HEADER ELECTRON TRANSPORT 08-DEC-09 3KZI
TITLE CRYSTAL STRUCTURE OF MONOMERIC FORM OF CYANOBACTERIAL PHOTOSYSTEM II
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOTOSYSTEM Q(B) PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 32 KDA THYLAKOID MEMBRANE PROTEIN 1, PHOTOSYSTEM II PROTEIN
COMPND 5 D1 1;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PHOTOSYSTEM II CORE LIGHT HARVESTING PROTEIN;
COMPND 8 CHAIN: B;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: PHOTOSYSTEM II CP43 PROTEIN;
COMPND 11 CHAIN: C;
COMPND 12 MOL_ID: 4;
COMPND 13 MOLECULE: PHOTOSYSTEM II D2 PROTEIN;
COMPND 14 CHAIN: D;
COMPND 15 SYNONYM: PHOTOSYSTEM II REACTION CENTER D2 PROTEIN, PSII D2 PROTEIN,
COMPND 16 PHOTOSYSTEM Q(A) PROTEIN;
COMPND 17 MOL_ID: 5;
COMPND 18 MOLECULE: CYTOCHROME B559 SUBUNIT ALPHA;
COMPND 19 CHAIN: E;
COMPND 20 SYNONYM: PSII REACTION CENTER SUBUNIT V;
COMPND 21 MOL_ID: 6;
COMPND 22 MOLECULE: CYTOCHROME B559 SUBUNIT BETA;
COMPND 23 CHAIN: F;
COMPND 24 SYNONYM: PSII REACTION CENTER SUBUNIT VI;
COMPND 25 MOL_ID: 7;
COMPND 26 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN H;
COMPND 27 CHAIN: H;
COMPND 28 SYNONYM: PSII-H;
COMPND 29 MOL_ID: 8;
COMPND 30 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN I;
COMPND 31 CHAIN: I;
COMPND 32 SYNONYM: PSII-I, PSII 4.4 KDA PROTEIN;
COMPND 33 MOL_ID: 9;
COMPND 34 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN J;
COMPND 35 CHAIN: J;
COMPND 36 SYNONYM: PSII-J;
COMPND 37 MOL_ID: 10;
COMPND 38 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN K;
COMPND 39 CHAIN: K;
COMPND 40 SYNONYM: PSII-K;
COMPND 41 MOL_ID: 11;
COMPND 42 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN L;
COMPND 43 CHAIN: L;
COMPND 44 SYNONYM: PSII-L, PSII 5 KDA PROTEIN;
COMPND 45 MOL_ID: 12;
COMPND 46 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN M;
COMPND 47 CHAIN: M;
COMPND 48 SYNONYM: PSII-M;
COMPND 49 MOL_ID: 13;
COMPND 50 MOLECULE: PHOTOSYSTEM II MANGANESE-STABILIZING POLYPEPTIDE;
COMPND 51 CHAIN: O;
COMPND 52 SYNONYM: MSP;
COMPND 53 MOL_ID: 14;
COMPND 54 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN T;
COMPND 55 CHAIN: T;
COMPND 56 SYNONYM: PSII-T, PSII-TC;
COMPND 57 MOL_ID: 15;
COMPND 58 MOLECULE: PHOTOSYSTEM II 12 KDA EXTRINSIC PROTEIN;
COMPND 59 CHAIN: U;
COMPND 60 SYNONYM: PS II COMPLEX 12 KDA EXTRINSIC PROTEIN, PSII-U;
COMPND 61 MOL_ID: 16;
COMPND 62 MOLECULE: CYTOCHROME C-550;
COMPND 63 CHAIN: V;
COMPND 64 SYNONYM: CYTOCHROME C550, LOW-POTENTIAL CYTOCHROME C, CYTOCHROME C-
COMPND 65 549;
COMPND 66 MOL_ID: 17;
COMPND 67 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN YCF12;
COMPND 68 CHAIN: y;
COMPND 69 SYNONYM: PROTEIN YCF12;
COMPND 70 MOL_ID: 18;
COMPND 71 MOLECULE: PHOTOSYSTEM II REACTION CENTER X PROTEIN;
COMPND 72 CHAIN: X;
COMPND 73 SYNONYM: PHOTOSYSTEM II PSBX PROTEIN;
COMPND 74 MOL_ID: 19;
COMPND 75 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN Z;
COMPND 76 CHAIN: Z;
COMPND 77 SYNONYM: PSII-Z
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 3 ORGANISM_TAXID: 197221;
SOURCE 4 STRAIN: BP-1;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 7 ORGANISM_TAXID: 197221;
SOURCE 8 STRAIN: BP-1;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 11 ORGANISM_TAXID: 197221;
SOURCE 12 STRAIN: BP-1;
SOURCE 13 MOL_ID: 4;
SOURCE 14 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 15 ORGANISM_TAXID: 197221;
SOURCE 16 STRAIN: BP-1;
SOURCE 17 MOL_ID: 5;
SOURCE 18 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 19 ORGANISM_TAXID: 197221;
SOURCE 20 STRAIN: BP-1;
SOURCE 21 MOL_ID: 6;
SOURCE 22 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 23 ORGANISM_TAXID: 197221;
SOURCE 24 STRAIN: BP-1;
SOURCE 25 MOL_ID: 7;
SOURCE 26 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 27 ORGANISM_TAXID: 197221;
SOURCE 28 STRAIN: BP-1;
SOURCE 29 MOL_ID: 8;
SOURCE 30 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 31 ORGANISM_TAXID: 197221;
SOURCE 32 STRAIN: BP-1;
SOURCE 33 MOL_ID: 9;
SOURCE 34 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 35 ORGANISM_TAXID: 197221;
SOURCE 36 STRAIN: BP-1;
SOURCE 37 MOL_ID: 10;
SOURCE 38 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 39 ORGANISM_TAXID: 197221;
SOURCE 40 STRAIN: BP-1;
SOURCE 41 MOL_ID: 11;
SOURCE 42 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 43 ORGANISM_TAXID: 197221;
SOURCE 44 STRAIN: BP-1;
SOURCE 45 MOL_ID: 12;
SOURCE 46 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 47 ORGANISM_TAXID: 197221;
SOURCE 48 STRAIN: BP-1;
SOURCE 49 MOL_ID: 13;
SOURCE 50 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 51 ORGANISM_TAXID: 197221;
SOURCE 52 STRAIN: BP-1;
SOURCE 53 MOL_ID: 14;
SOURCE 54 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 55 ORGANISM_TAXID: 197221;
SOURCE 56 STRAIN: BP-1;
SOURCE 57 MOL_ID: 15;
SOURCE 58 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 59 ORGANISM_TAXID: 197221;
SOURCE 60 STRAIN: BP-1;
SOURCE 61 MOL_ID: 16;
SOURCE 62 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 63 ORGANISM_TAXID: 197221;
SOURCE 64 STRAIN: BP-1;
SOURCE 65 MOL_ID: 17;
SOURCE 66 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 67 ORGANISM_TAXID: 197221;
SOURCE 68 STRAIN: BP-1;
SOURCE 69 MOL_ID: 18;
SOURCE 70 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 71 ORGANISM_TAXID: 197221;
SOURCE 72 STRAIN: BP-1;
SOURCE 73 MOL_ID: 19;
SOURCE 74 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 75 ORGANISM_TAXID: 197221;
SOURCE 76 STRAIN: BP-1
KEYWDS ELECTRON TRANSPORT PHOTOSYSTEM, PS II, PS2, MEMBRANE COMPLEX,
KEYWDS 2 TRANSMEMBRANE ALPHA-HELIX, IRON, METAL-BINDING, PHOTOSYNTHESIS,
KEYWDS 3 PHOTOSYSTEM II, THYLAKOID, HEME, REACTION CENTER, MANGANESE,
KEYWDS 4 ELECTRON TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR A.GABDULKHAKOV,A.GUSKOV,M.BROSER,J.KERN,A.ZOUNI,W.SAENGER
REVDAT 3 01-SEP-10 3KZI 1 JRNL
REVDAT 2 30-JUN-10 3KZI 1 JRNL
REVDAT 1 16-JUN-10 3KZI 0
JRNL AUTH M.BROSER,A.GABDULKHAKOV,J.KERN,A.GUSKOV,F.MUH,W.SAENGER,
JRNL AUTH 2 A.ZOUNI
JRNL TITL CRYSTAL STRUCTURE OF MONOMERIC PHOTOSYSTEM II FROM
JRNL TITL 2 THERMOSYNECHOCOCCUS ELONGATUS AT 3.6-A RESOLUTION
JRNL REF J.BIOL.CHEM. V. 285 26255 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20558739
JRNL DOI 10.1074/JBC.M110.127589
REMARK 2
REMARK 2 RESOLUTION. 3.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
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) : 3.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.500
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 11330360.960
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.2
REMARK 3 NUMBER OF REFLECTIONS : 47332
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) : 0.297
REMARK 3 FREE R VALUE : 0.308
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 946
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.83
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 71.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6144
REMARK 3 BIN R VALUE (WORKING SET) : 0.4540
REMARK 3 BIN FREE R VALUE : 0.4570
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 123
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.041
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 20318
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4360
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 162.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -16.38000
REMARK 3 B22 (A**2) : -5.03000
REMARK 3 B33 (A**2) : 21.41000
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) : 0.67
REMARK 3 ESD FROM SIGMAA (A) : 1.25
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) : 0.68
REMARK 3 ESD FROM C-V SIGMAA (A) : 1.07
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 2.10
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 18.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.22
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.140 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.010 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 6.700 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 7.620 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.30
REMARK 3 BSOL : 102.89
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : COF-NEW6.PARAM
REMARK 3 PARAMETER FILE 4 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 5 : MES.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : COF-NEW6.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : MES.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3KZI COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-DEC-09.
REMARK 100 THE RCSB ID CODE IS RCSB056642.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-FEB-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915
REMARK 200 MONOCHROMATOR : SI(311)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47417
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.2
REMARK 200 DATA REDUNDANCY : 4.110
REMARK 200 R MERGE (I) : 0.11200
REMARK 200 R SYM (I) : 0.07500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.3500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 68.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.24
REMARK 200 R MERGE FOR SHELL (I) : 0.47700
REMARK 200 R SYM FOR SHELL (I) : 0.63800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.340
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3BZ1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, PIPES, MES, CACL2, PH 7,
REMARK 280 BATCH, TEMPERATURE 291.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 168.64000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 168.64000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 59.94500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 112.34500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 59.94500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 112.34500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 168.64000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 59.94500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 112.34500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 168.64000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 59.94500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 112.34500
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 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: NONADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: NONADECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 68770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 104350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -457.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, H, I, J,
REMARK 350 AND CHAINS: K, L, M, O, T, U, V, y, X, Z
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 1
REMARK 465 THR A 2
REMARK 465 THR A 3
REMARK 465 THR A 4
REMARK 465 LEU A 5
REMARK 465 GLN A 6
REMARK 465 ARG A 7
REMARK 465 ARG A 8
REMARK 465 GLU A 9
REMARK 465 MET B 1
REMARK 465 SER B 487
REMARK 465 PRO B 488
REMARK 465 GLU B 489
REMARK 465 GLN B 490
REMARK 465 VAL B 491
REMARK 465 GLU B 492
REMARK 465 TRP B 493
REMARK 465 GLY B 494
REMARK 465 PHE B 495
REMARK 465 TYR B 496
REMARK 465 GLN B 497
REMARK 465 LYS B 498
REMARK 465 VAL B 499
REMARK 465 GLY B 500
REMARK 465 ASP B 501
REMARK 465 VAL B 502
REMARK 465 THR B 503
REMARK 465 THR B 504
REMARK 465 ARG B 505
REMARK 465 ARG B 506
REMARK 465 LYS B 507
REMARK 465 GLU B 508
REMARK 465 ALA B 509
REMARK 465 VAL B 510
REMARK 465 MET C 13
REMARK 465 VAL C 14
REMARK 465 THR C 15
REMARK 465 LEU C 16
REMARK 465 SER C 17
REMARK 465 SER C 18
REMARK 465 ASN C 19
REMARK 465 SER C 20
REMARK 465 ILE C 21
REMARK 465 PHE C 22
REMARK 465 ALA C 23
REMARK 465 THR C 24
REMARK 465 ASN C 25
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 ILE D 3
REMARK 465 ALA D 4
REMARK 465 ILE D 5
REMARK 465 GLY D 6
REMARK 465 ARG D 7
REMARK 465 ALA D 8
REMARK 465 PRO D 9
REMARK 465 ALA D 10
REMARK 465 GLU D 11
REMARK 465 ARG D 12
REMARK 465 ALA E 2
REMARK 465 GLY E 3
REMARK 465 THR E 4
REMARK 465 THR E 5
REMARK 465 GLY E 6
REMARK 465 GLU E 7
REMARK 465 THR F 2
REMARK 465 SER F 3
REMARK 465 ASN F 4
REMARK 465 THR F 5
REMARK 465 PRO F 6
REMARK 465 ASN F 7
REMARK 465 ASP I 36
REMARK 465 LEU I 37
REMARK 465 GLU I 38
REMARK 465 MET J 1
REMARK 465 MET J 2
REMARK 465 SER J 3
REMARK 465 GLU J 4
REMARK 465 GLY J 5
REMARK 465 GLY J 6
REMARK 465 SER M 35
REMARK 465 SER M 36
REMARK 465 ALA O 27
REMARK 465 LYS O 28
REMARK 465 GLN O 29
REMARK 465 LYS T 31
REMARK 465 LYS T 32
REMARK 465 ALA U 31
REMARK 465 THR U 32
REMARK 465 ALA U 33
REMARK 465 SER U 34
REMARK 465 THR U 35
REMARK 465 GLU U 36
REMARK 465 GLU U 37
REMARK 465 MET y 1
REMARK 465 GLY y 2
REMARK 465 ILE y 3
REMARK 465 PHE y 4
REMARK 465 ASN y 5
REMARK 465 GLY y 6
REMARK 465 ILE y 7
REMARK 465 ILE y 8
REMARK 465 GLU y 9
REMARK 465 PHE y 10
REMARK 465 LEU y 11
REMARK 465 SER y 12
REMARK 465 ASN y 13
REMARK 465 ILE y 14
REMARK 465 ASN y 15
REMARK 465 PHE y 16
REMARK 465 GLU y 17
REMARK 465 VAL y 18
REMARK 465 VAL X 46
REMARK 465 GLN X 47
REMARK 465 ARG X 48
REMARK 465 SER X 49
REMARK 465 LEU X 50
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 TYR C 143 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU C 462 CG CD OE1 OE2
REMARK 470 LYS H 20 CG CD CE NZ
REMARK 470 ARG O 53 CG CD NE CZ NH1 NH2
REMARK 470 GLU O 80 CG CD OE1 OE2
REMARK 470 LYS O 85 CG CD CE NZ
REMARK 470 ARG O 233 CG CD NE CZ NH1 NH2
REMARK 470 GLU V 41 CG CD OE1 OE2
REMARK 470 ARG y 43 CG CD NE CZ NH1 NH2
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 OXT ALA A 344 MN2 OEC A 368 1.58
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 B 484 C - N - CA ANGL. DEV. = 11.0 DEGREES
REMARK 500 LEU B 486 CA - CB - CG ANGL. DEV. = 16.1 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 12 105.64 128.38
REMARK 500 LEU A 13 -70.93 -32.43
REMARK 500 TRP A 97 19.72 -69.95
REMARK 500 GLN A 130 -6.12 -55.13
REMARK 500 TRP A 131 -60.41 -99.77
REMARK 500 PRO A 141 -119.35 -70.23
REMARK 500 TRP A 142 -18.05 45.73
REMARK 500 LEU A 159 -46.38 -138.50
REMARK 500 ILE A 176 -71.38 -56.08
REMARK 500 HIS A 215 -71.24 -45.09
REMARK 500 GLU A 226 8.50 -152.08
REMARK 500 GLU A 242 -60.41 -90.96
REMARK 500 ILE A 259 -80.43 -101.46
REMARK 500 PHE A 260 137.24 179.94
REMARK 500 GLN A 261 -64.01 -27.28
REMARK 500 TRP A 278 -71.10 -50.18
REMARK 500 PHE A 302 34.03 -96.42
REMARK 500 ARG A 334 -68.85 -27.10
REMARK 500 LEU A 343 58.99 -107.31
REMARK 500 VAL B 11 2.97 -60.93
REMARK 500 ILE B 13 -26.17 -37.96
REMARK 500 ASN B 14 64.74 -153.12
REMARK 500 ASP B 15 59.59 -147.11
REMARK 500 PRO B 16 -34.48 -33.38
REMARK 500 SER B 48 -19.19 -49.96
REMARK 500 ASP B 49 103.38 -160.55
REMARK 500 ASP B 119 52.22 -94.11
REMARK 500 ARG B 127 -78.81 -56.43
REMARK 500 SER B 177 179.05 178.01
REMARK 500 PRO B 183 -179.06 -50.17
REMARK 500 GLU B 184 101.47 -167.25
REMARK 500 ASP B 188 -0.45 -58.26
REMARK 500 LEU B 218 -68.55 -103.80
REMARK 500 LEU B 229 39.45 -80.21
REMARK 500 ARG B 230 47.31 16.58
REMARK 500 MET B 231 -179.20 -56.11
REMARK 500 GLU B 235 16.18 -67.21
REMARK 500 ALA B 261 -9.69 -59.24
REMARK 500 SER B 294 28.71 -75.28
REMARK 500 ASP B 313 41.15 -92.96
REMARK 500 LYS B 349 -48.32 -21.92
REMARK 500 PHE B 383 -69.44 -90.45
REMARK 500 PRO B 414 -65.28 -15.92
REMARK 500 GLU B 435 -76.00 -59.78
REMARK 500 THR B 436 -73.65 -21.43
REMARK 500 SER B 480 -19.63 75.80
REMARK 500 ILE B 482 -161.16 -119.43
REMARK 500 PRO B 484 -179.09 18.64
REMARK 500 GLU B 485 173.03 67.70
REMARK 500 GLN C 28 114.43 -163.92
REMARK 500
REMARK 500 THIS ENTRY HAS 213 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 TYR A 161 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 TYR U 72 22.9 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 OEC A 368
REMARK 610 DGD C 474
REMARK 610 LHG A 371
REMARK 610 SQD C 475
REMARK 610 LMG A 373
REMARK 610 LHG C 476
REMARK 610 DGD A 375
REMARK 610 LMG B 531
REMARK 610 DGD C 491
REMARK 610 DGD C 492
REMARK 610 LMG J 492
REMARK 610 LMG C 494
REMARK 610 LMG D 359
REMARK 610 LMG D 360
REMARK 610 SQD D 361
REMARK 610 DGD D 362
REMARK 610 LMT D 363
REMARK 610 SQD F 224
REMARK 610 DGD B 528
REMARK 610 LMG I 220
REMARK 610 LMG M 217
REMARK 610 SQD L 213
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 OEC A 368 MN1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 189 OE2
REMARK 620 2 HIS A 332 NE2 101.1
REMARK 620 3 ASP A 342 OD2 76.7 92.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM V 164 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS V 67 NE2
REMARK 620 2 HEM V 164 NA 84.1
REMARK 620 3 HEM V 164 NB 94.2 90.0
REMARK 620 4 HEM V 164 NC 94.9 178.0 91.7
REMARK 620 5 HEM V 164 ND 88.1 88.9 177.4 89.4
REMARK 620 6 HIS V 118 NE2 163.1 80.7 93.4 100.0 84.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 A 361 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 BCT D 353 O3
REMARK 620 2 HIS D 214 NE2 90.0
REMARK 620 3 HIS A 215 NE2 125.8 132.1
REMARK 620 4 HIS A 272 NE2 92.9 99.9 107.6
REMARK 620 5 HIS D 268 NE2 68.8 91.7 76.5 158.4
REMARK 620 6 BCT D 353 O2 53.9 143.9 78.7 83.6 76.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEC A 368 MN3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 354 OE2
REMARK 620 2 GLU A 333 OE1 78.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEC A 368 MN2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 342 OD1
REMARK 620 2 GLU C 354 OE1 75.2
REMARK 620 3 ALA A 344 O 116.0 124.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM F 85 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 23 NE2
REMARK 620 2 HEM F 85 NA 93.9
REMARK 620 3 HEM F 85 NB 104.4 88.7
REMARK 620 4 HEM F 85 NC 86.2 178.6 89.9
REMARK 620 5 HEM F 85 ND 78.0 92.5 177.2 88.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEC A 368 CA1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 189 OE1
REMARK 620 2 ALA A 344 O 133.0
REMARK 620 3 ASP A 170 OD1 140.6 78.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C 486 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C 39 OD1
REMARK 620 2 CLA C 486 NA 99.4
REMARK 620 3 CLA C 486 NB 76.2 88.7
REMARK 620 4 CLA C 486 NC 86.4 174.3 92.9
REMARK 620 5 CLA C 486 ND 108.8 87.0 173.8 91.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA K 56 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP K 19 OD2
REMARK 620 2 ASP K 23 OD1 151.7
REMARK 620 3 ASP K 23 OD2 132.7 43.5
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 361
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 362
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 363
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO A 365
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 366
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 367
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OEC A 368
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR A 369
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD C 474
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG A 371
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD C 475
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG A 373
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG C 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD A 375
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT A 376
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 522
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 523
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 524
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 525
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 526
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 527
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 529
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 530
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG B 531
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD B 533
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT B 535
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT D 536
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 478
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 479
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 480
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 481
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 482
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 483
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 484
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 485
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA K 483
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 486
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 487
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 488
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR C 489
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR C 490
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD C 491
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD C 492
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD C 493
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG J 492
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG C 494
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT D 353
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA D 354
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 364
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO D 355
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA D 356
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 D 357
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR D 358
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG D 359
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG D 360
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD D 361
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD D 362
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT D 363
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM F 85
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD F 224
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 225
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR X 107
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD B 528
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG I 220
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR J 115
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA K 56
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR J 112
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG M 217
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT T 226
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA O 273
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT I 274
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD L 213
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT O 274
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM V 164
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR Z 116
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3BZ1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CYANOBACTERIAL PHOTOSYSTEM II (PART 1
REMARK 900 OF 2). THIS FILE CONTAINS FIRST MONOMER OF PSII DIMER
REMARK 900 RELATED ID: 3BZ2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CYANOBACTERIAL PHOTOSYSTEM II (PART 2
REMARK 900 OF 2). THIS FILE CONTAINS SECOND MONOMER OF PSII DIMER
DBREF 3KZI A 1 344 UNP P0A444 PSBA1_THEEB 1 344
DBREF 3KZI B 1 510 UNP Q8DIQ1 Q8DIQ1_THEEB 1 510
DBREF 3KZI C 13 473 UNP Q8DIF8 Q8DIF8_THEEB 1 461
DBREF 3KZI D 1 352 UNP Q8CM25 PSBD_THEEB 1 352
DBREF 3KZI E 2 84 UNP Q8DIP0 PSBE_THEEB 2 84
DBREF 3KZI F 2 45 UNP Q8DIN9 PSBF_THEEB 2 45
DBREF 3KZI H 2 66 UNP Q8DJ43 PSBH_THEEB 2 66
DBREF 3KZI I 1 38 UNP Q8DJZ6 PSBI_THEEB 1 38
DBREF 3KZI J 1 40 UNP P59087 PSBJ_THEEB 1 40
DBREF 3KZI K 10 46 UNP Q9F1K9 PSBK_THEEB 10 46
DBREF 3KZI L 1 37 UNP Q8DIN8 PSBL_THEEB 1 37
DBREF 3KZI M 1 36 UNP Q8DHA7 PSBM_THEEB 1 36
DBREF 3KZI O 27 272 UNP P0A431 PSBO_THEEB 27 272
DBREF 3KZI T 1 32 UNP Q8DIQ0 PSBT_THEEB 1 32
DBREF 3KZI U 31 134 UNP Q9F1L5 PSBU_THEEB 31 134
DBREF 3KZI V 27 163 UNP P0A386 CY550_THEEB 27 163
DBREF 3KZI y 1 46 UNP Q8DJI1 YCF12_THEEB 1 46
DBREF 3KZI X 11 50 UNP Q9F1R6 PSBX_THEEB 2 41
DBREF 3KZI Z 1 62 UNP Q8DHJ2 PSBZ_THEEB 1 62
SEQRES 1 A 344 MET THR THR THR LEU GLN ARG ARG GLU SER ALA ASN LEU
SEQRES 2 A 344 TRP GLU ARG PHE CYS ASN TRP VAL THR SER THR ASP ASN
SEQRES 3 A 344 ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE MET ILE PRO
SEQRES 4 A 344 THR LEU LEU ALA ALA THR ILE CYS PHE VAL ILE ALA PHE
SEQRES 5 A 344 ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY ILE ARG GLU
SEQRES 6 A 344 PRO VAL SER GLY SER LEU LEU TYR GLY ASN ASN ILE ILE
SEQRES 7 A 344 THR GLY ALA VAL VAL PRO SER SER ASN ALA ILE GLY LEU
SEQRES 8 A 344 HIS PHE TYR PRO ILE TRP GLU ALA ALA SER LEU ASP GLU
SEQRES 9 A 344 TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU ILE ILE PHE
SEQRES 10 A 344 HIS PHE LEU LEU GLY ALA SER CYS TYR MET GLY ARG GLN
SEQRES 11 A 344 TRP GLU LEU SER TYR ARG LEU GLY MET ARG PRO TRP ILE
SEQRES 12 A 344 CYS VAL ALA TYR SER ALA PRO LEU ALA SER ALA PHE ALA
SEQRES 13 A 344 VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY SER PHE SER
SEQRES 14 A 344 ASP GLY MET PRO LEU GLY ILE SER GLY THR PHE ASN PHE
SEQRES 15 A 344 MET ILE VAL PHE GLN ALA GLU HIS ASN ILE LEU MET HIS
SEQRES 16 A 344 PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL PHE GLY GLY
SEQRES 17 A 344 ALA LEU PHE CYS ALA MET HIS GLY SER LEU VAL THR SER
SEQRES 18 A 344 SER LEU ILE ARG GLU THR THR GLU THR GLU SER ALA ASN
SEQRES 19 A 344 TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU THR TYR ASN
SEQRES 20 A 344 ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG LEU ILE PHE
SEQRES 21 A 344 GLN TYR ALA SER PHE ASN ASN SER ARG SER LEU HIS PHE
SEQRES 22 A 344 PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL TRP PHE THR
SEQRES 23 A 344 ALA LEU GLY ILE SER THR MET ALA PHE ASN LEU ASN GLY
SEQRES 24 A 344 PHE ASN PHE ASN HIS SER VAL ILE ASP ALA LYS GLY ASN
SEQRES 25 A 344 VAL ILE ASN THR TRP ALA ASP ILE ILE ASN ARG ALA ASN
SEQRES 26 A 344 LEU GLY MET GLU VAL MET HIS GLU ARG ASN ALA HIS ASN
SEQRES 27 A 344 PHE PRO LEU ASP LEU ALA
SEQRES 1 B 510 MET GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE
SEQRES 2 B 510 ASN ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS
SEQRES 3 B 510 THR ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU
SEQRES 4 B 510 TYR GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU
SEQRES 5 B 510 ASN PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE
SEQRES 6 B 510 MET ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP
SEQRES 7 B 510 SER ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP
SEQRES 8 B 510 SER PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER
SEQRES 9 B 510 GLY LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR
SEQRES 10 B 510 TRP ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU
SEQRES 11 B 510 PRO ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU
SEQRES 12 B 510 PHE LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE
SEQRES 13 B 510 HIS LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER
SEQRES 14 B 510 ASP PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA
SEQRES 15 B 510 PRO GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO
SEQRES 16 B 510 GLY GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL
SEQRES 17 B 510 GLY ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO
SEQRES 18 B 510 PRO GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE
SEQRES 19 B 510 GLU THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE
SEQRES 20 B 510 ALA ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER
SEQRES 21 B 510 ALA THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR
SEQRES 22 B 510 GLN TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG
SEQRES 23 B 510 ARG VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU
SEQRES 24 B 510 GLU ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR
SEQRES 25 B 510 ASP TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE
SEQRES 26 B 510 ARG THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN
SEQRES 27 B 510 ALA TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY
SEQRES 28 B 510 GLU GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU
SEQRES 29 B 510 SER PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL
SEQRES 30 B 510 LYS ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR
SEQRES 31 B 510 SER PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY
SEQRES 32 B 510 GLY GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR
SEQRES 33 B 510 VAL LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE
SEQRES 34 B 510 PHE GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE
SEQRES 35 B 510 PHE ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS
SEQRES 36 B 510 ALA VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP
SEQRES 37 B 510 HIS GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY
SEQRES 38 B 510 ILE ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY
SEQRES 39 B 510 PHE TYR GLN LYS VAL GLY ASP VAL THR THR ARG ARG LYS
SEQRES 40 B 510 GLU ALA VAL
SEQRES 1 C 461 MET VAL THR LEU SER SER ASN SER ILE PHE ALA THR ASN
SEQRES 2 C 461 ARG ASP GLN GLU SER SER GLY PHE ALA TRP TRP ALA GLY
SEQRES 3 C 461 ASN ALA ARG LEU ILE ASN LEU SER GLY LYS LEU LEU GLY
SEQRES 4 C 461 ALA HIS VAL ALA HIS ALA GLY LEU ILE VAL PHE TRP ALA
SEQRES 5 C 461 GLY ALA MET THR LEU PHE GLU LEU ALA HIS PHE ILE PRO
SEQRES 6 C 461 GLU LYS PRO MET TYR GLU GLN GLY LEU ILE LEU ILE PRO
SEQRES 7 C 461 HIS ILE ALA THR LEU GLY TRP GLY VAL GLY PRO GLY GLY
SEQRES 8 C 461 GLU VAL VAL ASP THR PHE PRO PHE PHE VAL VAL GLY VAL
SEQRES 9 C 461 VAL HIS LEU ILE SER SER ALA VAL LEU GLY PHE GLY GLY
SEQRES 10 C 461 VAL TYR HIS ALA ILE ARG GLY PRO GLU THR LEU GLU GLU
SEQRES 11 C 461 TYR SER SER PHE PHE GLY TYR ASP TRP LYS ASP LYS ASN
SEQRES 12 C 461 LYS MET THR THR ILE LEU GLY PHE HIS LEU ILE VAL LEU
SEQRES 13 C 461 GLY ILE GLY ALA LEU LEU LEU VAL ALA LYS ALA MET PHE
SEQRES 14 C 461 PHE GLY GLY LEU TYR ASP THR TRP ALA PRO GLY GLY GLY
SEQRES 15 C 461 ASP VAL ARG VAL ILE THR ASN PRO THR LEU ASP PRO ARG
SEQRES 16 C 461 VAL ILE PHE GLY TYR LEU LEU LYS SER PRO PHE GLY GLY
SEQRES 17 C 461 GLU GLY TRP ILE VAL SER VAL ASN ASN LEU GLU ASP VAL
SEQRES 18 C 461 VAL GLY GLY HIS ILE TRP ILE GLY LEU ILE CYS ILE ALA
SEQRES 19 C 461 GLY GLY ILE TRP HIS ILE LEU THR THR PRO PHE GLY TRP
SEQRES 20 C 461 ALA ARG ARG ALA PHE ILE TRP SER GLY GLU ALA TYR LEU
SEQRES 21 C 461 SER TYR SER LEU GLY ALA LEU SER MET MET GLY PHE ILE
SEQRES 22 C 461 ALA THR CYS PHE VAL TRP PHE ASN ASN THR VAL TYR PRO
SEQRES 23 C 461 SER GLU PHE TYR GLY PRO THR GLY PRO GLU ALA SER GLN
SEQRES 24 C 461 ALA GLN ALA MET THR PHE LEU ILE ARG ASP GLN LYS LEU
SEQRES 25 C 461 GLY ALA ASN VAL GLY SER ALA GLN GLY PRO THR GLY LEU
SEQRES 26 C 461 GLY LYS TYR LEU MET ARG SER PRO THR GLY GLU ILE ILE
SEQRES 27 C 461 PHE GLY GLY GLU THR MET ARG PHE TRP ASP PHE ARG GLY
SEQRES 28 C 461 PRO TRP LEU GLU PRO LEU ARG GLY PRO ASN GLY LEU ASP
SEQRES 29 C 461 LEU ASN LYS ILE LYS ASN ASP ILE GLN PRO TRP GLN GLU
SEQRES 30 C 461 ARG ARG ALA ALA GLU TYR MET THR HIS ALA PRO LEU GLY
SEQRES 31 C 461 SER LEU ASN SER VAL GLY GLY VAL ALA THR GLU ILE ASN
SEQRES 32 C 461 SER VAL ASN PHE VAL SER PRO ARG SER TRP LEU ALA THR
SEQRES 33 C 461 SER HIS PHE VAL LEU ALA PHE PHE PHE LEU VAL GLY HIS
SEQRES 34 C 461 LEU TRP HIS ALA GLY ARG ALA ARG ALA ALA ALA ALA GLY
SEQRES 35 C 461 PHE GLU LYS GLY ILE ASP ARG GLU SER GLU PRO VAL LEU
SEQRES 36 C 461 SER MET PRO SER LEU ASP
SEQRES 1 D 352 MET THR ILE ALA ILE GLY ARG ALA PRO ALA GLU ARG GLY
SEQRES 2 D 352 TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS ARG ASP ARG
SEQRES 3 D 352 PHE VAL PHE VAL GLY TRP SER GLY ILE LEU LEU PHE PRO
SEQRES 4 D 352 CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU THR GLY THR
SEQRES 5 D 352 THR PHE VAL THR SER TRP TYR THR HIS GLY LEU ALA SER
SEQRES 6 D 352 SER TYR LEU GLU GLY CYS ASN PHE LEU THR VAL ALA VAL
SEQRES 7 D 352 SER THR PRO ALA ASN SER MET GLY HIS SER LEU LEU LEU
SEQRES 8 D 352 LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE THR ARG TRP
SEQRES 9 D 352 CYS GLN LEU GLY GLY LEU TRP THR PHE ILE ALA LEU HIS
SEQRES 10 D 352 GLY ALA PHE GLY LEU ILE GLY PHE MET LEU ARG GLN PHE
SEQRES 11 D 352 GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO TYR ASN ALA
SEQRES 12 D 352 ILE ALA PHE SER ALA PRO ILE ALA VAL PHE VAL SER VAL
SEQRES 13 D 352 PHE LEU ILE TYR PRO LEU GLY GLN SER SER TRP PHE PHE
SEQRES 14 D 352 ALA PRO SER PHE GLY VAL ALA ALA ILE PHE ARG PHE LEU
SEQRES 15 D 352 LEU PHE PHE GLN GLY PHE HIS ASN TRP THR LEU ASN PRO
SEQRES 16 D 352 PHE HIS MET MET GLY VAL ALA GLY VAL LEU GLY GLY ALA
SEQRES 17 D 352 LEU LEU CYS ALA ILE HIS GLY ALA THR VAL GLU ASN THR
SEQRES 18 D 352 LEU PHE GLN ASP GLY GLU GLY ALA SER THR PHE ARG ALA
SEQRES 19 D 352 PHE ASN PRO THR GLN ALA GLU GLU THR TYR SER MET VAL
SEQRES 20 D 352 THR ALA ASN ARG PHE TRP SER GLN ILE PHE GLY ILE ALA
SEQRES 21 D 352 PHE SER ASN LYS ARG TRP LEU HIS PHE PHE MET LEU PHE
SEQRES 22 D 352 VAL PRO VAL THR GLY LEU TRP MET SER ALA ILE GLY VAL
SEQRES 23 D 352 VAL GLY LEU ALA LEU ASN LEU ARG SER TYR ASP PHE ILE
SEQRES 24 D 352 SER GLN GLU ILE ARG ALA ALA GLU ASP PRO GLU PHE GLU
SEQRES 25 D 352 THR PHE TYR THR LYS ASN LEU LEU LEU ASN GLU GLY ILE
SEQRES 26 D 352 ARG ALA TRP MET ALA PRO GLN ASP GLN PRO HIS GLU ASN
SEQRES 27 D 352 PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG GLY ASN ALA
SEQRES 28 D 352 LEU
SEQRES 1 E 83 ALA GLY THR THR GLY GLU ARG PRO PHE SER ASP ILE ILE
SEQRES 2 E 83 THR SER VAL ARG TYR TRP VAL ILE HIS SER ILE THR ILE
SEQRES 3 E 83 PRO ALA LEU PHE ILE ALA GLY TRP LEU PHE VAL SER THR
SEQRES 4 E 83 GLY LEU ALA TYR ASP VAL PHE GLY THR PRO ARG PRO ASP
SEQRES 5 E 83 SER TYR TYR ALA GLN GLU GLN ARG SER ILE PRO LEU VAL
SEQRES 6 E 83 THR ASP ARG PHE GLU ALA LYS GLN GLN VAL GLU THR PHE
SEQRES 7 E 83 LEU GLU GLN LEU LYS
SEQRES 1 F 44 THR SER ASN THR PRO ASN GLN GLU PRO VAL SER TYR PRO
SEQRES 2 F 44 ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR LEU ALA
SEQRES 3 F 44 VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA ALA MET
SEQRES 4 F 44 GLN PHE ILE GLN ARG
SEQRES 1 H 65 ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO LEU
SEQRES 2 H 65 ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY THR
SEQRES 3 H 65 THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU VAL
SEQRES 4 H 65 PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR LEU
SEQRES 5 H 65 ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU GLY
SEQRES 1 I 38 MET GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR
SEQRES 2 I 38 PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY
SEQRES 3 I 38 ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP LEU GLU
SEQRES 1 J 40 MET MET SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL
SEQRES 2 J 40 ALA THR VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY
SEQRES 3 J 40 LEU PHE PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER
SEQRES 4 J 40 LEU
SEQRES 1 K 37 LYS LEU PRO GLU ALA TYR ALA ILE PHE ASP PRO LEU VAL
SEQRES 2 K 37 ASP VAL LEU PRO VAL ILE PRO VAL LEU PHE LEU ALA LEU
SEQRES 3 K 37 ALA PHE VAL TRP GLN ALA ALA VAL GLY PHE ARG
SEQRES 1 L 37 MET GLU PRO ASN PRO ASN ARG GLN PRO VAL GLU LEU ASN
SEQRES 2 L 37 ARG THR SER LEU TYR LEU GLY LEU LEU LEU ILE LEU VAL
SEQRES 3 L 37 LEU ALA LEU LEU PHE SER SER TYR PHE PHE ASN
SEQRES 1 M 36 MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU
SEQRES 2 M 36 PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR
SEQRES 3 M 36 VAL GLN THR GLU SER GLN GLN LYS SER SER
SEQRES 1 O 246 ALA LYS GLN THR LEU THR TYR ASP ASP ILE VAL GLY THR
SEQRES 2 O 246 GLY LEU ALA ASN LYS CYS PRO THR LEU ASP ASP THR ALA
SEQRES 3 O 246 ARG GLY ALA TYR PRO ILE ASP SER SER GLN THR TYR ARG
SEQRES 4 O 246 ILE ALA ARG LEU CYS LEU GLN PRO THR THR PHE LEU VAL
SEQRES 5 O 246 LYS GLU GLU PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE
SEQRES 6 O 246 VAL PRO THR LYS LEU VAL THR ARG GLU THR THR SER LEU
SEQRES 7 O 246 ASP GLN ILE GLN GLY GLU LEU LYS VAL ASN SER ASP GLY
SEQRES 8 O 246 SER LEU THR PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN
SEQRES 9 O 246 PRO VAL THR VAL GLN MET ALA GLY GLY GLU ARG ILE PRO
SEQRES 10 O 246 LEU LEU PHE THR VAL LYS ASN LEU VAL ALA SER THR GLN
SEQRES 11 O 246 PRO ASN VAL THR SER ILE THR THR SER THR ASP PHE LYS
SEQRES 12 O 246 GLY GLU PHE ASN VAL PRO SER TYR ARG THR ALA ASN PHE
SEQRES 13 O 246 LEU ASP PRO LYS GLY ARG GLY LEU ALA SER GLY TYR ASP
SEQRES 14 O 246 SER ALA ILE ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU
SEQRES 15 O 246 ALA ARG ALA ASN VAL LYS ARG PHE SER LEU THR LYS GLY
SEQRES 16 O 246 GLN ILE SER LEU ASN VAL ALA LYS VAL ASP GLY ARG THR
SEQRES 17 O 246 GLY GLU ILE ALA GLY THR PHE GLU SER GLU GLN LEU SER
SEQRES 18 O 246 ASP ASP ASP MET GLY ALA HIS GLU PRO HIS GLU VAL LYS
SEQRES 19 O 246 ILE GLN GLY VAL PHE TYR ALA SER ILE GLU PRO ALA
SEQRES 1 T 32 MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE
SEQRES 2 T 32 ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO
SEQRES 3 T 32 PRO ARG ILE THR LYS LYS
SEQRES 1 U 104 ALA THR ALA SER THR GLU GLU GLU LEU VAL ASN VAL VAL
SEQRES 2 U 104 ASP GLU LYS LEU GLY THR ALA TYR GLY GLU LYS ILE ASP
SEQRES 3 U 104 LEU ASN ASN THR ASN ILE ALA ALA PHE ILE GLN TYR ARG
SEQRES 4 U 104 GLY LEU TYR PRO THR LEU ALA LYS LEU ILE VAL LYS ASN
SEQRES 5 U 104 ALA PRO TYR GLU SER VAL GLU ASP VAL LEU ASN ILE PRO
SEQRES 6 U 104 GLY LEU THR GLU ARG GLN LYS GLN ILE LEU ARG GLU ASN
SEQRES 7 U 104 LEU GLU HIS PHE THR VAL THR GLU VAL GLU THR ALA LEU
SEQRES 8 U 104 VAL GLU GLY GLY ASP ARG TYR ASN ASN GLY LEU TYR LYS
SEQRES 1 V 137 ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN
SEQRES 2 V 137 SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR
SEQRES 3 V 137 LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER
SEQRES 4 V 137 CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU
SEQRES 5 V 137 ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO
SEQRES 6 V 137 ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN
SEQRES 7 V 137 PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL
SEQRES 8 V 137 HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET
SEQRES 9 V 137 ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY
SEQRES 10 V 137 HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP
SEQRES 11 V 137 GLY GLY GLY LYS VAL TYR TYR
SEQRES 1 y 46 MET GLY ILE PHE ASN GLY ILE ILE GLU PHE LEU SER ASN
SEQRES 2 y 46 ILE ASN PHE GLU VAL ILE ALA GLN LEU THR MET ILE ALA
SEQRES 3 y 46 MET ILE GLY ILE ALA GLY PRO MET ILE ILE PHE LEU LEU
SEQRES 4 y 46 ALA VAL ARG ARG GLY ASN LEU
SEQRES 1 X 40 THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY LEU
SEQRES 2 X 40 LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA VAL
SEQRES 3 X 40 LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG SER
SEQRES 4 X 40 LEU
SEQRES 1 Z 62 MET THR ILE LEU PHE GLN LEU ALA LEU ALA ALA LEU VAL
SEQRES 2 Z 62 ILE LEU SER PHE VAL MET VAL ILE GLY VAL PRO VAL ALA
SEQRES 3 Z 62 TYR ALA SER PRO GLN ASP TRP ASP ARG SER LYS GLN LEU
SEQRES 4 Z 62 ILE PHE LEU GLY SER GLY LEU TRP ILE ALA LEU VAL LEU
SEQRES 5 Z 62 VAL VAL GLY VAL LEU ASN PHE PHE VAL VAL
HET FE2 A 361 1
HET CLA A 362 65
HET CLA A 363 65
HET PHO A 365 64
HET CLA A 366 65
HET MES A 367 12
HET OEC A 368 5
HET BCR A 369 40
HET DGD C 474 56
HET LHG A 371 39
HET SQD C 475 51
HET LMG A 373 51
HET LHG C 476 37
HET DGD A 375 52
HET LMT A 376 35
HET CLA B 511 65
HET CLA B 512 65
HET CLA B 513 65
HET CLA B 514 65
HET CLA B 515 65
HET CLA B 516 65
HET CLA B 517 65
HET CLA B 518 65
HET CLA B 519 65
HET CLA B 520 65
HET CLA B 521 65
HET CLA B 522 65
HET CLA B 523 65
HET CLA B 524 65
HET CLA B 525 65
HET CLA B 526 65
HET BCR B 527 40
HET BCR B 529 40
HET BCR B 530 40
HET LMG B 531 49
HET DGD B 533 66
HET LMT B 535 35
HET LMT D 536 35
HET CLA C 477 65
HET CLA C 478 65
HET CLA C 479 65
HET CLA C 480 65
HET CLA C 481 65
HET CLA C 482 65
HET CLA C 483 65
HET CLA C 484 65
HET CLA C 485 65
HET CLA K 483 65
HET CLA C 486 65
HET CLA C 487 65
HET CLA C 488 65
HET BCR C 489 40
HET BCR C 490 40
HET DGD C 491 53
HET DGD C 492 62
HET DGD C 493 66
HET LMG J 492 48
HET LMG C 494 45
HET BCT D 353 4
HET CLA D 354 65
HET CLA A 364 65
HET PHO D 355 64
HET CLA D 356 65
HET PL9 D 357 55
HET BCR D 358 40
HET LMG D 359 46
HET LMG D 360 48
HET SQD D 361 43
HET DGD D 362 63
HET LMT D 363 31
HET HEM F 85 43
HET SQD F 224 45
HET CA F 225 1
HET BCR X 107 40
HET DGD B 528 58
HET LMG I 220 43
HET BCR J 115 40
HET CA K 56 1
HET BCR J 112 40
HET LMG M 217 42
HET LMT T 226 35
HET CA O 273 1
HET LMT I 274 35
HET SQD L 213 47
HET LMT O 274 35
HET HEM V 164 43
HET BCR Z 116 40
HETNAM FE2 FE (II) ION
HETNAM CLA CHLOROPHYLL A
HETNAM PHO PHEOPHYTIN A
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM OEC OXYGEN EVOLVING SYSTEM
HETNAM BCR BETA-CAROTENE
HETNAM DGD DIGALACTOSYL DIACYL GLYCEROL (DGDG)
HETNAM LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE
HETNAM SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-
HETNAM 2 SQD GLUCOPYRANOSYL]-SN-GLYCEROL
HETNAM LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE
HETNAM LMT DODECYL-BETA-D-MALTOSIDE
HETNAM BCT BICARBONATE ION
HETNAM PL9 2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,
HETNAM 2 PL9 6,10,14,18,22,26,30,34-HEXATRIACONTANONAENYL-2,5-
HETNAM 3 PL9 CYCLOHEXADIENE-1,4-DIONE-2,3-DIMETHYL-5-SOLANESYL-1,4-
HETNAM 4 PL9 BENZOQUINONE
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM CA CALCIUM ION
HETSYN SQD SULFOQUINOVOSYLDIACYLGLYCEROL
HETSYN PL9 PLASTOQUINONE 9
HETSYN HEM HEME
FORMUL 20 FE2 FE 2+
FORMUL 21 CLA 35(C55 H72 MG N4 O5 2+)
FORMUL 23 PHO 2(C55 H74 N4 O5)
FORMUL 25 MES C6 H13 N O4 S
FORMUL 26 OEC CA MN4 O4
FORMUL 27 BCR 11(C40 H56)
FORMUL 28 DGD 8(C51 H96 O15)
FORMUL 29 LHG 2(C38 H75 O10 P)
FORMUL 30 SQD 4(C41 H78 O12 S)
FORMUL 31 LMG 8(C45 H86 O10)
FORMUL 34 LMT 7(C24 H46 O11)
FORMUL 78 BCT C H O3 1-
FORMUL 83 PL9 C53 H80 O2
FORMUL 90 HEM 2(C34 H32 FE N4 O4)
FORMUL 92 CA 3(CA 2+)
HELIX 1 1 ASN A 12 THR A 22 1 11
HELIX 2 2 PHE A 33 ALA A 55 1 23
HELIX 3 3 SER A 70 GLY A 74 5 5
HELIX 4 4 PRO A 95 ALA A 99 5 5
HELIX 5 5 SER A 101 ASN A 108 1 8
HELIX 6 6 GLY A 109 LEU A 137 1 29
HELIX 7 7 TRP A 142 TYR A 147 1 6
HELIX 8 8 TYR A 147 LEU A 159 1 13
HELIX 9 9 LEU A 159 GLY A 166 1 8
HELIX 10 10 SER A 167 GLY A 171 5 5
HELIX 11 11 ILE A 176 ASN A 191 1 16
HELIX 12 12 ILE A 192 MET A 194 5 3
HELIX 13 13 HIS A 195 SER A 222 1 28
HELIX 14 14 ASN A 247 ILE A 259 1 13
HELIX 15 15 PHE A 260 SER A 264 5 5
HELIX 16 16 ASN A 267 MET A 293 1 27
HELIX 17 17 THR A 316 HIS A 332 1 17
HELIX 18 18 PRO B 4 ILE B 13 5 10
HELIX 19 19 ASP B 15 ALA B 43 1 29
HELIX 20 20 PRO B 54 GLN B 58 5 5
HELIX 21 21 VAL B 62 ARG B 68 1 7
HELIX 22 22 SER B 92 TYR B 117 1 26
HELIX 23 23 LEU B 120 ARG B 124 5 5
HELIX 24 24 ASP B 134 HIS B 157 1 24
HELIX 25 25 GLY B 186 ASN B 191 5 6
HELIX 26 26 ASN B 194 VAL B 219 1 26
HELIX 27 27 PRO B 222 LEU B 229 1 8
HELIX 28 28 ASN B 233 GLY B 259 1 27
HELIX 29 29 PRO B 264 GLY B 269 1 6
HELIX 30 30 THR B 271 SER B 277 1 7
HELIX 31 31 SER B 278 SER B 294 1 17
HELIX 32 32 THR B 297 ILE B 305 1 9
HELIX 33 33 PRO B 306 ASP B 313 1 8
HELIX 34 34 TYR B 314 ASN B 318 5 5
HELIX 35 35 PRO B 329 GLY B 333 5 5
HELIX 36 36 ARG B 384 SER B 388 5 5
HELIX 37 37 SER B 391 GLY B 396 1 6
HELIX 38 38 ASP B 413 ILE B 425 1 13
HELIX 39 39 SER B 446 PHE B 475 1 30
HELIX 40 40 ALA C 34 ILE C 43 5 10
HELIX 41 41 GLY C 47 PHE C 75 1 29
HELIX 42 42 MET C 81 GLY C 85 5 5
HELIX 43 43 LEU C 88 LEU C 95 1 8
HELIX 44 44 GLY C 100 GLU C 104 5 5
HELIX 45 45 THR C 108 ARG C 135 1 28
HELIX 46 46 ASP C 153 PHE C 181 1 29
HELIX 47 47 ASP C 205 PHE C 210 1 6
HELIX 48 48 GLY C 211 LYS C 215 5 5
HELIX 49 49 GLY C 222 VAL C 227 5 6
HELIX 50 50 ASN C 229 LEU C 253 1 25
HELIX 51 51 GLY C 258 PHE C 264 1 7
HELIX 52 52 SER C 267 ASN C 293 1 27
HELIX 53 53 THR C 305 LEU C 324 1 20
HELIX 54 54 ASN C 327 ALA C 331 5 5
HELIX 55 55 GLY C 353 TRP C 359 5 7
HELIX 56 56 LEU C 366 ARG C 370 5 5
HELIX 57 57 ASP C 376 ASP C 383 1 8
HELIX 58 58 GLN C 385 THR C 397 1 13
HELIX 59 59 SER C 421 GLY C 454 1 34
HELIX 60 60 GLU C 464 MET C 469 5 6
HELIX 61 61 GLY D 13 LYS D 23 1 11
HELIX 62 62 VAL D 30 PHE D 54 1 25
HELIX 63 63 SER D 57 GLY D 62 1 6
HELIX 64 64 SER D 66 GLY D 70 5 5
HELIX 65 65 ASP D 100 LEU D 107 1 8
HELIX 66 66 GLY D 108 GLY D 137 1 30
HELIX 67 67 PRO D 140 PHE D 146 1 7
HELIX 68 68 PHE D 146 LEU D 158 1 13
HELIX 69 69 LEU D 158 GLN D 164 1 7
HELIX 70 70 SER D 166 ALA D 170 5 5
HELIX 71 71 VAL D 175 ASN D 190 1 16
HELIX 72 72 TRP D 191 LEU D 193 5 3
HELIX 73 73 ASN D 194 ASN D 220 1 27
HELIX 74 74 SER D 245 PHE D 257 1 13
HELIX 75 75 ASN D 263 LEU D 291 1 29
HELIX 76 76 PHE D 298 ASP D 308 1 11
HELIX 77 77 THR D 313 GLN D 334 1 22
HELIX 78 78 PRO D 335 ASN D 338 5 4
HELIX 79 79 PRO E 9 SER E 16 1 8
HELIX 80 80 SER E 16 THR E 40 1 25
HELIX 81 81 GLY E 41 PHE E 47 1 7
HELIX 82 82 GLU E 71 GLN E 82 1 12
HELIX 83 83 VAL F 18 LEU F 26 1 9
HELIX 84 84 ALA F 27 GLY F 35 1 9
HELIX 85 85 GLY F 35 GLN F 41 1 7
HELIX 86 86 THR H 5 ARG H 12 1 8
HELIX 87 87 THR H 27 ASN H 50 1 24
HELIX 88 88 MET I 1 SER I 25 1 25
HELIX 89 89 PRO J 9 ALA J 32 1 24
HELIX 90 90 PRO K 12 ILE K 17 5 6
HELIX 91 91 PHE K 18 ASP K 23 1 6
HELIX 92 92 VAL K 24 PRO K 26 5 3
HELIX 93 93 VAL K 27 VAL K 43 1 17
HELIX 94 94 ASN L 13 ASN L 37 1 25
HELIX 95 95 LEU M 6 SER M 31 1 26
HELIX 96 96 THR O 32 ILE O 36 5 5
HELIX 97 97 GLY O 40 LYS O 44 5 5
HELIX 98 98 LEU O 208 VAL O 213 1 6
HELIX 99 99 MET T 1 PHE T 23 1 23
HELIX 100 100 ASN U 41 LEU U 47 1 7
HELIX 101 101 ASN U 61 TYR U 68 5 8
HELIX 102 102 TYR U 72 ASN U 82 1 11
HELIX 103 103 SER U 87 ILE U 94 5 8
HELIX 104 104 THR U 98 LEU U 109 1 12
HELIX 105 105 GLU U 118 GLU U 123 1 6
HELIX 106 106 GLY U 124 ASP U 126 5 3
HELIX 107 107 THR V 30 LEU V 34 1 5
HELIX 108 108 THR V 48 CYS V 63 1 16
HELIX 109 109 CYS V 63 VAL V 68 1 6
HELIX 110 110 GLY V 69 ILE V 71 5 3
HELIX 111 111 ARG V 81 LEU V 87 1 7
HELIX 112 112 ASN V 94 MET V 102 1 9
HELIX 113 113 SER V 120 ALA V 124 5 5
HELIX 114 114 PRO V 128 LEU V 133 1 6
HELIX 115 115 THR V 134 GLY V 153 1 20
HELIX 116 116 GLY V 153 GLY V 158 1 6
HELIX 117 117 GLN y 21 ARG y 42 1 22
HELIX 118 118 THR X 13 GLN X 42 1 30
HELIX 119 119 MET Z 1 SER Z 29 1 29
HELIX 120 120 ARG Z 35 VAL Z 62 1 28
SHEET 1 A 2 ALA A 81 VAL A 82 0
SHEET 2 A 2 LEU A 174 GLY A 175 -1 O LEU A 174 N VAL A 82
SHEET 1 B 2 LEU A 297 ASN A 298 0
SHEET 2 B 2 GLY C 402 SER C 403 1 O GLY C 402 N ASN A 298
SHEET 1 C 2 MET B 166 VAL B 168 0
SHEET 2 C 2 SER B 177 GLN B 179 -1 O SER B 177 N VAL B 168
SHEET 1 D 2 ILE B 336 TRP B 340 0
SHEET 2 D 2 PHE B 430 ASP B 433 -1 O GLU B 431 N GLN B 338
SHEET 1 E 6 VAL B 377 ASP B 380 0
SHEET 2 E 6 ILE B 369 THR B 371 -1 N LEU B 370 O ALA B 379
SHEET 3 E 6 GLU B 353 VAL B 356 -1 N PHE B 355 O THR B 371
SHEET 4 E 6 HIS B 343 ARG B 347 -1 N PHE B 346 O LEU B 354
SHEET 5 E 6 THR B 398 TYR B 402 -1 O SER B 400 N VAL B 345
SHEET 6 E 6 THR B 410 PHE B 411 -1 O PHE B 411 N VAL B 399
SHEET 1 F 2 LEU C 185 ASP C 187 0
SHEET 2 F 2 ASP C 195 ARG C 197 -1 O ARG C 197 N LEU C 185
SHEET 1 G 2 LEU C 341 ARG C 343 0
SHEET 2 G 2 ILE C 349 PHE C 351 -1 O ILE C 350 N MET C 342
SHEET 1 H 2 ALA D 77 VAL D 78 0
SHEET 2 H 2 PHE D 173 GLY D 174 -1 O PHE D 173 N VAL D 78
SHEET 1 I 2 TYR O 56 PRO O 57 0
SHEET 2 I 2 SER O 161 ILE O 162 -1 O ILE O 162 N TYR O 56
SHEET 1 J10 PHE O 91 PRO O 93 0
SHEET 2 J10 ARG O 65 LYS O 79 -1 N VAL O 78 O VAL O 92
SHEET 3 J10 GLU O 258 GLU O 270 -1 O VAL O 264 N GLN O 72
SHEET 4 J10 GLU O 236 LEU O 246 -1 N SER O 243 O ILE O 261
SHEET 5 J10 LEU O 218 LYS O 229 -1 N LYS O 229 O ALA O 238
SHEET 6 J10 PHE O 168 PRO O 175 -1 N VAL O 174 O THR O 219
SHEET 7 J10 LYS O 149 SER O 154 -1 N LYS O 149 O ASN O 173
SHEET 8 J10 THR O 120 ILE O 127 -1 N PHE O 121 O ALA O 153
SHEET 9 J10 LEU O 104 GLU O 110 -1 N GLN O 108 O GLU O 124
SHEET 10 J10 ARG O 65 LYS O 79 -1 N ILE O 66 O GLY O 109
SHEET 1 K 3 LYS O 95 LEU O 96 0
SHEET 2 K 3 PHE O 129 GLN O 135 -1 O GLN O 135 N LYS O 95
SHEET 3 K 3 ARG O 141 THR O 147 -1 O ILE O 142 N VAL O 134
SHEET 1 L 2 ILE U 55 ASP U 56 0
SHEET 2 L 2 PHE U 112 THR U 113 1 O THR U 113 N ILE U 55
SHEET 1 M 2 THR V 35 PRO V 37 0
SHEET 2 M 2 THR V 44 THR V 46 -1 O ILE V 45 N VAL V 36
SSBOND 1 CYS O 45 CYS O 70 1555 1555 2.04
LINK OE2 GLU A 189 MN1 OEC A 368 1555 1555 1.73
LINK NE2 HIS V 67 FE HEM V 164 1555 1555 2.05
LINK FE FE2 A 361 O3 BCT D 353 1555 1555 2.08
LINK OE2 GLU C 354 MN3 OEC A 368 1555 1555 2.18
LINK OD1 ASP A 342 MN2 OEC A 368 1555 1555 2.23
LINK NE2 HIS A 332 MN1 OEC A 368 1555 1555 2.24
LINK NE2 HIS D 214 FE FE2 A 361 1555 1555 2.25
LINK OD2 ASP A 170 MN4 OEC A 368 1555 1555 2.26
LINK OE1 GLU A 333 MN3 OEC A 368 1555 1555 2.27
LINK NE2 HIS A 215 FE FE2 A 361 1555 1555 2.29
LINK NE2 HIS E 23 FE HEM F 85 1555 1555 2.33
LINK NE2 HIS V 118 FE HEM V 164 1555 1555 2.35
LINK OE1 GLU A 189 CA1 OEC A 368 1555 1555 2.36
LINK NE2 HIS A 272 FE FE2 A 361 1555 1555 2.43
LINK O ALA A 344 CA1 OEC A 368 1555 1555 2.43
LINK OD2 ASP A 342 MN1 OEC A 368 1555 1555 2.50
LINK NE2 HIS D 268 FE FE2 A 361 1555 1555 2.55
LINK OE1 GLU C 354 MN2 OEC A 368 1555 1555 2.55
LINK OD1 ASN C 39 MG CLA C 486 1555 1555 2.65
LINK FE FE2 A 361 O2 BCT D 353 1555 1555 2.69
LINK OD2 ASP K 19 CA CA K 56 1555 1555 2.74
LINK O ALA A 344 MN2 OEC A 368 1555 1555 2.78
LINK OE1 GLU O 140 CA CA O 273 1555 1555 2.84
LINK OD1 ASP A 170 CA1 OEC A 368 1555 1555 2.94
LINK OD1 ASP K 23 CA CA K 56 1555 1555 2.95
LINK OD2 ASP K 23 CA CA K 56 1555 1555 2.98
LINK O ARG F 45 CA CA F 225 1555 1555 3.16
CISPEP 1 THR V 89 PRO V 90 0 -0.04
SITE 1 AC1 5 HIS A 215 HIS A 272 HIS D 214 HIS D 268
SITE 2 AC1 5 BCT D 353
SITE 1 AC2 22 PHE A 119 TYR A 147 PRO A 150 SER A 153
SITE 2 AC2 22 ALA A 154 VAL A 157 PHE A 182 MET A 183
SITE 3 AC2 22 PHE A 186 GLN A 187 LEU A 193 HIS A 198
SITE 4 AC2 22 VAL A 205 THR A 286 ALA A 287 ILE A 290
SITE 5 AC2 22 CLA A 363 CLA A 364 PHO A 365 LEU D 182
SITE 6 AC2 22 CLA D 354 PHE T 17
SITE 1 AC3 18 THR A 45 VAL A 157 PHE A 158 MET A 172
SITE 2 AC3 18 ILE A 176 THR A 179 MET A 183 CLA A 362
SITE 3 AC3 18 PHO A 365 MET D 198 VAL D 201 ALA D 202
SITE 4 AC3 18 CLA D 354 PL9 D 357 LMG D 360 LEU L 30
SITE 5 AC3 18 PHE T 10 ILE T 14
SITE 1 AC4 19 LEU A 41 THR A 45 PHE A 48 PHE A 119
SITE 2 AC4 19 TYR A 126 GLN A 130 TYR A 147 PRO A 150
SITE 3 AC4 19 LEU A 174 CLA A 362 CLA A 363 LEU D 205
SITE 4 AC4 19 ALA D 208 LEU D 209 ALA D 212 ILE D 213
SITE 5 AC4 19 TRP D 253 PHE D 257 LMG D 360
SITE 1 AC5 18 VAL A 35 ILE A 36 PRO A 39 THR A 40
SITE 2 AC5 18 PHE A 93 ILE A 96 TRP A 97 LEU A 114
SITE 3 AC5 18 PHE A 117 HIS A 118 LEU A 121 BCR A 369
SITE 4 AC5 18 DGD C 474 CLA C 481 VAL I 8 TYR I 9
SITE 5 AC5 18 VAL I 12 PHE I 15
SITE 1 AC6 7 MET A 214 HIS A 215 LEU A 218 VAL A 219
SITE 2 AC6 7 TYR A 246 ALA A 251 LEU A 271
SITE 1 AC7 7 ASP A 170 GLU A 189 HIS A 332 GLU A 333
SITE 2 AC7 7 ASP A 342 ALA A 344 GLU C 354
SITE 1 AC8 11 VAL A 35 ILE A 38 PRO A 39 LEU A 42
SITE 2 AC8 11 ALA A 43 ILE A 46 ALA A 51 ALA A 55
SITE 3 AC8 11 TRP A 105 LEU A 106 CLA A 366
SITE 1 AC9 18 PHE A 93 PRO A 95 TRP A 97 GLU A 98
SITE 2 AC9 18 LEU A 121 PHE A 155 CLA A 366 LEU C 213
SITE 3 AC9 18 LEU C 214 LYS C 215 SER C 216 PRO C 217
SITE 4 AC9 18 TRP C 223 MET C 281 PHE C 284 CLA C 481
SITE 5 AC9 18 DGD C 491 LYS I 5
SITE 1 BC1 14 ARG A 140 TRP A 142 PHE A 273 TRP C 36
SITE 2 BC1 14 PHE C 436 TRP C 443 ARG C 447 SQD C 475
SITE 3 BC1 14 CLA C 480 CLA C 484 ALA D 229 SER D 230
SITE 4 BC1 14 THR D 231 PHE D 232
SITE 1 BC2 10 PHE A 273 LHG A 371 ALA C 34 TRP C 36
SITE 2 BC2 10 LHG C 476 CLA C 484 PHE D 232 ARG D 233
SITE 3 BC2 10 LMG D 359 BCR J 115
SITE 1 BC3 20 SER A 232 ASN A 234 TYR A 235 PRO B 4
SITE 2 BC3 20 TRP B 5 TYR B 6 CLA B 521 TRP D 266
SITE 3 BC3 20 PHE D 273 PL9 D 357 LMG D 360 GLU L 11
SITE 4 BC3 20 ASN L 13 SER L 16 GLY L 20 LEU L 23
SITE 5 BC3 20 ILE L 24 VAL L 26 PRO M 18 LEU M 22
SITE 1 BC4 3 SQD C 475 DGD C 492 BCR J 115
SITE 1 BC5 6 ILE A 46 ILE A 50 LMT A 376 LMG I 220
SITE 2 BC5 6 LMT I 274 LMT O 274
SITE 1 BC6 3 ALA A 54 ASP A 103 DGD A 375
SITE 1 BC7 6 TRP B 185 PRO B 187 PHE B 190 ALA B 204
SITE 2 BC7 6 CLA B 512 BCR X 107
SITE 1 BC8 17 GLY B 189 PHE B 190 PRO B 192 HIS B 201
SITE 2 BC8 17 ALA B 204 VAL B 208 PHE B 247 PHE B 250
SITE 3 BC8 17 CLA B 511 CLA B 513 DGD B 528 PHE H 38
SITE 4 BC8 17 PHE H 41 LEU H 42 ILE H 45 TYR H 49
SITE 5 BC8 17 BCR X 107
SITE 1 BC9 21 ARG B 68 LEU B 69 LEU B 149 CYS B 150
SITE 2 BC9 21 PHE B 153 MET B 166 HIS B 201 HIS B 202
SITE 3 BC9 21 PHE B 247 ALA B 248 VAL B 251 VAL B 252
SITE 4 BC9 21 THR B 255 THR B 262 CLA B 512 CLA B 514
SITE 5 BC9 21 CLA B 515 CLA B 516 CLA B 519 CLA B 520
SITE 6 BC9 21 PHE H 38
SITE 1 CC1 23 TRP B 33 PHE B 61 PHE B 65 ARG B 68
SITE 2 CC1 23 LEU B 148 LEU B 149 VAL B 245 ALA B 248
SITE 3 CC1 23 ALA B 249 VAL B 252 PHE B 451 HIS B 455
SITE 4 CC1 23 PHE B 458 ALA B 459 PHE B 462 CLA B 513
SITE 5 CC1 23 CLA B 515 CLA B 517 CLA B 520 CLA B 521
SITE 6 CC1 23 CLA B 522 CLA B 523 CLA B 525
SITE 1 CC2 21 THR B 27 VAL B 30 ALA B 31 TRP B 33
SITE 2 CC2 21 ALA B 34 VAL B 62 PHE B 65 MET B 66
SITE 3 CC2 21 ARG B 68 LEU B 69 HIS B 100 LEU B 103
SITE 4 CC2 21 GLY B 147 ALA B 205 CLA B 513 CLA B 514
SITE 5 CC2 21 CLA B 516 CLA B 519 CLA B 520 CLA B 522
SITE 6 CC2 21 BCR B 530
SITE 1 CC3 16 TRP B 91 VAL B 96 ALA B 99 HIS B 100
SITE 2 CC3 16 LEU B 103 LEU B 106 LEU B 149 GLY B 152
SITE 3 CC3 16 PHE B 153 PHE B 156 HIS B 157 PHE B 162
SITE 4 CC3 16 PRO B 164 CLA B 513 CLA B 515 CLA B 526
SITE 1 CC4 22 TRP B 33 MET B 37 TYR B 40 GLN B 58
SITE 2 CC4 22 GLY B 59 PHE B 61 PHE B 325 ARG B 326
SITE 3 CC4 22 THR B 327 GLY B 328 PRO B 329 TRP B 450
SITE 4 CC4 22 PHE B 451 ALA B 454 CLA B 514 CLA B 523
SITE 5 CC4 22 BCR B 529 LMG B 531 DGD B 533 MET D 199
SITE 6 CC4 22 MET D 281 PHE M 14
SITE 1 CC5 17 THR B 236 SER B 239 SER B 240 ALA B 243
SITE 2 CC5 17 PHE B 246 PHE B 247 HIS B 466 CLA B 519
SITE 3 CC5 17 CLA B 520 PHE D 120 ILE D 123 MET D 126
SITE 4 CC5 17 LEU D 127 PHE D 130 CLA D 356 SQD D 361
SITE 5 CC5 17 LEU H 43
SITE 1 CC6 20 PHE B 139 VAL B 208 ALA B 212 PHE B 215
SITE 2 CC6 20 HIS B 216 ARG B 220 PRO B 221 PRO B 222
SITE 3 CC6 20 LEU B 225 LEU B 229 CLA B 513 CLA B 515
SITE 4 CC6 20 CLA B 518 CLA B 520 THR H 27 THR H 28
SITE 5 CC6 20 MET H 31 PHE H 34 LEU H 46 BCR X 107
SITE 1 CC7 14 PHE B 139 HIS B 142 LEU B 143 MET B 231
SITE 2 CC7 14 ILE B 234 VAL B 237 SER B 240 CLA B 513
SITE 3 CC7 14 CLA B 514 CLA B 515 CLA B 518 CLA B 519
SITE 4 CC7 14 CLA B 522 CLA B 525
SITE 1 CC8 20 LMG A 373 TRP B 5 TYR B 6 ARG B 7
SITE 2 CC8 20 HIS B 9 ILE B 242 LEU B 461 PHE B 462
SITE 3 CC8 20 PHE B 464 GLY B 465 TRP B 468 HIS B 469
SITE 4 CC8 20 ARG B 472 PHE B 479 CLA B 514 CLA B 522
SITE 5 CC8 20 CLA B 523 CLA B 524 LMG B 531 PHE M 21
SITE 1 CC9 17 HIS B 9 HIS B 23 HIS B 26 THR B 27
SITE 2 CC9 17 ILE B 234 GLU B 235 VAL B 237 LEU B 238
SITE 3 CC9 17 SER B 241 ILE B 242 CLA B 514 CLA B 515
SITE 4 CC9 17 CLA B 520 CLA B 521 CLA B 523 CLA B 524
SITE 5 CC9 17 CLA B 525
SITE 1 DC1 12 HIS B 9 HIS B 26 VAL B 30 TRP B 33
SITE 2 DC1 12 PHE B 462 CLA B 514 CLA B 517 CLA B 521
SITE 3 DC1 12 CLA B 522 CLA B 524 BCR B 527 LMG B 531
SITE 1 DC2 12 VAL B 8 HIS B 9 ALA B 22 TRP B 115
SITE 2 DC2 12 CLA B 521 CLA B 522 CLA B 523 BCR B 527
SITE 3 DC2 12 DGD B 533 VAL L 10 PHE M 21 LEU M 25
SITE 1 DC3 11 HIS B 23 LEU B 24 MET B 138 HIS B 142
SITE 2 DC3 11 LEU B 145 CLA B 514 CLA B 520 CLA B 522
SITE 3 DC3 11 CLA B 526 BCR B 530 LEU H 14
SITE 1 DC4 10 LEU B 24 ALA B 110 TRP B 113 HIS B 114
SITE 2 DC4 10 CLA B 516 CLA B 525 BCR B 530 THR H 5
SITE 3 DC4 10 LEU H 7 GLY H 8
SITE 1 DC5 9 MET B 25 LEU B 29 ALA B 111 TRP B 115
SITE 2 DC5 9 CLA B 523 CLA B 524 BCR B 529 DGD B 533
SITE 3 DC5 9 LEU M 13
SITE 1 DC6 6 LEU B 29 TRP B 33 GLY B 105 CLA B 517
SITE 2 DC6 6 BCR B 527 DGD B 533
SITE 1 DC7 4 CLA B 515 CLA B 525 CLA B 526 LMT B 535
SITE 1 DC8 17 ALA A 233 TYR B 6 ARG B 7 PHE B 464
SITE 2 DC8 17 TRP B 468 PHE B 479 CLA B 517 CLA B 521
SITE 3 DC8 17 CLA B 523 DGD B 533 ARG D 139 TYR D 141
SITE 4 DC8 17 PHE D 269 LEU D 272 VAL D 276 PHE M 14
SITE 5 DC8 17 PRO M 18
SITE 1 DC9 16 THR B 327 LYS B 332 LEU B 461 CLA B 517
SITE 2 DC9 16 CLA B 524 BCR B 527 BCR B 529 LMG B 531
SITE 3 DC9 16 ILE D 284 PHE L 35 ASN M 4 LEU M 6
SITE 4 DC9 16 ALA M 10 LEU M 13 PHE M 14 VAL M 17
SITE 1 EC1 3 TRP B 91 LEU B 149 BCR B 530
SITE 1 EC2 6 LYS B 227 ASP D 19 ASP D 20 LYS D 23
SITE 2 EC2 6 SQD D 361 MET H 35
SITE 1 EC3 16 LEU C 95 LEU C 168 GLY C 171 ALA C 172
SITE 2 EC3 16 TRP C 223 ILE C 224 HIS C 237 ILE C 240
SITE 3 EC3 16 PHE C 289 VAL C 296 TYR C 297 CLA C 478
SITE 4 EC3 16 CLA C 479 CLA C 482 CLA C 483 BCR C 490
SITE 1 EC4 20 TRP C 63 HIS C 91 LEU C 174 LEU C 175
SITE 2 EC4 20 LYS C 178 PHE C 182 LEU C 279 MET C 282
SITE 3 EC4 20 GLY C 283 ALA C 286 VAL C 290 TYR C 297
SITE 4 EC4 20 HIS C 430 LEU C 433 ALA C 434 PHE C 437
SITE 5 EC4 20 CLA C 477 CLA C 479 CLA C 480 CLA K 483
SITE 1 EC5 14 ILE C 60 VAL C 61 TRP C 63 ALA C 64
SITE 2 EC5 14 THR C 68 LEU C 88 HIS C 91 LEU C 95
SITE 3 EC5 14 VAL C 114 HIS C 118 CLA C 477 CLA C 478
SITE 4 EC5 14 LMG C 494 CLA K 483
SITE 1 EC6 18 VAL A 281 LHG A 371 TRP C 63 MET C 67
SITE 2 EC6 18 PHE C 70 GLN C 84 GLY C 85 LEU C 404
SITE 3 EC6 18 TRP C 425 LEU C 426 SER C 429 CLA C 478
SITE 4 EC6 18 CLA C 484 DGD C 492 DGD C 493 LMG J 492
SITE 5 EC6 18 PRO K 26 CLA K 483
SITE 1 EC7 18 PHE A 33 MET A 127 GLY A 128 TRP A 131
SITE 2 EC7 18 CLA A 366 PHE C 264 ILE C 265 TYR C 274
SITE 3 EC7 18 GLY C 277 MET C 281 HIS C 441 LEU C 442
SITE 4 EC7 18 ALA C 445 ARG C 449 DGD C 474 CLA C 483
SITE 5 EC7 18 BCR C 490 PHE I 23
SITE 1 EC8 15 LEU C 161 LEU C 165 ILE C 243 CYS C 244
SITE 2 EC8 15 TRP C 250 HIS C 251 THR C 255 PRO C 256
SITE 3 EC8 15 PHE C 257 TRP C 259 ALA C 260 PHE C 264
SITE 4 EC8 15 CLA C 477 CLA C 483 BCR C 490
SITE 1 EC9 16 MET C 157 LEU C 161 HIS C 164 LEU C 165
SITE 2 EC9 16 LEU C 168 ILE C 240 PHE C 264 TRP C 266
SITE 3 EC9 16 TYR C 271 TYR C 274 SER C 275 CLA C 477
SITE 4 EC9 16 CLA C 481 CLA C 482 CLA C 485 BCR C 490
SITE 1 FC1 19 LHG A 371 TRP C 36 ALA C 37 GLY C 38
SITE 2 FC1 19 ASN C 39 ALA C 40 GLU C 269 LEU C 276
SITE 3 FC1 19 PHE C 436 PHE C 437 GLY C 440 TRP C 443
SITE 4 FC1 19 HIS C 444 ARG C 447 SQD C 475 CLA C 480
SITE 5 FC1 19 CLA C 485 CLA C 486 CLA K 483
SITE 1 FC2 18 ASN C 39 ILE C 43 LEU C 49 ALA C 52
SITE 2 FC2 18 HIS C 53 HIS C 56 TRP C 151 HIS C 164
SITE 3 FC2 18 GLY C 268 TYR C 271 LEU C 272 SER C 275
SITE 4 FC2 18 LEU C 276 LEU C 279 CLA C 483 CLA C 484
SITE 5 FC2 18 CLA C 487 CLA K 483
SITE 1 FC3 16 HIS C 56 LEU C 59 ILE C 60 TRP C 63
SITE 2 FC3 16 LEU C 279 PHE C 436 PHE C 437 CLA C 478
SITE 3 FC3 16 CLA C 479 CLA C 480 CLA C 484 CLA C 485
SITE 4 FC3 16 CLA C 486 PRO K 29 VAL K 30 LEU K 33
SITE 1 FC4 28 GLN C 28 TRP C 35 GLY C 38 ASN C 39
SITE 2 FC4 28 ARG C 41 LEU C 42 LEU C 45 LYS C 48
SITE 3 FC4 28 ALA C 52 ALA C 123 PHE C 127 VAL C 130
SITE 4 FC4 28 ALA C 133 ILE C 134 CLA C 484 BCR C 489
SITE 5 FC4 28 PHE K 32 LEU K 33 PHE K 37 TRP K 39
SITE 6 FC4 28 GLN K 40 CLA K 483 MET Z 19 VAL Z 20
SITE 7 FC4 28 PRO Z 24 ILE y 35 LEU y 39 ASN y 45
SITE 1 FC5 14 HIS C 53 VAL C 54 ALA C 57 LEU C 125
SITE 2 FC5 14 ILE C 160 PHE C 163 HIS C 164 VAL C 167
SITE 3 FC5 14 ILE C 170 GLY C 171 LEU C 174 CLA C 485
SITE 4 FC5 14 CLA C 488 BCR Z 116
SITE 1 FC6 9 VAL C 54 VAL C 124 LEU C 125 GLY C 128
SITE 2 FC6 9 TYR C 131 HIS C 132 PHE C 147 CLA C 487
SITE 3 FC6 9 BCR Z 116
SITE 1 FC7 15 ALA C 55 GLY C 58 LEU C 59 VAL C 116
SITE 2 FC7 15 LEU C 119 SER C 122 ALA C 123 CLA C 486
SITE 3 FC7 15 BCR J 112 TYR K 15 PHE K 18 LEU K 21
SITE 4 FC7 15 LEU Z 9 VAL Z 13 VAL Z 20
SITE 1 FC8 15 ILE C 209 PHE C 210 TYR C 212 LEU C 213
SITE 2 FC8 15 VAL C 227 ASP C 232 VAL C 233 HIS C 237
SITE 3 FC8 15 ILE C 240 PHE C 264 CLA C 477 CLA C 481
SITE 4 FC8 15 CLA C 482 CLA C 483 PHE I 23
SITE 1 FC9 18 PHE A 155 ILE A 160 PRO C 217 PHE C 218
SITE 2 FC9 18 GLY C 219 GLY C 220 TRP C 223 VAL C 225
SITE 3 FC9 18 PHE C 284 CYS C 288 PHE C 292 ASN C 293
SITE 4 FC9 18 ASN C 294 THR C 295 ASP C 360 ARG C 362
SITE 5 FC9 18 LEU C 438 DGD C 474
SITE 1 GC1 18 PHE A 197 THR A 292 GLU C 83 GLN C 84
SITE 2 GC1 18 GLY C 85 SER C 406 ASN C 418 PHE C 419
SITE 3 GC1 18 VAL C 420 TRP C 425 VAL C 432 LHG C 476
SITE 4 GC1 18 CLA C 480 DGD C 493 PHE J 29 TYR J 33
SITE 5 GC1 18 BCR J 115 LMG J 492
SITE 1 GC2 24 LEU A 200 ALA A 203 TRP A 278 VAL A 281
SITE 2 GC2 24 PHE A 300 CLA A 364 LEU C 404 ASN C 405
SITE 3 GC2 24 SER C 406 VAL C 407 ASN C 415 SER C 416
SITE 4 GC2 24 VAL C 417 ASN C 418 CLA C 480 DGD C 492
SITE 5 GC2 24 LMG D 359 PHE J 29 ALA J 32 TYR J 33
SITE 6 GC2 24 GLY J 37 SER J 38 SER J 39 LEU J 40
SITE 1 GC3 7 HIS C 74 CLA C 480 DGD C 492 ILE J 22
SITE 2 GC3 7 BCR J 115 VAL K 30 ILE y 25
SITE 1 GC4 7 PHE C 109 PRO C 110 VAL C 113 VAL C 114
SITE 2 GC4 7 VAL C 117 CLA C 479 BCR Z 116
SITE 1 GC5 8 HIS A 215 TYR A 246 HIS A 272 FE2 A 361
SITE 2 GC5 8 HIS D 214 TYR D 244 LYS D 264 HIS D 268
SITE 1 GC6 25 PHE A 206 CLA A 362 CLA A 363 CLA A 364
SITE 2 GC6 25 TRP D 48 LEU D 122 PRO D 149 VAL D 152
SITE 3 GC6 25 SER D 155 VAL D 156 PHE D 181 LEU D 182
SITE 4 GC6 25 PHE D 185 GLN D 186 TRP D 191 THR D 192
SITE 5 GC6 25 HIS D 197 VAL D 201 VAL D 204 LEU D 279
SITE 6 GC6 25 SER D 282 ALA D 283 VAL D 286 PHO D 355
SITE 7 GC6 25 LMG D 359
SITE 1 GC7 14 GLN A 199 VAL A 202 ALA A 203 CLA A 362
SITE 2 GC7 14 DGD C 493 PHE D 153 PHE D 157 VAL D 175
SITE 3 GC7 14 ILE D 178 PHE D 181 LEU D 182 CLA D 354
SITE 4 GC7 14 PHO D 355 LMG D 359
SITE 1 GC8 20 LEU A 210 MET A 214 ILE A 259 CLA A 364
SITE 2 GC8 20 LEU D 37 ALA D 41 ALA D 44 TRP D 48
SITE 3 GC8 20 GLY D 118 GLY D 121 LEU D 122 PHE D 125
SITE 4 GC8 20 ASN D 142 PHE D 146 ALA D 148 PRO D 149
SITE 5 GC8 20 GLY D 174 PRO D 275 LEU D 279 CLA D 354
SITE 1 GC9 16 CLA B 518 ILE D 35 PRO D 39 LEU D 43
SITE 2 GC9 16 LEU D 89 LEU D 90 LEU D 91 LEU D 92
SITE 3 GC9 16 TRP D 93 TRP D 104 THR D 112 PHE D 113
SITE 4 GC9 16 HIS D 117 VAL H 40 LEU X 23 GLY X 26
SITE 1 HC1 18 ILE A 53 CLA A 363 LMG A 373 ALA D 202
SITE 2 HC1 18 LEU D 210 ILE D 213 HIS D 214 THR D 217
SITE 3 HC1 18 MET D 246 TRP D 253 ALA D 260 PHE D 261
SITE 4 HC1 18 LEU D 267 VAL D 274 LMG D 360 VAL L 26
SITE 5 HC1 18 LEU L 29 PHE T 10
SITE 1 HC2 12 TYR D 42 GLY D 46 GLY D 47 LEU D 49
SITE 2 HC2 12 THR D 50 PHE D 113 LMG D 359 PRO F 29
SITE 3 HC2 12 PHE F 33 LEU F 34 VAL J 21 VAL J 25
SITE 1 HC3 15 CLA A 364 SQD C 475 DGD C 493 TYR D 67
SITE 2 HC3 15 CYS D 71 CLA D 354 BCR D 358 LEU F 26
SITE 3 HC3 15 ILE F 37 MET F 40 GLN F 41 PHE J 28
SITE 4 HC3 15 GLY J 31 ALA J 32 GLY J 37
SITE 1 HC4 18 CLA A 363 PHO A 365 LMG A 373 ILE D 259
SITE 2 HC4 18 ALA D 260 PHE D 261 SER D 262 ASN D 263
SITE 3 HC4 18 TRP D 266 PL9 D 357 THR L 15 LEU L 19
SITE 4 HC4 18 LEU L 22 PHE T 10 ILE T 13 PHE T 17
SITE 5 HC4 18 ALA T 20 ILE T 21
SITE 1 HC5 9 LYS B 227 ARG B 230 CLA B 518 LYS D 23
SITE 2 HC5 9 TRP D 32 ARG D 134 LEU D 135 LMT D 536
SITE 3 HC5 9 PHE X 34
SITE 1 HC6 3 PHE D 101 ARG D 103 SQD F 224
SITE 1 HC7 4 GLU B 350 GLN D 98 GLY D 99 ILE X 21
SITE 1 HC8 14 ARG E 8 PHE E 10 ILE E 13 ARG E 18
SITE 2 HC8 14 TYR E 19 HIS E 23 THR E 26 LEU E 30
SITE 3 HC8 14 PHE F 16 ARG F 19 TRP F 20 HIS F 24
SITE 4 HC8 14 ALA F 27 ILE F 31
SITE 1 HC9 9 TRP D 21 ARG D 24 DGD D 362 PRO F 14
SITE 2 HC9 9 PHE F 16 THR F 17 VAL F 18 TRP F 20
SITE 3 HC9 9 ILE X 40
SITE 1 IC1 2 ARG F 45 GLU V 49
SITE 1 IC2 10 CLA B 511 CLA B 512 CLA B 519 MET H 35
SITE 2 IC2 10 PHE H 38 PHE H 41 THR X 11 ILE X 12
SITE 3 IC2 10 LEU X 16 PHE X 20
SITE 1 IC3 18 TYR B 193 PHE B 250 GLY B 254 TYR B 258
SITE 2 IC3 18 TYR B 273 SER B 277 PHE B 463 CLA B 512
SITE 3 IC3 18 GLY D 86 HIS D 87 PHE D 120 ILE D 159
SITE 4 IC3 18 LEU D 162 SER D 165 LEU H 46 TYR H 49
SITE 5 IC3 18 VAL H 60 SER H 61
SITE 1 IC4 2 DGD A 375 LMT I 274
SITE 1 IC5 9 SQD C 475 LHG C 476 DGD C 492 VAL J 21
SITE 2 IC5 9 ILE J 22 PHE J 29 TYR J 30 TYR J 33
SITE 3 IC5 9 LMG J 492
SITE 1 IC6 2 ASP K 19 ASP K 23
SITE 1 IC7 15 BCR C 489 ALA J 14 THR J 15 GLY J 18
SITE 2 IC7 15 MET J 19 LEU K 21 LEU K 31 PHE K 32
SITE 3 IC7 15 PHE K 37 VAL K 38 SER Z 16 PHE Z 17
SITE 4 IC7 15 ILE y 28 GLY y 29 GLY y 32
SITE 1 IC8 4 SQD L 213 ILE M 23 GLU M 30 SER M 31
SITE 1 IC9 3 MET M 1 MET T 1 PHE T 8
SITE 1 JC1 2 GLU O 140 HIS O 257
SITE 1 JC2 6 ALA A 100 DGD A 375 MET I 1 LEU I 4
SITE 2 JC2 6 LMG I 220 LYS O 95
SITE 1 JC3 4 ARG L 14 LEU L 21 LMG M 217 PHE T 19
SITE 1 JC4 1 DGD A 375
SITE 1 JC5 14 ALA C 393 ALA V 62 CYS V 63 CYS V 66
SITE 2 JC5 14 HIS V 67 THR V 74 ASN V 75 LEU V 78
SITE 3 JC5 14 LEU V 80 LEU V 85 TYR V 101 MET V 102
SITE 4 JC5 14 TYR V 108 HIS V 118
SITE 1 JC6 11 VAL C 116 SER C 121 LEU C 125 CLA C 487
SITE 2 JC6 11 CLA C 488 LMG C 494 TYR K 15 VAL Z 51
SITE 3 JC6 11 VAL Z 54 GLY Z 55 ASN Z 58
CRYST1 119.890 224.690 337.280 90.00 90.00 90.00 C 2 2 21 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 0.008341 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004451 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002965 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
