HEADER ELECTRON TRANSPORT 06-SEP-05 2AXT
TITLE CRYSTAL STRUCTURE OF PHOTOSYSTEM II FROM THERMOSYNECHOCOCCUS ELONGATUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOTOSYSTEM Q(B) PROTEIN;
COMPND 3 CHAIN: A, a;
COMPND 4 FRAGMENT: RESIDUES 1-344;
COMPND 5 SYNONYM: REACTION CENTRE SUBUNIT D1, 32 KDA THYLAKOID MEMBRANE
COMPND 6 PROTEIN, PHOTOSYSTEM II PROTEIN D1;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: CP47 PROTEIN;
COMPND 9 CHAIN: B, b;
COMPND 10 SYNONYM: ANTENNA SUBUNIT CP47;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: PHOTOSYSTEM II CP43 PROTEIN;
COMPND 13 CHAIN: C, c;
COMPND 14 SYNONYM: ANTENNA SUBUNIT CP43;
COMPND 15 MOL_ID: 4;
COMPND 16 MOLECULE: PHOTOSYSTEM II REACTION CENTER D2 PROTEIN;
COMPND 17 CHAIN: D, d;
COMPND 18 SYNONYM: REACTION CENTRE SUBUNIT D2;
COMPND 19 MOL_ID: 5;
COMPND 20 MOLECULE: CYTOCHROME B559 ALPHA SUBUNIT;
COMPND 21 CHAIN: E, e;
COMPND 22 SYNONYM: CYT B-559 SUBUNIT ALPHA, PSII REACTION CENTER SUBUNIT V;
COMPND 23 MOL_ID: 6;
COMPND 24 MOLECULE: CYTOCHROME B559 BETA SUBUNIT;
COMPND 25 CHAIN: F, f;
COMPND 26 SYNONYM: CYT B-559 SUBUNIT BETA, PSII REACTION CENTER SUBUNIT VI;
COMPND 27 MOL_ID: 7;
COMPND 28 MOLECULE: PHOTOSYSTEM II REACTION CENTER H PROTEIN;
COMPND 29 CHAIN: H, h;
COMPND 30 SYNONYM: SUBUNIT PSBH, PSII-H;
COMPND 31 MOL_ID: 8;
COMPND 32 MOLECULE: PHOTOSYSTEM II REACTION CENTER I PROTEIN;
COMPND 33 CHAIN: I, i;
COMPND 34 SYNONYM: SUBUNIT PSBI, PSII 4.4 KDA PROTEIN;
COMPND 35 MOL_ID: 9;
COMPND 36 MOLECULE: PHOTOSYSTEM II REACTION CENTER J PROTEIN;
COMPND 37 CHAIN: J, j;
COMPND 38 SYNONYM: SUBUNIT PSBJ;
COMPND 39 MOL_ID: 10;
COMPND 40 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN K;
COMPND 41 CHAIN: K, k;
COMPND 42 SYNONYM: SUBUNIT PSBK, PSII-K;
COMPND 43 MOL_ID: 11;
COMPND 44 MOLECULE: PHOTOSYSTEM II REACTION CENTER L PROTEIN;
COMPND 45 CHAIN: L, l;
COMPND 46 SYNONYM: SUBUNIT PSBL, PSII-L, PSII 5 KDA PROTEIN;
COMPND 47 MOL_ID: 12;
COMPND 48 MOLECULE: PHOTOSYSTEM II REACTION CENTER M PROTEIN;
COMPND 49 CHAIN: M, m;
COMPND 50 SYNONYM: SUBUNIT PSBM, PSII-M;
COMPND 51 MOL_ID: 13;
COMPND 52 MOLECULE: PHOTOSYSTEM II MANGANESE-STABILIZING POLYPEPTIDE;
COMPND 53 CHAIN: O, o;
COMPND 54 SYNONYM: SUBUNIT PSBO, MSP;
COMPND 55 MOL_ID: 14;
COMPND 56 MOLECULE: PHOTOSYSTEM II REACTION CENTER T PROTEIN;
COMPND 57 CHAIN: T, t;
COMPND 58 SYNONYM: SUBUNIT PSBT, PSII-T, PSII-TC;
COMPND 59 MOL_ID: 15;
COMPND 60 MOLECULE: PHOTOSYSTEM II 12 KDA EXTRINSIC PROTEIN;
COMPND 61 CHAIN: U, u;
COMPND 62 SYNONYM: SUBUNIT PSBU, PS II COMPLEX 12 KDA EXTRINSIC PROTEIN, PSII-
COMPND 63 U;
COMPND 64 MOL_ID: 16;
COMPND 65 MOLECULE: CYTOCHROME C-550;
COMPND 66 CHAIN: V, v;
COMPND 67 SYNONYM: CYT C-550, SUBUNIT PSBV, CYTOCHROME C550, LOW POTENTIAL
COMPND 68 CYTOCHROME C;
COMPND 69 MOL_ID: 17;
COMPND 70 MOLECULE: UNASSIGNED SUBUNITS;
COMPND 71 CHAIN: X, x;
COMPND 72 MOL_ID: 18;
COMPND 73 MOLECULE: PHOTOSYSTEM II REACTION CENTER Z PROTEIN;
COMPND 74 CHAIN: Z, z;
COMPND 75 SYNONYM: SUBUNIT PSBZ
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 3 ORGANISM_TAXID: 146786;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 6 ORGANISM_TAXID: 197221;
SOURCE 7 STRAIN: BP-1;
SOURCE 8 MOL_ID: 3;
SOURCE 9 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 10 ORGANISM_TAXID: 197221;
SOURCE 11 STRAIN: BP-1;
SOURCE 12 MOL_ID: 4;
SOURCE 13 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 14 ORGANISM_TAXID: 197221;
SOURCE 15 STRAIN: BP-1;
SOURCE 16 MOL_ID: 5;
SOURCE 17 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 18 ORGANISM_TAXID: 146786;
SOURCE 19 MOL_ID: 6;
SOURCE 20 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 21 ORGANISM_TAXID: 146786;
SOURCE 22 MOL_ID: 7;
SOURCE 23 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 24 ORGANISM_TAXID: 146786;
SOURCE 25 MOL_ID: 8;
SOURCE 26 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 27 ORGANISM_TAXID: 146786;
SOURCE 28 MOL_ID: 9;
SOURCE 29 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 30 ORGANISM_TAXID: 146786;
SOURCE 31 MOL_ID: 10;
SOURCE 32 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 33 ORGANISM_TAXID: 146786;
SOURCE 34 MOL_ID: 11;
SOURCE 35 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 36 ORGANISM_TAXID: 146786;
SOURCE 37 MOL_ID: 12;
SOURCE 38 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 39 ORGANISM_TAXID: 146786;
SOURCE 40 MOL_ID: 13;
SOURCE 41 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 42 ORGANISM_TAXID: 146786;
SOURCE 43 MOL_ID: 14;
SOURCE 44 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 45 ORGANISM_TAXID: 146786;
SOURCE 46 MOL_ID: 15;
SOURCE 47 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 48 ORGANISM_TAXID: 146786;
SOURCE 49 MOL_ID: 16;
SOURCE 50 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 51 ORGANISM_TAXID: 146786;
SOURCE 52 MOL_ID: 17;
SOURCE 53 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 54 ORGANISM_TAXID: 146786;
SOURCE 55 MOL_ID: 18;
SOURCE 56 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 57 ORGANISM_TAXID: 146786
KEYWDS PHOTOSYSTEM, PS II, PS2, MEMBRANE COMPLEX, TRANSMEMBRANE ALPHA-HELIX,
KEYWDS 2 ELECTRON TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR B.LOLL,J.KERN,W.SAENGER,A.ZOUNI,J.BIESIADKA
REVDAT 4 20-DEC-17 2AXT 1 ATOM
REVDAT 3 13-JUL-11 2AXT 1 VERSN
REVDAT 2 10-FEB-09 2AXT 1 VERSN ATOM
REVDAT 1 27-DEC-05 2AXT 0
JRNL AUTH B.LOLL,J.KERN,W.SAENGER,A.ZOUNI,J.BIESIADKA
JRNL TITL TOWARDS COMPLETE COFACTOR ARRANGEMENT IN THE 3.0 A
JRNL TITL 2 RESOLUTION STRUCTURE OF PHOTOSYSTEM II
JRNL REF NATURE V. 438 1040 2005
JRNL REFN ISSN 0028-0836
JRNL PMID 16355230
JRNL DOI 10.1038/NATURE04224
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 4628278.020
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 75.6
REMARK 3 NUMBER OF REFLECTIONS : 129965
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) : 0.234
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1620
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.18
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 50.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 14106
REMARK 3 BIN R VALUE (WORKING SET) : 0.3430
REMARK 3 BIN FREE R VALUE : 0.3830
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 1.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 182
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.028
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 40684
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 7570
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) : 71.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 27.02000
REMARK 3 B22 (A**2) : -2.46000
REMARK 3 B33 (A**2) : -24.56000
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) : 0.43
REMARK 3 ESD FROM SIGMAA (A) : 0.65
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) : 0.52
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.78
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 18.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.800
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) : 1.070 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.820 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.750 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.520 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.30
REMARK 3 BSOL : 39.65
REMARK 3
REMARK 3 NCS MODEL : CONSTR
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-NEW2.PARAM
REMARK 3 PARAMETER FILE 4 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2AXT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-OCT-05.
REMARK 100 THE DEPOSITION ID IS D_1000034441.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-FEB-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 155380
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.2
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.8300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 73.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.46600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.170
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 2000, PIPES, MAGNESIUM CHLORIDE,
REMARK 280 PH 7.0, BATCH, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 63.84600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 153.05300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 112.70150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 153.05300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 63.84600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 112.70150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 36-MERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, H, I, J, K,
REMARK 350 AND CHAINS: L, M, O, T, U, V, X, Z, a,
REMARK 350 AND CHAINS: b, c, d, e, f, h, i, j, k, l,
REMARK 350 AND CHAINS: m, o, t, u, v, 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 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 1
REMARK 465 LYS C 2
REMARK 465 THR C 3
REMARK 465 LEU C 4
REMARK 465 SER C 5
REMARK 465 SER C 6
REMARK 465 GLN C 7
REMARK 465 LYS C 8
REMARK 465 ARG C 9
REMARK 465 TYR C 10
REMARK 465 SER C 11
REMARK 465 PRO C 12
REMARK 465 VAL 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 ARG C 26
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 MET E 1
REMARK 465 ALA E 2
REMARK 465 MET F 1
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 GLN F 8
REMARK 465 GLU F 9
REMARK 465 PRO F 10
REMARK 465 MET H 1
REMARK 465 GLY H 66
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 ALA O 26
REMARK 465 ALA O 27
REMARK 465 LYS O 28
REMARK 465 GLN O 29
REMARK 465 ALA O 272
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 UNK X 32
REMARK 465 UNK X 33
REMARK 465 UNK X 34
REMARK 465 UNK X 35
REMARK 465 UNK X 36
REMARK 465 UNK X 37
REMARK 465 UNK X 38
REMARK 465 UNK X 39
REMARK 465 UNK X 40
REMARK 465 UNK X 41
REMARK 465 UNK X 42
REMARK 465 UNK X 43
REMARK 465 UNK X 44
REMARK 465 UNK X 45
REMARK 465 UNK X 46
REMARK 465 UNK X 47
REMARK 465 UNK X 48
REMARK 465 UNK X 49
REMARK 465 UNK X 93
REMARK 465 UNK X 94
REMARK 465 UNK X 95
REMARK 465 UNK X 96
REMARK 465 UNK X 97
REMARK 465 UNK X 98
REMARK 465 UNK X 99
REMARK 465 MET a 5001
REMARK 465 THR a 5002
REMARK 465 THR a 5003
REMARK 465 THR a 5004
REMARK 465 LEU a 5005
REMARK 465 GLN a 5006
REMARK 465 ARG a 5007
REMARK 465 ARG a 5008
REMARK 465 GLU a 5009
REMARK 465 MET b 5001
REMARK 465 GLN b 5490
REMARK 465 VAL b 5491
REMARK 465 GLU b 5492
REMARK 465 TRP b 5493
REMARK 465 GLY b 5494
REMARK 465 PHE b 5495
REMARK 465 TYR b 5496
REMARK 465 GLN b 5497
REMARK 465 LYS b 5498
REMARK 465 VAL b 5499
REMARK 465 GLY b 5500
REMARK 465 ASP b 5501
REMARK 465 VAL b 5502
REMARK 465 THR b 5503
REMARK 465 THR b 5504
REMARK 465 ARG b 5505
REMARK 465 ARG b 5506
REMARK 465 LYS b 5507
REMARK 465 GLU b 5508
REMARK 465 ALA b 5509
REMARK 465 VAL b 5510
REMARK 465 MET c 5001
REMARK 465 LYS c 5002
REMARK 465 THR c 5003
REMARK 465 LEU c 5004
REMARK 465 SER c 5005
REMARK 465 SER c 5006
REMARK 465 GLN c 5007
REMARK 465 LYS c 5008
REMARK 465 ARG c 5009
REMARK 465 TYR c 5010
REMARK 465 SER c 5011
REMARK 465 PRO c 5012
REMARK 465 VAL c 5013
REMARK 465 VAL c 5014
REMARK 465 THR c 5015
REMARK 465 LEU c 5016
REMARK 465 SER c 5017
REMARK 465 SER c 5018
REMARK 465 ASN c 5019
REMARK 465 SER c 5020
REMARK 465 ILE c 5021
REMARK 465 PHE c 5022
REMARK 465 ALA c 5023
REMARK 465 THR c 5024
REMARK 465 ASN c 5025
REMARK 465 ARG c 5026
REMARK 465 MET d 5001
REMARK 465 THR d 5002
REMARK 465 ILE d 5003
REMARK 465 ALA d 5004
REMARK 465 ILE d 5005
REMARK 465 GLY d 5006
REMARK 465 ARG d 5007
REMARK 465 ALA d 5008
REMARK 465 PRO d 5009
REMARK 465 ALA d 5010
REMARK 465 GLU d 5011
REMARK 465 ARG d 5012
REMARK 465 MET e 5001
REMARK 465 ALA e 5002
REMARK 465 MET f 5001
REMARK 465 THR f 5002
REMARK 465 SER f 5003
REMARK 465 ASN f 5004
REMARK 465 THR f 5005
REMARK 465 PRO f 5006
REMARK 465 ASN f 5007
REMARK 465 GLN f 5008
REMARK 465 GLU f 5009
REMARK 465 PRO f 5010
REMARK 465 MET h 5001
REMARK 465 GLY h 5066
REMARK 465 ASP i 5036
REMARK 465 LEU i 5037
REMARK 465 GLU i 5038
REMARK 465 MET j 5001
REMARK 465 MET j 5002
REMARK 465 SER j 5003
REMARK 465 GLU j 5004
REMARK 465 GLY j 5005
REMARK 465 GLY j 5006
REMARK 465 ALA o 5026
REMARK 465 ALA o 5027
REMARK 465 LYS o 5028
REMARK 465 GLN o 5029
REMARK 465 ALA o 5272
REMARK 465 LYS t 5031
REMARK 465 LYS t 5032
REMARK 465 ALA u 5031
REMARK 465 THR u 5032
REMARK 465 ALA u 5033
REMARK 465 SER u 5034
REMARK 465 THR u 5035
REMARK 465 GLU u 5036
REMARK 465 UNK x 5032
REMARK 465 UNK x 5033
REMARK 465 UNK x 5034
REMARK 465 UNK x 5035
REMARK 465 UNK x 5036
REMARK 465 UNK x 5037
REMARK 465 UNK x 5038
REMARK 465 UNK x 5039
REMARK 465 UNK x 5040
REMARK 465 UNK x 5041
REMARK 465 UNK x 5042
REMARK 465 UNK x 5043
REMARK 465 UNK x 5044
REMARK 465 UNK x 5045
REMARK 465 UNK x 5046
REMARK 465 UNK x 5047
REMARK 465 UNK x 5048
REMARK 465 UNK x 5049
REMARK 465 UNK x 5093
REMARK 465 UNK x 5094
REMARK 465 UNK x 5095
REMARK 465 UNK x 5096
REMARK 465 UNK x 5097
REMARK 465 UNK x 5098
REMARK 465 UNK x 5099
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 SER A 10 OG
REMARK 470 GLU A 229 CG CD OE1 OE2
REMARK 470 ARG B 127 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 224 CG CD NE CZ NH1 NH2
REMARK 470 THR B 297 OG1 CG2
REMARK 470 ILE B 482 CG1 CG2 CD1
REMARK 470 ASP B 483 CG OD1 OD2
REMARK 470 GLU B 485 CG CD OE1 OE2
REMARK 470 LEU B 486 CG CD1 CD2
REMARK 470 SER B 487 OG
REMARK 470 PRO B 488 CG CD
REMARK 470 GLU B 489 CG CD OE1 OE2
REMARK 470 GLN C 28 CG CD OE1 NE2
REMARK 470 GLU C 104 CG CD OE1 OE2
REMARK 470 ARG C 135 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 141 CG CD OE1 OE2
REMARK 470 TYR C 143 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER C 144 OG
REMARK 470 LYS C 156 CG CD CE NZ
REMARK 470 GLU C 462 CG CD OE1 OE2
REMARK 470 ARG D 24 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 239 CG CD OE1 NE2
REMARK 470 ARG E 8 CG CD NE CZ NH1 NH2
REMARK 470 ASP E 12 CG OD1 OD2
REMARK 470 ARG E 61 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 84 CG CD CE NZ
REMARK 470 SER F 12 OG
REMARK 470 ILE F 15 CG1 CG2 CD1
REMARK 470 ARG H 4 CG CD NE CZ NH1 NH2
REMARK 470 LYS H 20 CG CD CE NZ
REMARK 470 SER H 61 OG
REMARK 470 LEU H 65 CG CD1 CD2
REMARK 470 ARG J 7 CG CD NE CZ NH1 NH2
REMARK 470 LEU J 10 CG CD1 CD2
REMARK 470 LYS K 10 CG CD CE NZ
REMARK 470 MET L 1 CG SD CE
REMARK 470 LYS M 34 CG CD CE NZ
REMARK 470 LEU O 31 CG CD1 CD2
REMARK 470 ASP O 49 CG OD1 OD2
REMARK 470 ARG O 53 CG CD NE CZ NH1 NH2
REMARK 470 ILE O 58 CG1 CG2 CD1
REMARK 470 SER O 61 OG
REMARK 470 GLN O 62 CG CD OE1 NE2
REMARK 470 LYS O 79 CG CD CE NZ
REMARK 470 GLU O 80 CG CD OE1 OE2
REMARK 470 LYS O 83 CG CD CE NZ
REMARK 470 ASN O 84 CG OD1 ND2
REMARK 470 LYS O 85 CG CD CE NZ
REMARK 470 ARG O 86 CG CD NE CZ NH1 NH2
REMARK 470 GLN O 87 CG CD OE1 NE2
REMARK 470 GLU O 88 CG CD OE1 OE2
REMARK 470 GLU O 90 CG CD OE1 OE2
REMARK 470 LYS O 95 CG CD CE NZ
REMARK 470 GLU O 124 CG CD OE1 OE2
REMARK 470 VAL O 159 CG1 CG2
REMARK 470 SER O 161 OG
REMARK 470 SER O 165 OG
REMARK 470 GLN O 222 CG CD OE1 NE2
REMARK 470 ASN O 226 CG OD1 ND2
REMARK 470 LYS O 229 CG CD CE NZ
REMARK 470 ARG O 233 CG CD NE CZ NH1 NH2
REMARK 470 SER O 247 OG
REMARK 470 THR T 30 OG1 CG2
REMARK 470 GLU U 37 CG CD OE1 OE2
REMARK 470 GLU U 99 CG CD OE1 OE2
REMARK 470 GLN Z 31 CG CD OE1 NE2
REMARK 470 ASP Z 32 CG OD1 OD2
REMARK 470 TRP Z 33 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP Z 33 CZ3 CH2
REMARK 470 ASP Z 34 CG OD1 OD2
REMARK 470 ARG Z 35 CG CD NE CZ NH1 NH2
REMARK 470 SER Z 36 OG
REMARK 470 LYS Z 37 CG CD CE NZ
REMARK 470 GLN Z 38 CG CD OE1 NE2
REMARK 470 VAL Z 62 CG1 CG2
REMARK 470 SER a5010 OG
REMARK 470 GLU a5229 CG CD OE1 OE2
REMARK 470 ARG b5127 CG CD NE CZ NH1 NH2
REMARK 470 ARG b5224 CG CD NE CZ NH1 NH2
REMARK 470 THR b5297 OG1 CG2
REMARK 470 ILE b5482 CG1 CG2 CD1
REMARK 470 ASP b5483 CG OD1 OD2
REMARK 470 GLU b5485 CG CD OE1 OE2
REMARK 470 LEU b5486 CG CD1 CD2
REMARK 470 SER b5487 OG
REMARK 470 PRO b5488 CG CD
REMARK 470 GLU b5489 CG CD OE1 OE2
REMARK 470 GLN c5028 CG CD OE1 NE2
REMARK 470 GLU c5104 CG CD OE1 OE2
REMARK 470 ARG c5135 CG CD NE CZ NH1 NH2
REMARK 470 GLU c5141 CG CD OE1 OE2
REMARK 470 TYR c5143 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER c5144 OG
REMARK 470 LYS c5156 CG CD CE NZ
REMARK 470 GLU c5462 CG CD OE1 OE2
REMARK 470 ARG d5024 CG CD NE CZ NH1 NH2
REMARK 470 GLN d5239 CG CD OE1 NE2
REMARK 470 ARG e5008 CG CD NE CZ NH1 NH2
REMARK 470 ASP e5012 CG OD1 OD2
REMARK 470 ARG e5061 CG CD NE CZ NH1 NH2
REMARK 470 LYS e5084 CG CD CE NZ
REMARK 470 SER f5012 OG
REMARK 470 ILE f5015 CG1 CG2 CD1
REMARK 470 ARG h5004 CG CD NE CZ NH1 NH2
REMARK 470 LYS h5020 CG CD CE NZ
REMARK 470 SER h5061 OG
REMARK 470 LEU h5065 CG CD1 CD2
REMARK 470 ARG j5007 CG CD NE CZ NH1 NH2
REMARK 470 LEU j5010 CG CD1 CD2
REMARK 470 LYS k5010 CG CD CE NZ
REMARK 470 MET l5001 CG SD CE
REMARK 470 LYS m5034 CG CD CE NZ
REMARK 470 LEU o5031 CG CD1 CD2
REMARK 470 ASP o5049 CG OD1 OD2
REMARK 470 ARG o5053 CG CD NE CZ NH1 NH2
REMARK 470 ILE o5058 CG1 CG2 CD1
REMARK 470 SER o5061 OG
REMARK 470 GLN o5062 CG CD OE1 NE2
REMARK 470 LYS o5079 CG CD CE NZ
REMARK 470 GLU o5080 CG CD OE1 OE2
REMARK 470 LYS o5083 CG CD CE NZ
REMARK 470 ASN o5084 CG OD1 ND2
REMARK 470 LYS o5085 CG CD CE NZ
REMARK 470 ARG o5086 CG CD NE CZ NH1 NH2
REMARK 470 GLN o5087 CG CD OE1 NE2
REMARK 470 GLU o5088 CG CD OE1 OE2
REMARK 470 GLU o5090 CG CD OE1 OE2
REMARK 470 LYS o5095 CG CD CE NZ
REMARK 470 GLU o5124 CG CD OE1 OE2
REMARK 470 VAL o5159 CG1 CG2
REMARK 470 SER o5161 OG
REMARK 470 SER o5165 OG
REMARK 470 GLN o5222 CG CD OE1 NE2
REMARK 470 ASN o5226 CG OD1 ND2
REMARK 470 LYS o5229 CG CD CE NZ
REMARK 470 ARG o5233 CG CD NE CZ NH1 NH2
REMARK 470 SER o5247 OG
REMARK 470 THR t5030 OG1 CG2
REMARK 470 GLU u5037 CG CD OE1 OE2
REMARK 470 GLU u5099 CG CD OE1 OE2
REMARK 470 GLN z5031 CG CD OE1 NE2
REMARK 470 ASP z5032 CG OD1 OD2
REMARK 470 TRP z5033 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP z5033 CZ3 CH2
REMARK 470 ASP z5034 CG OD1 OD2
REMARK 470 ARG z5035 CG CD NE CZ NH1 NH2
REMARK 470 SER z5036 OG
REMARK 470 LYS z5037 CG CD CE NZ
REMARK 470 GLN z5038 CG CD OE1 NE2
REMARK 470 VAL z5062 CG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O GLY v 5159 N VAL v 5161 2.08
REMARK 500 O GLY V 159 N VAL V 161 2.08
REMARK 500 OE1 GLN M 28 OXT SER m 5036 2.16
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 C 298 C - N - CA ANGL. DEV. = 10.7 DEGREES
REMARK 500 PRO O 46 C - N - CA ANGL. DEV. = 10.3 DEGREES
REMARK 500 PRO O 271 CA - C - O ANGL. DEV. = 17.2 DEGREES
REMARK 500 PRO U 73 C - N - CD ANGL. DEV. = -14.7 DEGREES
REMARK 500 PRO a5340 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 PRO c5298 C - N - CA ANGL. DEV. = 11.4 DEGREES
REMARK 500 PRO o5046 C - N - CA ANGL. DEV. = 10.5 DEGREES
REMARK 500 PRO u5073 C - N - CD ANGL. DEV. = -13.8 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 ALA A 11 42.02 172.21
REMARK 500 ASN A 12 105.68 52.02
REMARK 500 ARG A 27 -56.19 -25.32
REMARK 500 ALA A 55 120.50 165.27
REMARK 500 ASP A 59 72.97 -63.13
REMARK 500 ASP A 61 -175.90 -64.95
REMARK 500 ILE A 63 -149.17 -52.67
REMARK 500 GLU A 65 75.46 -119.27
REMARK 500 LEU A 72 1.28 -61.67
REMARK 500 TYR A 94 75.76 -109.99
REMARK 500 GLN A 130 18.35 -63.28
REMARK 500 TRP A 131 -53.08 -128.97
REMARK 500 PRO A 141 -108.12 -69.78
REMARK 500 TRP A 142 -12.48 26.64
REMARK 500 MET A 172 123.60 -21.70
REMARK 500 SER A 217 -76.26 -61.04
REMARK 500 GLU A 226 27.59 -147.68
REMARK 500 THR A 230 55.90 -104.15
REMARK 500 GLU A 231 132.99 -177.34
REMARK 500 SER A 232 144.46 -34.28
REMARK 500 GLU A 242 -79.40 -44.17
REMARK 500 ILE A 259 -70.21 -103.20
REMARK 500 PHE A 260 133.89 173.50
REMARK 500 GLN A 261 -69.19 -17.84
REMARK 500 ALA A 263 34.15 -90.73
REMARK 500 ASN A 266 -4.24 -174.08
REMARK 500 SER A 305 -151.78 -97.82
REMARK 500 VAL A 306 65.97 23.62
REMARK 500 ASN A 315 125.34 54.46
REMARK 500 LEU A 343 40.69 -102.94
REMARK 500 VAL B 11 10.76 -57.49
REMARK 500 ILE B 13 -8.87 -59.74
REMARK 500 ASN B 14 43.12 -152.03
REMARK 500 PRO B 16 -23.91 -35.38
REMARK 500 THR B 44 -5.29 -140.53
REMARK 500 ASP B 87 93.37 -162.11
REMARK 500 TRP B 91 67.63 -64.76
REMARK 500 ALA B 132 148.93 -171.58
REMARK 500 HIS B 157 -80.83 -72.93
REMARK 500 PHE B 162 81.07 -154.90
REMARK 500 ALA B 228 -78.40 -42.10
REMARK 500 ARG B 230 59.77 4.50
REMARK 500 MET B 231 -174.39 -57.52
REMARK 500 GLU B 235 9.22 -66.27
REMARK 500 SER B 260 135.13 144.70
REMARK 500 THR B 297 151.93 -49.63
REMARK 500 ASP B 313 41.49 -89.95
REMARK 500 ALA B 361 101.54 -54.34
REMARK 500 PHE B 362 -40.27 168.56
REMARK 500 ASP B 372 -158.46 -75.72
REMARK 500
REMARK 500 THIS ENTRY HAS 588 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 B 273 0.07 SIDE CHAIN
REMARK 500 TYR b5273 0.07 SIDE CHAIN
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 CLA A 563
REMARK 610 PQ9 A 564
REMARK 610 LHG A 567
REMARK 610 SQD A 5212
REMARK 610 CLA B 511
REMARK 610 CLA B 524
REMARK 610 CLA C 492
REMARK 610 CLA C 494
REMARK 610 CLA C 499
REMARK 610 CLA C 502
REMARK 610 CLA C 503
REMARK 610 DGD C 507
REMARK 610 DGD C 508
REMARK 610 DGD C 509
REMARK 610 CLA D 355
REMARK 610 PQ9 D 356
REMARK 610 MGE D 358
REMARK 610 MGE D 359
REMARK 610 DGD H 208
REMARK 610 SQD L 5213
REMARK 610 SQD a 212
REMARK 610 CLA a 5563
REMARK 610 PQ9 a 5564
REMARK 610 LHG a 5567
REMARK 610 CLA b 5511
REMARK 610 CLA b 5524
REMARK 610 CLA c 5492
REMARK 610 CLA c 5494
REMARK 610 CLA c 5499
REMARK 610 CLA c 5502
REMARK 610 CLA c 5503
REMARK 610 DGD c 5507
REMARK 610 DGD c 5508
REMARK 610 DGD c 5509
REMARK 610 CLA d 5355
REMARK 610 PQ9 d 5356
REMARK 610 MGE d 5359
REMARK 610 MGE d 5360
REMARK 610 DGD h 5208
REMARK 610 SQD t 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 HEM F 51 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 23 NE2
REMARK 620 2 HEM F 51 NA 87.1
REMARK 620 3 HEM F 51 NB 92.1 88.2
REMARK 620 4 HEM F 51 NC 94.0 177.5 89.6
REMARK 620 5 HEM F 51 ND 91.3 90.4 176.3 91.8
REMARK 620 6 HIS F 24 NE2 157.6 75.9 73.2 102.5 103.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM V 552 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS V 67 NE2
REMARK 620 2 HEM V 552 NA 88.9
REMARK 620 3 HEM V 552 NB 81.9 89.8
REMARK 620 4 HEM V 552 NC 93.5 176.8 88.5
REMARK 620 5 HEM V 552 ND 102.2 92.0 175.6 89.5
REMARK 620 6 HIS V 118 NE2 163.5 85.3 82.7 91.7 93.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 A 557 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 215 NE2
REMARK 620 2 HIS A 272 NE2 95.9
REMARK 620 3 HIS D 214 NE2 114.4 92.0
REMARK 620 4 HIS D 268 NE2 88.2 166.0 98.5
REMARK 620 5 BCT D 353 O3 155.3 91.2 88.9 79.9
REMARK 620 6 BCT D 353 O2 98.7 80.5 146.8 85.7 59.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM f5051 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS e5023 NE2
REMARK 620 2 HEM f5051 NA 85.5
REMARK 620 3 HEM f5051 NB 91.0 87.3
REMARK 620 4 HEM f5051 NC 92.8 177.2 90.6
REMARK 620 5 HEM f5051 ND 89.2 90.6 177.8 91.6
REMARK 620 6 HIS f5024 NE2 156.3 75.9 73.8 105.2 105.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM v5552 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS v5067 NE2
REMARK 620 2 HEM v5552 NA 88.3
REMARK 620 3 HEM v5552 NB 80.7 89.9
REMARK 620 4 HEM v5552 NC 93.8 177.0 88.4
REMARK 620 5 HEM v5552 ND 102.4 92.0 176.4 89.6
REMARK 620 6 HIS v5118 NE2 161.5 83.1 82.9 94.3 94.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 a5557 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS a5215 NE2
REMARK 620 2 HIS a5272 NE2 95.8
REMARK 620 3 HIS d5214 NE2 113.3 93.6
REMARK 620 4 HIS d5268 NE2 86.8 165.0 98.9
REMARK 620 5 BCT d5353 O3 155.9 88.9 89.9 83.0
REMARK 620 6 BCT d5353 O2 98.3 78.8 148.1 86.2 59.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEC A 565 CA1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 189 OE1
REMARK 620 2 ALA A 344 O 136.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEC A 565 MN1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 189 OE2
REMARK 620 2 ASP A 342 OD2 82.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA A 558 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 198 NE2
REMARK 620 2 CLA A 558 NA 88.3
REMARK 620 3 CLA A 558 NB 109.7 90.0
REMARK 620 4 CLA A 558 NC 108.8 161.9 89.5
REMARK 620 5 CLA A 558 ND 87.6 88.5 162.6 86.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEC A 565 MN3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 333 OE1
REMARK 620 2 GLU C 354 OE2 95.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEC A 565 MN2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 342 OD1
REMARK 620 2 ALA A 344 OXT 107.0
REMARK 620 3 GLU C 354 OE1 86.1 66.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B 524 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 9 NE2
REMARK 620 2 CLA B 524 NA 90.0
REMARK 620 3 CLA B 524 NB 84.3 88.8
REMARK 620 4 CLA B 524 NC 106.7 163.0 89.5
REMARK 620 5 CLA B 524 ND 113.2 89.0 162.4 87.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B 512 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 201 ND1
REMARK 620 2 CLA B 512 NA 99.3
REMARK 620 3 CLA B 512 NB 99.8 89.7
REMARK 620 4 CLA B 512 NC 97.8 162.9 88.1
REMARK 620 5 CLA B 512 ND 97.7 90.0 162.3 87.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B 513 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 202 NE2
REMARK 620 2 CLA B 513 NA 87.1
REMARK 620 3 CLA B 513 NB 100.9 90.9
REMARK 620 4 CLA B 513 NC 110.5 162.2 88.2
REMARK 620 5 CLA B 513 ND 96.6 88.3 162.4 87.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B 514 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 455 NE2
REMARK 620 2 CLA B 514 NA 101.3
REMARK 620 3 CLA B 514 NB 108.4 89.6
REMARK 620 4 CLA B 514 NC 96.7 161.4 89.2
REMARK 620 5 CLA B 514 ND 89.3 89.3 162.1 86.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B 518 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 466 NE2
REMARK 620 2 CLA B 518 NA 95.4
REMARK 620 3 CLA B 518 NB 111.8 89.5
REMARK 620 4 CLA B 518 NC 100.8 162.9 89.3
REMARK 620 5 CLA B 518 ND 85.1 88.8 163.1 87.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B 521 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 469 NE2
REMARK 620 2 CLA B 521 NA 82.9
REMARK 620 3 CLA B 521 NB 102.1 90.5
REMARK 620 4 CLA B 521 NC 114.2 162.7 88.5
REMARK 620 5 CLA B 521 ND 94.8 88.9 162.9 87.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C 39 OD1
REMARK 620 2 CLA C 501 NA 108.8
REMARK 620 3 CLA C 501 NB 92.9 90.1
REMARK 620 4 CLA C 501 NC 87.7 163.5 89.1
REMARK 620 5 CLA C 501 ND 102.9 89.1 163.6 87.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C 493 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 118 NE2
REMARK 620 2 CLA C 493 NA 99.5
REMARK 620 3 CLA C 493 NB 104.1 90.8
REMARK 620 4 CLA C 493 NC 97.6 162.4 88.5
REMARK 620 5 CLA C 493 ND 92.1 89.1 163.6 86.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C 503 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 132 NE2
REMARK 620 2 CLA C 503 NA 83.0
REMARK 620 3 CLA C 503 NB 107.9 89.7
REMARK 620 4 CLA C 503 NC 113.4 162.9 89.6
REMARK 620 5 CLA C 503 ND 89.4 88.6 162.3 86.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C 491 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 237 NE2
REMARK 620 2 CLA C 491 NA 101.6
REMARK 620 3 CLA C 491 NB 101.7 90.2
REMARK 620 4 CLA C 491 NC 94.4 163.8 88.8
REMARK 620 5 CLA C 491 ND 94.1 90.1 163.8 86.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C 496 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 251 NE2
REMARK 620 2 CLA C 496 NA 100.1
REMARK 620 3 CLA C 496 NB 84.5 89.8
REMARK 620 4 CLA C 496 NC 97.5 162.0 88.1
REMARK 620 5 CLA C 496 ND 113.8 88.7 161.6 87.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C 492 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 430 NE2
REMARK 620 2 CLA C 492 NA 84.2
REMARK 620 3 CLA C 492 NB 114.5 89.4
REMARK 620 4 CLA C 492 NC 110.2 164.8 88.9
REMARK 620 5 CLA C 492 ND 81.5 91.2 164.0 86.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C 498 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 444 NE2
REMARK 620 2 CLA C 498 NA 85.6
REMARK 620 3 CLA C 498 NB 96.6 88.1
REMARK 620 4 CLA C 498 NC 112.0 162.4 89.9
REMARK 620 5 CLA C 498 ND 101.4 89.9 161.7 86.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA D 354 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 197 NE2
REMARK 620 2 CLA D 354 NA 108.3
REMARK 620 3 CLA D 354 NB 97.2 90.2
REMARK 620 4 CLA D 354 NC 90.1 161.5 88.5
REMARK 620 5 CLA D 354 ND 101.6 89.2 160.4 85.9
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 OD1
REMARK 620 2 ASP K 23 OD2 62.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEC a5565 CA1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU a5189 OE1
REMARK 620 2 ALA a5344 O 130.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEC a5565 MN1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU a5189 OE2
REMARK 620 2 ASP a5342 OD2 77.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA a5558 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS a5198 NE2
REMARK 620 2 CLA a5558 NA 89.6
REMARK 620 3 CLA a5558 NB 110.6 89.5
REMARK 620 4 CLA a5558 NC 107.5 162.1 89.3
REMARK 620 5 CLA a5558 ND 86.6 89.3 162.8 86.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEC a5565 MN3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU a5333 OE1
REMARK 620 2 GLU c5354 OE2 98.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEC a5565 MN2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP a5342 OD1
REMARK 620 2 ALA a5344 OXT 110.6
REMARK 620 3 GLU c5354 OE1 88.9 69.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA b5524 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS b5009 NE2
REMARK 620 2 CLA b5524 NA 92.6
REMARK 620 3 CLA b5524 NB 84.9 89.0
REMARK 620 4 CLA b5524 NC 104.8 162.2 88.9
REMARK 620 5 CLA b5524 ND 112.5 89.4 162.6 87.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA b5512 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS b5201 ND1
REMARK 620 2 CLA b5512 NA 98.6
REMARK 620 3 CLA b5512 NB 99.9 90.7
REMARK 620 4 CLA b5512 NC 98.3 163.0 88.3
REMARK 620 5 CLA b5512 ND 97.6 89.4 162.3 86.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA b5513 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS b5202 NE2
REMARK 620 2 CLA b5513 NA 88.7
REMARK 620 3 CLA b5513 NB 99.9 90.9
REMARK 620 4 CLA b5513 NC 108.3 162.8 88.1
REMARK 620 5 CLA b5513 ND 96.7 88.6 163.3 87.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA b5514 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS b5455 NE2
REMARK 620 2 CLA b5514 NA 100.5
REMARK 620 3 CLA b5514 NB 108.4 89.2
REMARK 620 4 CLA b5514 NC 97.5 161.5 89.2
REMARK 620 5 CLA b5514 ND 89.4 89.6 162.1 86.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA b5518 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS b5466 NE2
REMARK 620 2 CLA b5518 NA 94.6
REMARK 620 3 CLA b5518 NB 112.3 89.2
REMARK 620 4 CLA b5518 NC 101.5 162.9 89.8
REMARK 620 5 CLA b5518 ND 84.2 89.0 163.5 87.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA b5521 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS b5469 NE2
REMARK 620 2 CLA b5521 NA 83.1
REMARK 620 3 CLA b5521 NB 101.2 89.7
REMARK 620 4 CLA b5521 NC 113.3 163.6 88.1
REMARK 620 5 CLA b5521 ND 95.0 90.8 163.7 86.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA c5501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN c5039 OD1
REMARK 620 2 CLA c5501 NA 109.7
REMARK 620 3 CLA c5501 NB 94.9 89.6
REMARK 620 4 CLA c5501 NC 87.1 163.2 89.0
REMARK 620 5 CLA c5501 ND 101.3 89.8 163.0 86.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA c5493 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS c5118 NE2
REMARK 620 2 CLA c5493 NA 99.5
REMARK 620 3 CLA c5493 NB 104.5 90.7
REMARK 620 4 CLA c5493 NC 97.9 162.3 88.6
REMARK 620 5 CLA c5493 ND 92.0 89.1 163.3 86.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA c5503 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS c5132 NE2
REMARK 620 2 CLA c5503 NA 82.8
REMARK 620 3 CLA c5503 NB 107.0 90.5
REMARK 620 4 CLA c5503 NC 112.8 163.7 89.1
REMARK 620 5 CLA c5503 ND 89.4 88.1 163.3 87.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA c5491 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS c5237 NE2
REMARK 620 2 CLA c5491 NA 100.5
REMARK 620 3 CLA c5491 NB 104.4 89.3
REMARK 620 4 CLA c5491 NC 96.9 162.3 89.2
REMARK 620 5 CLA c5491 ND 92.7 89.0 162.8 87.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA c5492 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS c5430 NE2
REMARK 620 2 CLA c5492 NA 85.1
REMARK 620 3 CLA c5492 NB 114.9 89.4
REMARK 620 4 CLA c5492 NC 109.4 164.5 89.2
REMARK 620 5 CLA c5492 ND 80.9 91.1 164.2 86.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA c5498 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS c5444 NE2
REMARK 620 2 CLA c5498 NA 85.7
REMARK 620 3 CLA c5498 NB 96.1 88.1
REMARK 620 4 CLA c5498 NC 112.4 161.9 89.6
REMARK 620 5 CLA c5498 ND 102.1 89.5 161.4 87.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA d5354 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS d5197 NE2
REMARK 620 2 CLA d5354 NA 107.1
REMARK 620 3 CLA d5354 NB 96.7 90.1
REMARK 620 4 CLA d5354 NC 89.8 163.1 88.9
REMARK 620 5 CLA d5354 ND 101.0 89.2 161.6 86.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA k5056 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP k5019 OD1
REMARK 620 2 ASP k5019 OD2 49.3
REMARK 620 3 ASP k5023 OD2 66.2 68.6
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 CA K 56
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 557
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT D 353
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA k 5056
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 a 5557
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT d 5353
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 558
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA D 354
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 559
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 560
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO A 561
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO A 562
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 563
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA D 355
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 522
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 523
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 524
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 525
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 526
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 491
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 492
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 493
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 494
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 495
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 496
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 497
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 498
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM F 51
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM V 552
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PQ9 D 356
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PQ9 A 564
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OEC A 565
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR A 566
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 527
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR t 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 528
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 529
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR H 107
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR D 357
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR X 130
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR C 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR C 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGE I 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD C 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG A 567
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD A 568
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD C 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD C 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGE D 358
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD H 208
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGE D 359
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGE L 210
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGE D 360
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD a 212
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD t 213
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGE B 530
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT A 569
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT m 216
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT T 217
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 5558
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA d 5354
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 5559
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 5560
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO a 5561
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO a 5562
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 5563
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA d 5355
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5511
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5512
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5513
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5514
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5515
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5516
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5517
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5518
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5519
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5520
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5521
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5522
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5523
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5524
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5525
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5526
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 5491
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 5492
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 5493
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 5494
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 5495
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 5496
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 5497
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 5498
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 5499
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 5500
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 5501
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 5502
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 5503
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM f 5051
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM v 5552
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PQ9 d 5356
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PQ9 a 5564
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OEC a 5565
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR a 5566
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR b 5527
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR T 5104
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR b 5528
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR b 5529
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR h 5107
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR d 5357
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR x 5130
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR c 5504
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR c 5505
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR c 5506
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGE i 5201
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD c 5507
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG a 5567
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD d 5358
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD c 5508
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD c 5509
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGE d 5359
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD h 5208
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGE d 5360
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGE l 5210
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGE d 5361
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD A 5212
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD L 5213
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGE b 5530
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT a 5568
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT M 5216
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT t 5217
DBREF 2AXT A 1 344 UNP P0A445 PSBA1_SYNEN 1 344
DBREF 2AXT B 1 510 GB 11761354 BAB19261 1 510
DBREF 2AXT C 1 473 GB 22295356 BAC09183 1 473
DBREF 2AXT D 1 352 GB 22295355 BAC09182 1 352
DBREF 2AXT E 1 84 UNP Q8DIP0 PSBE_SYNEL 0 83
DBREF 2AXT F 1 45 UNP Q8DIN9 PSBF_SYNEL 1 45
DBREF 2AXT H 1 66 UNP Q8DJ43 PSBH_SYNEL 1 66
DBREF 2AXT I 1 38 UNP Q8DJZ6 PSBI_SYNEL 1 38
DBREF 2AXT J 1 40 UNP P59087 PSBJ_SYNEL 1 40
DBREF 2AXT K 10 46 UNP Q9F1K9 PSBK_SYNEL 10 46
DBREF 2AXT L 1 37 UNP Q8DIN8 PSBL_SYNEL 1 37
DBREF 2AXT M 1 36 UNP Q8DHA7 PSBM_SYNEL 1 36
DBREF 2AXT O 26 272 UNP P0A431 PSBO_SYNEL 26 272
DBREF 2AXT T 1 32 UNP Q8DIQ0 PSBT_SYNEL 1 32
DBREF 2AXT U 31 134 UNP Q9F1L5 PSBU_SYNEL 31 134
DBREF 2AXT V 27 163 UNP P0A386 CY550_SYNEL 27 163
DBREF 2AXT Z 1 62 UNP Q8DHJ2 PSBZ_SYNEL 1 62
DBREF 2AXT a 5001 5344 UNP P0A445 PSBA1_SYNEN 1 344
DBREF 2AXT b 5001 5510 GB 11761354 BAB19261 1 510
DBREF 2AXT c 5001 5473 GB 22295356 BAC09183 1 473
DBREF 2AXT d 5001 5352 GB 22295355 BAC09182 1 352
DBREF 2AXT e 5001 5084 UNP Q8DIP0 PSBE_SYNEL 0 83
DBREF 2AXT f 5001 5045 UNP Q8DIN9 PSBF_SYNEL 1 45
DBREF 2AXT h 5001 5066 UNP Q8DJ43 PSBH_SYNEL 1 66
DBREF 2AXT i 5001 5038 UNP Q8DJZ6 PSBI_SYNEL 1 38
DBREF 2AXT j 5001 5040 UNP P59087 PSBJ_SYNEL 1 40
DBREF 2AXT k 5010 5046 UNP Q9F1K9 PSBK_SYNEL 10 46
DBREF 2AXT l 5001 5037 UNP Q8DIN8 PSBL_SYNEL 1 37
DBREF 2AXT m 5001 5036 UNP Q8DHA7 PSBM_SYNEL 1 36
DBREF 2AXT o 5026 5272 UNP P0A431 PSBO_SYNEL 26 272
DBREF 2AXT t 5001 5032 UNP Q8DIQ0 PSBT_SYNEL 1 32
DBREF 2AXT u 5031 5134 UNP Q9F1L5 PSBU_SYNEL 31 134
DBREF 2AXT v 5027 5163 UNP P0A386 CY550_SYNEL 27 163
DBREF 2AXT z 5001 5062 UNP Q8DHJ2 PSBZ_SYNEL 1 62
DBREF 2AXT X 1 129 PDB 2AXT 2AXT 1 129
DBREF 2AXT x 5001 5129 PDB 2AXT 2AXT 5001 5129
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 473 MET LYS THR LEU SER SER GLN LYS ARG TYR SER PRO VAL
SEQRES 2 C 473 VAL THR LEU SER SER ASN SER ILE PHE ALA THR ASN ARG
SEQRES 3 C 473 ASP GLN GLU SER SER GLY PHE ALA TRP TRP ALA GLY ASN
SEQRES 4 C 473 ALA ARG LEU ILE ASN LEU SER GLY LYS LEU LEU GLY ALA
SEQRES 5 C 473 HIS VAL ALA HIS ALA GLY LEU ILE VAL PHE TRP ALA GLY
SEQRES 6 C 473 ALA MET THR LEU PHE GLU LEU ALA HIS PHE ILE PRO GLU
SEQRES 7 C 473 LYS PRO MET TYR GLU GLN GLY LEU ILE LEU ILE PRO HIS
SEQRES 8 C 473 ILE ALA THR LEU GLY TRP GLY VAL GLY PRO GLY GLY GLU
SEQRES 9 C 473 VAL VAL ASP THR PHE PRO PHE PHE VAL VAL GLY VAL VAL
SEQRES 10 C 473 HIS LEU ILE SER SER ALA VAL LEU GLY PHE GLY GLY VAL
SEQRES 11 C 473 TYR HIS ALA ILE ARG GLY PRO GLU THR LEU GLU GLU TYR
SEQRES 12 C 473 SER SER PHE PHE GLY TYR ASP TRP LYS ASP LYS ASN LYS
SEQRES 13 C 473 MET THR THR ILE LEU GLY PHE HIS LEU ILE VAL LEU GLY
SEQRES 14 C 473 ILE GLY ALA LEU LEU LEU VAL ALA LYS ALA MET PHE PHE
SEQRES 15 C 473 GLY GLY LEU TYR ASP THR TRP ALA PRO GLY GLY GLY ASP
SEQRES 16 C 473 VAL ARG VAL ILE THR ASN PRO THR LEU ASP PRO ARG VAL
SEQRES 17 C 473 ILE PHE GLY TYR LEU LEU LYS SER PRO PHE GLY GLY GLU
SEQRES 18 C 473 GLY TRP ILE VAL SER VAL ASN ASN LEU GLU ASP VAL VAL
SEQRES 19 C 473 GLY GLY HIS ILE TRP ILE GLY LEU ILE CYS ILE ALA GLY
SEQRES 20 C 473 GLY ILE TRP HIS ILE LEU THR THR PRO PHE GLY TRP ALA
SEQRES 21 C 473 ARG ARG ALA PHE ILE TRP SER GLY GLU ALA TYR LEU SER
SEQRES 22 C 473 TYR SER LEU GLY ALA LEU SER MET MET GLY PHE ILE ALA
SEQRES 23 C 473 THR CYS PHE VAL TRP PHE ASN ASN THR VAL TYR PRO SER
SEQRES 24 C 473 GLU PHE TYR GLY PRO THR GLY PRO GLU ALA SER GLN ALA
SEQRES 25 C 473 GLN ALA MET THR PHE LEU ILE ARG ASP GLN LYS LEU GLY
SEQRES 26 C 473 ALA ASN VAL GLY SER ALA GLN GLY PRO THR GLY LEU GLY
SEQRES 27 C 473 LYS TYR LEU MET ARG SER PRO THR GLY GLU ILE ILE PHE
SEQRES 28 C 473 GLY GLY GLU THR MET ARG PHE TRP ASP PHE ARG GLY PRO
SEQRES 29 C 473 TRP LEU GLU PRO LEU ARG GLY PRO ASN GLY LEU ASP LEU
SEQRES 30 C 473 ASN LYS ILE LYS ASN ASP ILE GLN PRO TRP GLN GLU ARG
SEQRES 31 C 473 ARG ALA ALA GLU TYR MET THR HIS ALA PRO LEU GLY SER
SEQRES 32 C 473 LEU ASN SER VAL GLY GLY VAL ALA THR GLU ILE ASN SER
SEQRES 33 C 473 VAL ASN PHE VAL SER PRO ARG SER TRP LEU ALA THR SER
SEQRES 34 C 473 HIS PHE VAL LEU ALA PHE PHE PHE LEU VAL GLY HIS LEU
SEQRES 35 C 473 TRP HIS ALA GLY ARG ALA ARG ALA ALA ALA ALA GLY PHE
SEQRES 36 C 473 GLU LYS GLY ILE ASP ARG GLU SER GLU PRO VAL LEU SER
SEQRES 37 C 473 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 84 MET ALA GLY THR THR GLY GLU ARG PRO PHE SER ASP ILE
SEQRES 2 E 84 ILE THR SER VAL ARG TYR TRP VAL ILE HIS SER ILE THR
SEQRES 3 E 84 ILE PRO ALA LEU PHE ILE ALA GLY TRP LEU PHE VAL SER
SEQRES 4 E 84 THR GLY LEU ALA TYR ASP VAL PHE GLY THR PRO ARG PRO
SEQRES 5 E 84 ASP SER TYR TYR ALA GLN GLU GLN ARG SER ILE PRO LEU
SEQRES 6 E 84 VAL THR ASP ARG PHE GLU ALA LYS GLN GLN VAL GLU THR
SEQRES 7 E 84 PHE LEU GLU GLN LEU LYS
SEQRES 1 F 45 MET THR SER ASN THR PRO ASN GLN GLU PRO VAL SER TYR
SEQRES 2 F 45 PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR LEU
SEQRES 3 F 45 ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA ALA
SEQRES 4 F 45 MET GLN PHE ILE GLN ARG
SEQRES 1 H 66 MET ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO
SEQRES 2 H 66 LEU ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY
SEQRES 3 H 66 THR THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU
SEQRES 4 H 66 VAL PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR
SEQRES 5 H 66 LEU ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU
SEQRES 6 H 66 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 247 ALA ALA LYS GLN THR LEU THR TYR ASP ASP ILE VAL GLY
SEQRES 2 O 247 THR GLY LEU ALA ASN LYS CYS PRO THR LEU ASP ASP THR
SEQRES 3 O 247 ALA ARG GLY ALA TYR PRO ILE ASP SER SER GLN THR TYR
SEQRES 4 O 247 ARG ILE ALA ARG LEU CYS LEU GLN PRO THR THR PHE LEU
SEQRES 5 O 247 VAL LYS GLU GLU PRO LYS ASN LYS ARG GLN GLU ALA GLU
SEQRES 6 O 247 PHE VAL PRO THR LYS LEU VAL THR ARG GLU THR THR SER
SEQRES 7 O 247 LEU ASP GLN ILE GLN GLY GLU LEU LYS VAL ASN SER ASP
SEQRES 8 O 247 GLY SER LEU THR PHE VAL GLU GLU ASP GLY ILE ASP PHE
SEQRES 9 O 247 GLN PRO VAL THR VAL GLN MET ALA GLY GLY GLU ARG ILE
SEQRES 10 O 247 PRO LEU LEU PHE THR VAL LYS ASN LEU VAL ALA SER THR
SEQRES 11 O 247 GLN PRO ASN VAL THR SER ILE THR THR SER THR ASP PHE
SEQRES 12 O 247 LYS GLY GLU PHE ASN VAL PRO SER TYR ARG THR ALA ASN
SEQRES 13 O 247 PHE LEU ASP PRO LYS GLY ARG GLY LEU ALA SER GLY TYR
SEQRES 14 O 247 ASP SER ALA ILE ALA LEU PRO GLN ALA LYS GLU GLU GLU
SEQRES 15 O 247 LEU ALA ARG ALA ASN VAL LYS ARG PHE SER LEU THR LYS
SEQRES 16 O 247 GLY GLN ILE SER LEU ASN VAL ALA LYS VAL ASP GLY ARG
SEQRES 17 O 247 THR GLY GLU ILE ALA GLY THR PHE GLU SER GLU GLN LEU
SEQRES 18 O 247 SER ASP ASP ASP MET GLY ALA HIS GLU PRO HIS GLU VAL
SEQRES 19 O 247 LYS 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 X 129 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 2 X 129 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 3 X 129 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 4 X 129 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 5 X 129 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 6 X 129 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 7 X 129 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 8 X 129 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 9 X 129 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 10 X 129 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
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
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 473 MET LYS THR LEU SER SER GLN LYS ARG TYR SER PRO VAL
SEQRES 2 c 473 VAL THR LEU SER SER ASN SER ILE PHE ALA THR ASN ARG
SEQRES 3 c 473 ASP GLN GLU SER SER GLY PHE ALA TRP TRP ALA GLY ASN
SEQRES 4 c 473 ALA ARG LEU ILE ASN LEU SER GLY LYS LEU LEU GLY ALA
SEQRES 5 c 473 HIS VAL ALA HIS ALA GLY LEU ILE VAL PHE TRP ALA GLY
SEQRES 6 c 473 ALA MET THR LEU PHE GLU LEU ALA HIS PHE ILE PRO GLU
SEQRES 7 c 473 LYS PRO MET TYR GLU GLN GLY LEU ILE LEU ILE PRO HIS
SEQRES 8 c 473 ILE ALA THR LEU GLY TRP GLY VAL GLY PRO GLY GLY GLU
SEQRES 9 c 473 VAL VAL ASP THR PHE PRO PHE PHE VAL VAL GLY VAL VAL
SEQRES 10 c 473 HIS LEU ILE SER SER ALA VAL LEU GLY PHE GLY GLY VAL
SEQRES 11 c 473 TYR HIS ALA ILE ARG GLY PRO GLU THR LEU GLU GLU TYR
SEQRES 12 c 473 SER SER PHE PHE GLY TYR ASP TRP LYS ASP LYS ASN LYS
SEQRES 13 c 473 MET THR THR ILE LEU GLY PHE HIS LEU ILE VAL LEU GLY
SEQRES 14 c 473 ILE GLY ALA LEU LEU LEU VAL ALA LYS ALA MET PHE PHE
SEQRES 15 c 473 GLY GLY LEU TYR ASP THR TRP ALA PRO GLY GLY GLY ASP
SEQRES 16 c 473 VAL ARG VAL ILE THR ASN PRO THR LEU ASP PRO ARG VAL
SEQRES 17 c 473 ILE PHE GLY TYR LEU LEU LYS SER PRO PHE GLY GLY GLU
SEQRES 18 c 473 GLY TRP ILE VAL SER VAL ASN ASN LEU GLU ASP VAL VAL
SEQRES 19 c 473 GLY GLY HIS ILE TRP ILE GLY LEU ILE CYS ILE ALA GLY
SEQRES 20 c 473 GLY ILE TRP HIS ILE LEU THR THR PRO PHE GLY TRP ALA
SEQRES 21 c 473 ARG ARG ALA PHE ILE TRP SER GLY GLU ALA TYR LEU SER
SEQRES 22 c 473 TYR SER LEU GLY ALA LEU SER MET MET GLY PHE ILE ALA
SEQRES 23 c 473 THR CYS PHE VAL TRP PHE ASN ASN THR VAL TYR PRO SER
SEQRES 24 c 473 GLU PHE TYR GLY PRO THR GLY PRO GLU ALA SER GLN ALA
SEQRES 25 c 473 GLN ALA MET THR PHE LEU ILE ARG ASP GLN LYS LEU GLY
SEQRES 26 c 473 ALA ASN VAL GLY SER ALA GLN GLY PRO THR GLY LEU GLY
SEQRES 27 c 473 LYS TYR LEU MET ARG SER PRO THR GLY GLU ILE ILE PHE
SEQRES 28 c 473 GLY GLY GLU THR MET ARG PHE TRP ASP PHE ARG GLY PRO
SEQRES 29 c 473 TRP LEU GLU PRO LEU ARG GLY PRO ASN GLY LEU ASP LEU
SEQRES 30 c 473 ASN LYS ILE LYS ASN ASP ILE GLN PRO TRP GLN GLU ARG
SEQRES 31 c 473 ARG ALA ALA GLU TYR MET THR HIS ALA PRO LEU GLY SER
SEQRES 32 c 473 LEU ASN SER VAL GLY GLY VAL ALA THR GLU ILE ASN SER
SEQRES 33 c 473 VAL ASN PHE VAL SER PRO ARG SER TRP LEU ALA THR SER
SEQRES 34 c 473 HIS PHE VAL LEU ALA PHE PHE PHE LEU VAL GLY HIS LEU
SEQRES 35 c 473 TRP HIS ALA GLY ARG ALA ARG ALA ALA ALA ALA GLY PHE
SEQRES 36 c 473 GLU LYS GLY ILE ASP ARG GLU SER GLU PRO VAL LEU SER
SEQRES 37 c 473 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 84 MET ALA GLY THR THR GLY GLU ARG PRO PHE SER ASP ILE
SEQRES 2 e 84 ILE THR SER VAL ARG TYR TRP VAL ILE HIS SER ILE THR
SEQRES 3 e 84 ILE PRO ALA LEU PHE ILE ALA GLY TRP LEU PHE VAL SER
SEQRES 4 e 84 THR GLY LEU ALA TYR ASP VAL PHE GLY THR PRO ARG PRO
SEQRES 5 e 84 ASP SER TYR TYR ALA GLN GLU GLN ARG SER ILE PRO LEU
SEQRES 6 e 84 VAL THR ASP ARG PHE GLU ALA LYS GLN GLN VAL GLU THR
SEQRES 7 e 84 PHE LEU GLU GLN LEU LYS
SEQRES 1 f 45 MET THR SER ASN THR PRO ASN GLN GLU PRO VAL SER TYR
SEQRES 2 f 45 PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR LEU
SEQRES 3 f 45 ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA ALA
SEQRES 4 f 45 MET GLN PHE ILE GLN ARG
SEQRES 1 h 66 MET ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO
SEQRES 2 h 66 LEU ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY
SEQRES 3 h 66 THR THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU
SEQRES 4 h 66 VAL PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR
SEQRES 5 h 66 LEU ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU
SEQRES 6 h 66 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 247 ALA ALA LYS GLN THR LEU THR TYR ASP ASP ILE VAL GLY
SEQRES 2 o 247 THR GLY LEU ALA ASN LYS CYS PRO THR LEU ASP ASP THR
SEQRES 3 o 247 ALA ARG GLY ALA TYR PRO ILE ASP SER SER GLN THR TYR
SEQRES 4 o 247 ARG ILE ALA ARG LEU CYS LEU GLN PRO THR THR PHE LEU
SEQRES 5 o 247 VAL LYS GLU GLU PRO LYS ASN LYS ARG GLN GLU ALA GLU
SEQRES 6 o 247 PHE VAL PRO THR LYS LEU VAL THR ARG GLU THR THR SER
SEQRES 7 o 247 LEU ASP GLN ILE GLN GLY GLU LEU LYS VAL ASN SER ASP
SEQRES 8 o 247 GLY SER LEU THR PHE VAL GLU GLU ASP GLY ILE ASP PHE
SEQRES 9 o 247 GLN PRO VAL THR VAL GLN MET ALA GLY GLY GLU ARG ILE
SEQRES 10 o 247 PRO LEU LEU PHE THR VAL LYS ASN LEU VAL ALA SER THR
SEQRES 11 o 247 GLN PRO ASN VAL THR SER ILE THR THR SER THR ASP PHE
SEQRES 12 o 247 LYS GLY GLU PHE ASN VAL PRO SER TYR ARG THR ALA ASN
SEQRES 13 o 247 PHE LEU ASP PRO LYS GLY ARG GLY LEU ALA SER GLY TYR
SEQRES 14 o 247 ASP SER ALA ILE ALA LEU PRO GLN ALA LYS GLU GLU GLU
SEQRES 15 o 247 LEU ALA ARG ALA ASN VAL LYS ARG PHE SER LEU THR LYS
SEQRES 16 o 247 GLY GLN ILE SER LEU ASN VAL ALA LYS VAL ASP GLY ARG
SEQRES 17 o 247 THR GLY GLU ILE ALA GLY THR PHE GLU SER GLU GLN LEU
SEQRES 18 o 247 SER ASP ASP ASP MET GLY ALA HIS GLU PRO HIS GLU VAL
SEQRES 19 o 247 LYS 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 x 129 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 2 x 129 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 3 x 129 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 4 x 129 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 5 x 129 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 6 x 129 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 7 x 129 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 8 x 129 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 9 x 129 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 10 x 129 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
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 557 1
HET CLA A 558 65
HET CLA A 559 65
HET CLA A 560 65
HET PHO A 561 64
HET PHO A 562 64
HET CLA A 563 55
HET PQ9 A 564 30
HET OEC A 565 5
HET BCR A 566 40
HET LHG A 567 39
HET SQD A 568 54
HET LMT A 569 35
HET SQD A5212 26
HET CLA B 511 41
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 56
HET CLA B 525 65
HET CLA B 526 65
HET BCR B 527 40
HET BCR B 528 40
HET BCR B 529 40
HET MGE B 530 48
HET CLA C 491 65
HET CLA C 492 60
HET CLA C 493 65
HET CLA C 494 46
HET CLA C 495 65
HET CLA C 496 65
HET CLA C 497 65
HET CLA C 498 65
HET CLA C 499 47
HET CLA C 500 65
HET CLA C 501 65
HET CLA C 502 51
HET CLA C 503 50
HET BCR C 504 40
HET BCR C 505 40
HET BCR C 506 40
HET DGD C 507 53
HET DGD C 508 47
HET DGD C 509 57
HET BCT D 353 4
HET CLA D 354 65
HET CLA D 355 50
HET PQ9 D 356 30
HET BCR D 357 40
HET MGE D 358 47
HET MGE D 359 41
HET MGE D 360 48
HET HEM F 51 43
HET BCR H 107 40
HET DGD H 208 54
HET MGE I 201 48
HET CA K 56 1
HET MGE L 210 48
HET SQD L5213 47
HET LMT M5216 35
HET LMT T 217 35
HET BCR T5104 40
HET HEM V 552 43
HET BCR X 130 40
HET FE2 a5557 1
HET SQD a 212 26
HET CLA a5558 65
HET CLA a5559 65
HET CLA a5560 65
HET PHO a5561 64
HET PHO a5562 64
HET CLA a5563 55
HET PQ9 a5564 30
HET OEC a5565 5
HET BCR a5566 40
HET LHG a5567 39
HET LMT a5568 35
HET CLA b5511 41
HET CLA b5512 65
HET CLA b5513 65
HET CLA b5514 65
HET CLA b5515 65
HET CLA b5516 65
HET CLA b5517 65
HET CLA b5518 65
HET CLA b5519 65
HET CLA b5520 65
HET CLA b5521 65
HET CLA b5522 65
HET CLA b5523 65
HET CLA b5524 56
HET CLA b5525 65
HET CLA b5526 65
HET BCR b5527 40
HET BCR b5528 40
HET BCR b5529 40
HET MGE b5530 48
HET CLA c5491 65
HET CLA c5492 60
HET CLA c5493 65
HET CLA c5494 46
HET CLA c5495 65
HET CLA c5496 65
HET CLA c5497 65
HET CLA c5498 65
HET CLA c5499 47
HET CLA c5500 65
HET CLA c5501 65
HET CLA c5502 51
HET CLA c5503 50
HET BCR c5504 40
HET BCR c5505 40
HET BCR c5506 40
HET DGD c5507 53
HET DGD c5508 47
HET DGD c5509 57
HET BCT d5353 4
HET CLA d5354 65
HET CLA d5355 50
HET PQ9 d5356 30
HET BCR d5357 40
HET SQD d5358 54
HET MGE d5359 47
HET MGE d5360 41
HET MGE d5361 48
HET HEM f5051 43
HET BCR h5107 40
HET DGD h5208 54
HET MGE i5201 48
HET CA k5056 1
HET MGE l5210 48
HET LMT m 216 35
HET BCR t 104 40
HET SQD t 213 47
HET LMT t5217 35
HET HEM v5552 43
HET BCR x5130 40
HETNAM FE2 FE (II) ION
HETNAM CLA CHLOROPHYLL A
HETNAM PHO PHEOPHYTIN A
HETNAM PQ9 5-[(2E,6E,10E,14E,18E,22E)-3,7,11,15,19,23,27-
HETNAM 2 PQ9 HEPTAMETHYLOCTACOSA-2,6,10,14,18,22,26-HEPTAENYL]-2,3-
HETNAM 3 PQ9 DIMETHYLBENZO-1,4-QUINONE
HETNAM OEC OXYGEN EVOLVING SYSTEM
HETNAM BCR BETA-CAROTENE
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 LMT DODECYL-BETA-D-MALTOSIDE
HETNAM MGE (1S)-2-(ALPHA-L-ALLOPYRANOSYLOXY)-1-[(TRIDECANOYLOXY)
HETNAM 2 MGE METHYL]ETHYL PALMITATE
HETNAM DGD DIGALACTOSYL DIACYL GLYCEROL (DGDG)
HETNAM BCT BICARBONATE ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM CA CALCIUM ION
HETSYN SQD SULFOQUINOVOSYLDIACYLGLYCEROL
HETSYN MGE MONOGALACTOSYL-DIACYLGLYCEROL
HETSYN HEM HEME
FORMUL 37 FE2 2(FE 2+)
FORMUL 38 CLA 70(C55 H72 MG N4 O5 2+)
FORMUL 41 PHO 4(C55 H74 N4 O5)
FORMUL 44 PQ9 4(C43 H64 O2)
FORMUL 45 OEC 2(CA MN4 O4)
FORMUL 46 BCR 22(C40 H56)
FORMUL 47 LHG 2(C38 H75 O10 P)
FORMUL 48 SQD 6(C41 H78 O12 S)
FORMUL 49 LMT 6(C24 H46 O11)
FORMUL 70 MGE 12(C38 H72 O10)
FORMUL 04 DGD 8(C51 H96 O15)
FORMUL 07 BCT 2(C H O3 1-)
FORMUL 15 HEM 4(C34 H32 FE N4 O4)
FORMUL 19 CA 2(CA 2+)
HELIX 1 1 ASN A 12 THR A 22 1 11
HELIX 2 2 PHE A 33 ALA A 54 1 22
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 GLY A 175 ASN A 191 1 17
HELIX 11 11 ILE A 192 MET A 194 5 3
HELIX 12 12 HIS A 195 SER A 222 1 28
HELIX 13 13 ALA A 233 TYR A 237 5 5
HELIX 14 14 ASN A 247 ILE A 259 1 13
HELIX 15 15 ASN A 267 MET A 293 1 27
HELIX 16 16 THR A 316 HIS A 332 1 17
HELIX 17 17 PRO B 4 VAL B 11 5 8
HELIX 18 18 ASP B 15 ALA B 43 1 29
HELIX 19 19 PRO B 54 GLY B 59 5 6
HELIX 20 20 VAL B 62 LEU B 69 1 8
HELIX 21 21 SER B 92 TYR B 117 1 26
HELIX 22 22 LEU B 120 ARG B 124 5 5
HELIX 23 23 ASP B 134 HIS B 157 1 24
HELIX 24 24 GLY B 186 ASN B 191 5 6
HELIX 25 25 ASN B 194 VAL B 219 1 26
HELIX 26 26 PRO B 222 LEU B 229 1 8
HELIX 27 27 ILE B 234 TYR B 258 1 25
HELIX 28 28 ARG B 272 SER B 277 1 6
HELIX 29 29 SER B 278 SER B 294 1 17
HELIX 30 30 THR B 297 SER B 303 1 7
HELIX 31 31 PRO B 306 ASP B 313 1 8
HELIX 32 32 TYR B 314 ASN B 318 5 5
HELIX 33 33 PRO B 329 GLY B 333 5 5
HELIX 34 34 ARG B 384 SER B 388 5 5
HELIX 35 35 ASP B 413 ILE B 425 1 13
HELIX 36 36 SER B 446 LEU B 474 1 29
HELIX 37 37 PHE B 475 PHE B 479 5 5
HELIX 38 38 ALA C 34 ARG C 41 5 8
HELIX 39 39 LEU C 45 PHE C 75 1 31
HELIX 40 40 MET C 81 GLY C 85 5 5
HELIX 41 41 LEU C 88 LEU C 95 1 8
HELIX 42 42 GLY C 100 GLU C 104 5 5
HELIX 43 43 THR C 108 ALA C 133 1 26
HELIX 44 44 ASN C 155 PHE C 181 1 27
HELIX 45 45 ASP C 205 TYR C 212 1 8
HELIX 46 46 LEU C 213 LYS C 215 5 3
HELIX 47 47 ASN C 229 LEU C 253 1 25
HELIX 48 48 PHE C 257 ARG C 262 1 6
HELIX 49 49 SER C 267 ASN C 293 1 27
HELIX 50 50 THR C 305 LYS C 323 1 19
HELIX 51 51 GLY C 353 TRP C 359 5 7
HELIX 52 52 LEU C 366 ARG C 370 5 5
HELIX 53 53 ASP C 376 ASP C 383 1 8
HELIX 54 54 GLN C 385 THR C 397 1 13
HELIX 55 55 SER C 421 ALA C 452 1 32
HELIX 56 56 ASP C 460 MET C 469 5 10
HELIX 57 57 TRP D 14 LYS D 23 1 10
HELIX 58 58 SER D 33 PHE D 54 1 22
HELIX 59 59 ALA D 82 GLY D 86 5 5
HELIX 60 60 ASP D 100 GLY D 108 1 9
HELIX 61 61 GLY D 108 GLY D 137 1 30
HELIX 62 62 PHE D 146 PHE D 157 1 12
HELIX 63 63 LEU D 158 GLN D 164 1 7
HELIX 64 64 SER D 166 ALA D 170 5 5
HELIX 65 65 VAL D 175 HIS D 189 1 15
HELIX 66 66 ASN D 190 LEU D 193 5 4
HELIX 67 67 ASN D 194 ASN D 220 1 27
HELIX 68 68 SER D 245 PHE D 257 1 13
HELIX 69 69 ASN D 263 ALA D 290 1 28
HELIX 70 70 PHE D 298 ASP D 308 1 11
HELIX 71 71 THR D 313 GLN D 334 1 22
HELIX 72 72 PRO D 335 ASN D 338 5 4
HELIX 73 73 PRO E 9 SER E 16 1 8
HELIX 74 74 SER E 16 THR E 40 1 25
HELIX 75 75 GLY E 41 PHE E 47 1 7
HELIX 76 76 GLU E 71 LEU E 83 1 13
HELIX 77 77 THR F 17 GLN F 41 1 25
HELIX 78 78 THR H 5 ARG H 12 1 8
HELIX 79 79 THR H 27 ASN H 50 1 24
HELIX 80 80 GLU I 2 SER I 25 1 24
HELIX 81 81 PRO J 9 ALA J 32 1 24
HELIX 82 82 PRO K 12 ILE K 17 5 6
HELIX 83 83 PHE K 18 LEU K 25 1 8
HELIX 84 84 VAL K 27 VAL K 43 1 17
HELIX 85 85 ASN L 13 ASN L 37 1 25
HELIX 86 86 LEU M 6 SER M 31 1 26
HELIX 87 87 GLN M 32 LYS M 34 5 3
HELIX 88 88 THR O 32 VAL O 37 1 6
HELIX 89 89 GLU O 205 GLU O 207 5 3
HELIX 90 90 LEU O 208 VAL O 213 1 6
HELIX 91 91 MET T 1 PHE T 23 1 23
HELIX 92 92 ASN U 41 LEU U 47 1 7
HELIX 93 93 ASN U 61 ILE U 66 5 6
HELIX 94 94 TYR U 72 ASN U 82 1 11
HELIX 95 95 SER U 87 ILE U 94 5 8
HELIX 96 96 ARG U 100 LEU U 109 1 10
HELIX 97 97 GLU U 118 GLU U 123 1 6
HELIX 98 98 GLY U 124 ASP U 126 5 3
HELIX 99 99 THR V 48 CYS V 63 1 16
HELIX 100 100 CYS V 63 VAL V 68 1 6
HELIX 101 101 GLY V 69 ILE V 71 5 3
HELIX 102 102 ARG V 81 LEU V 87 1 7
HELIX 103 103 ASN V 94 ASN V 104 1 11
HELIX 104 104 SER V 120 ALA V 124 5 5
HELIX 105 105 PRO V 128 LEU V 133 1 6
HELIX 106 106 THR V 134 GLY V 153 1 20
HELIX 107 107 GLY V 153 GLY V 158 1 6
HELIX 108 108 GLY V 159 TYR V 163 5 5
HELIX 109 109 UNK X 4 UNK X 27 1 24
HELIX 110 110 UNK X 54 UNK X 85 1 32
HELIX 111 111 UNK X 100 UNK X 111 1 12
HELIX 112 112 UNK X 113 UNK X 123 1 11
HELIX 113 113 MET Z 1 SER Z 29 1 29
HELIX 114 114 ASP Z 34 VAL Z 62 1 29
HELIX 115 115 ASN a 5012 THR a 5022 1 11
HELIX 116 116 PHE a 5033 ALA a 5054 1 22
HELIX 117 117 SER a 5070 GLY a 5074 5 5
HELIX 118 118 PRO a 5095 ALA a 5099 5 5
HELIX 119 119 SER a 5101 ASN a 5108 1 8
HELIX 120 120 GLY a 5109 LEU a 5137 1 29
HELIX 121 121 TRP a 5142 TYR a 5147 1 6
HELIX 122 122 TYR a 5147 LEU a 5159 1 13
HELIX 123 123 LEU a 5159 GLY a 5166 1 8
HELIX 124 124 ILE a 5176 ASN a 5191 1 16
HELIX 125 125 ILE a 5192 MET a 5194 5 3
HELIX 126 126 HIS a 5195 SER a 5222 1 28
HELIX 127 127 SER a 5232 TYR a 5237 5 6
HELIX 128 128 ASN a 5247 PHE a 5260 1 14
HELIX 129 129 ASN a 5267 MET a 5293 1 27
HELIX 130 130 THR a 5316 HIS a 5332 1 17
HELIX 131 131 PRO b 5004 ILE b 5013 5 10
HELIX 132 132 ASP b 5015 ALA b 5043 1 29
HELIX 133 133 PRO b 5054 GLY b 5059 5 6
HELIX 134 134 VAL b 5062 LEU b 5069 1 8
HELIX 135 135 SER b 5092 TYR b 5117 1 26
HELIX 136 136 LEU b 5120 ARG b 5124 5 5
HELIX 137 137 ASP b 5134 HIS b 5157 1 24
HELIX 138 138 GLY b 5186 ASN b 5191 5 6
HELIX 139 139 ASN b 5194 VAL b 5219 1 26
HELIX 140 140 PRO b 5222 LEU b 5229 1 8
HELIX 141 141 ASN b 5233 GLU b 5235 5 3
HELIX 142 142 THR b 5236 TYR b 5258 1 23
HELIX 143 143 THR b 5271 SER b 5277 1 7
HELIX 144 144 SER b 5278 SER b 5294 1 17
HELIX 145 145 THR b 5297 SER b 5303 1 7
HELIX 146 146 PRO b 5306 ASP b 5313 1 8
HELIX 147 147 TYR b 5314 ASN b 5318 5 5
HELIX 148 148 PRO b 5329 ASP b 5334 1 6
HELIX 149 149 ARG b 5384 SER b 5388 5 5
HELIX 150 150 ASP b 5413 ILE b 5425 1 13
HELIX 151 151 SER b 5446 LEU b 5474 1 29
HELIX 152 152 PHE b 5475 PHE b 5479 5 5
HELIX 153 153 ALA c 5034 ARG c 5041 5 8
HELIX 154 154 LEU c 5045 ALA c 5073 1 29
HELIX 155 155 MET c 5081 GLY c 5085 5 5
HELIX 156 156 LEU c 5088 LEU c 5095 1 8
HELIX 157 157 GLY c 5100 GLU c 5104 5 5
HELIX 158 158 THR c 5108 ALA c 5133 1 26
HELIX 159 159 ASN c 5155 PHE c 5181 1 27
HELIX 160 160 ASP c 5205 TYR c 5212 1 8
HELIX 161 161 LEU c 5213 LYS c 5215 5 3
HELIX 162 162 ASN c 5229 LEU c 5253 1 25
HELIX 163 163 PHE c 5257 ARG c 5262 1 6
HELIX 164 164 SER c 5267 ASN c 5293 1 27
HELIX 165 165 THR c 5305 LYS c 5323 1 19
HELIX 166 166 GLY c 5353 TRP c 5359 5 7
HELIX 167 167 LEU c 5366 ARG c 5370 5 5
HELIX 168 168 ASP c 5376 ASP c 5383 1 8
HELIX 169 169 GLN c 5385 THR c 5397 1 13
HELIX 170 170 SER c 5421 ALA c 5452 1 32
HELIX 171 171 ASP c 5460 MET c 5469 5 10
HELIX 172 172 TRP d 5014 LYS d 5023 1 10
HELIX 173 173 SER d 5033 PHE d 5054 1 22
HELIX 174 174 ALA d 5082 GLY d 5086 5 5
HELIX 175 175 ASP d 5100 GLY d 5108 1 9
HELIX 176 176 GLY d 5108 GLY d 5137 1 30
HELIX 177 177 PHE d 5146 PHE d 5157 1 12
HELIX 178 178 LEU d 5158 GLN d 5164 1 7
HELIX 179 179 SER d 5166 ALA d 5170 5 5
HELIX 180 180 VAL d 5175 HIS d 5189 1 15
HELIX 181 181 ASN d 5190 LEU d 5193 5 4
HELIX 182 182 ASN d 5194 ASN d 5220 1 27
HELIX 183 183 SER d 5245 PHE d 5257 1 13
HELIX 184 184 ASN d 5263 ALA d 5290 1 28
HELIX 185 185 PHE d 5298 ASP d 5308 1 11
HELIX 186 186 THR d 5313 GLN d 5334 1 22
HELIX 187 187 PRO d 5335 ASN d 5338 5 4
HELIX 188 188 PRO e 5009 SER e 5016 1 8
HELIX 189 189 SER e 5016 THR e 5040 1 25
HELIX 190 190 GLY e 5041 PHE e 5047 1 7
HELIX 191 191 GLU e 5071 LEU e 5083 1 13
HELIX 192 192 THR f 5017 GLN f 5041 1 25
HELIX 193 193 THR h 5005 ARG h 5012 1 8
HELIX 194 194 THR h 5027 ASN h 5050 1 24
HELIX 195 195 GLU i 5002 SER i 5025 1 24
HELIX 196 196 PRO j 5009 ALA j 5032 1 24
HELIX 197 197 PRO k 5012 ILE k 5017 5 6
HELIX 198 198 PHE k 5018 LEU k 5025 1 8
HELIX 199 199 VAL k 5027 VAL k 5043 1 17
HELIX 200 200 ASN l 5013 ASN l 5037 1 25
HELIX 201 201 LEU m 5006 SER m 5031 1 26
HELIX 202 202 GLN m 5032 LYS m 5034 5 3
HELIX 203 203 THR o 5032 VAL o 5037 1 6
HELIX 204 204 GLU o 5205 GLU o 5207 5 3
HELIX 205 205 LEU o 5208 VAL o 5213 1 6
HELIX 206 206 MET t 5001 PHE t 5023 1 23
HELIX 207 207 ASN u 5041 LEU u 5047 1 7
HELIX 208 208 ASN u 5061 ILE u 5066 5 6
HELIX 209 209 TYR u 5072 ASN u 5082 1 11
HELIX 210 210 SER u 5087 ILE u 5094 5 8
HELIX 211 211 ARG u 5100 LEU u 5109 1 10
HELIX 212 212 GLU u 5118 GLU u 5123 1 6
HELIX 213 213 GLY u 5124 ASP u 5126 5 3
HELIX 214 214 THR v 5048 CYS v 5063 1 16
HELIX 215 215 CYS v 5063 VAL v 5068 1 6
HELIX 216 216 GLY v 5069 ILE v 5071 5 3
HELIX 217 217 ARG v 5081 LEU v 5087 1 7
HELIX 218 218 ASN v 5094 ASN v 5104 1 11
HELIX 219 219 SER v 5120 ALA v 5124 5 5
HELIX 220 220 PRO v 5128 LEU v 5133 1 6
HELIX 221 221 THR v 5134 GLY v 5153 1 20
HELIX 222 222 GLY v 5153 GLY v 5158 1 6
HELIX 223 223 GLY v 5159 TYR v 5163 5 5
HELIX 224 224 UNK x 5004 UNK x 5027 1 24
HELIX 225 225 UNK x 5054 UNK x 5085 1 32
HELIX 226 226 UNK x 5100 UNK x 5111 1 12
HELIX 227 227 UNK x 5113 UNK x 5123 1 11
HELIX 228 228 MET z 5001 SER z 5029 1 29
HELIX 229 229 ASP z 5034 VAL z 5062 1 29
SHEET 1 A 2 LEU A 297 ASN A 298 0
SHEET 2 A 2 GLY C 402 SER C 403 1 O GLY C 402 N ASN A 298
SHEET 1 B 2 MET B 166 VAL B 168 0
SHEET 2 B 2 SER B 177 GLN B 179 -1 O SER B 177 N VAL B 168
SHEET 1 C 2 ILE B 336 TRP B 340 0
SHEET 2 C 2 PHE B 430 ASP B 433 -1 O ASP B 433 N ILE B 336
SHEET 1 D 6 VAL B 377 ASP B 380 0
SHEET 2 D 6 ILE B 369 THR B 371 -1 N LEU B 370 O ALA B 379
SHEET 3 D 6 GLU B 353 VAL B 356 -1 N PHE B 355 O THR B 371
SHEET 4 D 6 HIS B 343 ARG B 347 -1 N PHE B 346 O LEU B 354
SHEET 5 D 6 THR B 398 TYR B 402 -1 O TYR B 402 N HIS B 343
SHEET 6 D 6 THR B 410 PHE B 411 -1 O PHE B 411 N VAL B 399
SHEET 1 E 2 LEU C 341 ARG C 343 0
SHEET 2 E 2 ILE C 349 PHE C 351 -1 O ILE C 350 N MET C 342
SHEET 1 F 6 ASP O 125 ILE O 127 0
SHEET 2 F 6 LEU O 104 VAL O 113 -1 N ASP O 105 O ILE O 127
SHEET 3 F 6 TYR O 64 LYS O 79 -1 N LEU O 71 O LEU O 104
SHEET 4 F 6 PHE O 91 LEU O 96 -1 O VAL O 92 N VAL O 78
SHEET 5 F 6 PHE O 129 MET O 136 -1 O GLN O 135 N LYS O 95
SHEET 6 F 6 ARG O 141 THR O 147 -1 O ILE O 142 N VAL O 134
SHEET 1 G12 ASP O 125 ILE O 127 0
SHEET 2 G12 LEU O 104 VAL O 113 -1 N ASP O 105 O ILE O 127
SHEET 3 G12 LEU O 119 VAL O 122 -1 O THR O 120 N LYS O 112
SHEET 4 G12 LYS O 149 THR O 155 -1 O ALA O 153 N PHE O 121
SHEET 5 G12 ASP O 167 VAL O 174 -1 O LYS O 169 N SER O 154
SHEET 6 G12 THR O 219 LYS O 229 -1 O THR O 219 N VAL O 174
SHEET 7 G12 GLU O 236 LEU O 246 -1 O ALA O 238 N ALA O 228
SHEET 8 G12 GLU O 258 GLU O 270 -1 O ILE O 261 N SER O 243
SHEET 9 G12 TYR O 64 LYS O 79 -1 N ARG O 65 O GLU O 270
SHEET 10 G12 PHE O 91 LEU O 96 -1 O VAL O 92 N VAL O 78
SHEET 11 G12 PHE O 129 MET O 136 -1 O GLN O 135 N LYS O 95
SHEET 12 G12 ARG O 141 THR O 147 -1 O ILE O 142 N VAL O 134
SHEET 1 H 2 ILE U 55 ASP U 56 0
SHEET 2 H 2 PHE U 112 THR U 113 1 O THR U 113 N ILE U 55
SHEET 1 I 2 THR V 35 PRO V 37 0
SHEET 2 I 2 THR V 44 THR V 46 -1 O ILE V 45 N VAL V 36
SHEET 1 J 2 ALA a5081 VAL a5082 0
SHEET 2 J 2 LEU a5174 GLY a5175 -1 O LEU a5174 N VAL a5082
SHEET 1 K 2 LEU a5297 ASN a5298 0
SHEET 2 K 2 GLY c5402 SER c5403 1 O GLY c5402 N ASN a5298
SHEET 1 L 2 MET b5166 VAL b5168 0
SHEET 2 L 2 SER b5177 GLN b5179 -1 O SER b5177 N VAL b5168
SHEET 1 M 2 ILE b5336 TRP b5340 0
SHEET 2 M 2 PHE b5430 ASP b5433 -1 O GLU b5431 N GLN b5338
SHEET 1 N 6 VAL b5377 ASP b5380 0
SHEET 2 N 6 ILE b5369 THR b5371 -1 N LEU b5370 O ALA b5379
SHEET 3 N 6 GLU b5353 VAL b5356 -1 N PHE b5355 O THR b5371
SHEET 4 N 6 HIS b5343 ARG b5347 -1 N PHE b5346 O LEU b5354
SHEET 5 N 6 THR b5398 TYR b5402 -1 O TYR b5402 N HIS b5343
SHEET 6 N 6 THR b5410 PHE b5411 -1 O PHE b5411 N VAL b5399
SHEET 1 O 2 LEU c5341 ARG c5343 0
SHEET 2 O 2 ILE c5349 PHE c5351 -1 O ILE c5350 N MET c5342
SHEET 1 P 6 ASP o5125 ILE o5127 0
SHEET 2 P 6 LEU o5104 VAL o5113 -1 N ASP o5105 O ILE o5127
SHEET 3 P 6 TYR o5064 LYS o5079 -1 N LEU o5071 O LEU o5104
SHEET 4 P 6 PHE o5091 LEU o5096 -1 O VAL o5092 N VAL o5078
SHEET 5 P 6 PHE o5129 MET o5136 -1 O GLN o5135 N LYS o5095
SHEET 6 P 6 ARG o5141 THR o5147 -1 O ILE o5142 N VAL o5134
SHEET 1 Q12 ASP o5125 ILE o5127 0
SHEET 2 Q12 LEU o5104 VAL o5113 -1 N ASP o5105 O ILE o5127
SHEET 3 Q12 LEU o5119 VAL o5122 -1 O THR o5120 N LYS o5112
SHEET 4 Q12 LYS o5149 SER o5154 -1 O ALA o5153 N PHE o5121
SHEET 5 Q12 ASP o5167 VAL o5174 -1 O LYS o5169 N SER o5154
SHEET 6 Q12 THR o5219 LYS o5229 -1 O THR o5219 N VAL o5174
SHEET 7 Q12 GLU o5236 LEU o5246 -1 O ALA o5238 N ALA o5228
SHEET 8 Q12 GLU o5258 GLU o5270 -1 O ILE o5261 N SER o5243
SHEET 9 Q12 TYR o5064 LYS o5079 -1 N GLN o5072 O VAL o5264
SHEET 10 Q12 PHE o5091 LEU o5096 -1 O VAL o5092 N VAL o5078
SHEET 11 Q12 PHE o5129 MET o5136 -1 O GLN o5135 N LYS o5095
SHEET 12 Q12 ARG o5141 THR o5147 -1 O ILE o5142 N VAL o5134
SHEET 1 R 2 ILE u5055 ASP u5056 0
SHEET 2 R 2 PHE u5112 THR u5113 1 O THR u5113 N ILE u5055
SHEET 1 S 2 THR v5035 PRO v5037 0
SHEET 2 S 2 THR v5044 THR v5046 -1 O ILE v5045 N VAL v5036
SSBOND 1 CYS O 45 CYS O 70 1555 1555 2.05
SSBOND 2 CYS o 5045 CYS o 5070 1555 1555 2.07
LINK FE HEM F 51 NE2 HIS E 23 1555 1555 1.99
LINK FE HEM F 51 NE2 HIS F 24 1555 1555 2.41
LINK FE HEM V 552 NE2 HIS V 67 1555 1555 2.06
LINK FE HEM V 552 NE2 HIS V 118 1555 1555 2.15
LINK FE FE2 A 557 NE2 HIS A 215 1555 1555 1.87
LINK FE FE2 A 557 NE2 HIS A 272 1555 1555 2.39
LINK FE HEM f5051 NE2 HIS e5023 1555 1555 2.07
LINK FE HEM f5051 NE2 HIS f5024 1555 1555 2.34
LINK FE HEM v5552 NE2 HIS v5067 1555 1555 2.10
LINK FE HEM v5552 NE2 HIS v5118 1555 1555 2.16
LINK FE FE2 a5557 NE2 HIS a5215 1555 1555 1.91
LINK FE FE2 a5557 NE2 HIS a5272 1555 1555 2.39
LINK OD1 ASP A 170 MN4 OEC A 565 1555 1555 2.39
LINK OE1 GLU A 189 CA1 OEC A 565 1555 1555 2.52
LINK OE2 GLU A 189 MN1 OEC A 565 1555 1555 1.81
LINK NE2 HIS A 198 MG CLA A 558 1555 1555 2.25
LINK OE1 GLU A 333 MN3 OEC A 565 1555 1555 2.31
LINK OD1 ASP A 342 MN2 OEC A 565 1555 1555 2.18
LINK OD2 ASP A 342 MN1 OEC A 565 1555 1555 2.42
LINK O ALA A 344 CA1 OEC A 565 1555 1555 2.61
LINK OXT ALA A 344 MN2 OEC A 565 1555 1555 1.77
LINK NE2 HIS B 9 MG CLA B 524 1555 1555 2.24
LINK ND1 HIS B 201 MG CLA B 512 1555 1555 2.13
LINK NE2 HIS B 202 MG CLA B 513 1555 1555 2.12
LINK NE2 HIS B 455 MG CLA B 514 1555 1555 2.17
LINK NE2 HIS B 466 MG CLA B 518 1555 1555 2.34
LINK NE2 HIS B 469 MG CLA B 521 1555 1555 2.24
LINK OD1 ASN C 39 MG CLA C 501 1555 1555 2.21
LINK NE2 HIS C 118 MG CLA C 493 1555 1555 2.35
LINK NE2 HIS C 132 MG CLA C 503 1555 1555 2.38
LINK NE2 HIS C 237 MG CLA C 491 1555 1555 2.18
LINK NE2 HIS C 251 MG CLA C 496 1555 1555 2.50
LINK OE1 GLU C 354 MN2 OEC A 565 1555 1555 2.48
LINK OE2 GLU C 354 MN3 OEC A 565 1555 1555 2.12
LINK NE2 HIS C 430 MG CLA C 492 1555 1555 2.50
LINK NE2 HIS C 444 MG CLA C 498 1555 1555 2.39
LINK NE2 HIS D 197 MG CLA D 354 1555 1555 2.16
LINK NE2 HIS D 214 FE FE2 A 557 1555 1555 2.23
LINK NE2 HIS D 268 FE FE2 A 557 1555 1555 2.29
LINK OD1 ASP K 19 CA CA K 56 1555 1555 2.84
LINK OD2 ASP K 23 CA CA K 56 1555 1555 2.86
LINK OE1 GLU a5189 CA1 OEC a5565 1555 1555 2.74
LINK OE2 GLU a5189 MN1 OEC a5565 1555 1555 1.84
LINK NE2 HIS a5198 MG CLA a5558 1555 1555 2.24
LINK OE1 GLU a5333 MN3 OEC a5565 1555 1555 2.20
LINK OE2 GLU a5333 MN4 OEC a5565 1555 1555 2.17
LINK OD1 ASP a5342 MN2 OEC a5565 1555 1555 2.14
LINK OD2 ASP a5342 MN1 OEC a5565 1555 1555 2.49
LINK O ALA a5344 CA1 OEC a5565 1555 1555 2.53
LINK OXT ALA a5344 MN2 OEC a5565 1555 1555 1.69
LINK NE2 HIS b5009 MG CLA b5524 1555 1555 2.20
LINK ND1 HIS b5201 MG CLA b5512 1555 1555 2.15
LINK NE2 HIS b5202 MG CLA b5513 1555 1555 2.15
LINK NE2 HIS b5455 MG CLA b5514 1555 1555 2.21
LINK NE2 HIS b5466 MG CLA b5518 1555 1555 2.35
LINK NE2 HIS b5469 MG CLA b5521 1555 1555 2.28
LINK OD1 ASN c5039 MG CLA c5501 1555 1555 2.18
LINK NE2 HIS c5118 MG CLA c5493 1555 1555 2.33
LINK NE2 HIS c5132 MG CLA c5503 1555 1555 2.40
LINK NE2 HIS c5237 MG CLA c5491 1555 1555 2.13
LINK OE1 GLU c5354 MN2 OEC a5565 1555 1555 2.32
LINK OE2 GLU c5354 MN3 OEC a5565 1555 1555 2.12
LINK NE2 HIS c5430 MG CLA c5492 1555 1555 2.46
LINK NE2 HIS c5444 MG CLA c5498 1555 1555 2.33
LINK NE2 HIS d5197 MG CLA d5354 1555 1555 2.22
LINK NE2 HIS d5214 FE FE2 a5557 1555 1555 2.18
LINK NE2 HIS d5268 FE FE2 a5557 1555 1555 2.27
LINK OD1 ASP k5019 CA CA k5056 1555 1555 2.59
LINK OD2 ASP k5019 CA CA k5056 1555 1555 2.73
LINK OD2 ASP k5023 CA CA k5056 1555 1555 2.78
LINK FE FE2 A 557 O3 BCT D 353 1555 1555 2.34
LINK FE FE2 A 557 O2 BCT D 353 1555 1555 2.31
LINK FE FE2 a5557 O3 BCT d5353 1555 1555 2.31
LINK FE FE2 a5557 O2 BCT d5353 1555 1555 2.34
CISPEP 1 THR V 89 PRO V 90 0 -0.27
CISPEP 2 THR v 5089 PRO v 5090 0 -0.07
SITE 1 AC1 3 ASP K 19 ASP K 23 UNK X 2
SITE 1 AC2 5 HIS A 215 HIS A 272 HIS D 214 HIS D 268
SITE 2 AC2 5 BCT D 353
SITE 1 AC3 9 HIS A 215 GLU A 244 TYR A 246 HIS A 272
SITE 2 AC3 9 FE2 A 557 HIS D 214 TYR D 244 LYS D 264
SITE 3 AC3 9 HIS D 268
SITE 1 AC4 3 ASP k5019 ASP k5023 UNK x5002
SITE 1 AC5 5 HIS a5215 HIS a5272 HIS d5214 HIS d5268
SITE 2 AC5 5 BCT d5353
SITE 1 AC6 9 HIS a5215 GLU a5244 TYR a5246 HIS a5272
SITE 2 AC6 9 FE2 a5557 HIS d5214 TYR d5244 LYS d5264
SITE 3 AC6 9 HIS d5268
SITE 1 AC7 20 PHE A 119 TYR A 147 PRO A 150 SER A 153
SITE 2 AC7 20 VAL A 157 MET A 183 ILE A 184 PHE A 186
SITE 3 AC7 20 GLN A 187 LEU A 193 HIS A 198 GLY A 201
SITE 4 AC7 20 VAL A 205 THR A 286 ILE A 290 CLA A 559
SITE 5 AC7 20 CLA A 560 PHO A 561 CLA D 354 MGE D 360
SITE 1 AC8 23 MET A 183 PHE A 206 CLA A 558 CLA A 559
SITE 2 AC8 23 CLA A 560 PHO A 562 VAL D 152 VAL D 156
SITE 3 AC8 23 PHE D 181 LEU D 182 PHE D 185 GLN D 186
SITE 4 AC8 23 TRP D 191 THR D 192 HIS D 197 GLY D 200
SITE 5 AC8 23 VAL D 201 VAL D 204 LEU D 279 SER D 282
SITE 6 AC8 23 ALA D 283 VAL D 286 MGE D 358
SITE 1 AC9 18 THR A 45 VAL A 157 PHE A 158 MET A 172
SITE 2 AC9 18 ILE A 176 THR A 179 PHE A 180 MET A 183
SITE 3 AC9 18 CLA A 558 PHO A 561 UNK C 474 MET D 198
SITE 4 AC9 18 VAL D 201 ALA D 202 GLY D 206 LEU D 209
SITE 5 AC9 18 CLA D 354 MGE L 210
SITE 1 BC1 14 GLN A 199 VAL A 202 ALA A 203 GLY A 207
SITE 2 BC1 14 LEU A 210 TRP A 278 CLA A 558 PHO A 562
SITE 3 BC1 14 DGD C 509 PHE D 157 VAL D 175 PHE D 179
SITE 4 BC1 14 LEU D 182 CLA D 354
SITE 1 BC2 21 LEU A 41 ALA A 44 THR A 45 ILE A 115
SITE 2 BC2 21 PHE A 119 TYR A 126 GLN A 130 TYR A 147
SITE 3 BC2 21 PRO A 150 PHE A 158 LEU A 174 PRO A 279
SITE 4 BC2 21 VAL A 283 CLA A 558 CLA A 559 LEU D 205
SITE 5 BC2 21 ALA D 208 LEU D 209 ILE D 213 TRP D 253
SITE 6 BC2 21 PHE D 257
SITE 1 BC3 21 PHE A 206 ALA A 209 LEU A 210 ALA A 213
SITE 2 BC3 21 MET A 214 LEU A 258 CLA A 560 LEU D 37
SITE 3 BC3 21 ALA D 41 LEU D 45 TRP D 48 LEU D 122
SITE 4 BC3 21 PHE D 125 GLN D 129 ASN D 142 PHE D 146
SITE 5 BC3 21 PRO D 149 PHE D 153 PRO D 275 LEU D 279
SITE 6 BC3 21 CLA D 354
SITE 1 BC4 14 ILE A 36 PRO A 39 PHE A 93 PRO A 95
SITE 2 BC4 14 ILE A 96 TRP A 97 LEU A 114 PHE A 117
SITE 3 BC4 14 HIS A 118 TYR I 9 VAL I 12 THR I 13
SITE 4 BC4 14 PHE I 15 MGE I 201
SITE 1 BC5 17 UNK C 480 LEU D 36 PRO D 39 LEU D 43
SITE 2 BC5 17 LEU D 89 LEU D 90 LEU D 91 LEU D 92
SITE 3 BC5 17 TRP D 93 THR D 112 PHE D 113 HIS D 117
SITE 4 BC5 17 PHE D 120 BCR D 357 UNK X 63 UNK X 64
SITE 5 BC5 17 UNK X 67
SITE 1 BC6 5 TRP B 185 PHE B 190 CLA B 512 PHE H 41
SITE 2 BC6 5 BCR H 107
SITE 1 BC7 19 GLY B 189 PHE B 190 GLY B 197 ALA B 200
SITE 2 BC7 19 HIS B 201 ALA B 204 ALA B 205 VAL B 208
SITE 3 BC7 19 PHE B 247 PHE B 250 CLA B 511 CLA B 513
SITE 4 BC7 19 CLA B 518 LEU D 158 ILE D 159 PHE H 38
SITE 5 BC7 19 ILE H 45 LEU H 46 TYR H 49
SITE 1 BC8 18 ARG B 68 LEU B 69 ALA B 146 LEU B 149
SITE 2 BC8 18 CYS B 150 PHE B 153 LEU B 158 HIS B 201
SITE 3 BC8 18 HIS B 202 PHE B 247 VAL B 252 THR B 262
SITE 4 BC8 18 CLA B 512 CLA B 514 CLA B 515 CLA B 516
SITE 5 BC8 18 PHE H 38 LEU H 39
SITE 1 BC9 19 TRP B 33 PHE B 61 PHE B 65 ARG B 68
SITE 2 BC9 19 LEU B 149 VAL B 245 ALA B 248 ALA B 249
SITE 3 BC9 19 VAL B 252 PHE B 451 HIS B 455 PHE B 458
SITE 4 BC9 19 PHE B 462 CLA B 513 CLA B 515 CLA B 517
SITE 5 BC9 19 CLA B 522 CLA B 523 CLA B 525
SITE 1 CC1 18 THR B 27 VAL B 30 ALA B 31 TRP B 33
SITE 2 CC1 18 ALA B 34 VAL B 62 PHE B 65 MET B 66
SITE 3 CC1 18 ARG B 68 LEU B 69 VAL B 96 HIS B 100
SITE 4 CC1 18 GLY B 147 ALA B 205 CLA B 513 CLA B 514
SITE 5 CC1 18 CLA B 516 CLA B 520
SITE 1 CC2 16 LEU B 69 GLY B 70 TRP B 91 ALA B 99
SITE 2 CC2 16 HIS B 100 LEU B 103 GLY B 152 PHE B 153
SITE 3 CC2 16 PHE B 156 HIS B 157 PHE B 162 GLY B 163
SITE 4 CC2 16 PRO B 164 CLA B 513 CLA B 515 BCR B 529
SITE 1 CC3 20 TRP B 33 TYR B 40 GLN B 58 GLY B 59
SITE 2 CC3 20 PHE B 61 LEU B 324 PHE B 325 THR B 327
SITE 3 CC3 20 GLY B 328 PRO B 329 TRP B 450 PHE B 451
SITE 4 CC3 20 HIS B 455 CLA B 514 MGE B 530 PHE D 196
SITE 5 CC3 20 MET D 281 LEU L 27 PHE M 14 BCR t 104
SITE 1 CC4 18 THR B 236 SER B 239 ALA B 243 PHE B 246
SITE 2 CC4 18 PHE B 463 HIS B 466 LEU B 474 CLA B 512
SITE 3 CC4 18 CLA B 519 CLA B 520 UNK C 481 UNK C 482
SITE 4 CC4 18 ILE D 123 MET D 126 LEU D 127 PHE D 130
SITE 5 CC4 18 LEU H 43 LEU H 46
SITE 1 CC5 13 PHE B 139 ALA B 212 PHE B 215 HIS B 216
SITE 2 CC5 13 PRO B 221 LEU B 229 CLA B 518 CLA B 520
SITE 3 CC5 13 THR H 27 THR H 28 MET H 31 PHE H 34
SITE 4 CC5 13 BCR H 107
SITE 1 CC6 13 LEU B 135 PRO B 136 PHE B 139 HIS B 142
SITE 2 CC6 13 MET B 231 VAL B 237 SER B 240 SER B 241
SITE 3 CC6 13 CLA B 515 CLA B 518 CLA B 519 CLA B 522
SITE 4 CC6 13 CLA B 525
SITE 1 CC7 19 TRP B 5 TYR B 6 ARG B 7 VAL B 8
SITE 2 CC7 19 HIS B 9 LEU B 238 ILE B 242 LEU B 461
SITE 3 CC7 19 PHE B 462 PHE B 464 GLY B 465 TRP B 468
SITE 4 CC7 19 HIS B 469 ARG B 472 PHE B 479 CLA B 522
SITE 5 CC7 19 CLA B 523 CLA B 524 MGE D 359
SITE 1 CC8 16 HIS B 9 LEU B 12 LEU B 19 ALA B 22
SITE 2 CC8 16 HIS B 23 HIS B 26 THR B 27 VAL B 237
SITE 3 CC8 16 LEU B 238 SER B 241 VAL B 245 CLA B 514
SITE 4 CC8 16 CLA B 520 CLA B 521 CLA B 523 CLA B 525
SITE 1 CC9 11 HIS B 9 HIS B 26 VAL B 30 PHE B 462
SITE 2 CC9 11 CLA B 514 CLA B 521 CLA B 522 CLA B 524
SITE 3 CC9 11 BCR B 527 BCR B 528 MGE D 359
SITE 1 DC1 15 VAL B 8 HIS B 9 LEU B 12 ALA B 22
SITE 2 DC1 15 MET B 25 LEU B 29 TRP B 115 CLA B 521
SITE 3 DC1 15 CLA B 523 BCR B 527 ARG L 7 VAL L 10
SITE 4 DC1 15 MGE L 210 UNK c5475 UNK c5476
SITE 1 DC2 11 ILE B 20 HIS B 23 MET B 138 ILE B 141
SITE 2 DC2 11 HIS B 142 LEU B 145 CLA B 514 CLA B 520
SITE 3 DC2 11 CLA B 522 CLA B 526 LEU H 14
SITE 1 DC3 9 ILE B 20 LEU B 24 ALA B 110 TRP B 113
SITE 2 DC3 9 HIS B 114 LEU B 120 CLA B 525 THR H 5
SITE 3 DC3 9 LEU H 7
SITE 1 DC4 16 LEU C 95 LEU C 168 GLY C 171 ALA C 172
SITE 2 DC4 16 ILE C 224 VAL C 233 HIS C 237 ILE C 240
SITE 3 DC4 16 ALA C 278 MET C 281 MET C 282 VAL C 296
SITE 4 DC4 16 TYR C 297 CLA C 492 CLA C 493 BCR C 506
SITE 1 DC5 14 TRP C 63 HIS C 91 GLY C 171 LEU C 175
SITE 2 DC5 14 LYS C 178 ALA C 286 TYR C 297 HIS C 430
SITE 3 DC5 14 LEU C 433 PHE C 437 CLA C 491 CLA C 493
SITE 4 DC5 14 CLA C 494 CLA C 500
SITE 1 DC6 16 ILE C 60 VAL C 61 ALA C 64 THR C 68
SITE 2 DC6 16 LEU C 88 HIS C 91 ILE C 92 LEU C 95
SITE 3 DC6 16 VAL C 114 HIS C 118 LEU C 279 UNK C 477
SITE 4 DC6 16 CLA C 491 CLA C 492 CLA C 500 CLA C 502
SITE 1 DC7 14 TRP C 63 MET C 67 PHE C 70 GLY C 85
SITE 2 DC7 14 ILE C 87 SER C 406 TRP C 425 SER C 429
SITE 3 DC7 14 HIS C 430 UNK C 478 CLA C 492 CLA C 500
SITE 4 DC7 14 DGD C 508 PRO K 26
SITE 1 DC8 15 ILE A 36 SER A 124 MET A 127 TRP A 131
SITE 2 DC8 15 ILE C 265 TYR C 274 GLY C 277 ALA C 278
SITE 3 DC8 15 LEU C 438 HIS C 441 LEU C 442 ALA C 445
SITE 4 DC8 15 ARG C 449 CLA C 497 PHE I 23
SITE 1 DC9 12 LEU C 165 ILE C 243 GLY C 247 TRP C 250
SITE 2 DC9 12 HIS C 251 PRO C 256 PHE C 257 TRP C 259
SITE 3 DC9 12 PHE C 264 CLA C 497 BCR C 506 LEU I 24
SITE 1 EC1 14 MET C 157 LEU C 161 HIS C 164 LEU C 168
SITE 2 EC1 14 PHE C 264 TRP C 266 TYR C 271 TYR C 274
SITE 3 EC1 14 SER C 275 LEU C 279 MET C 282 CLA C 495
SITE 4 EC1 14 CLA C 496 CLA C 499
SITE 1 EC2 15 LHG A 567 TRP C 36 ALA C 37 ASN C 39
SITE 2 EC2 15 ALA C 40 GLU C 269 LEU C 276 PHE C 436
SITE 3 EC2 15 PHE C 437 GLY C 440 TRP C 443 HIS C 444
SITE 4 EC2 15 ARG C 447 CLA C 499 CLA C 500
SITE 1 EC3 11 ASN C 39 LEU C 49 ALA C 52 HIS C 53
SITE 2 EC3 11 HIS C 56 GLY C 268 GLU C 269 SER C 275
SITE 3 EC3 11 CLA C 497 CLA C 498 CLA C 500
SITE 1 EC4 15 ASN C 39 HIS C 56 LEU C 59 LEU C 279
SITE 2 EC4 15 PHE C 436 PHE C 437 CLA C 492 CLA C 493
SITE 3 EC4 15 CLA C 494 CLA C 498 CLA C 499 CLA C 501
SITE 4 EC4 15 PRO K 29 VAL K 30 LEU K 33
SITE 1 EC5 19 ASP C 27 TRP C 35 GLY C 38 ASN C 39
SITE 2 EC5 19 ARG C 41 LEU C 42 LEU C 45 LYS C 48
SITE 3 EC5 19 ALA C 52 PHE C 127 ALA C 133 ILE C 134
SITE 4 EC5 19 CLA C 500 BCR C 504 TRP K 39 GLN K 40
SITE 5 EC5 19 UNK X 31 VAL Z 20 PRO Z 24
SITE 1 EC6 10 HIS C 53 PHE C 147 PHE C 163 HIS C 164
SITE 2 EC6 10 VAL C 167 LEU C 168 GLY C 171 CLA C 493
SITE 3 EC6 10 CLA C 503 BCR C 505
SITE 1 EC7 9 LEU C 50 GLY C 128 TYR C 131 HIS C 132
SITE 2 EC7 9 PRO C 137 LEU C 140 PHE C 147 CLA C 502
SITE 3 EC7 9 BCR C 505
SITE 1 EC8 12 ILE E 13 ARG E 18 TYR E 19 HIS E 23
SITE 2 EC8 12 THR E 26 ILE E 27 ARG F 19 TRP F 20
SITE 3 EC8 12 HIS F 24 ALA F 27 ILE F 31 UNK X 116
SITE 1 EC9 12 ALA V 62 CYS V 63 CYS V 66 HIS V 67
SITE 2 EC9 12 THR V 74 LEU V 78 ASP V 79 LEU V 80
SITE 3 EC9 12 THR V 84 TYR V 101 TYR V 108 HIS V 118
SITE 1 FC1 12 UNK C 474 LEU D 209 LEU D 210 HIS D 214
SITE 2 FC1 12 THR D 217 ASN D 250 TRP D 253 ALA D 260
SITE 3 FC1 12 PHE D 261 LEU D 267 PHE D 270 VAL D 274
SITE 1 FC2 9 HIS A 215 LEU A 218 ALA A 251 HIS A 252
SITE 2 FC2 9 PHE A 255 SER A 264 PHE A 265 LEU A 271
SITE 3 FC2 9 PHE A 274
SITE 1 FC3 7 ASP A 170 GLU A 189 HIS A 332 GLU A 333
SITE 2 FC3 7 ASP A 342 ALA A 344 GLU C 354
SITE 1 FC4 6 ILE A 38 ALA A 43 ALA A 51 ALA A 54
SITE 2 FC4 6 TRP A 105 PHE I 15
SITE 1 FC5 10 MET B 25 LEU B 29 TRP B 115 CLA B 523
SITE 2 FC5 10 CLA B 524 BCR B 528 MGE B 530 ALA M 10
SITE 3 FC5 10 BCR t 104 PHE t5019
SITE 1 FC6 13 TRP B 33 SER B 36 MET B 37 LEU B 109
SITE 2 FC6 13 CLA B 517 BCR B 527 BCR B 528 SQD a 212
SITE 3 FC6 13 ILE t5004 PHE t5008 ALA t5011 PHE t5018
SITE 4 FC6 13 PHE t5022
SITE 1 FC7 9 LEU B 29 GLY B 32 TRP B 33 SER B 36
SITE 2 FC7 9 ILE B 101 VAL B 102 CLA B 523 BCR B 527
SITE 3 FC7 9 BCR t 104
SITE 1 FC8 6 LEU B 106 CYS B 112 VAL B 116 TYR B 117
SITE 2 FC8 6 CLA B 516 SQD a 212
SITE 1 FC9 7 CLA B 511 CLA B 519 MET H 35 PHE H 38
SITE 2 FC9 7 PHE H 41 UNK X 52 UNK X 57
SITE 1 GC1 14 TYR D 42 LEU D 43 GLY D 46 GLY D 47
SITE 2 GC1 14 LEU D 49 THR D 50 PHE D 113 CLA D 355
SITE 3 GC1 14 PRO F 29 THR F 30 PHE F 33 ILE F 37
SITE 4 GC1 14 VAL J 21 VAL J 25
SITE 1 GC2 14 BCR C 504 ALA J 14 THR J 15 GLY J 18
SITE 2 GC2 14 MET J 19 LEU K 21 LEU K 31 ALA K 34
SITE 3 GC2 14 PHE K 37 VAL K 38 UNK X 13 UNK X 14
SITE 4 GC2 14 UNK X 17 VAL Z 13
SITE 1 GC3 15 ALA C 55 GLY C 58 LEU C 59 VAL C 116
SITE 2 GC3 15 LEU C 119 SER C 122 ALA C 123 GLY C 126
SITE 3 GC3 15 CLA C 501 BCR C 505 TYR K 15 PHE K 18
SITE 4 GC3 15 PHE K 32 ALA K 36 BCR X 130
SITE 1 GC4 11 PHE C 112 VAL C 116 ILE C 120 SER C 121
SITE 2 GC4 11 VAL C 124 LEU C 125 CLA C 502 CLA C 503
SITE 3 GC4 11 BCR C 504 TYR K 15 GLY Z 55
SITE 1 GC5 14 ILE C 209 TYR C 212 LEU C 213 ILE C 224
SITE 2 GC5 14 VAL C 227 ASP C 232 VAL C 233 HIS C 237
SITE 3 GC5 14 PHE C 264 CLA C 491 CLA C 496 VAL I 20
SITE 4 GC5 14 PHE I 23 LEU I 24
SITE 1 GC6 11 PHE A 93 TRP A 97 LEU A 121 CLA A 563
SITE 2 GC6 11 SER C 216 PHE C 218 TRP C 223 MET C 281
SITE 3 GC6 11 PHE C 284 LYS I 5 TYR I 9
SITE 1 GC7 17 PHE A 155 ILE A 160 ILE A 163 PRO C 217
SITE 2 GC7 17 PHE C 218 GLY C 219 GLY C 220 GLY C 222
SITE 3 GC7 17 VAL C 225 SER C 226 ASN C 228 PHE C 284
SITE 4 GC7 17 CYS C 288 PHE C 292 ASN C 294 ARG C 362
SITE 5 GC7 17 LEU C 438
SITE 1 GC8 15 ARG A 140 TRP A 142 PHE A 273 SQD A 568
SITE 2 GC8 15 TRP C 36 PHE C 436 TRP C 443 ARG C 447
SITE 3 GC8 15 CLA C 498 GLU D 219 ASN D 220 ALA D 229
SITE 4 GC8 15 SER D 230 THR D 231 PHE D 232
SITE 1 GC9 10 ASN A 267 SER A 270 PHE A 273 PHE A 274
SITE 2 GC9 10 LHG A 567 GLU C 29 TRP C 36 SER D 230
SITE 3 GC9 10 PHE D 232 ARG D 233
SITE 1 HC1 14 PHE A 197 GLU C 83 GLN C 84 GLY C 85
SITE 2 HC1 14 SER C 406 ASN C 418 PHE C 419 VAL C 420
SITE 3 HC1 14 TRP C 425 THR C 428 UNK C 479 CLA C 494
SITE 4 HC1 14 DGD C 509 TYR J 33
SITE 1 HC2 20 GLN A 199 LEU A 200 PHE A 300 ASN A 301
SITE 2 HC2 20 PHE A 302 SER A 305 CLA A 560 ASN C 405
SITE 3 HC2 20 ASN C 415 SER C 416 ASN C 418 DGD C 508
SITE 4 HC2 20 MGE D 358 PHE J 29 ALA J 32 TYR J 33
SITE 5 HC2 20 GLY J 37 SER J 38 SER J 39 GLN V 60
SITE 1 HC3 12 DGD C 509 TYR D 67 GLY D 70 CYS D 71
SITE 2 HC3 12 CLA D 354 THR F 30 MET F 40 GLN F 41
SITE 3 HC3 12 GLY J 31 ALA J 32 GLY J 35 GLY J 37
SITE 1 HC4 14 TYR B 193 PHE B 250 TYR B 258 TYR B 273
SITE 2 HC4 14 SER B 277 PHE B 463 HIS D 87 ILE D 123
SITE 3 HC4 14 LEU D 162 SER D 165 TYR H 49 VAL H 60
SITE 4 HC4 14 SER H 61 TRP H 62
SITE 1 HC5 13 ASN A 234 TRP B 5 TYR B 6 ARG B 7
SITE 2 HC5 13 PHE B 464 TRP B 468 CLA B 521 CLA B 523
SITE 3 HC5 13 ARG D 139 TYR D 141 PHE D 269 PHE D 273
SITE 4 HC5 13 MGE L 210
SITE 1 HC6 14 SER A 232 ASN A 234 CLA A 559 TRP B 5
SITE 2 HC6 14 TYR B 6 CLA B 524 UNK C 474 TRP D 266
SITE 3 HC6 14 PHE D 270 PHE D 273 MGE D 359 GLU L 11
SITE 4 HC6 14 SER L 16 GLY L 20
SITE 1 HC7 14 CLA A 558 ILE D 259 ALA D 260 PHE D 261
SITE 2 HC7 14 SER D 262 ASN D 263 TRP D 266 PHE D 270
SITE 3 HC7 14 THR L 15 TYR L 18 LEU L 19 PHE T 10
SITE 4 HC7 14 PHE T 17 ALA T 20
SITE 1 HC8 8 TRP B 113 TYR B 117 BCR B 529 TRP a5020
SITE 2 HC8 8 ASN a5026 ARG a5027 LEU a5028 BCR t 104
SITE 1 HC9 7 ARG B 18 LEU B 29 SER B 104 ARG l5014
SITE 2 HC9 7 TYR l5018 PHE t5019 PHE t5023
SITE 1 IC1 10 THR B 327 GLY B 328 PRO B 329 PHE B 453
SITE 2 IC1 10 CLA B 517 BCR B 527 PHE L 35 ASN M 4
SITE 3 IC1 10 LEU M 6 LMT M5216
SITE 1 IC2 11 ILE A 50 LEU A 72 TYR A 73 UNK C 488
SITE 2 IC2 11 UNK C 489 ARG D 304 GLY O 139 GLU O 140
SITE 3 IC2 11 LMT T 217 ALA b5043 LEU b5098
SITE 1 IC3 9 MET M 1 LMT M5216 MET T 1 ILE T 4
SITE 2 IC3 9 LMT T 217 TYR b5040 MGE b5530 GLN m5005
SITE 3 IC3 9 LEU m5006
SITE 1 IC4 11 LEU A 72 LMT A 569 MET T 1 ILE T 4
SITE 2 IC4 11 ALA T 11 ILE T 14 TYR b5040 ALA b5043
SITE 3 IC4 11 THR b5044 BCR b5528 LMT m 216
SITE 1 IC5 21 PHE a5119 TYR a5147 PRO a5150 SER a5153
SITE 2 IC5 21 VAL a5157 MET a5183 ILE a5184 PHE a5186
SITE 3 IC5 21 GLN a5187 LEU a5193 HIS a5198 GLY a5201
SITE 4 IC5 21 VAL a5205 THR a5286 ILE a5290 CLA a5559
SITE 5 IC5 21 CLA a5560 PHO a5561 LEU d5182 CLA d5354
SITE 6 IC5 21 MGE d5361
SITE 1 IC6 23 MET a5183 PHE a5206 CLA a5558 CLA a5559
SITE 2 IC6 23 CLA a5560 PHO a5562 VAL d5152 VAL d5156
SITE 3 IC6 23 PHE d5181 LEU d5182 PHE d5185 GLN d5186
SITE 4 IC6 23 TRP d5191 THR d5192 HIS d5197 GLY d5200
SITE 5 IC6 23 VAL d5201 VAL d5204 LEU d5279 SER d5282
SITE 6 IC6 23 ALA d5283 VAL d5286 MGE d5359
SITE 1 IC7 18 THR a5045 VAL a5157 PHE a5158 MET a5172
SITE 2 IC7 18 ILE a5176 THR a5179 PHE a5180 MET a5183
SITE 3 IC7 18 CLA a5558 UNK c5474 MET d5198 VAL d5201
SITE 4 IC7 18 ALA d5202 GLY d5206 LEU d5209 CLA d5354
SITE 5 IC7 18 MGE d5361 MGE l5210
SITE 1 IC8 15 GLN a5199 VAL a5202 ALA a5203 GLY a5207
SITE 2 IC8 15 LEU a5210 TRP a5278 CLA a5558 PHO a5562
SITE 3 IC8 15 DGD c5509 PHE d5157 VAL d5175 PHE d5179
SITE 4 IC8 15 LEU d5182 CLA d5354 MGE d5359
SITE 1 IC9 20 LEU a5041 ALA a5044 THR a5045 ILE a5115
SITE 2 IC9 20 PHE a5119 TYR a5126 GLN a5130 TYR a5147
SITE 3 IC9 20 PRO a5150 PHE a5158 LEU a5174 PRO a5279
SITE 4 IC9 20 VAL a5283 CLA a5558 LEU d5205 ALA d5208
SITE 5 IC9 20 LEU d5209 ILE d5213 TRP d5253 PHE d5257
SITE 1 JC1 22 PHE a5206 ALA a5209 LEU a5210 ALA a5213
SITE 2 JC1 22 MET a5214 LEU a5258 CLA a5560 LEU d5037
SITE 3 JC1 22 ALA d5041 LEU d5045 TRP d5048 GLY d5118
SITE 4 JC1 22 LEU d5122 PHE d5125 GLN d5129 ASN d5142
SITE 5 JC1 22 PHE d5146 PRO d5149 PHE d5153 PRO d5275
SITE 6 JC1 22 LEU d5279 CLA d5354
SITE 1 JC2 15 ILE a5036 PRO a5039 THR a5040 PHE a5093
SITE 2 JC2 15 PRO a5095 ILE a5096 TRP a5097 LEU a5114
SITE 3 JC2 15 PHE a5117 HIS a5118 LEU a5121 TYR i5009
SITE 4 JC2 15 THR i5013 PHE i5015 MGE i5201
SITE 1 JC3 16 UNK c5480 LEU d5036 PRO d5039 LEU d5043
SITE 2 JC3 16 LEU d5089 LEU d5090 LEU d5091 LEU d5092
SITE 3 JC3 16 TRP d5093 THR d5112 PHE d5113 HIS d5117
SITE 4 JC3 16 PHE d5120 BCR d5357 UNK x5063 UNK x5064
SITE 1 JC4 5 TRP b5185 PHE b5190 CLA b5512 PHE h5041
SITE 2 JC4 5 BCR h5107
SITE 1 JC5 20 GLY b5189 PHE b5190 GLY b5197 ALA b5200
SITE 2 JC5 20 HIS b5201 ALA b5204 ALA b5205 VAL b5208
SITE 3 JC5 20 PHE b5247 PHE b5250 CLA b5511 CLA b5513
SITE 4 JC5 20 CLA b5518 LEU d5158 ILE d5159 PHE h5038
SITE 5 JC5 20 PHE h5041 ILE h5045 LEU h5046 TYR h5049
SITE 1 JC6 19 ARG b5068 LEU b5069 ALA b5146 LEU b5149
SITE 2 JC6 19 CYS b5150 PHE b5153 LEU b5158 HIS b5201
SITE 3 JC6 19 HIS b5202 PHE b5247 VAL b5252 THR b5262
SITE 4 JC6 19 CLA b5512 CLA b5514 CLA b5515 CLA b5516
SITE 5 JC6 19 CLA b5520 PHE h5038 LEU h5039
SITE 1 JC7 19 TRP b5033 PHE b5061 PHE b5065 ARG b5068
SITE 2 JC7 19 LEU b5148 VAL b5245 ALA b5248 ALA b5249
SITE 3 JC7 19 VAL b5252 PHE b5451 HIS b5455 PHE b5458
SITE 4 JC7 19 PHE b5462 CLA b5513 CLA b5515 CLA b5517
SITE 5 JC7 19 CLA b5522 CLA b5523 CLA b5525
SITE 1 JC8 17 THR b5027 VAL b5030 ALA b5031 TRP b5033
SITE 2 JC8 17 ALA b5034 VAL b5062 PHE b5065 MET b5066
SITE 3 JC8 17 ARG b5068 LEU b5069 HIS b5100 GLY b5147
SITE 4 JC8 17 ALA b5205 CLA b5513 CLA b5514 CLA b5516
SITE 5 JC8 17 CLA b5520
SITE 1 JC9 16 LEU b5069 GLY b5070 TRP b5091 ALA b5099
SITE 2 JC9 16 HIS b5100 LEU b5103 GLY b5152 PHE b5153
SITE 3 JC9 16 PHE b5156 HIS b5157 PHE b5162 GLY b5163
SITE 4 JC9 16 PRO b5164 CLA b5513 CLA b5515 BCR b5529
SITE 1 KC1 20 BCR T5104 TRP b5033 TYR b5040 GLN b5058
SITE 2 KC1 20 GLY b5059 PHE b5061 LEU b5324 PHE b5325
SITE 3 KC1 20 THR b5327 GLY b5328 PRO b5329 TRP b5450
SITE 4 KC1 20 PHE b5451 HIS b5455 CLA b5514 MGE b5530
SITE 5 KC1 20 PHE d5196 MET d5281 LEU l5027 PHE m5014
SITE 1 KC2 18 THR b5236 SER b5239 ALA b5243 PHE b5246
SITE 2 KC2 18 PHE b5463 HIS b5466 LEU b5474 CLA b5512
SITE 3 KC2 18 CLA b5519 CLA b5520 UNK c5481 UNK c5482
SITE 4 KC2 18 ILE d5123 MET d5126 LEU d5127 PHE d5130
SITE 5 KC2 18 LEU h5043 LEU h5046
SITE 1 KC3 13 PHE b5139 ALA b5212 PHE b5215 HIS b5216
SITE 2 KC3 13 PRO b5221 LEU b5229 CLA b5518 CLA b5520
SITE 3 KC3 13 THR h5027 THR h5028 MET h5031 PHE h5034
SITE 4 KC3 13 BCR h5107
SITE 1 KC4 13 LEU b5135 PRO b5136 PHE b5139 HIS b5142
SITE 2 KC4 13 MET b5231 VAL b5237 SER b5240 CLA b5513
SITE 3 KC4 13 CLA b5515 CLA b5518 CLA b5519 CLA b5522
SITE 4 KC4 13 CLA b5525
SITE 1 KC5 19 TRP b5005 TYR b5006 ARG b5007 VAL b5008
SITE 2 KC5 19 HIS b5009 LEU b5238 ILE b5242 LEU b5461
SITE 3 KC5 19 PHE b5462 PHE b5464 GLY b5465 TRP b5468
SITE 4 KC5 19 HIS b5469 ARG b5472 PHE b5479 CLA b5522
SITE 5 KC5 19 CLA b5523 CLA b5524 MGE d5360
SITE 1 KC6 16 HIS b5009 LEU b5012 LEU b5019 ALA b5022
SITE 2 KC6 16 HIS b5023 HIS b5026 THR b5027 VAL b5237
SITE 3 KC6 16 LEU b5238 SER b5241 VAL b5245 CLA b5514
SITE 4 KC6 16 CLA b5520 CLA b5521 CLA b5523 CLA b5525
SITE 1 KC7 11 HIS b5009 HIS b5026 VAL b5030 PHE b5462
SITE 2 KC7 11 CLA b5514 CLA b5521 CLA b5522 CLA b5524
SITE 3 KC7 11 BCR b5527 BCR b5528 MGE d5360
SITE 1 KC8 15 UNK C 475 UNK C 476 VAL b5008 HIS b5009
SITE 2 KC8 15 LEU b5012 ALA b5022 LEU b5029 TRP b5115
SITE 3 KC8 15 CLA b5521 CLA b5523 BCR b5527 ARG l5007
SITE 4 KC8 15 VAL l5010 MGE l5210 PHE m5021
SITE 1 KC9 11 ILE b5020 HIS b5023 MET b5138 ILE b5141
SITE 2 KC9 11 HIS b5142 LEU b5145 CLA b5514 CLA b5520
SITE 3 KC9 11 CLA b5522 CLA b5526 LEU h5014
SITE 1 LC1 9 ILE b5020 LEU b5024 ALA b5110 TRP b5113
SITE 2 LC1 9 HIS b5114 LEU b5120 CLA b5525 THR h5005
SITE 3 LC1 9 LEU h5007
SITE 1 LC2 14 LEU c5095 LEU c5168 GLY c5171 ALA c5172
SITE 2 LC2 14 VAL c5233 HIS c5237 ILE c5240 ALA c5278
SITE 3 LC2 14 MET c5281 VAL c5296 TYR c5297 CLA c5492
SITE 4 LC2 14 CLA c5493 BCR c5506
SITE 1 LC3 14 TRP c5063 HIS c5091 TRP c5097 GLY c5171
SITE 2 LC3 14 LYS c5178 ALA c5286 TYR c5297 HIS c5430
SITE 3 LC3 14 LEU c5433 PHE c5437 CLA c5491 CLA c5493
SITE 4 LC3 14 CLA c5494 CLA c5500
SITE 1 LC4 16 ILE c5060 VAL c5061 ALA c5064 THR c5068
SITE 2 LC4 16 LEU c5088 HIS c5091 ILE c5092 LEU c5095
SITE 3 LC4 16 VAL c5114 HIS c5118 LEU c5279 UNK c5477
SITE 4 LC4 16 CLA c5491 CLA c5492 CLA c5500 CLA c5502
SITE 1 LC5 14 TRP c5063 MET c5067 PHE c5070 GLY c5085
SITE 2 LC5 14 ILE c5087 SER c5406 TRP c5425 SER c5429
SITE 3 LC5 14 HIS c5430 UNK c5478 CLA c5492 CLA c5500
SITE 4 LC5 14 DGD c5508 PRO k5026
SITE 1 LC6 15 ILE a5036 SER a5124 MET a5127 TRP a5131
SITE 2 LC6 15 ILE c5265 TYR c5274 GLY c5277 ALA c5278
SITE 3 LC6 15 LEU c5438 HIS c5441 LEU c5442 ALA c5445
SITE 4 LC6 15 ARG c5449 CLA c5497 PHE i5023
SITE 1 LC7 12 LEU c5165 ILE c5243 GLY c5247 TRP c5250
SITE 2 LC7 12 HIS c5251 PRO c5256 PHE c5257 TRP c5259
SITE 3 LC7 12 PHE c5264 CLA c5497 BCR c5506 LEU i5024
SITE 1 LC8 14 MET c5157 LEU c5161 HIS c5164 LEU c5168
SITE 2 LC8 14 PHE c5264 TRP c5266 TYR c5271 TYR c5274
SITE 3 LC8 14 SER c5275 LEU c5279 MET c5282 CLA c5495
SITE 4 LC8 14 CLA c5496 CLA c5499
SITE 1 LC9 16 LHG a5567 TRP c5036 ALA c5037 ASN c5039
SITE 2 LC9 16 ALA c5040 GLU c5269 LEU c5272 LEU c5276
SITE 3 LC9 16 PHE c5436 PHE c5437 GLY c5440 TRP c5443
SITE 4 LC9 16 HIS c5444 ARG c5447 CLA c5499 CLA c5500
SITE 1 MC1 11 ASN c5039 LEU c5049 ALA c5052 HIS c5053
SITE 2 MC1 11 HIS c5056 GLU c5269 LEU c5272 SER c5275
SITE 3 MC1 11 CLA c5497 CLA c5498 CLA c5500
SITE 1 MC2 14 ASN c5039 HIS c5056 LEU c5059 LEU c5279
SITE 2 MC2 14 PHE c5436 PHE c5437 CLA c5492 CLA c5493
SITE 3 MC2 14 CLA c5494 CLA c5498 CLA c5499 PRO k5029
SITE 4 MC2 14 VAL k5030 LEU k5033
SITE 1 MC3 18 ASP c5027 TRP c5035 GLY c5038 ASN c5039
SITE 2 MC3 18 ARG c5041 LEU c5042 LEU c5045 LYS c5048
SITE 3 MC3 18 ALA c5052 PHE c5127 ALA c5133 ILE c5134
SITE 4 MC3 18 BCR c5504 TRP k5039 GLN k5040 UNK x5031
SITE 5 MC3 18 VAL z5020 PRO z5024
SITE 1 MC4 10 HIS c5053 PHE c5147 PHE c5163 HIS c5164
SITE 2 MC4 10 VAL c5167 LEU c5168 GLY c5171 CLA c5493
SITE 3 MC4 10 CLA c5503 BCR c5505
SITE 1 MC5 10 LEU c5050 VAL c5124 GLY c5128 TYR c5131
SITE 2 MC5 10 HIS c5132 PRO c5137 LEU c5140 PHE c5147
SITE 3 MC5 10 CLA c5502 BCR c5505
SITE 1 MC6 12 ILE e5013 ARG e5018 TYR e5019 HIS e5023
SITE 2 MC6 12 THR e5026 ILE e5027 ARG f5019 TRP f5020
SITE 3 MC6 12 HIS f5024 ALA f5027 ILE f5031 UNK x5116
SITE 1 MC7 12 ALA v5062 CYS v5063 CYS v5066 HIS v5067
SITE 2 MC7 12 THR v5074 LEU v5078 ASP v5079 LEU v5080
SITE 3 MC7 12 THR v5084 TYR v5101 TYR v5108 HIS v5118
SITE 1 MC8 12 UNK c5474 LEU d5209 LEU d5210 HIS d5214
SITE 2 MC8 12 THR d5217 TRP d5253 ALA d5260 PHE d5261
SITE 3 MC8 12 LEU d5267 PHE d5270 VAL d5274 THR d5277
SITE 1 MC9 9 HIS a5215 LEU a5218 ALA a5251 HIS a5252
SITE 2 MC9 9 PHE a5255 SER a5264 PHE a5265 LEU a5271
SITE 3 MC9 9 PHE a5274
SITE 1 NC1 7 ASP a5170 GLU a5189 HIS a5332 GLU a5333
SITE 2 NC1 7 ASP a5342 ALA a5344 GLU c5354
SITE 1 NC2 6 ILE a5038 ALA a5043 ALA a5051 ALA a5054
SITE 2 NC2 6 TRP a5105 PHE i5015
SITE 1 NC3 9 PHE T 19 BCR T5104 MET b5025 LEU b5029
SITE 2 NC3 9 TRP b5115 CLA b5523 CLA b5524 BCR b5528
SITE 3 NC3 9 MGE b5530
SITE 1 NC4 16 SQD A5212 ILE T 4 PHE T 8 ALA T 11
SITE 2 NC4 16 ALA T 15 PHE T 17 PHE T 18 ILE T 21
SITE 3 NC4 16 PHE T 22 TRP b5033 SER b5036 MET b5037
SITE 4 NC4 16 LEU b5109 CLA b5517 BCR b5527 BCR b5528
SITE 1 NC5 10 LMT T 217 BCR T5104 LEU b5029 GLY b5032
SITE 2 NC5 10 TRP b5033 SER b5036 ILE b5101 VAL b5102
SITE 3 NC5 10 CLA b5523 BCR b5527
SITE 1 NC6 8 SQD A5212 PHE T 18 PHE T 22 LEU b5106
SITE 2 NC6 8 CYS b5112 VAL b5116 TYR b5117 CLA b5516
SITE 1 NC7 6 CLA b5511 CLA b5519 PHE h5038 PHE h5041
SITE 2 NC7 6 UNK x5052 UNK x5057
SITE 1 NC8 15 TYR d5042 LEU d5043 GLY d5046 GLY d5047
SITE 2 NC8 15 LEU d5049 THR d5050 PHE d5101 PHE d5113
SITE 3 NC8 15 CLA d5355 PRO f5029 THR f5030 PHE f5033
SITE 4 NC8 15 ILE f5037 VAL j5021 VAL j5025
SITE 1 NC9 14 BCR c5504 ALA j5014 THR j5015 GLY j5018
SITE 2 NC9 14 MET j5019 LEU k5021 LEU k5031 ALA k5034
SITE 3 NC9 14 PHE k5037 VAL k5038 UNK x5013 UNK x5014
SITE 4 NC9 14 UNK x5017 VAL z5013
SITE 1 OC1 14 ALA c5055 GLY c5058 LEU c5059 VAL c5116
SITE 2 OC1 14 LEU c5119 SER c5122 ALA c5123 CLA c5501
SITE 3 OC1 14 BCR c5505 TYR k5015 PHE k5018 PHE k5032
SITE 4 OC1 14 ALA k5036 BCR x5130
SITE 1 OC2 11 PHE c5112 VAL c5116 ILE c5120 SER c5121
SITE 2 OC2 11 VAL c5124 LEU c5125 CLA c5502 CLA c5503
SITE 3 OC2 11 BCR c5504 TYR k5015 GLY z5055
SITE 1 OC3 12 ILE c5209 TYR c5212 ILE c5224 VAL c5227
SITE 2 OC3 12 ASP c5232 HIS c5237 PHE c5264 CLA c5491
SITE 3 OC3 12 CLA c5496 VAL i5020 PHE i5023 LEU i5024
SITE 1 OC4 11 PHE a5093 TRP a5097 LEU a5121 CLA a5563
SITE 2 OC4 11 SER c5216 PHE c5218 TRP c5223 MET c5281
SITE 3 OC4 11 PHE c5284 LYS i5005 TYR i5009
SITE 1 OC5 17 PHE a5155 ILE a5160 ILE a5163 PRO c5217
SITE 2 OC5 17 PHE c5218 GLY c5219 GLY c5220 GLY c5222
SITE 3 OC5 17 VAL c5225 SER c5226 ASN c5228 PHE c5284
SITE 4 OC5 17 CYS c5288 PHE c5292 ASN c5294 ARG c5362
SITE 5 OC5 17 LEU c5438
SITE 1 OC6 15 ARG a5140 TRP a5142 PHE a5273 TRP c5036
SITE 2 OC6 15 PHE c5436 TRP c5443 ARG c5447 CLA c5498
SITE 3 OC6 15 GLU d5219 ASN d5220 ALA d5229 SER d5230
SITE 4 OC6 15 THR d5231 PHE d5232 SQD d5358
SITE 1 OC7 9 ASN a5267 SER a5270 PHE a5274 LHG a5567
SITE 2 OC7 9 GLU c5029 TRP c5036 SER d5230 PHE d5232
SITE 3 OC7 9 ARG d5233
SITE 1 OC8 14 PHE a5197 GLU c5083 GLN c5084 GLY c5085
SITE 2 OC8 14 SER c5406 ASN c5418 PHE c5419 VAL c5420
SITE 3 OC8 14 TRP c5425 THR c5428 UNK c5479 CLA c5494
SITE 4 OC8 14 DGD c5509 TYR j5033
SITE 1 OC9 20 GLN a5199 LEU a5200 PHE a5300 ASN a5301
SITE 2 OC9 20 SER a5305 CLA a5560 ASN c5405 VAL c5407
SITE 3 OC9 20 ASN c5415 SER c5416 ASN c5418 DGD c5508
SITE 4 OC9 20 MGE d5359 PHE j5029 ALA j5032 TYR j5033
SITE 5 OC9 20 GLY j5037 SER j5038 SER j5039 GLN v5060
SITE 1 PC1 12 CLA a5560 DGD c5509 TYR d5067 GLY d5070
SITE 2 PC1 12 CYS d5071 PHE d5073 CLA d5354 THR f5030
SITE 3 PC1 12 GLN f5041 GLY j5031 ALA j5032 GLY j5037
SITE 1 PC2 14 TYR b5193 PHE b5250 TYR b5258 TYR b5273
SITE 2 PC2 14 SER b5277 PHE b5463 HIS d5087 ILE d5123
SITE 3 PC2 14 LEU d5162 SER d5165 TYR h5049 VAL h5060
SITE 4 PC2 14 SER h5061 TRP h5062
SITE 1 PC3 12 TRP b5005 TYR b5006 ARG b5007 PHE b5464
SITE 2 PC3 12 TRP b5468 CLA b5521 CLA b5523 ARG d5139
SITE 3 PC3 12 TYR d5141 PHE d5269 PHE d5273 MGE l5210
SITE 1 PC4 14 SER a5232 ASN a5234 CLA a5559 TRP b5005
SITE 2 PC4 14 TYR b5006 CLA b5524 UNK c5474 TRP d5266
SITE 3 PC4 14 PHE d5270 PHE d5273 MGE d5360 GLU l5011
SITE 4 PC4 14 SER l5016 GLY l5020
SITE 1 PC5 16 CLA a5558 CLA a5559 ILE d5259 ALA d5260
SITE 2 PC5 16 PHE d5261 SER d5262 ASN d5263 TRP d5266
SITE 3 PC5 16 PHE d5270 ASN l5013 THR l5015 TYR l5018
SITE 4 PC5 16 LEU l5019 PHE t5010 PHE t5017 ALA t5020
SITE 1 PC6 8 TRP A 20 ASN A 26 ARG A 27 LEU A 28
SITE 2 PC6 8 BCR T5104 TRP b5113 TYR b5117 BCR b5529
SITE 1 PC7 8 ARG L 14 TYR L 18 LEU L 21 PHE T 19
SITE 2 PC7 8 PHE T 23 ARG b5018 LEU b5029 SER b5104
SITE 1 PC8 11 THR b5327 GLY b5328 PRO b5329 LYS b5332
SITE 2 PC8 11 PHE b5453 CLA b5517 BCR b5527 PHE l5035
SITE 3 PC8 11 LMT m 216 ASN m5004 LEU m5006
SITE 1 PC9 11 ALA B 43 LEU B 98 ILE a5050 LEU a5072
SITE 2 PC9 11 TYR a5073 UNK c5488 UNK c5489 ARG d5304
SITE 3 PC9 11 GLY o5139 GLU o5140 LMT t5217
SITE 1 QC1 9 TYR B 40 MGE B 530 GLN M 5 LEU M 6
SITE 2 QC1 9 LMT m 216 MET m5001 MET t5001 ILE t5004
SITE 3 QC1 9 LMT t5217
SITE 1 QC2 8 TYR B 40 ALA B 43 THR B 44 LMT M5216
SITE 2 QC2 8 LEU a5072 LMT a5568 MET t5001 ILE t5004
CRYST1 127.692 225.403 306.106 90.00 90.00 90.00 P 21 21 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 0.007831 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004436 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003267 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
