQRES 20 B 743 ALA VAL ASP ILE ARG GLU THR PHE ARG ARG MET ALA MET
SEQRES 21 B 743 ASN ASP VAL GLU THR ALA ALA LEU ILE VAL GLY GLY HIS
SEQRES 22 B 743 THR PHE GLY LYS THR HIS GLY ALA GLY PRO ALA ASP LEU
SEQRES 23 B 743 VAL GLY PRO GLU PRO GLU ALA ALA PRO LEU GLU GLN MET
SEQRES 24 B 743 GLY LEU GLY TRP LYS SER SER TYR GLY THR GLY THR GLY
SEQRES 25 B 743 LYS ASP ALA ILE THR SER GLY ILE GLU VAL VAL TRP THR
SEQRES 26 B 743 ASN THR PRO THR LYS TRP ASP ASN SER PHE LEU GLU ILE
SEQRES 27 B 743 LEU TYR GLY TYR GLU TRP GLU LEU THR LYS SER PRO ALA
SEQRES 28 B 743 GLY ALA TRP GLN TYR THR ALA LYS ASP GLY ALA GLY ALA
SEQRES 29 B 743 GLY THR ILE PRO ASP PRO PHE GLY GLY PRO GLY ARG SER
SEQRES 30 B 743 PRO THR MET LEU ALA THR ASP LEU SER LEU ARG VAL ASP
SEQRES 31 B 743 PRO ILE TYR GLU ARG ILE THR ARG ARG TRP LEU GLU HIS
SEQRES 32 B 743 PRO GLU GLU LEU ALA ASP GLU PHE ALA LYS ALA TRP TYR
SEQRES 33 B 743 LYS LEU ILE HIS ARG ASP MET GLY PRO VAL ALA ARG TYR
SEQRES 34 B 743 LEU GLY PRO LEU VAL PRO LYS GLN THR LEU LEU TRP GLN
SEQRES 35 B 743 ASP PRO VAL PRO ALA VAL SER HIS ASP LEU VAL GLY GLU
SEQRES 36 B 743 ALA GLU ILE ALA SER LEU LYS SER GLN ILE ARG ALA SER
SEQRES 37 B 743 GLY LEU THR VAL SER GLN LEU VAL SER THR ALA TRP ALA
SEQRES 38 B 743 ALA ALA SER SER PHE ARG GLY SER ASP LYS ARG GLY GLY
SEQRES 39 B 743 ALA ASN GLY GLY ARG ILE ARG LEU GLN PRO GLN VAL GLY
SEQRES 40 B 743 TRP GLU VAL ASN ASP PRO ASP GLY ASP LEU ARG LYS VAL
SEQRES 41 B 743 ILE ARG THR LEU GLU GLU ILE GLN GLU SER PHE ASN SER
SEQRES 42 B 743 ALA ALA PRO GLY ASN ILE LYS VAL SER PHE ALA ASP LEU
SEQRES 43 B 743 VAL VAL LEU GLY GLY CYS ALA ALA ILE GLU LYS ALA ALA
SEQRES 44 B 743 LYS ALA ALA GLY HIS ASN ILE THR VAL PRO PHE THR PRO
SEQRES 45 B 743 GLY ARG THR ASP ALA SER GLN GLU GLN THR ASP VAL GLU
SEQRES 46 B 743 SER PHE ALA VAL LEU GLU PRO LYS ALA ASP GLY PHE ARG
SEQRES 47 B 743 ASN TYR LEU GLY LYS GLY ASN PRO LEU PRO ALA GLU TYR
SEQRES 48 B 743 MET LEU LEU ASP LYS ALA ASN LEU LEU THR LEU SER ALA
SEQRES 49 B 743 PRO GLU MET THR VAL LEU VAL GLY GLY LEU ARG VAL LEU
SEQRES 50 B 743 GLY ALA ASN TYR LYS ARG LEU PRO LEU GLY VAL PHE THR
SEQRES 51 B 743 GLU ALA SER GLU SER LEU THR ASN ASP PHE PHE VAL ASN
SEQRES 52 B 743 LEU LEU ASP MET GLY ILE THR TRP GLU PRO SER PRO ALA
SEQRES 53 B 743 ASP ASP GLY THR TYR GLN GLY LYS ASP GLY SER GLY LYS
SEQRES 54 B 743 VAL LYS TRP THR GLY SER ARG VAL ASP LEU VAL PHE GLY
SEQRES 55 B 743 SER ASN SER GLU LEU ARG ALA LEU VAL GLU VAL TYR GLY
SEQRES 56 B 743 ALA ASP ASP ALA GLN PRO LYS PHE VAL GLN ASP PHE VAL
SEQRES 57 B 743 ALA ALA TRP ASP LYS VAL MET ASN LEU ASP ARG PHE ASP
SEQRES 58 B 743 VAL ARG
HET HEM A1500 43
HET GOL A1194 6
HET GOL A1195 6
HET GOL A1196 6
HET HEM B1500 43
HET GOL B2194 6
HET GOL B2195 6
HET GOL B2196 6
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM GOL GLYCEROL
HETSYN HEM HEME
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 GOL 6(C3 H8 O3)
FORMUL 11 HOH *703(H2 O)
HELIX 1 1 TYR A 28 GLY A 32 5 5
HELIX 2 2 GLY A 34 TRP A 38 5 5
HELIX 3 3 ASN A 44 GLN A 50 5 7
HELIX 4 4 PRO A 52 ASP A 56 5 5
HELIX 5 5 ASP A 63 ALA A 69 1 7
HELIX 6 6 ASP A 72 THR A 85 1 14
HELIX 7 7 ALA A 93 HIS A 97 5 5
HELIX 8 8 TYR A 98 THR A 112 1 15
HELIX 9 9 GLY A 125 PHE A 129 5 5
HELIX 10 10 PRO A 131 ALA A 139 5 9
HELIX 11 11 SER A 140 LEU A 148 1 9
HELIX 12 12 LEU A 148 GLY A 156 1 9
HELIX 13 13 LYS A 157 LEU A 159 5 3
HELIX 14 14 SER A 160 MET A 176 1 17
HELIX 15 15 GLY A 234 ASN A 238 5 5
HELIX 16 16 ASP A 240 ARG A 254 1 15
HELIX 17 17 ASN A 258 HIS A 270 1 13
HELIX 18 18 GLU A 287 ALA A 291 5 5
HELIX 19 19 PRO A 292 MET A 296 5 5
HELIX 20 20 THR A 308 ALA A 312 5 5
HELIX 21 21 ASN A 330 TYR A 339 1 10
HELIX 22 22 ASP A 357 ALA A 359 5 3
HELIX 23 23 LEU A 378 ASP A 387 1 10
HELIX 24 24 ASP A 387 HIS A 400 1 14
HELIX 25 25 HIS A 400 ARG A 418 1 19
HELIX 26 26 ASP A 419 GLY A 421 5 3
HELIX 27 27 PRO A 422 TYR A 426 5 5
HELIX 28 28 LEU A 436 ASP A 440 5 5
HELIX 29 29 GLY A 451 ALA A 464 1 14
HELIX 30 30 THR A 468 SER A 481 1 14
HELIX 31 31 GLY A 495 LEU A 499 5 5
HELIX 32 32 PRO A 501 TRP A 505 5 5
HELIX 33 33 ASP A 509 GLY A 512 5 4
HELIX 34 34 ASP A 513 ALA A 532 1 20
HELIX 35 35 SER A 539 ALA A 559 1 21
HELIX 36 36 SER A 575 THR A 579 5 5
HELIX 37 37 ASP A 580 ALA A 585 1 6
HELIX 38 38 VAL A 586 GLU A 588 5 3
HELIX 39 39 GLY A 593 ASN A 596 5 4
HELIX 40 40 PRO A 605 LEU A 617 1 13
HELIX 41 41 SER A 620 LEU A 634 1 15
HELIX 42 42 ASN A 637 LEU A 641 5 5
HELIX 43 43 ASN A 655 LEU A 662 1 8
HELIX 44 44 SER A 692 ASN A 701 1 10
HELIX 45 45 ASN A 701 GLY A 712 1 12
HELIX 46 46 ALA A 716 ASN A 733 1 18
HELIX 47 47 ARG A 736 ARG A 740 5 5
HELIX 48 48 GLY B 34 TRP B 38 5 5
HELIX 49 49 ASN B 44 HIS B 49 5 6
HELIX 50 50 PRO B 52 ASP B 56 5 5
HELIX 51 51 ASP B 63 ALA B 69 1 7
HELIX 52 52 ASP B 72 THR B 85 1 14
HELIX 53 53 ALA B 93 HIS B 97 5 5
HELIX 54 54 TYR B 98 GLY B 111 1 14
HELIX 55 55 GLY B 125 PHE B 129 5 5
HELIX 56 56 PRO B 131 ALA B 139 5 9
HELIX 57 57 SER B 140 LEU B 148 1 9
HELIX 58 58 LEU B 148 GLY B 156 1 9
HELIX 59 59 LYS B 157 LEU B 159 5 3
HELIX 60 60 SER B 160 MET B 176 1 17
HELIX 61 61 GLY B 234 ASN B 238 5 5
HELIX 62 62 ASP B 240 ARG B 254 1 15
HELIX 63 63 ASN B 258 HIS B 270 1 13
HELIX 64 64 PRO B 280 VAL B 284 5 5
HELIX 65 65 GLU B 287 ALA B 291 5 5
HELIX 66 66 PRO B 292 MET B 296 5 5
HELIX 67 67 THR B 308 ALA B 312 5 5
HELIX 68 68 ASN B 330 TYR B 339 1 10
HELIX 69 69 ASP B 357 ALA B 359 5 3
HELIX 70 70 LEU B 378 ASP B 387 1 10
HELIX 71 71 ASP B 387 HIS B 400 1 14
HELIX 72 72 HIS B 400 ARG B 418 1 19
HELIX 73 73 PRO B 422 TYR B 426 5 5
HELIX 74 74 LEU B 436 ASP B 440 5 5
HELIX 75 75 GLY B 451 GLY B 466 1 16
HELIX 76 76 THR B 468 SER B 481 1 14
HELIX 77 77 GLY B 495 ARG B 498 5 4
HELIX 78 78 LEU B 499 TRP B 505 1 7
HELIX 79 79 GLU B 506 ASP B 509 5 4
HELIX 80 80 GLY B 512 ALA B 531 1 20
HELIX 81 81 SER B 539 ALA B 558 1 20
HELIX 82 82 SER B 575 THR B 579 5 5
HELIX 83 83 GLY B 593 ASN B 596 5 4
HELIX 84 84 PRO B 605 LEU B 617 1 13
HELIX 85 85 SER B 620 LEU B 634 1 15
HELIX 86 86 ASN B 637 LEU B 641 5 5
HELIX 87 87 ASN B 655 LEU B 662 1 8
HELIX 88 88 ARG B 693 ASN B 701 1 9
HELIX 89 89 ASN B 701 GLY B 712 1 12
HELIX 90 90 ALA B 716 LEU B 734 1 19
SHEET 1 A 2 TYR A 210 SER A 211 0
SHEET 2 A 2 ASP A 215 LEU A 216 -1 O ASP A 215 N SER A 211
SHEET 1 B 3 TRP A 341 LYS A 345 0
SHEET 2 B 3 TRP A 351 ALA A 355 -1 O GLN A 352 N THR A 344
SHEET 3 B 3 THR A 376 MET A 377 -1 O MET A 377 N TYR A 353
SHEET 1 C 2 ALA A 591 ASP A 592 0
SHEET 2 C 2 TYR A 597 LEU A 598 -1 O TYR A 597 N ASP A 592
SHEET 1 D 3 THR A 667 PRO A 670 0
SHEET 2 D 3 TYR A 678 LYS A 681 -1 O LYS A 681 N THR A 667
SHEET 3 D 3 VAL A 687 GLY A 691 -1 O TRP A 689 N GLY A 680
SHEET 1 E 2 TYR B 210 SER B 211 0
SHEET 2 E 2 ASP B 215 LEU B 216 -1 O ASP B 215 N SER B 211
SHEET 1 F 3 TRP B 341 LYS B 345 0
SHEET 2 F 3 TRP B 351 ALA B 355 -1 O THR B 354 N GLU B 342
SHEET 3 F 3 THR B 376 MET B 377 -1 O MET B 377 N TYR B 353
SHEET 1 G 2 ALA B 591 ASP B 592 0
SHEET 2 G 2 TYR B 597 LEU B 598 -1 O TYR B 597 N ASP B 592
SHEET 1 H 3 THR B 667 PRO B 670 0
SHEET 2 H 3 THR B 677 LYS B 681 -1 O LYS B 681 N THR B 667
SHEET 3 H 3 VAL B 687 SER B 692 -1 O TRP B 689 N GLY B 680
LINK NE2 HIS A 270 FE HEM A1500 1555 1555 2.48
LINK NE2 HIS B 270 FE HEM B1500 1555 1555 2.49
CISPEP 1 ALA A 130 PRO A 131 0 -0.36
CISPEP 2 ASN A 218 PRO A 219 0 0.27
CISPEP 3 GLN A 500 PRO A 501 0 0.45
CISPEP 4 ALA B 130 PRO B 131 0 -0.03
CISPEP 5 ASN B 218 PRO B 219 0 0.10
SITE 1 AC1 18 PRO A 100 ILE A 103 ARG A 104 TRP A 107
SITE 2 AC1 18 LEU A 265 GLY A 269 HIS A 270 GLY A 273
SITE 3 AC1 18 LYS A 274 THR A 275 HIS A 276 THR A 314
SITE 4 AC1 18 SER A 315 TRP A 321 TRP A 412 HOH A1504
SITE 5 AC1 18 HOH A1507 HOH A1769
SITE 1 AC2 22 PRO B 100 LEU B 101 ILE B 103 ARG B 104
SITE 2 AC2 22 TRP B 107 PRO B 232 LEU B 265 ILE B 266
SITE 3 AC2 22 GLY B 269 HIS B 270 GLY B 273 LYS B 274
SITE 4 AC2 22 THR B 275 HIS B 276 THR B 314 SER B 315
SITE 5 AC2 22 TRP B 321 THR B 380 TRP B 412 HOH B2199
SITE 6 AC2 22 HOH B2216 HOH B2415
SITE 1 AC3 10 PHE A 62 TYR A 64 LYS A 152 GLY A 156
SITE 2 AC3 10 LYS A 157 ASP A 189 TRP A 191 HOH A1527
SITE 3 AC3 10 HOH A1537 HOH A1551
SITE 1 AC4 6 ARG A 42 LEU A 43 GLU A 607 TYR A 608
SITE 2 AC4 6 ASN A 701 HOH A1545
SITE 1 AC5 5 SER A 482 LEU A 587 LYS A 613 LEU A 616
SITE 2 AC5 5 HOH A1808
SITE 1 AC6 4 MET B 58 LYS B 152 LYS B 157 ASP B 189
SITE 1 AC7 7 ARG B 42 LEU B 43 GLU B 607 TYR B 608
SITE 2 AC7 7 VAL B 697 ASN B 701 HOH B2504
SITE 1 AC8 6 ARG B 484 PRO B 589 ALA B 591 LYS B 613
SITE 2 AC8 6 LEU B 616 HOH B2466
CRYST1 150.330 150.330 154.281 90.00 90.00 90.00 P 42 21 2 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 0.006652 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006652 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006482 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
