HEADER PHOTOSYNTHETIC REACTION CENTER 01-AUG-97 5PRC
TITLE PHOTOSYNTHETIC REACTION CENTER FROM RHODOPSEUDOMONAS VIRIDIS (ATRAZINE
TITLE 2 COMPLEX)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOTOSYNTHETIC REACTION CENTER;
COMPND 3 CHAIN: C;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: PHOTOSYNTHETIC REACTION CENTER;
COMPND 6 CHAIN: L;
COMPND 7 MOL_ID: 3;
COMPND 8 MOLECULE: PHOTOSYNTHETIC REACTION CENTER;
COMPND 9 CHAIN: M;
COMPND 10 MOL_ID: 4;
COMPND 11 MOLECULE: PHOTOSYNTHETIC REACTION CENTER;
COMPND 12 CHAIN: H
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BLASTOCHLORIS VIRIDIS;
SOURCE 3 ORGANISM_TAXID: 1079;
SOURCE 4 ATCC: DSM 133;
SOURCE 5 COLLECTION: DSM 133;
SOURCE 6 CELLULAR_LOCATION: INTRACYTOPLASMIC MEMBRANE (ICM);
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: BLASTOCHLORIS VIRIDIS;
SOURCE 9 ORGANISM_TAXID: 1079;
SOURCE 10 COLLECTION: DSM 133;
SOURCE 11 CELLULAR_LOCATION: INTRACYTOPLASMIC MEMBRANE (ICM);
SOURCE 12 MOL_ID: 3;
SOURCE 13 ORGANISM_SCIENTIFIC: BLASTOCHLORIS VIRIDIS;
SOURCE 14 ORGANISM_TAXID: 1079;
SOURCE 15 COLLECTION: DSM 133;
SOURCE 16 CELLULAR_LOCATION: INTRACYTOPLASMIC MEMBRANE (ICM);
SOURCE 17 MOL_ID: 4;
SOURCE 18 ORGANISM_SCIENTIFIC: BLASTOCHLORIS VIRIDIS;
SOURCE 19 ORGANISM_TAXID: 1079;
SOURCE 20 COLLECTION: DSM 133;
SOURCE 21 CELLULAR_LOCATION: INTRACYTOPLASMIC MEMBRANE (ICM)
KEYWDS PHOTOSYNTHETIC REACTION CENTER, SECONDARY QUINONE (QB), TRIAZINE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.R.D.LANCASTER,H.MICHEL
REVDAT 6 09-AUG-23 5PRC 1 REMARK LINK
REVDAT 5 16-NOV-11 5PRC 1 HETATM
REVDAT 4 13-JUL-11 5PRC 1 VERSN
REVDAT 3 31-MAR-09 5PRC 1 HETNAM
REVDAT 2 24-FEB-09 5PRC 1 VERSN
REVDAT 1 06-APR-99 5PRC 0
JRNL AUTH C.R.LANCASTER,H.MICHEL
JRNL TITL REFINED CRYSTAL STRUCTURES OF REACTION CENTRES FROM
JRNL TITL 2 RHODOPSEUDOMONAS VIRIDIS IN COMPLEXES WITH THE HERBICIDE
JRNL TITL 3 ATRAZINE AND TWO CHIRAL ATRAZINE DERIVATIVES ALSO LEAD TO A
JRNL TITL 4 NEW MODEL OF THE BOUND CAROTENOID.
JRNL REF J.MOL.BIOL. V. 286 883 1999
JRNL REFN ISSN 0022-2836
JRNL PMID 10024457
JRNL DOI 10.1006/JMBI.1998.2532
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.R.D.LANCASTER
REMARK 1 TITL UBIQUINONE REDUCTION AND PROTONATION IN THE REACTION CENTRE
REMARK 1 TITL 2 OF RHODOPSEUDOMONAS VIRIDIS: X-RAY STRUCTURES AND THEIR
REMARK 1 TITL 3 FUNCTIONAL IMPLICATIONS
REMARK 1 REF BIOCHIM.BIOPHYS.ACTA V.1365 143 1998
REMARK 1 REFN ISSN 0006-3002
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.R.LANCASTER,H.MICHEL
REMARK 1 TITL THE COUPLING OF LIGHT-INDUCED ELECTRON TRANSFER AND PROTON
REMARK 1 TITL 2 UPTAKE AS DERIVED FROM CRYSTAL STRUCTURES OF REACTION
REMARK 1 TITL 3 CENTRES FROM RHODOPSEUDOMONAS VIRIDIS MODIFIED AT THE
REMARK 1 TITL 4 BINDING SITE OF THE SECONDARY QUINONE, QB
REMARK 1 REF STRUCTURE V. 5 1339 1997
REMARK 1 REFN ISSN 0969-2126
REMARK 1 REFERENCE 3
REMARK 1 AUTH J.DEISENHOFER,O.EPP,I.SINNING,H.MICHEL
REMARK 1 TITL CRYSTALLOGRAPHIC REFINEMENT AT 2.3 A RESOLUTION AND REFINED
REMARK 1 TITL 2 MODEL OF THE PHOTOSYNTHETIC REACTION CENTRE FROM
REMARK 1 TITL 3 RHODOPSEUDOMONAS VIRIDIS
REMARK 1 REF J.MOL.BIOL. V. 246 429 1995
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 4
REMARK 1 AUTH J.DEISENHOFER,H.MICHEL
REMARK 1 TITL THE PHOTOSYNTHETIC REACTION CENTER FROM THE PURPLE BACTERIUM
REMARK 1 TITL 2 RHODOPSEUDOMONAS VIRIDIS
REMARK 1 REF SCIENCE V. 245 1463 1989
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 5
REMARK 1 AUTH J.DEISENHOFER,O.EPP,K.MIKI,R.HUBER,H.MICHEL
REMARK 1 TITL STRUCTURE OF THE PROTEIN SUBUNITS IN THE PHOTOSYNTHETIC
REMARK 1 TITL 2 REACTION CENTRE OF RHODOPSEUDOMONAS VIRIDIS AT 3 ANGSTROMS
REMARK 1 TITL 3 RESOLUTION
REMARK 1 REF NATURE V. 318 618 1985
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 6
REMARK 1 AUTH J.DEISENHOFER,O.EPP,K.MIKI,R.HUBER,H.MICHEL
REMARK 1 TITL X-RAY STRUCTURE ANALYSIS OF A MEMBRANE PROTEIN COMPLEX.
REMARK 1 TITL 2 ELECTRON DENSITY MAP AT 3 A RESOLUTION AND A MODEL OF THE
REMARK 1 TITL 3 CHROMOPHORES OF THE PHOTOSYNTHETIC REACTION CENTER FROM
REMARK 1 TITL 4 RHODOPSEUDOMONAS VIRIDIS
REMARK 1 REF J.MOL.BIOL. V. 180 385 1984
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 7
REMARK 1 AUTH H.MICHEL
REMARK 1 TITL THREE-DIMENSIONAL CRYSTALS OF A MEMBRANE PROTEIN COMPLEX.
REMARK 1 TITL 2 THE PHOTOSYNTHETIC REACTION CENTRE FROM RHODOPSEUDOMONAS
REMARK 1 TITL 3 VIRIDIS
REMARK 1 REF J.MOL.BIOL. V. 158 567 1982
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
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) (%) : 78.5
REMARK 3 NUMBER OF REFLECTIONS : 92322
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : A POSTERIORI
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9237
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 : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 57.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7493
REMARK 3 BIN R VALUE (WORKING SET) : 0.2960
REMARK 3 BIN FREE R VALUE : 0.3360
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 854
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9342
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 785
REMARK 3 SOLVENT ATOMS : 343
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.40
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) : 0.26
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) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 2.220
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) : 1.500 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.000 ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.000 ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.500 ; 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 : PARHCSDX_TEST.PRO
REMARK 3 PARAMETER FILE 2 : PARAM19.ION
REMARK 3 PARAMETER FILE 3 : PARHCSDX_IUB.RCV
REMARK 3 PARAMETER FILE 4 : PARAM19.SOL, PARHCSDX.TRZ
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH19.ION
REMARK 3 TOPOLOGY FILE 3 : TOPHCSDX_IUB.RCV
REMARK 3 TOPOLOGY FILE 4 : TOPH19.SOL, TOPHCSDX.TRZ
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: N(OBS)/N(PAR) = 2.20
REMARK 4
REMARK 4 5PRC 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_1000179759.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : SEP-93
REMARK 200 TEMPERATURE (KELVIN) : 263
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 6
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MPG/DESY, HAMBURG
REMARK 200 BEAMLINE : BW6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : TOROIDAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (ROTAVATA, AGROVATA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 96950
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 76.2
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : 0.07900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 48.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.60
REMARK 200 R MERGE FOR SHELL (I) : 0.28200
REMARK 200 R SYM FOR SHELL (I) : 0.28200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER / SA
REMARK 200 OMIT MAPS
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: PDB ENTRY 6PRC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 56.80000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 111.75000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 111.75000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 85.20000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 111.75000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 111.75000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 28.40000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 111.75000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 111.75000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 85.20000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 111.75000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 111.75000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 28.40000
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 56.80000
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: 49460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -417.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, L, M, H
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH H1094 LIES ON A SPECIAL POSITION.
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 C 333
REMARK 465 ALA C 334
REMARK 465 ALA C 335
REMARK 465 LYS C 336
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS C 332 CG CD CE NZ
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 PRO H 46
REMARK 475 LEU H 47
REMARK 475 GLY H 48
REMARK 475 LEU H 49
REMARK 475 VAL H 50
REMARK 475 LYS H 51
REMARK 475 LEU H 52
REMARK 475 ALA H 53
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS C 32 CD CE NZ
REMARK 480 LYS C 46 CD CE NZ
REMARK 480 GLU C 48 CG CD OE1 OE2
REMARK 480 GLN C 54 CD OE1 NE2
REMARK 480 LYS C 57 CD CE NZ
REMARK 480 LYS C 60 CD CE NZ
REMARK 480 ASN C 64 OD1 ND2
REMARK 480 GLU C 93 CD OE1 OE2
REMARK 480 ASN C 94 OD1 ND2
REMARK 480 GLN C 127 CD OE1 NE2
REMARK 480 THR C 159 CB OG1 CG2
REMARK 480 ARG C 165 NH1 NH2
REMARK 480 ARG C 169 CD NE CZ NH1 NH2
REMARK 480 LYS C 198 CD CE NZ
REMARK 480 ARG C 199 CZ NH1 NH2
REMARK 480 LYS C 218 CD CE NZ
REMARK 480 LYS C 323 CE NZ
REMARK 480 ILE L 17 CD1
REMARK 480 PRO L 57 O
REMARK 480 LYS L 72 CE NZ
REMARK 480 ASP L 202 OD1 OD2
REMARK 480 LYS L 205 CD CE NZ
REMARK 480 ILE L 269 CD1
REMARK 480 PHE L 271 CD1 CD2 CE1 CE2 CZ
REMARK 480 GLU M 22 CD OE1 OE2
REMARK 480 ASP M 25 OD1 OD2
REMARK 480 ASN M 26 OD1 ND2
REMARK 480 LYS M 31 CG CD CE NZ
REMARK 480 ILE M 104 CD1
REMARK 480 ARG M 136 NH1 NH2
REMARK 480 LYS M 298 NZ
REMARK 480 LYS M 323 CG CD CE NZ
REMARK 480 GLN H 8 CB CG CD OE1 NE2
REMARK 480 HIS H 9 CG ND1 CD2 CE1 NE2
REMARK 480 GLU H 45 C O CG CD OE1 OE2
REMARK 480 GLU H 55 CD OE1 OE2
REMARK 480 ARG H 81 CD NE CZ NH1 NH2
REMARK 480 THR H 85 CB OG1 CG2
REMARK 480 GLU H 87 CG CD OE1 OE2
REMARK 480 LYS H 89 CD CE NZ
REMARK 480 GLN H 92 CD OE1 NE2
REMARK 480 ASP H 94 CB CG OD1 OD2
REMARK 480 GLU H 97 OE1 OE2
REMARK 480 LYS H 131 CE NZ
REMARK 480 GLU H 147 CG CD OE1 OE2
REMARK 480 LYS H 205 CD CE NZ
REMARK 480 LYS H 207 NZ
REMARK 480 GLU H 216 CD OE1 OE2
REMARK 480 ARG H 223 NH1 NH2
REMARK 480 GLN H 225 OE1 NE2
REMARK 480 ARG H 227 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU M 318 O - C - N ANGL. DEV. = 11.7 DEGREES
REMARK 500 ALA H 53 CB - CA - C ANGL. DEV. = -15.9 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 TYR C 38 107.94 -48.10
REMARK 500 ALA C 43 140.70 -33.85
REMARK 500 ASN C 58 47.99 -108.43
REMARK 500 ALA C 126 -131.67 55.72
REMARK 500 ASN C 186 43.15 -86.95
REMARK 500 TRP C 256 -153.81 -111.82
REMARK 500 LEU C 285 0.59 -65.24
REMARK 500 ASP C 304 -154.92 -126.46
REMARK 500 ASP L 23 79.16 -68.07
REMARK 500 VAL L 31 -87.86 -93.85
REMARK 500 LEU L 165 -59.70 62.36
REMARK 500 ASP L 202 -126.33 42.11
REMARK 500 LYS L 207 -157.66 -86.50
REMARK 500 LEU M 51 -110.79 -71.99
REMARK 500 CYS M 160 -60.01 -122.35
REMARK 500 ASN M 193 96.12 82.04
REMARK 500 ASP M 238 78.86 -153.19
REMARK 500 ARG M 239 125.47 -35.72
REMARK 500 PRO M 319 106.61 -54.59
REMARK 500 PRO M 322 -171.34 -56.10
REMARK 500 HIS H 9 36.14 -151.83
REMARK 500 TYR H 31 -75.89 -99.94
REMARK 500 PRO H 46 -173.96 -65.99
REMARK 500 LEU H 52 -3.95 -141.65
REMARK 500 PRO H 54 71.54 -65.76
REMARK 500 ASP H 94 -144.03 -123.99
REMARK 500 ASP H 142 4.26 -68.88
REMARK 500 HIS H 178 62.45 62.78
REMARK 500 ALA H 191 60.31 -113.04
REMARK 500 SER H 256 124.96 -33.88
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 C 15 0.09 SIDE CHAIN
REMARK 500 PHE C 190 0.08 SIDE CHAIN
REMARK 500 TYR C 227 0.10 SIDE CHAIN
REMARK 500 ARG C 272 0.08 SIDE CHAIN
REMARK 500 TYR C 325 0.06 SIDE CHAIN
REMARK 500 TYR L 51 0.13 SIDE CHAIN
REMARK 500 TYR L 148 0.07 SIDE CHAIN
REMARK 500 TYR L 164 0.07 SIDE CHAIN
REMARK 500 HIS L 230 0.10 SIDE CHAIN
REMARK 500 ARG M 28 0.08 SIDE CHAIN
REMARK 500 TYR M 208 0.06 SIDE CHAIN
REMARK 500 TYR H 18 0.10 SIDE CHAIN
REMARK 500 ARG H 34 0.08 SIDE CHAIN
REMARK 500 TYR H 64 0.08 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 TRP C 121 -10.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 LDA L 705
REMARK 615 BPB M 401
REMARK 615 NS5 M 600
REMARK 615 LDA M 706
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 337 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET C 74 SD
REMARK 620 2 HEM C 337 NA 89.0
REMARK 620 3 HEM C 337 NB 92.2 90.9
REMARK 620 4 HEM C 337 NC 93.3 177.3 90.3
REMARK 620 5 HEM C 337 ND 86.7 88.5 178.8 90.3
REMARK 620 6 HIS C 91 NE2 175.4 90.5 92.4 87.1 88.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 338 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET C 110 SD
REMARK 620 2 HEM C 338 NA 88.4
REMARK 620 3 HEM C 338 NB 88.0 94.6
REMARK 620 4 HEM C 338 NC 91.3 179.7 85.3
REMARK 620 5 HEM C 338 ND 88.7 89.0 174.9 91.0
REMARK 620 6 HIS C 136 NE2 175.8 87.4 92.1 92.9 91.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 340 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 124 NE2
REMARK 620 2 HEM C 340 NA 87.6
REMARK 620 3 HEM C 340 NB 89.8 90.7
REMARK 620 4 HEM C 340 NC 91.2 177.9 87.5
REMARK 620 5 HEM C 340 ND 86.6 90.6 176.1 91.1
REMARK 620 6 HIS C 309 NE2 177.7 90.1 90.0 91.1 93.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 339 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET C 233 SD
REMARK 620 2 HEM C 339 NA 89.7
REMARK 620 3 HEM C 339 NB 85.1 91.2
REMARK 620 4 HEM C 339 NC 91.7 178.4 89.7
REMARK 620 5 HEM C 339 ND 90.6 87.5 175.6 91.7
REMARK 620 6 HIS C 248 NE2 175.2 85.9 92.9 92.7 91.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 BCB L 304 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS L 153 NE2
REMARK 620 2 BCB L 304 NA 97.7
REMARK 620 3 BCB L 304 NB 98.4 90.6
REMARK 620 4 BCB L 304 NC 93.3 168.5 91.3
REMARK 620 5 BCB L 304 ND 96.2 87.6 165.5 87.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 BCB L 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS L 173 NE2
REMARK 620 2 BCB L 302 NA 86.3
REMARK 620 3 BCB L 302 NB 87.2 90.9
REMARK 620 4 BCB L 302 NC 104.3 169.3 91.0
REMARK 620 5 BCB L 302 ND 99.8 89.2 173.0 87.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 M 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS L 190 NE2
REMARK 620 2 HIS L 230 NE2 87.2
REMARK 620 3 HIS M 217 NE2 110.1 91.6
REMARK 620 4 GLU M 232 OE2 148.1 81.7 100.0
REMARK 620 5 GLU M 232 OE1 94.4 96.2 154.7 57.7
REMARK 620 6 HIS M 264 NE2 90.3 174.7 84.9 102.8 88.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 BCB M 805 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS M 180 NE2
REMARK 620 2 BCB M 805 NA 93.4
REMARK 620 3 BCB M 805 NB 98.8 89.4
REMARK 620 4 BCB M 805 NC 99.2 167.1 91.1
REMARK 620 5 BCB M 805 ND 94.6 89.5 166.6 87.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 BCB M 806 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS M 200 NE2
REMARK 620 2 BCB M 806 NA 97.5
REMARK 620 3 BCB M 806 NB 96.9 90.0
REMARK 620 4 BCB M 806 NC 95.4 166.8 91.5
REMARK 620 5 BCB M 806 ND 96.4 88.1 166.7 87.5
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 FE2 M 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 M 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 M 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 M 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCB M 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCB L 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCB M 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCB L 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BPB M 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BPB L 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MQ7 M 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 337
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 338
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 339
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 340
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NS5 M 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATZ L 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA H 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA L 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA H 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA M 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA L 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA M 706
DBREF 5PRC C 1 336 UNP P07173 CYCR_RHOVI 21 356
DBREF 5PRC L 1 273 UNP P06009 RCEL_RHOVI 1 273
DBREF 5PRC M 1 323 UNP P06010 RCEM_RHOVI 1 323
DBREF 5PRC H 2 258 UNP P06008 RCEH_RHOVI 2 258
SEQRES 1 C 336 CYS PHE GLU PRO PRO PRO ALA THR THR THR GLN THR GLY
SEQRES 2 C 336 PHE ARG GLY LEU SER MET GLY GLU VAL LEU HIS PRO ALA
SEQRES 3 C 336 THR VAL LYS ALA LYS LYS GLU ARG ASP ALA GLN TYR PRO
SEQRES 4 C 336 PRO ALA LEU ALA ALA VAL LYS ALA GLU GLY PRO PRO VAL
SEQRES 5 C 336 SER GLN VAL TYR LYS ASN VAL LYS VAL LEU GLY ASN LEU
SEQRES 6 C 336 THR GLU ALA GLU PHE LEU ARG THR MET THR ALA ILE THR
SEQRES 7 C 336 GLU TRP VAL SER PRO GLN GLU GLY CYS THR TYR CYS HIS
SEQRES 8 C 336 ASP GLU ASN ASN LEU ALA SER GLU ALA LYS TYR PRO TYR
SEQRES 9 C 336 VAL VAL ALA ARG ARG MET LEU GLU MET THR ARG ALA ILE
SEQRES 10 C 336 ASN THR ASN TRP THR GLN HIS VAL ALA GLN THR GLY VAL
SEQRES 11 C 336 THR CYS TYR THR CYS HIS ARG GLY THR PRO LEU PRO PRO
SEQRES 12 C 336 TYR VAL ARG TYR LEU GLU PRO THR LEU PRO LEU ASN ASN
SEQRES 13 C 336 ARG GLU THR PRO THR HIS VAL GLU ARG VAL GLU THR ARG
SEQRES 14 C 336 SER GLY TYR VAL VAL ARG LEU ALA LYS TYR THR ALA TYR
SEQRES 15 C 336 SER ALA LEU ASN TYR ASP PRO PHE THR MET PHE LEU ALA
SEQRES 16 C 336 ASN ASP LYS ARG GLN VAL ARG VAL VAL PRO GLN THR ALA
SEQRES 17 C 336 LEU PRO LEU VAL GLY VAL SER ARG GLY LYS GLU ARG ARG
SEQRES 18 C 336 PRO LEU SER ASP ALA TYR ALA THR PHE ALA LEU MET MET
SEQRES 19 C 336 SER ILE SER ASP SER LEU GLY THR ASN CYS THR PHE CYS
SEQRES 20 C 336 HIS ASN ALA GLN THR PHE GLU SER TRP GLY LYS LYS SER
SEQRES 21 C 336 THR PRO GLN ARG ALA ILE ALA TRP TRP GLY ILE ARG MET
SEQRES 22 C 336 VAL ARG ASP LEU ASN MET ASN TYR LEU ALA PRO LEU ASN
SEQRES 23 C 336 ALA SER LEU PRO ALA SER ARG LEU GLY ARG GLN GLY GLU
SEQRES 24 C 336 ALA PRO GLN ALA ASP CYS ARG THR CYS HIS GLN GLY VAL
SEQRES 25 C 336 THR LYS PRO LEU PHE GLY ALA SER ARG LEU LYS ASP TYR
SEQRES 26 C 336 PRO GLU LEU GLY PRO ILE LYS ALA ALA ALA LYS
SEQRES 1 L 273 ALA LEU LEU SER PHE GLU ARG LYS TYR ARG VAL ARG GLY
SEQRES 2 L 273 GLY THR LEU ILE GLY GLY ASP LEU PHE ASP PHE TRP VAL
SEQRES 3 L 273 GLY PRO TYR PHE VAL GLY PHE PHE GLY VAL SER ALA ILE
SEQRES 4 L 273 PHE PHE ILE PHE LEU GLY VAL SER LEU ILE GLY TYR ALA
SEQRES 5 L 273 ALA SER GLN GLY PRO THR TRP ASP PRO PHE ALA ILE SER
SEQRES 6 L 273 ILE ASN PRO PRO ASP LEU LYS TYR GLY LEU GLY ALA ALA
SEQRES 7 L 273 PRO LEU LEU GLU GLY GLY PHE TRP GLN ALA ILE THR VAL
SEQRES 8 L 273 CYS ALA LEU GLY ALA PHE ILE SER TRP MET LEU ARG GLU
SEQRES 9 L 273 VAL GLU ILE SER ARG LYS LEU GLY ILE GLY TRP HIS VAL
SEQRES 10 L 273 PRO LEU ALA PHE CYS VAL PRO ILE PHE MET PHE CYS VAL
SEQRES 11 L 273 LEU GLN VAL PHE ARG PRO LEU LEU LEU GLY SER TRP GLY
SEQRES 12 L 273 HIS ALA PHE PRO TYR GLY ILE LEU SER HIS LEU ASP TRP
SEQRES 13 L 273 VAL ASN ASN PHE GLY TYR GLN TYR LEU ASN TRP HIS TYR
SEQRES 14 L 273 ASN PRO GLY HIS MET SER SER VAL SER PHE LEU PHE VAL
SEQRES 15 L 273 ASN ALA MET ALA LEU GLY LEU HIS GLY GLY LEU ILE LEU
SEQRES 16 L 273 SER VAL ALA ASN PRO GLY ASP GLY ASP LYS VAL LYS THR
SEQRES 17 L 273 ALA GLU HIS GLU ASN GLN TYR PHE ARG ASP VAL VAL GLY
SEQRES 18 L 273 TYR SER ILE GLY ALA LEU SER ILE HIS ARG LEU GLY LEU
SEQRES 19 L 273 PHE LEU ALA SER ASN ILE PHE LEU THR GLY ALA PHE GLY
SEQRES 20 L 273 THR ILE ALA SER GLY PRO PHE TRP THR ARG GLY TRP PRO
SEQRES 21 L 273 GLU TRP TRP GLY TRP TRP LEU ASP ILE PRO PHE TRP SER
SEQRES 1 M 323 ALA ASP TYR GLN THR ILE TYR THR GLN ILE GLN ALA ARG
SEQRES 2 M 323 GLY PRO HIS ILE THR VAL SER GLY GLU TRP GLY ASP ASN
SEQRES 3 M 323 ASP ARG VAL GLY LYS PRO PHE TYR SER TYR TRP LEU GLY
SEQRES 4 M 323 LYS ILE GLY ASP ALA GLN ILE GLY PRO ILE TYR LEU GLY
SEQRES 5 M 323 ALA SER GLY ILE ALA ALA PHE ALA PHE GLY SER THR ALA
SEQRES 6 M 323 ILE LEU ILE ILE LEU PHE ASN MET ALA ALA GLU VAL HIS
SEQRES 7 M 323 PHE ASP PRO LEU GLN PHE PHE ARG GLN PHE PHE TRP LEU
SEQRES 8 M 323 GLY LEU TYR PRO PRO LYS ALA GLN TYR GLY MET GLY ILE
SEQRES 9 M 323 PRO PRO LEU HIS ASP GLY GLY TRP TRP LEU MET ALA GLY
SEQRES 10 M 323 LEU PHE MET THR LEU SER LEU GLY SER TRP TRP ILE ARG
SEQRES 11 M 323 VAL TYR SER ARG ALA ARG ALA LEU GLY LEU GLY THR HIS
SEQRES 12 M 323 ILE ALA TRP ASN PHE ALA ALA ALA ILE PHE PHE VAL LEU
SEQRES 13 M 323 CYS ILE GLY CYS ILE HIS PRO THR LEU VAL GLY SER TRP
SEQRES 14 M 323 SER GLU GLY VAL PRO PHE GLY ILE TRP PRO HIS ILE ASP
SEQRES 15 M 323 TRP LEU THR ALA PHE SER ILE ARG TYR GLY ASN PHE TYR
SEQRES 16 M 323 TYR CYS PRO TRP HIS GLY PHE SER ILE GLY PHE ALA TYR
SEQRES 17 M 323 GLY CYS GLY LEU LEU PHE ALA ALA HIS GLY ALA THR ILE
SEQRES 18 M 323 LEU ALA VAL ALA ARG PHE GLY GLY ASP ARG GLU ILE GLU
SEQRES 19 M 323 GLN ILE THR ASP ARG GLY THR ALA VAL GLU ARG ALA ALA
SEQRES 20 M 323 LEU PHE TRP ARG TRP THR ILE GLY PHE ASN ALA THR ILE
SEQRES 21 M 323 GLU SER VAL HIS ARG TRP GLY TRP PHE PHE SER LEU MET
SEQRES 22 M 323 VAL MET VAL SER ALA SER VAL GLY ILE LEU LEU THR GLY
SEQRES 23 M 323 THR PHE VAL ASP ASN TRP TYR LEU TRP CYS VAL LYS HIS
SEQRES 24 M 323 GLY ALA ALA PRO ASP TYR PRO ALA TYR LEU PRO ALA THR
SEQRES 25 M 323 PRO ASP PRO ALA SER LEU PRO GLY ALA PRO LYS
SEQRES 1 H 258 FME TYR HIS GLY ALA LEU ALA GLN HIS LEU ASP ILE ALA
SEQRES 2 H 258 GLN LEU VAL TRP TYR ALA GLN TRP LEU VAL ILE TRP THR
SEQRES 3 H 258 VAL VAL LEU LEU TYR LEU ARG ARG GLU ASP ARG ARG GLU
SEQRES 4 H 258 GLY TYR PRO LEU VAL GLU PRO LEU GLY LEU VAL LYS LEU
SEQRES 5 H 258 ALA PRO GLU ASP GLY GLN VAL TYR GLU LEU PRO TYR PRO
SEQRES 6 H 258 LYS THR PHE VAL LEU PRO HIS GLY GLY THR VAL THR VAL
SEQRES 7 H 258 PRO ARG ARG ARG PRO GLU THR ARG GLU LEU LYS LEU ALA
SEQRES 8 H 258 GLN THR ASP GLY PHE GLU GLY ALA PRO LEU GLN PRO THR
SEQRES 9 H 258 GLY ASN PRO LEU VAL ASP ALA VAL GLY PRO ALA SER TYR
SEQRES 10 H 258 ALA GLU ARG ALA GLU VAL VAL ASP ALA THR VAL ASP GLY
SEQRES 11 H 258 LYS ALA LYS ILE VAL PRO LEU ARG VAL ALA THR ASP PHE
SEQRES 12 H 258 SER ILE ALA GLU GLY ASP VAL ASP PRO ARG GLY LEU PRO
SEQRES 13 H 258 VAL VAL ALA ALA ASP GLY VAL GLU ALA GLY THR VAL THR
SEQRES 14 H 258 ASP LEU TRP VAL ASP ARG SER GLU HIS TYR PHE ARG TYR
SEQRES 15 H 258 LEU GLU LEU SER VAL ALA GLY SER ALA ARG THR ALA LEU
SEQRES 16 H 258 ILE PRO LEU GLY PHE CYS ASP VAL LYS LYS ASP LYS ILE
SEQRES 17 H 258 VAL VAL THR SER ILE LEU SER GLU GLN PHE ALA ASN VAL
SEQRES 18 H 258 PRO ARG LEU GLN SER ARG ASP GLN ILE THR LEU ARG GLU
SEQRES 19 H 258 GLU ASP LYS VAL SER ALA TYR TYR ALA GLY GLY LEU LEU
SEQRES 20 H 258 TYR ALA THR PRO GLU ARG ALA GLU SER LEU LEU
MODRES 5PRC FME H 1 MET N-FORMYLMETHIONINE
HET FME H 1 10
HET HEM C 337 43
HET HEM C 338 43
HET HEM C 339 43
HET HEM C 340 43
HET BCB L 302 66
HET BCB L 304 66
HET BPB L 402 65
HET ATZ L 502 14
HET LDA L 702 16
HET LDA L 705 16
HET FE2 M 500 1
HET SO4 M 802 5
HET SO4 M 803 5
HET SO4 M 804 5
HET BCB M 805 66
HET BCB M 806 66
HET BPB M 401 65
HET MQ7 M 501 48
HET NS5 M 600 40
HET LDA M 704 16
HET LDA M 706 16
HET SO4 H 801 5
HET LDA H 701 16
HET LDA H 703 16
HETNAM FME N-FORMYLMETHIONINE
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM BCB BACTERIOCHLOROPHYLL B
HETNAM BPB BACTERIOPHEOPHYTIN B
HETNAM ATZ 2-CHLORO-4-ISOPROPYLAMINO-6-ETHYLAMINO -1,3,5-TRIAZINE
HETNAM LDA LAURYL DIMETHYLAMINE-N-OXIDE
HETNAM FE2 FE (II) ION
HETNAM SO4 SULFATE ION
HETNAM MQ7 MENAQUINONE-7
HETNAM NS5 15-CIS-1,2-DIHYDRONEUROSPORENE
HETSYN HEM HEME
HETSYN ATZ ATRAZINE
FORMUL 4 FME C6 H11 N O3 S
FORMUL 5 HEM 4(C34 H32 FE N4 O4)
FORMUL 9 BCB 4(C55 H72 MG N4 O6 2+)
FORMUL 11 BPB 2(C55 H74 N4 O6)
FORMUL 12 ATZ C8 H14 CL N5
FORMUL 13 LDA 6(C14 H31 N O)
FORMUL 15 FE2 FE 2+
FORMUL 16 SO4 4(O4 S 2-)
FORMUL 22 MQ7 C46 H64 O2
FORMUL 23 NS5 C40 H60
FORMUL 29 HOH *343(H2 O)
HELIX 1 1 PRO C 25 GLN C 37 1N-TERMINAL HELIX 13
HELIX 2 3 GLU C 67 TRP C 80 1ASSOCIATED WITH HEME 1 14
HELIX 3 5 TYR C 102 ASN C 120 1ASSOCIATED WITH HEME 2 19
HELIX 4 7 CYS C 132 HIS C 136 1HEME 2 ATTACHMENT SITE 5
HELIX 5 8 ARG C 169 TYR C 179 5 11
HELIX 6 9 PRO C 189 PHE C 193 1 5
HELIX 7 11 LEU C 223 LEU C 240 5ASSOCIATED WITH HEME 3 18
HELIX 8 15 PRO C 262 ASN C 280 1ASSOCIATED WITH HEME 4 19
HELIX 9 16 ALA C 283 ALA C 287 5 5
HELIX 10 18 CYS C 305 HIS C 309 1HEME 4 ATTACHMENT SITE 5
HELIX 11 22 GLY L 32 GLN L 55 1TRANSMEMBRANE HELIX LA 24
HELIX 12 25 GLY L 84 LEU L 111 1TRANSMEMBRANE HELIX LB 28
HELIX 13 26 HIS L 116 LEU L 139 1TRANSMEMBRANE HELIX LC 24
HELIX 14 29 SER L 152 TYR L 164 1PERIPLASMIC HELIX LCD 13
HELIX 15 31 PRO L 171 ALA L 198 1TRANSMEMBRANE HELIX LD 28
HELIX 16 32 ALA L 209 VAL L 220 1CYTOPLASMIC HELIX LDE 12
HELIX 17 33 ALA L 226 PRO L 253 1TRANSMEMBRANE HELIX LE 28
HELIX 18 34 TRP L 259 LEU L 267 1PERIPLASMIC C-TERMINAL 9
HELIX 19 37 ALA M 53 VAL M 77 1TRANSMEMBRANE HELIX MA 25
HELIX 20 38 PRO M 81 ARG M 86 1PERIPLASMIC HELIX MAB 6
HELIX 21 41 GLY M 111 LEU M 138 1TRANSMEMBRANE HELIX MB 28
HELIX 22 42 HIS M 143 VAL M 166 1TRANSMEMBRANE HELIX MC 24
HELIX 23 45 ILE M 177 ARG M 190 1PERIPLASMIC HELIX MCD 14
HELIX 24 47 PRO M 198 PHE M 227 1TRANSMEMBRANE HELIX MD 30
HELIX 25 48 GLU M 232 THR M 237 1CYTOPLASMIC HELIX 6
HELIX 26 49 THR M 241 ILE M 254 1CYTOPLASMIC HELIX MDE 14
HELIX 27 50 SER M 262 LEU M 284 1TRANSMEMBRANE HELIX ME 23
HELIX 28 51 TRP M 292 HIS M 299 1PERIPLASMIC C-TERMINAL 8
HELIX 29 53 ILE H 12 LEU H 30 1TRANSMEMBRANE HELIX 19
HELIX 30 54 LEU H 32 ARG H 37 1PI-HELICAL EXTENSION OF TM 6
HELIX 31 55 ASP H 56 TYR H 60 1SHORT HELIX 5
HELIX 32 56 PRO H 107 ASP H 110 1SHORT HELIX 4
HELIX 33 59 SER H 215 ASN H 220 5SHORT HELIX 6
HELIX 34 60 LEU H 232 TYR H 248 1C-TERMINAL HELIX 17
SHEET 1 A 2 ALA C 7 THR C 9 0
SHEET 2 A 2 VAL C 22 HIS C 24 -1 N LEU C 23 O THR C 8
SHEET 1 B 2 LYS H 66 VAL H 69 0
SHEET 2 B 2 THR H 75 VAL H 78 -1 N VAL H 78 O LYS H 66
SHEET 1 C 2 LEU H 90 GLN H 92 0
SHEET 2 C 2 LEU H 101 PRO H 103 -1 N GLN H 102 O ALA H 91
SHEET 1 D 4 ILE H 134 PRO H 136 0
SHEET 2 D 4 GLY H 166 ASP H 174 -1 N VAL H 173 O VAL H 135
SHEET 3 D 4 TYR H 182 VAL H 187 -1 N SER H 186 O THR H 167
SHEET 4 D 4 THR H 193 PRO H 197 -1 N ILE H 196 O LEU H 183
SHEET 1 E 2 CYS H 201 VAL H 203 0
SHEET 2 E 2 ILE H 208 VAL H 210 -1 N VAL H 209 O ASP H 202
SHEET 1 F 2 PRO H 156 VAL H 158 0
SHEET 2 F 2 GLU H 164 THR H 167 -1 N GLY H 166 O VAL H 157
LINK SG CYS C 87 CAB HEM C 337 1555 1555 1.75
LINK SG CYS C 90 CAC HEM C 337 1555 1555 1.79
LINK SG CYS C 132 CAB HEM C 338 1555 1555 1.81
LINK SG CYS C 135 CAC HEM C 338 1555 1555 1.78
LINK SG CYS C 244 CAB HEM C 339 1555 1555 1.77
LINK SG CYS C 247 CAC HEM C 339 1555 1555 1.79
LINK SG CYS C 305 CAB HEM C 340 1555 1555 1.76
LINK SG CYS C 308 CAC HEM C 340 1555 1555 1.76
LINK C FME H 1 N TYR H 2 1555 1555 1.33
LINK SD MET C 74 FE HEM C 337 1555 1555 2.18
LINK NE2 HIS C 91 FE HEM C 337 1555 1555 1.90
LINK SD MET C 110 FE HEM C 338 1555 1555 2.16
LINK NE2 HIS C 124 FE HEM C 340 1555 1555 1.94
LINK NE2 HIS C 136 FE HEM C 338 1555 1555 1.97
LINK SD MET C 233 FE HEM C 339 1555 1555 2.09
LINK NE2 HIS C 248 FE HEM C 339 1555 1555 1.94
LINK NE2 HIS C 309 FE HEM C 340 1555 1555 1.98
LINK NE2 HIS L 153 MG BCB L 304 1555 1555 2.11
LINK NE2 HIS L 173 MG BCB L 302 1555 1555 2.04
LINK NE2 HIS L 190 FE FE2 M 500 1555 1555 1.86
LINK NE2 HIS L 230 FE FE2 M 500 1555 1555 2.25
LINK NE2 HIS M 180 MG BCB M 805 1555 1555 2.06
LINK NE2 HIS M 200 MG BCB M 806 1555 1555 2.06
LINK NE2 HIS M 217 FE FE2 M 500 1555 1555 2.00
LINK OE2 GLU M 232 FE FE2 M 500 1555 1555 1.99
LINK OE1 GLU M 232 FE FE2 M 500 1555 1555 2.45
LINK NE2 HIS M 264 FE FE2 M 500 1555 1555 2.10
CISPEP 1 PRO C 5 PRO C 6 0 -1.18
CISPEP 2 LEU C 152 PRO C 153 0 -16.13
CISPEP 3 GLY C 329 PRO C 330 0 7.41
CISPEP 4 GLY M 47 PRO M 48 0 -11.89
CISPEP 5 TYR H 41 PRO H 42 0 8.44
CISPEP 6 VAL H 78 PRO H 79 0 1.83
SITE 1 AC1 5 HIS L 190 HIS L 230 HIS M 217 GLU M 232
SITE 2 AC1 5 HIS M 264
SITE 1 AC2 7 ARG H 33 ARG H 37 TYR H 41 HOH H1059
SITE 2 AC2 7 HOH H1060 HOH H1061 ARG M 251
SITE 1 AC3 5 HOH H1224 ASN L 199 HOH L1127 HIS M 143
SITE 2 AC3 5 ARG M 265
SITE 1 AC4 4 LEU H 246 ALA M 1 ARG M 226 HOH M1226
SITE 1 AC5 8 TRP M 23 TYR M 50 ALA M 53 SER M 54
SITE 2 AC5 8 SER M 133 LDA M 704 HOH M1030 HOH M1064
SITE 1 AC6 19 HIS L 168 MET L 174 VAL L 177 SER L 178
SITE 2 AC6 19 VAL L 182 MET L 185 VAL L 220 BCB L 302
SITE 3 AC6 19 HOH L 993 MET M 120 VAL M 155 ILE M 177
SITE 4 AC6 19 TRP M 178 HIS M 180 ILE M 181 LEU M 184
SITE 5 AC6 19 BPB M 401 NS5 M 600 BCB M 806
SITE 1 AC7 20 PRO L 124 MET L 127 PHE L 128 VAL L 157
SITE 2 AC7 20 PHE L 160 GLY L 161 TRP L 167 HIS L 168
SITE 3 AC7 20 HIS L 173 SER L 176 VAL L 177 PHE L 241
SITE 4 AC7 20 GLY L 244 THR L 248 BCB L 304 BPB L 402
SITE 5 AC7 20 TYR M 195 TYR M 208 BCB M 805 BCB M 806
SITE 1 AC8 22 VAL L 157 TYR L 162 PHE L 181 BCB L 302
SITE 2 AC8 22 BCB L 304 PHE M 148 PHE M 154 VAL M 155
SITE 3 AC8 22 LEU M 184 PHE M 187 SER M 188 PHE M 194
SITE 4 AC8 22 TYR M 195 HIS M 200 SER M 203 ILE M 204
SITE 5 AC8 22 TYR M 208 MET M 275 ALA M 278 ILE M 282
SITE 6 AC8 22 BPB M 401 BCB M 805
SITE 1 AC9 15 PHE L 128 PHE L 146 ILE L 150 HIS L 153
SITE 2 AC9 15 LEU L 154 VAL L 157 BCB L 302 BPB L 402
SITE 3 AC9 15 GLY M 201 ILE M 204 GLY M 205 TYR M 208
SITE 4 AC9 15 GLY M 209 BCB M 806 HOH M 991
SITE 1 BC1 17 PHE L 181 MET L 185 LEU L 189 VAL L 220
SITE 2 BC1 17 PHE M 59 SER M 63 ILE M 66 SER M 123
SITE 3 BC1 17 LEU M 124 TRP M 127 ILE M 144 ASN M 147
SITE 4 BC1 17 PHE M 148 SER M 271 MET M 275 BCB M 805
SITE 5 BC1 17 BCB M 806
SITE 1 BC2 16 PHE L 97 TRP L 100 GLU L 104 VAL L 117
SITE 2 BC2 16 PHE L 121 PRO L 124 TYR L 148 HIS L 153
SITE 3 BC2 16 ALA L 237 BCB L 302 BCB L 304 TYR M 208
SITE 4 BC2 16 LEU M 212 TRP M 250 ILE M 254 MQ7 M 501
SITE 1 BC3 10 TYR L 29 BPB L 402 ALA M 216 HIS M 217
SITE 2 BC3 10 THR M 220 ALA M 246 TRP M 250 ALA M 258
SITE 3 BC3 10 VAL M 263 PHE M 270
SITE 1 BC4 21 TYR C 56 LYS C 57 ASN C 58 VAL C 59
SITE 2 BC4 21 LYS C 60 VAL C 61 LEU C 62 PHE C 70
SITE 3 BC4 21 LEU C 71 MET C 74 THR C 78 SER C 82
SITE 4 BC4 21 CYS C 87 CYS C 90 HIS C 91 LEU C 96
SITE 5 BC4 21 ALA C 97 TYR C 104 ALA C 107 ARG C 108
SITE 6 BC4 21 VAL C 212
SITE 1 BC5 16 TYR C 89 TYR C 102 VAL C 106 MET C 110
SITE 2 BC5 16 LEU C 111 MET C 113 THR C 114 CYS C 132
SITE 3 BC5 16 CYS C 135 HIS C 136 PRO C 140 LEU C 141
SITE 4 BC5 16 PRO C 142 LEU C 289 ARG C 293 PRO C 301
SITE 1 BC6 20 VAL C 201 ARG C 202 VAL C 203 VAL C 204
SITE 2 BC6 20 MET C 233 SER C 237 LEU C 240 ASN C 243
SITE 3 BC6 20 CYS C 244 CYS C 247 HIS C 248 PHE C 253
SITE 4 BC6 20 GLU C 254 ARG C 264 ALA C 267 TRP C 268
SITE 5 BC6 20 ARG C 272 HOH C 938 HOH C 940 HOH C 973
SITE 1 BC7 21 HIS C 124 THR C 128 GLY C 129 VAL C 130
SITE 2 BC7 21 ILE C 236 GLN C 263 ILE C 266 GLY C 270
SITE 3 BC7 21 ILE C 271 MET C 273 VAL C 274 ASP C 304
SITE 4 BC7 21 CYS C 305 CYS C 308 HIS C 309 THR C 313
SITE 5 BC7 21 LYS C 314 PRO C 315 HOH C 967 HOH C1203
SITE 6 BC7 21 HOH C1235
SITE 1 BC8 8 GLY M 117 THR M 121 GLY M 159 CYS M 160
SITE 2 BC8 8 VAL M 173 GLY M 176 HIS M 180 BCB M 805
SITE 1 BC9 8 GLU L 212 ASN L 213 PHE L 216 TYR L 222
SITE 2 BC9 8 SER L 223 ILE L 224 GLY L 225 ALA L 226
SITE 1 CC1 5 ARG H 33 PRO H 54 ASP H 56 LDA L 705
SITE 2 CC1 5 TRP M 266
SITE 1 CC2 6 ASP L 60 PHE L 62 TYR M 195 TRP M 295
SITE 2 CC2 6 CYS M 296 ALA M 301
SITE 1 CC3 7 PRO H 42 VAL H 59 TYR H 60 LEU H 62
SITE 2 CC3 7 TYR H 64 PRO H 65 ARG H 80
SITE 1 CC4 7 TRP M 23 ALA M 53 SER M 54 ALA M 57
SITE 2 CC4 7 SER M 126 SER M 133 SO4 M 804
SITE 1 CC5 3 LDA H 701 HOH H1060 PHE M 256
SITE 1 CC6 3 PHE M 71 ASN M 72 TRP M 112
CRYST1 223.500 223.500 113.600 90.00 90.00 90.00 P 43 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.004474 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004474 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008803 0.00000
(ATOM LINES ARE NOT SHOWN.)
END