HEADER PHOTOSYNTHESIS 13-APR-14 4PBU
TITLE SERIAL TIME-RESOLVED CRYSTALLOGRAPHY OF PHOTOSYSTEM II USING A
TITLE 2 FEMTOSECOND X-RAY LASER THE S1 STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOTOSYSTEM Q(B) PROTEIN 1;
COMPND 3 CHAIN: A, a;
COMPND 4 SYNONYM: 32 KDA THYLAKOID MEMBRANE PROTEIN 1, PHOTOSYSTEM II PROTEIN
COMPND 5 D-1, PHOTOSYSTEM II D-1 PROTEIN;
COMPND 6 EC: 1.10.3.9;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PHOTOSYSTEM II CORE LIGHT HARVESTING PROTEIN;
COMPND 9 CHAIN: B, b;
COMPND 10 SYNONYM: PHOTOSYSTEM II CP47 PROTEIN;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: PHOTOSYSTEM II CP43 PROTEIN;
COMPND 13 CHAIN: C, c;
COMPND 14 MOL_ID: 4;
COMPND 15 MOLECULE: PHOTOSYSTEM II D2 PROTEIN;
COMPND 16 CHAIN: D, d;
COMPND 17 SYNONYM: PSII D2 PROTEIN, PHOTOSYSTEM Q(A) PROTEIN, PHOTOSYSTEM II D2
COMPND 18 PROTEIN;
COMPND 19 EC: 1.10.3.9;
COMPND 20 MOL_ID: 5;
COMPND 21 MOLECULE: CYTOCHROME B559 SUBUNIT ALPHA;
COMPND 22 CHAIN: E, e;
COMPND 23 SYNONYM: PSII REACTION CENTER SUBUNIT V;
COMPND 24 MOL_ID: 6;
COMPND 25 MOLECULE: CYTOCHROME B559 SUBUNIT BETA;
COMPND 26 CHAIN: F, f;
COMPND 27 SYNONYM: PSII REACTION CENTER SUBUNIT VI;
COMPND 28 MOL_ID: 7;
COMPND 29 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN H;
COMPND 30 CHAIN: H, h;
COMPND 31 SYNONYM: PSII-H;
COMPND 32 MOL_ID: 8;
COMPND 33 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN I;
COMPND 34 CHAIN: I, i;
COMPND 35 SYNONYM: PSII-I, PSII 4.4 KDA PROTEIN;
COMPND 36 MOL_ID: 9;
COMPND 37 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN J;
COMPND 38 CHAIN: J, j;
COMPND 39 SYNONYM: PSII-J;
COMPND 40 MOL_ID: 10;
COMPND 41 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN K;
COMPND 42 CHAIN: K, k;
COMPND 43 SYNONYM: PSII-K;
COMPND 44 MOL_ID: 11;
COMPND 45 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN L;
COMPND 46 CHAIN: L, l;
COMPND 47 SYNONYM: PSII-L, PSII 5 KDA PROTEIN;
COMPND 48 MOL_ID: 12;
COMPND 49 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN M;
COMPND 50 CHAIN: M, m;
COMPND 51 SYNONYM: PSII-M;
COMPND 52 MOL_ID: 13;
COMPND 53 MOLECULE: PHOTOSYSTEM II MANGANESE-STABILIZING POLYPEPTIDE;
COMPND 54 CHAIN: O, o;
COMPND 55 SYNONYM: MSP;
COMPND 56 MOL_ID: 14;
COMPND 57 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN T;
COMPND 58 CHAIN: T, t;
COMPND 59 SYNONYM: PSII-TC;
COMPND 60 MOL_ID: 15;
COMPND 61 MOLECULE: PHOTOSYSTEM II 12 KDA EXTRINSIC PROTEIN;
COMPND 62 CHAIN: U, u;
COMPND 63 SYNONYM: PS II COMPLEX 12 KDA EXTRINSIC PROTEIN,PSII-U;
COMPND 64 MOL_ID: 16;
COMPND 65 MOLECULE: CYTOCHROME C-550;
COMPND 66 CHAIN: V, v;
COMPND 67 SYNONYM: CYTOCHROME C-549, CYTOCHROME C550, LOW-POTENTIAL CYTOCHROME
COMPND 68 C;
COMPND 69 MOL_ID: 17;
COMPND 70 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN YCF12;
COMPND 71 CHAIN: Y, y;
COMPND 72 MOL_ID: 18;
COMPND 73 MOLECULE: PHOTOSYSTEM II REACTION CENTER X PROTEIN;
COMPND 74 CHAIN: X, x;
COMPND 75 MOL_ID: 19;
COMPND 76 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN Z;
COMPND 77 CHAIN: Z, z;
COMPND 78 SYNONYM: PSII-Z
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 3 ORGANISM_TAXID: 197221;
SOURCE 4 STRAIN: BP-1;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 7 ORGANISM_TAXID: 197221;
SOURCE 8 STRAIN: BP-1;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 11 ORGANISM_TAXID: 197221;
SOURCE 12 STRAIN: BP-1;
SOURCE 13 MOL_ID: 4;
SOURCE 14 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 15 ORGANISM_TAXID: 197221;
SOURCE 16 STRAIN: BP-1;
SOURCE 17 MOL_ID: 5;
SOURCE 18 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 19 ORGANISM_TAXID: 197221;
SOURCE 20 STRAIN: BP-1;
SOURCE 21 MOL_ID: 6;
SOURCE 22 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 23 ORGANISM_TAXID: 197221;
SOURCE 24 STRAIN: BP-1;
SOURCE 25 MOL_ID: 7;
SOURCE 26 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 27 ORGANISM_TAXID: 197221;
SOURCE 28 STRAIN: BP-1;
SOURCE 29 MOL_ID: 8;
SOURCE 30 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 31 ORGANISM_TAXID: 197221;
SOURCE 32 STRAIN: BP-1;
SOURCE 33 MOL_ID: 9;
SOURCE 34 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 35 ORGANISM_TAXID: 197221;
SOURCE 36 STRAIN: BP-1;
SOURCE 37 MOL_ID: 10;
SOURCE 38 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 39 ORGANISM_TAXID: 197221;
SOURCE 40 STRAIN: BP-1;
SOURCE 41 MOL_ID: 11;
SOURCE 42 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 43 ORGANISM_TAXID: 197221;
SOURCE 44 STRAIN: BP-1;
SOURCE 45 MOL_ID: 12;
SOURCE 46 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 47 ORGANISM_TAXID: 197221;
SOURCE 48 STRAIN: BP-1;
SOURCE 49 MOL_ID: 13;
SOURCE 50 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 51 ORGANISM_TAXID: 197221;
SOURCE 52 STRAIN: BP-1;
SOURCE 53 MOL_ID: 14;
SOURCE 54 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 55 ORGANISM_TAXID: 197221;
SOURCE 56 STRAIN: BP-1;
SOURCE 57 MOL_ID: 15;
SOURCE 58 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 59 ORGANISM_TAXID: 197221;
SOURCE 60 STRAIN: BP-1;
SOURCE 61 MOL_ID: 16;
SOURCE 62 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 63 ORGANISM_TAXID: 197221;
SOURCE 64 STRAIN: BP-1;
SOURCE 65 MOL_ID: 17;
SOURCE 66 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 67 ORGANISM_TAXID: 197221;
SOURCE 68 STRAIN: BP-1;
SOURCE 69 MOL_ID: 18;
SOURCE 70 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 71 ORGANISM_TAXID: 197221;
SOURCE 72 STRAIN: BP-1;
SOURCE 73 MOL_ID: 19;
SOURCE 74 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 75 ORGANISM_TAXID: 197221;
SOURCE 76 STRAIN: BP-1
KEYWDS PHOTOSYSTEM II, TIME RESOLVED, FREE ELECTRON LASER, PHOTOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR C.KUPITZ,S.BASU,I.GROTJOHANN,R.FROMME,N.ZATSEPIN,K.N.RENDEK,M.HUNTER,
AUTHOR 2 R.L.SHOEMAN,T.A.WHITE,D.WANG,D.JAMES,J.H.YANG,D.E.COBB,B.REEDER,
AUTHOR 3 R.G.SIERRA,H.LIU,A.BARTY,A.AQUILA,D.DEPONTE,R.A.KIRIAN,S.BARI,
AUTHOR 4 J.J.BERGKAMP,K.BEYERLEIN,M.J.BOGAN,C.CALEMAN,T.-C.CHAO,C.E.CONRAD,
AUTHOR 5 K.M.DAVIS,H.FLECKENSTEIN,L.GALLI,S.P.HAU-RIEGE,S.KASSEMEYER,
AUTHOR 6 H.LAKSMONO,M.LIANG,L.LOMB,S.MARCHESINI,A.V.MARTIN,M.MESSERSCHMIDT,
AUTHOR 7 D.MILATHIANAKI,K.NASS,A.ROS,S.ROY-CHOWDHURY,K.SCHMIDT,M.SEIBERT,
AUTHOR 8 J.STEINBRENER,F.STELLATO,L.YAN,C.YOON,T.A.MOORE,A.L.MOORE,Y.PUSHKAR,
AUTHOR 9 G.J.WILLIAMS,S.BOUTET,R.B.DOAK,U.WEIERSTALL,M.FRANK,H.N.CHAPMAN,
AUTHOR 10 J.C.H.SPENCE,P.FROMME
REVDAT 9 27-NOV-19 4PBU 1 REMARK
REVDAT 8 19-SEP-18 4PBU 1 REMARK
REVDAT 7 22-NOV-17 4PBU 1 REMARK
REVDAT 6 06-SEP-17 4PBU 1 REMARK
REVDAT 5 23-SEP-15 4PBU 1 REMARK
REVDAT 4 01-OCT-14 4PBU 1 JRNL
REVDAT 3 06-AUG-14 4PBU 1 AUTHOR
REVDAT 2 30-JUL-14 4PBU 1 JRNL
REVDAT 1 16-JUL-14 4PBU 0
JRNL AUTH C.KUPITZ,S.BASU,I.GROTJOHANN,R.FROMME,N.A.ZATSEPIN,
JRNL AUTH 2 K.N.RENDEK,M.S.HUNTER,R.L.SHOEMAN,T.A.WHITE,D.WANG,D.JAMES,
JRNL AUTH 3 J.H.YANG,D.E.COBB,B.REEDER,R.G.SIERRA,H.LIU,A.BARTY,
JRNL AUTH 4 A.L.AQUILA,D.DEPONTE,R.A.KIRIAN,S.BARI,J.J.BERGKAMP,
JRNL AUTH 5 K.R.BEYERLEIN,M.J.BOGAN,C.CALEMAN,T.C.CHAO,C.E.CONRAD,
JRNL AUTH 6 K.M.DAVIS,H.FLECKENSTEIN,L.GALLI,S.P.HAU-RIEGE,S.KASSEMEYER,
JRNL AUTH 7 H.LAKSMONO,M.LIANG,L.LOMB,S.MARCHESINI,A.V.MARTIN,
JRNL AUTH 8 M.MESSERSCHMIDT,D.MILATHIANAKI,K.NASS,A.ROS,S.ROY-CHOWDHURY,
JRNL AUTH 9 K.SCHMIDT,M.SEIBERT,J.STEINBRENER,F.STELLATO,L.YAN,C.YOON,
JRNL AUTH10 T.A.MOORE,A.L.MOORE,Y.PUSHKAR,G.J.WILLIAMS,S.BOUTET,
JRNL AUTH11 R.B.DOAK,U.WEIERSTALL,M.FRANK,H.N.CHAPMAN,J.C.SPENCE,
JRNL AUTH12 P.FROMME
JRNL TITL SERIAL TIME-RESOLVED CRYSTALLOGRAPHY OF PHOTOSYSTEM II USING
JRNL TITL 2 A FEMTOSECOND X-RAY LASER.
JRNL REF NATURE V. 513 261 2014
JRNL REFN ESSN 1476-4687
JRNL PMID 25043005
JRNL DOI 10.1038/NATURE13453
REMARK 2
REMARK 2 RESOLUTION. 5.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 5.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.64
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 40946
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.261
REMARK 3 R VALUE (WORKING SET) : 0.261
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 2056
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1100.6583 - 12.3240 1.00 2781 141 0.3308 0.3492
REMARK 3 2 12.3240 - 9.7846 1.00 2649 146 0.2021 0.2183
REMARK 3 3 9.7846 - 8.5485 1.00 2617 152 0.1916 0.1719
REMARK 3 4 8.5485 - 7.7672 1.00 2588 135 0.2071 0.2055
REMARK 3 5 7.7672 - 7.2107 1.00 2634 118 0.2360 0.2221
REMARK 3 6 7.2107 - 6.7856 1.00 2617 116 0.2407 0.2425
REMARK 3 7 6.7856 - 6.4459 1.00 2533 160 0.2454 0.2503
REMARK 3 8 6.4459 - 6.1653 1.00 2579 136 0.2601 0.2509
REMARK 3 9 6.1653 - 5.9280 1.00 2569 144 0.2766 0.2731
REMARK 3 10 5.9280 - 5.7235 1.00 2567 135 0.2859 0.2517
REMARK 3 11 5.7235 - 5.5445 1.00 2531 128 0.2959 0.2806
REMARK 3 12 5.5445 - 5.3860 1.00 2559 138 0.3080 0.2834
REMARK 3 13 5.3860 - 5.2442 1.00 2564 133 0.3120 0.2985
REMARK 3 14 5.2442 - 5.1163 1.00 2532 134 0.3246 0.3632
REMARK 3 15 5.1163 - 5.0000 1.00 2570 140 0.3502 0.3434
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.600
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.720
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 285.0
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.039 51301
REMARK 3 ANGLE : 3.029 70757
REMARK 3 CHIRALITY : 0.491 7125
REMARK 3 PLANARITY : 0.020 8628
REMARK 3 DIHEDRAL : 21.659 18204
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 19
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN A
REMARK 3 ATOM PAIRS NUMBER : 3021
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN B
REMARK 3 SELECTION : CHAIN B
REMARK 3 ATOM PAIRS NUMBER : 4445
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 3
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN C
REMARK 3 SELECTION : CHAIN C
REMARK 3 ATOM PAIRS NUMBER : 4054
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 4
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN D
REMARK 3 SELECTION : CHAIN D
REMARK 3 ATOM PAIRS NUMBER : 3154
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 5
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN E
REMARK 3 SELECTION : CHAIN E
REMARK 3 ATOM PAIRS NUMBER : 735
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 6
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN F
REMARK 3 SELECTION : CHAIN F
REMARK 3 ATOM PAIRS NUMBER : 290
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 7
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN H
REMARK 3 SELECTION : CHAIN H
REMARK 3 ATOM PAIRS NUMBER : 568
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 8
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN I
REMARK 3 SELECTION : CHAIN I
REMARK 3 ATOM PAIRS NUMBER : 342
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 9
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN J
REMARK 3 SELECTION : CHAIN J
REMARK 3 ATOM PAIRS NUMBER : 312
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 10
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN K
REMARK 3 SELECTION : CHAIN K
REMARK 3 ATOM PAIRS NUMBER : 336
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 11
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN L
REMARK 3 SELECTION : CHAIN L
REMARK 3 ATOM PAIRS NUMBER : 348
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 12
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN M
REMARK 3 SELECTION : CHAIN M
REMARK 3 ATOM PAIRS NUMBER : 302
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 13
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN O
REMARK 3 SELECTION : CHAIN O
REMARK 3 ATOM PAIRS NUMBER : 2194
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 14
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN T
REMARK 3 SELECTION : CHAIN T
REMARK 3 ATOM PAIRS NUMBER : 273
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 15
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN U
REMARK 3 SELECTION : CHAIN U
REMARK 3 ATOM PAIRS NUMBER : 930
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 16
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN V
REMARK 3 SELECTION : CHAIN V
REMARK 3 ATOM PAIRS NUMBER : 1264
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 17
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN X
REMARK 3 SELECTION : CHAIN X
REMARK 3 ATOM PAIRS NUMBER : 313
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 18
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN Y
REMARK 3 SELECTION : CHAIN Y
REMARK 3 ATOM PAIRS NUMBER : 251
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 19
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN Z
REMARK 3 SELECTION : CHAIN Z
REMARK 3 ATOM PAIRS NUMBER : 531
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4PBU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1000201052.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JAN-12
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : FREE ELECTRON LASER
REMARK 200 BEAMLINE : CXI
REMARK 200 X-RAY GENERATOR MODEL : SLAC LCLS BEAMLINE CXI
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 2.04
REMARK 200 MONOCHROMATOR : NONE
REMARK 200 OPTICS : SEVERAL DAYS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : CS-PAD CXI-2
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40964
REMARK 200 RESOLUTION RANGE HIGH (A) : 5.000
REMARK 200 RESOLUTION RANGE LOW (A) : 100.638
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 684.0
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 5.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 5.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 617.0
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3ARC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM PIPES PH 7.0, 5 MM CACL2, 10 MM
REMARK 280 TOCOPHEROL, AND 10-17% PEG 2000, LIQUID DIFFUSION, TEMPERATURE
REMARK 280 283K
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 66.62500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 153.54500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 113.13000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 153.54500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 66.62500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 113.13000
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: 38-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, Y, X, Z,
REMARK 350 AND CHAINS: a, b, c, d, e, f, h, i, j, k,
REMARK 350 AND CHAINS: l, m, o, t, u, v, y, x, z
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASN C 19
REMARK 465 SER C 20
REMARK 465 ILE C 21
REMARK 465 PHE C 22
REMARK 465 MET J 1
REMARK 465 MET J 2
REMARK 465 GLU d 11
REMARK 465 SER f 12
REMARK 465 TYR f 13
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 SG CYS V 37 CAB HEM V 202 2.03
REMARK 500 SG CYS V 40 CAC HEM V 202 2.03
REMARK 500 NZ LYS c 457 O GLU d 227 2.08
REMARK 500 SG CYS v 40 CAC HEM v 202 2.12
REMARK 500 SG CYS v 37 CAB HEM v 202 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O THR O 37 CG ASN c 19 2455 0.56
REMARK 500 O THR O 37 ND2 ASN c 19 2455 0.91
REMARK 500 NE2 GLN O 36 CA ASN c 19 2455 0.99
REMARK 500 N THR O 37 OD1 ASN c 19 2455 1.04
REMARK 500 NE2 GLN O 36 C ASN c 19 2455 1.05
REMARK 500 O SER O 35 OG SER c 20 2455 1.43
REMARK 500 NE2 GLN O 36 N ASN c 19 2455 1.56
REMARK 500 C THR O 37 OD1 ASN c 19 2455 1.59
REMARK 500 O THR O 37 CB ASN c 19 2455 1.60
REMARK 500 O THR O 37 OD1 ASN c 19 2455 1.73
REMARK 500 OE1 GLN O 36 N SER c 20 2455 1.77
REMARK 500 CA GLN O 36 CB SER c 20 2455 1.77
REMARK 500 CD GLN O 36 N ASN c 19 2455 1.89
REMARK 500 C GLN O 36 OD1 ASN c 19 2455 1.94
REMARK 500 CD GLN O 36 C ASN c 19 2455 1.97
REMARK 500 OE1 GLN O 36 O SER c 20 2455 2.03
REMARK 500 C SER O 35 OG SER c 20 2455 2.06
REMARK 500 CA THR O 37 CG ASN c 19 2455 2.09
REMARK 500 N TYR O 38 ND2 ASN c 19 2455 2.12
REMARK 500 OD2 ASP O 33 CA ALA c 23 2455 2.14
REMARK 500 OXT ALA O 246 CB ASN c 19 2455 2.14
REMARK 500 NE2 GLN O 36 CB ASN c 19 2455 2.17
REMARK 500 O SER O 35 CB SER c 20 2455 2.18
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 VAL A 30 -82.90 -93.24
REMARK 500 LEU A 159 -54.97 -124.71
REMARK 500 ILE A 259 -93.51 -101.21
REMARK 500 TYR B 117 55.86 -92.30
REMARK 500 ASP B 313 45.52 -93.51
REMARK 500 PHE B 383 -77.83 -86.85
REMARK 500 ASP C 107 114.00 -160.69
REMARK 500 GLU C 221 -65.05 -125.05
REMARK 500 TRP C 223 -137.61 46.74
REMARK 500 THR C 295 -60.12 -100.82
REMARK 500 SER C 416 -49.33 175.15
REMARK 500 ARG D 12 42.42 -156.08
REMARK 500 VAL D 30 -70.48 -107.17
REMARK 500 SER D 65 14.90 -148.63
REMARK 500 PRO D 140 44.95 -91.64
REMARK 500 ALA D 234 32.70 -77.87
REMARK 500 PRO D 309 1.78 -66.02
REMARK 500 ALA D 351 -52.26 71.42
REMARK 500 LYS H 63 31.95 -82.84
REMARK 500 LEU H 65 -88.06 -150.65
REMARK 500 LYS I 33 -119.87 -110.34
REMARK 500 SER J 39 -4.07 73.51
REMARK 500 ASN O 58 -3.58 149.42
REMARK 500 ARG O 73 -163.40 70.15
REMARK 500 THR O 138 8.18 -69.31
REMARK 500 ASN U 29 -37.10 -138.98
REMARK 500 TYR U 103 -144.13 -112.85
REMARK 500 ASN V 49 81.88 -158.76
REMARK 500 ASP V 67 36.37 -89.53
REMARK 500 PHE V 101 79.42 -116.65
REMARK 500 ASP X 35 68.47 -116.95
REMARK 500 VAL a 30 -82.54 -93.21
REMARK 500 LEU a 159 -51.87 -129.14
REMARK 500 ILE a 259 -93.41 -100.44
REMARK 500 TYR b 117 53.82 -97.25
REMARK 500 PHE b 162 81.66 -155.10
REMARK 500 ASP b 313 47.84 -92.88
REMARK 500 PHE b 383 -79.05 -85.83
REMARK 500 GLU b 485 50.74 -104.45
REMARK 500 LEU c 45 79.59 -118.73
REMARK 500 ASP c 107 115.56 -165.52
REMARK 500 GLU c 221 -69.01 -122.97
REMARK 500 TRP c 223 -140.99 51.01
REMARK 500 SER c 416 -48.89 169.61
REMARK 500 SER c 463 54.69 -143.92
REMARK 500 VAL d 30 -67.35 -105.41
REMARK 500 SER d 65 11.52 -141.44
REMARK 500 PRO d 140 44.42 -90.50
REMARK 500 ALA d 234 31.78 -78.14
REMARK 500 PRO d 309 2.78 -69.27
REMARK 500
REMARK 500 THIS ENTRY HAS 67 RAMACHANDRAN OUTLIERS.
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 LHG A 615
REMARK 610 DGD C 516
REMARK 610 DGD C 517
REMARK 610 DGD C 518
REMARK 610 DGD D 406
REMARK 610 SQD F 101
REMARK 610 DGD H 102
REMARK 610 LHG a 413
REMARK 610 DGD c 916
REMARK 610 DGD c 917
REMARK 610 DGD d 406
REMARK 610 SQD d 407
REMARK 610 DGD h 102
REMARK 610 DGD j 101
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 OEX A 601 MN4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 170 OD1
REMARK 620 2 OEX A 601 O5 99.7
REMARK 620 3 OEX A 601 O4 90.4 92.5
REMARK 620 4 GLU A 333 OE2 171.6 84.4 96.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX A 601 CA1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 170 OD2
REMARK 620 2 OEX A 601 O1 155.9
REMARK 620 3 OEX A 601 O2 84.6 75.2
REMARK 620 4 OEX A 601 O5 111.5 76.8 76.7
REMARK 620 5 ALA A 344 O 84.3 78.3 76.2 147.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX A 601 MN1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 189 OE2
REMARK 620 2 OEX A 601 O1 93.2
REMARK 620 3 OEX A 601 O5 96.4 82.4
REMARK 620 4 OEX A 601 O3 174.1 92.0 81.7
REMARK 620 5 HIS A 332 NE2 86.4 178.3 99.3 88.4
REMARK 620 6 ASP A 342 OD2 94.2 91.9 168.2 88.3 86.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 A 602 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 215 NE2
REMARK 620 2 HIS A 272 NE2 93.0
REMARK 620 3 HIS D 214 NE2 110.9 91.0
REMARK 620 4 HIS D 268 NE2 89.0 177.3 89.9
REMARK 620 5 BCT A 605 O3 155.9 92.3 92.4 85.1
REMARK 620 6 BCT A 605 O2 99.4 84.4 149.5 93.6 57.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX A 601 MN3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 333 OE1
REMARK 620 2 OEX A 601 O2 176.3
REMARK 620 3 OEX A 601 O3 88.7 93.2
REMARK 620 4 OEX A 601 O4 95.0 83.2 175.9
REMARK 620 5 OEX A 601 O5 91.1 92.3 81.5 96.6
REMARK 620 6 GLU C 354 OE2 87.7 89.2 86.1 95.9 167.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX A 601 MN2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 342 OD1
REMARK 620 2 OEX A 601 O1 90.2
REMARK 620 3 OEX A 601 O2 179.2 89.0
REMARK 620 4 OEX A 601 O3 93.3 78.9 86.8
REMARK 620 5 ALA A 344 OXT 90.1 94.4 89.7 172.5
REMARK 620 6 GLU C 354 OE1 93.7 168.2 87.1 89.8 96.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C 511 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C 39 OD1
REMARK 620 2 CLA C 511 NA 100.0
REMARK 620 3 CLA C 511 NB 102.4 87.7
REMARK 620 4 CLA C 511 NC 97.8 160.9 95.1
REMARK 620 5 CLA C 511 ND 98.8 90.5 158.7 80.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM E 101 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 23 NE2
REMARK 620 2 HEM E 101 NA 96.8
REMARK 620 3 HEM E 101 NB 100.1 88.7
REMARK 620 4 HEM E 101 NC 88.5 174.6 90.6
REMARK 620 5 HEM E 101 ND 79.6 93.0 178.3 87.7
REMARK 620 6 HIS F 24 NE2 174.0 83.4 85.8 91.3 94.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 102 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG F 45 O
REMARK 620 2 ARG F 45 OXT 43.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA O 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR O 138 O
REMARK 620 2 ASN O 200 OD1 149.7
REMARK 620 3 VAL O 201 O 78.6 75.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM V 202 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS V 41 NE2
REMARK 620 2 HEM V 202 NA 88.7
REMARK 620 3 HEM V 202 NB 87.3 91.4
REMARK 620 4 HEM V 202 NC 91.8 179.4 88.4
REMARK 620 5 HEM V 202 ND 91.2 88.5 178.5 91.8
REMARK 620 6 HIS V 92 NE2 177.7 93.3 91.5 86.2 90.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 401 MN4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP a 170 OD1
REMARK 620 2 OEX a 401 O5 108.8
REMARK 620 3 OEX a 401 O4 91.1 96.4
REMARK 620 4 GLU a 333 OE2 168.6 78.6 96.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 401 CA1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP a 170 OD2
REMARK 620 2 OEX a 401 O1 158.7
REMARK 620 3 OEX a 401 O2 85.2 75.8
REMARK 620 4 OEX a 401 O5 108.4 76.8 77.1
REMARK 620 5 ALA a 344 O 88.9 76.9 73.9 144.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 401 MN1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU a 189 OE2
REMARK 620 2 OEX a 401 O1 94.3
REMARK 620 3 OEX a 401 O5 97.6 92.9
REMARK 620 4 OEX a 401 O3 168.9 95.4 76.6
REMARK 620 5 HIS a 332 NE2 83.5 177.4 88.6 86.9
REMARK 620 6 ASP a 342 OD2 90.8 90.1 170.8 94.5 88.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 a 403 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS a 215 NE2
REMARK 620 2 HIS a 272 NE2 92.5
REMARK 620 3 HIS d 214 NE2 109.1 87.4
REMARK 620 4 HIS d 268 NE2 95.2 172.2 91.2
REMARK 620 5 BCT a 414 O2 106.9 84.2 143.4 92.5
REMARK 620 6 BCT a 414 O3 166.5 86.9 84.4 85.4 59.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 401 MN3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU a 333 OE1
REMARK 620 2 OEX a 401 O2 175.6
REMARK 620 3 OEX a 401 O3 90.8 90.9
REMARK 620 4 OEX a 401 O4 91.7 86.7 176.4
REMARK 620 5 OEX a 401 O5 86.5 97.8 78.7 98.8
REMARK 620 6 GLU c 354 OE2 89.1 87.0 86.6 96.1 164.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 401 MN2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP a 342 OD1
REMARK 620 2 OEX a 401 O1 87.5
REMARK 620 3 OEX a 401 O2 179.0 93.5
REMARK 620 4 OEX a 401 O3 95.4 80.3 84.7
REMARK 620 5 ALA a 344 OXT 88.1 95.8 91.8 174.6
REMARK 620 6 GLU c 354 OE1 91.0 167.8 88.0 87.8 96.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA c 901 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE c 22 O
REMARK 620 2 THR c 24 O 84.3
REMARK 620 3 ASP c 27 OD1 130.4 96.1
REMARK 620 4 ASP c 27 OD2 80.9 79.7 50.9
REMARK 620 5 GLU c 29 OE1 96.2 175.5 87.0 104.8
REMARK 620 6 SER c 30 OG 151.8 89.8 77.6 125.1 87.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA c 912 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN c 39 OD1
REMARK 620 2 CLA c 912 NA 108.1
REMARK 620 3 CLA c 912 NB 107.0 91.6
REMARK 620 4 CLA c 912 NC 94.5 154.9 91.8
REMARK 620 5 CLA c 912 ND 100.4 89.4 150.7 75.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM e 101 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS e 23 NE2
REMARK 620 2 HEM e 101 NA 100.7
REMARK 620 3 HEM e 101 NB 99.2 88.4
REMARK 620 4 HEM e 101 NC 84.8 174.5 91.0
REMARK 620 5 HEM e 101 ND 80.2 92.5 179.0 88.1
REMARK 620 6 HIS f 24 NE2 168.3 81.1 92.4 93.4 88.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA f 102 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG f 45 O
REMARK 620 2 ARG f 45 OXT 43.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG j 102 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY j 31 O
REMARK 620 2 ALA j 34 O 75.9
REMARK 620 3 LEU j 36 O 104.7 108.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA o 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR o 138 O
REMARK 620 2 ASN o 200 OD1 154.7
REMARK 620 3 VAL o 201 O 83.9 72.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM v 202 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS v 41 NE2
REMARK 620 2 HEM v 202 NA 94.3
REMARK 620 3 HEM v 202 NB 88.5 86.8
REMARK 620 4 HEM v 202 NC 86.6 179.1 93.5
REMARK 620 5 HEM v 202 ND 89.6 92.9 178.1 86.7
REMARK 620 6 HIS v 92 NE2 171.4 93.6 95.4 85.5 86.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OEX A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE2 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 A 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG A 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG B 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 D 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD D 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG D 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG D 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG D 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM E 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD F 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR H 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD H 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR K 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD L 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA O 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR T 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR T 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM V 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR Y 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OEX a 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD a 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE2 a 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR a 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 a 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD a 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO a 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG a 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT a 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA b 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG b 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA c 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 906
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 907
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 908
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 909
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 910
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 911
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 912
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 913
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 914
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 915
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 916
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 917
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 918
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO d 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 d 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD d 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD d 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG d 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG d 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG d 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM e 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR f 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA f 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR h 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD h 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD j 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG j 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR k 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR k 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD l 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA o 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM v 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand THR O 37 bound to ASN c
REMARK 800 19
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand THR O 37 bound to ASN c
REMARK 800 19
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand THR O 37 bound to ASN c
REMARK 800 19
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand GLN O 36 bound to SER c
REMARK 800 20
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand GLN O 36 bound to SER c
REMARK 800 20
DBREF 4PBU A 11 344 UNP P0A444 PSBA1_THEEB 11 344
DBREF 4PBU B 2 505 UNP Q8DIQ1 Q8DIQ1_THEEB 2 505
DBREF 4PBU C 19 473 UNP Q8DIF8 Q8DIF8_THEEB 7 461
DBREF 4PBU D 11 352 UNP Q8CM25 PSBD_THEEB 11 352
DBREF 4PBU E 4 84 UNP Q8DIP0 PSBE_THEEB 4 84
DBREF 4PBU F 12 45 UNP Q8DIN9 PSBF_THEEB 12 45
DBREF 4PBU H 2 66 UNP Q8DJ43 PSBH_THEEB 2 66
DBREF 4PBU I 1 38 UNP Q8DJZ6 PSBI_THEEB 1 38
DBREF 4PBU J 1 40 UNP P59087 PSBJ_THEEB 1 40
DBREF 4PBU K 10 46 UNP Q9F1K9 PSBK_THEEB 10 46
DBREF 4PBU L 1 37 UNP Q8DIN8 PSBL_THEEB 1 37
DBREF 4PBU M 1 34 UNP Q8DHA7 PSBM_THEEB 1 34
DBREF 4PBU O 4 246 UNP P0A431 PSBO_THEEB 30 272
DBREF 4PBU T 1 30 UNP Q8DIQ0 PSBT_THEEB 1 30
DBREF 4PBU U 8 104 UNP Q9F1L5 PSBU_THEEB 38 134
DBREF 4PBU V 1 137 UNP P0A386 CY550_THEEB 27 163
DBREF 4PBU Y 18 46 UNP Q8DJI1 YCF12_THEEB 18 46
DBREF 4PBU X 2 40 UNP Q9F1R6 PSBX_THEEB 2 40
DBREF 4PBU Z 1 62 UNP Q8DHJ2 PSBZ_THEEB 1 62
DBREF 4PBU a 11 344 UNP P0A444 PSBA1_THEEB 11 344
DBREF 4PBU b 2 505 UNP Q8DIQ1 Q8DIQ1_THEEB 2 505
DBREF 4PBU c 19 473 UNP Q8DIF8 Q8DIF8_THEEB 7 461
DBREF 4PBU d 11 352 UNP Q8CM25 PSBD_THEEB 11 352
DBREF 4PBU e 4 84 UNP Q8DIP0 PSBE_THEEB 4 84
DBREF 4PBU f 12 45 UNP Q8DIN9 PSBF_THEEB 12 45
DBREF 4PBU h 2 66 UNP Q8DJ43 PSBH_THEEB 2 66
DBREF 4PBU i 1 38 UNP Q8DJZ6 PSBI_THEEB 1 38
DBREF 4PBU j 1 40 UNP P59087 PSBJ_THEEB 1 40
DBREF 4PBU k 10 46 UNP Q9F1K9 PSBK_THEEB 10 46
DBREF 4PBU l 1 37 UNP Q8DIN8 PSBL_THEEB 1 37
DBREF 4PBU m 1 34 UNP Q8DHA7 PSBM_THEEB 1 34
DBREF 4PBU o 4 246 UNP P0A431 PSBO_THEEB 30 272
DBREF 4PBU t 1 30 UNP Q8DIQ0 PSBT_THEEB 1 30
DBREF 4PBU u 8 104 UNP Q9F1L5 PSBU_THEEB 38 134
DBREF 4PBU v 1 137 UNP P0A386 CY550_THEEB 27 163
DBREF 4PBU y 18 46 UNP Q8DJI1 YCF12_THEEB 18 46
DBREF 4PBU x 2 40 UNP Q9F1R6 PSBX_THEEB 2 40
DBREF 4PBU z 1 62 UNP Q8DHJ2 PSBZ_THEEB 1 62
SEQADV 4PBU ALA A 286 UNP P0A444 THR 286 CONFLICT
SEQADV 4PBU ALA a 286 UNP P0A444 THR 286 CONFLICT
SEQRES 1 A 334 ALA ASN LEU TRP GLU ARG PHE CYS ASN TRP VAL THR SER
SEQRES 2 A 334 THR ASP ASN ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE
SEQRES 3 A 334 MET ILE PRO THR LEU LEU ALA ALA THR ILE CYS PHE VAL
SEQRES 4 A 334 ILE ALA PHE ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY
SEQRES 5 A 334 ILE ARG GLU PRO VAL SER GLY SER LEU LEU TYR GLY ASN
SEQRES 6 A 334 ASN ILE ILE THR GLY ALA VAL VAL PRO SER SER ASN ALA
SEQRES 7 A 334 ILE GLY LEU HIS PHE TYR PRO ILE TRP GLU ALA ALA SER
SEQRES 8 A 334 LEU ASP GLU TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU
SEQRES 9 A 334 ILE ILE PHE HIS PHE LEU LEU GLY ALA SER CYS TYR MET
SEQRES 10 A 334 GLY ARG GLN TRP GLU LEU SER TYR ARG LEU GLY MET ARG
SEQRES 11 A 334 PRO TRP ILE CYS VAL ALA TYR SER ALA PRO LEU ALA SER
SEQRES 12 A 334 ALA PHE ALA VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY
SEQRES 13 A 334 SER PHE SER ASP GLY MET PRO LEU GLY ILE SER GLY THR
SEQRES 14 A 334 PHE ASN PHE MET ILE VAL PHE GLN ALA GLU HIS ASN ILE
SEQRES 15 A 334 LEU MET HIS PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL
SEQRES 16 A 334 PHE GLY GLY ALA LEU PHE CYS ALA MET HIS GLY SER LEU
SEQRES 17 A 334 VAL THR SER SER LEU ILE ARG GLU THR THR GLU THR GLU
SEQRES 18 A 334 SER ALA ASN TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU
SEQRES 19 A 334 THR TYR ASN ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG
SEQRES 20 A 334 LEU ILE PHE GLN TYR ALA SER PHE ASN ASN SER ARG SER
SEQRES 21 A 334 LEU HIS PHE PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL
SEQRES 22 A 334 TRP PHE ALA ALA LEU GLY ILE SER THR MET ALA PHE ASN
SEQRES 23 A 334 LEU ASN GLY PHE ASN PHE ASN HIS SER VAL ILE ASP ALA
SEQRES 24 A 334 LYS GLY ASN VAL ILE ASN THR TRP ALA ASP ILE ILE ASN
SEQRES 25 A 334 ARG ALA ASN LEU GLY MET GLU VAL MET HIS GLU ARG ASN
SEQRES 26 A 334 ALA HIS ASN PHE PRO LEU ASP LEU ALA
SEQRES 1 B 504 GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE ASN
SEQRES 2 B 504 ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS THR
SEQRES 3 B 504 ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU TYR
SEQRES 4 B 504 GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU ASN
SEQRES 5 B 504 PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE MET
SEQRES 6 B 504 ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP SER
SEQRES 7 B 504 ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP SER
SEQRES 8 B 504 PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER GLY
SEQRES 9 B 504 LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR TRP
SEQRES 10 B 504 ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU PRO
SEQRES 11 B 504 ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU PHE
SEQRES 12 B 504 LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE HIS
SEQRES 13 B 504 LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER ASP
SEQRES 14 B 504 PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA PRO
SEQRES 15 B 504 GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO GLY
SEQRES 16 B 504 GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL GLY
SEQRES 17 B 504 ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO PRO
SEQRES 18 B 504 GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE GLU
SEQRES 19 B 504 THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE ALA
SEQRES 20 B 504 ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER ALA
SEQRES 21 B 504 THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR GLN
SEQRES 22 B 504 TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG ARG
SEQRES 23 B 504 VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU GLU
SEQRES 24 B 504 ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR ASP
SEQRES 25 B 504 TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE ARG
SEQRES 26 B 504 THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN ALA
SEQRES 27 B 504 TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY GLU
SEQRES 28 B 504 GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU SER
SEQRES 29 B 504 PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL LYS
SEQRES 30 B 504 ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR SER
SEQRES 31 B 504 PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY GLY
SEQRES 32 B 504 GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR VAL
SEQRES 33 B 504 LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE PHE
SEQRES 34 B 504 GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE PHE
SEQRES 35 B 504 ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS ALA
SEQRES 36 B 504 VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP HIS
SEQRES 37 B 504 GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY ILE
SEQRES 38 B 504 ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY PHE
SEQRES 39 B 504 TYR GLN LYS VAL GLY ASP VAL THR THR ARG
SEQRES 1 C 455 ASN SER ILE PHE ALA THR ASN ARG ASP GLN GLU SER SER
SEQRES 2 C 455 GLY PHE ALA TRP TRP ALA GLY ASN ALA ARG LEU ILE ASN
SEQRES 3 C 455 LEU SER GLY LYS LEU LEU GLY ALA HIS VAL ALA HIS ALA
SEQRES 4 C 455 GLY LEU ILE VAL PHE TRP ALA GLY ALA MET THR LEU PHE
SEQRES 5 C 455 GLU LEU ALA HIS PHE ILE PRO GLU LYS PRO MET TYR GLU
SEQRES 6 C 455 GLN GLY LEU ILE LEU ILE PRO HIS ILE ALA THR LEU GLY
SEQRES 7 C 455 TRP GLY VAL GLY PRO GLY GLY GLU VAL VAL ASP THR PHE
SEQRES 8 C 455 PRO PHE PHE VAL VAL GLY VAL VAL HIS LEU ILE SER SER
SEQRES 9 C 455 ALA VAL LEU GLY PHE GLY GLY VAL TYR HIS ALA ILE ARG
SEQRES 10 C 455 GLY PRO GLU THR LEU GLU GLU TYR SER SER PHE PHE GLY
SEQRES 11 C 455 TYR ASP TRP LYS ASP LYS ASN LYS MET THR THR ILE LEU
SEQRES 12 C 455 GLY PHE HIS LEU ILE VAL LEU GLY ILE GLY ALA LEU LEU
SEQRES 13 C 455 LEU VAL ALA LYS ALA MET PHE PHE GLY GLY LEU TYR ASP
SEQRES 14 C 455 THR TRP ALA PRO GLY GLY GLY ASP VAL ARG VAL ILE THR
SEQRES 15 C 455 ASN PRO THR LEU ASP PRO ARG VAL ILE PHE GLY TYR LEU
SEQRES 16 C 455 LEU LYS SER PRO PHE GLY GLY GLU GLY TRP ILE VAL SER
SEQRES 17 C 455 VAL ASN ASN LEU GLU ASP VAL VAL GLY GLY HIS ILE TRP
SEQRES 18 C 455 ILE GLY LEU ILE CYS ILE ALA GLY GLY ILE TRP HIS ILE
SEQRES 19 C 455 LEU THR THR PRO PHE GLY TRP ALA ARG ARG ALA PHE ILE
SEQRES 20 C 455 TRP SER GLY GLU ALA TYR LEU SER TYR SER LEU GLY ALA
SEQRES 21 C 455 LEU SER MET MET GLY PHE ILE ALA THR CYS PHE VAL TRP
SEQRES 22 C 455 PHE ASN ASN THR VAL TYR PRO SER GLU PHE TYR GLY PRO
SEQRES 23 C 455 THR GLY PRO GLU ALA SER GLN ALA GLN ALA MET THR PHE
SEQRES 24 C 455 LEU ILE ARG ASP GLN LYS LEU GLY ALA ASN VAL GLY SER
SEQRES 25 C 455 ALA GLN GLY PRO THR GLY LEU GLY LYS TYR LEU MET ARG
SEQRES 26 C 455 SER PRO THR GLY GLU ILE ILE PHE GLY GLY GLU THR MET
SEQRES 27 C 455 ARG PHE TRP ASP PHE ARG GLY PRO TRP LEU GLU PRO LEU
SEQRES 28 C 455 ARG GLY PRO ASN GLY LEU ASP LEU ASN LYS ILE LYS ASN
SEQRES 29 C 455 ASP ILE GLN PRO TRP GLN GLU ARG ARG ALA ALA GLU TYR
SEQRES 30 C 455 MET THR HIS ALA PRO LEU GLY SER LEU ASN SER VAL GLY
SEQRES 31 C 455 GLY VAL ALA THR GLU ILE ASN SER VAL ASN PHE VAL SER
SEQRES 32 C 455 PRO ARG SER TRP LEU ALA THR SER HIS PHE VAL LEU ALA
SEQRES 33 C 455 PHE PHE PHE LEU VAL GLY HIS LEU TRP HIS ALA GLY ARG
SEQRES 34 C 455 ALA ARG ALA ALA ALA ALA GLY PHE GLU LYS GLY ILE ASP
SEQRES 35 C 455 ARG GLU SER GLU PRO VAL LEU SER MET PRO SER LEU ASP
SEQRES 1 D 342 GLU ARG GLY TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS
SEQRES 2 D 342 ARG ASP ARG PHE VAL PHE VAL GLY TRP SER GLY ILE LEU
SEQRES 3 D 342 LEU PHE PRO CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU
SEQRES 4 D 342 THR GLY THR THR PHE VAL THR SER TRP TYR THR HIS GLY
SEQRES 5 D 342 LEU ALA SER SER TYR LEU GLU GLY CYS ASN PHE LEU THR
SEQRES 6 D 342 VAL ALA VAL SER THR PRO ALA ASN SER MET GLY HIS SER
SEQRES 7 D 342 LEU LEU LEU LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE
SEQRES 8 D 342 THR ARG TRP CYS GLN LEU GLY GLY LEU TRP THR PHE ILE
SEQRES 9 D 342 ALA LEU HIS GLY ALA PHE GLY LEU ILE GLY PHE MET LEU
SEQRES 10 D 342 ARG GLN PHE GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO
SEQRES 11 D 342 TYR ASN ALA ILE ALA PHE SER ALA PRO ILE ALA VAL PHE
SEQRES 12 D 342 VAL SER VAL PHE LEU ILE TYR PRO LEU GLY GLN SER SER
SEQRES 13 D 342 TRP PHE PHE ALA PRO SER PHE GLY VAL ALA ALA ILE PHE
SEQRES 14 D 342 ARG PHE LEU LEU PHE PHE GLN GLY PHE HIS ASN TRP THR
SEQRES 15 D 342 LEU ASN PRO PHE HIS MET MET GLY VAL ALA GLY VAL LEU
SEQRES 16 D 342 GLY GLY ALA LEU LEU CYS ALA ILE HIS GLY ALA THR VAL
SEQRES 17 D 342 GLU ASN THR LEU PHE GLN ASP GLY GLU GLY ALA SER THR
SEQRES 18 D 342 PHE ARG ALA PHE ASN PRO THR GLN ALA GLU GLU THR TYR
SEQRES 19 D 342 SER MET VAL THR ALA ASN ARG PHE TRP SER GLN ILE PHE
SEQRES 20 D 342 GLY ILE ALA PHE SER ASN LYS ARG TRP LEU HIS PHE PHE
SEQRES 21 D 342 MET LEU PHE VAL PRO VAL THR GLY LEU TRP MET SER ALA
SEQRES 22 D 342 ILE GLY VAL VAL GLY LEU ALA LEU ASN LEU ARG SER TYR
SEQRES 23 D 342 ASP PHE ILE SER GLN GLU ILE ARG ALA ALA GLU ASP PRO
SEQRES 24 D 342 GLU PHE GLU THR PHE TYR THR LYS ASN LEU LEU LEU ASN
SEQRES 25 D 342 GLU GLY ILE ARG ALA TRP MET ALA PRO GLN ASP GLN PRO
SEQRES 26 D 342 HIS GLU ASN PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG
SEQRES 27 D 342 GLY ASN ALA LEU
SEQRES 1 E 81 THR THR GLY GLU ARG PRO PHE SER ASP ILE ILE THR SER
SEQRES 2 E 81 VAL ARG TYR TRP VAL ILE HIS SER ILE THR ILE PRO ALA
SEQRES 3 E 81 LEU PHE ILE ALA GLY TRP LEU PHE VAL SER THR GLY LEU
SEQRES 4 E 81 ALA TYR ASP VAL PHE GLY THR PRO ARG PRO ASP SER TYR
SEQRES 5 E 81 TYR ALA GLN GLU GLN ARG SER ILE PRO LEU VAL THR ASP
SEQRES 6 E 81 ARG PHE GLU ALA LYS GLN GLN VAL GLU THR PHE LEU GLU
SEQRES 7 E 81 GLN LEU LYS
SEQRES 1 F 34 SER TYR PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS
SEQRES 2 F 34 THR LEU ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE
SEQRES 3 F 34 ALA ALA MET GLN PHE ILE GLN ARG
SEQRES 1 H 65 ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO LEU
SEQRES 2 H 65 ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY THR
SEQRES 3 H 65 THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU VAL
SEQRES 4 H 65 PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR LEU
SEQRES 5 H 65 ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU GLY
SEQRES 1 I 38 MET GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR
SEQRES 2 I 38 PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY
SEQRES 3 I 38 ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP LEU GLU
SEQRES 1 J 40 MET MET SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL
SEQRES 2 J 40 ALA THR VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY
SEQRES 3 J 40 LEU PHE PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER
SEQRES 4 J 40 LEU
SEQRES 1 K 37 LYS LEU PRO GLU ALA TYR ALA ILE PHE ASP PRO LEU VAL
SEQRES 2 K 37 ASP VAL LEU PRO VAL ILE PRO VAL LEU PHE LEU ALA LEU
SEQRES 3 K 37 ALA PHE VAL TRP GLN ALA ALA VAL GLY PHE ARG
SEQRES 1 L 37 MET GLU PRO ASN PRO ASN ARG GLN PRO VAL GLU LEU ASN
SEQRES 2 L 37 ARG THR SER LEU TYR LEU GLY LEU LEU LEU ILE LEU VAL
SEQRES 3 L 37 LEU ALA LEU LEU PHE SER SER TYR PHE PHE ASN
SEQRES 1 M 34 MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU
SEQRES 2 M 34 PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR
SEQRES 3 M 34 VAL GLN THR GLU SER GLN GLN LYS
SEQRES 1 O 243 THR LEU THR TYR ASP ASP ILE VAL GLY THR GLY LEU ALA
SEQRES 2 O 243 ASN LYS CYS PRO THR LEU ASP ASP THR ALA ARG GLY ALA
SEQRES 3 O 243 TYR PRO ILE ASP SER SER GLN THR TYR ARG ILE ALA ARG
SEQRES 4 O 243 LEU CYS LEU GLN PRO THR THR PHE LEU VAL LYS GLU GLU
SEQRES 5 O 243 PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE VAL PRO THR
SEQRES 6 O 243 LYS LEU VAL THR ARG GLU THR THR SER LEU ASP GLN ILE
SEQRES 7 O 243 GLN GLY GLU LEU LYS VAL ASN SER ASP GLY SER LEU THR
SEQRES 8 O 243 PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN PRO VAL THR
SEQRES 9 O 243 VAL GLN MET ALA GLY GLY GLU ARG ILE PRO LEU LEU PHE
SEQRES 10 O 243 THR VAL LYS ASN LEU VAL ALA SER THR GLN PRO ASN VAL
SEQRES 11 O 243 THR SER ILE THR THR SER THR ASP PHE LYS GLY GLU PHE
SEQRES 12 O 243 ASN VAL PRO SER TYR ARG THR ALA ASN PHE LEU ASP PRO
SEQRES 13 O 243 LYS GLY ARG GLY LEU ALA SER GLY TYR ASP SER ALA ILE
SEQRES 14 O 243 ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU ALA ARG ALA
SEQRES 15 O 243 ASN VAL LYS ARG PHE SER LEU THR LYS GLY GLN ILE SER
SEQRES 16 O 243 LEU ASN VAL ALA LYS VAL ASP GLY ARG THR GLY GLU ILE
SEQRES 17 O 243 ALA GLY THR PHE GLU SER GLU GLN LEU SER ASP ASP ASP
SEQRES 18 O 243 MET GLY ALA HIS GLU PRO HIS GLU VAL LYS ILE GLN GLY
SEQRES 19 O 243 VAL PHE TYR ALA SER ILE GLU PRO ALA
SEQRES 1 T 30 MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE
SEQRES 2 T 30 ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO
SEQRES 3 T 30 PRO ARG ILE THR
SEQRES 1 U 97 GLU LEU VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA
SEQRES 2 U 97 TYR GLY GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA
SEQRES 3 U 97 ALA PHE ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA
SEQRES 4 U 97 LYS LEU ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU
SEQRES 5 U 97 ASP VAL LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS
SEQRES 6 U 97 GLN ILE LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR
SEQRES 7 U 97 GLU VAL GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR
SEQRES 8 U 97 ASN ASN GLY LEU TYR LYS
SEQRES 1 V 137 ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN
SEQRES 2 V 137 SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR
SEQRES 3 V 137 LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER
SEQRES 4 V 137 CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU
SEQRES 5 V 137 ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO
SEQRES 6 V 137 ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN
SEQRES 7 V 137 PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL
SEQRES 8 V 137 HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET
SEQRES 9 V 137 ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY
SEQRES 10 V 137 HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP
SEQRES 11 V 137 GLY GLY GLY LYS VAL TYR TYR
SEQRES 1 Y 29 VAL ILE ALA GLN LEU THR MET ILE ALA MET ILE GLY ILE
SEQRES 2 Y 29 ALA GLY PRO MET ILE ILE PHE LEU LEU ALA VAL ARG ARG
SEQRES 3 Y 29 GLY ASN LEU
SEQRES 1 X 39 THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY LEU
SEQRES 2 X 39 LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA VAL
SEQRES 3 X 39 LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG SER
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 334 ALA ASN LEU TRP GLU ARG PHE CYS ASN TRP VAL THR SER
SEQRES 2 a 334 THR ASP ASN ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE
SEQRES 3 a 334 MET ILE PRO THR LEU LEU ALA ALA THR ILE CYS PHE VAL
SEQRES 4 a 334 ILE ALA PHE ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY
SEQRES 5 a 334 ILE ARG GLU PRO VAL SER GLY SER LEU LEU TYR GLY ASN
SEQRES 6 a 334 ASN ILE ILE THR GLY ALA VAL VAL PRO SER SER ASN ALA
SEQRES 7 a 334 ILE GLY LEU HIS PHE TYR PRO ILE TRP GLU ALA ALA SER
SEQRES 8 a 334 LEU ASP GLU TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU
SEQRES 9 a 334 ILE ILE PHE HIS PHE LEU LEU GLY ALA SER CYS TYR MET
SEQRES 10 a 334 GLY ARG GLN TRP GLU LEU SER TYR ARG LEU GLY MET ARG
SEQRES 11 a 334 PRO TRP ILE CYS VAL ALA TYR SER ALA PRO LEU ALA SER
SEQRES 12 a 334 ALA PHE ALA VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY
SEQRES 13 a 334 SER PHE SER ASP GLY MET PRO LEU GLY ILE SER GLY THR
SEQRES 14 a 334 PHE ASN PHE MET ILE VAL PHE GLN ALA GLU HIS ASN ILE
SEQRES 15 a 334 LEU MET HIS PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL
SEQRES 16 a 334 PHE GLY GLY ALA LEU PHE CYS ALA MET HIS GLY SER LEU
SEQRES 17 a 334 VAL THR SER SER LEU ILE ARG GLU THR THR GLU THR GLU
SEQRES 18 a 334 SER ALA ASN TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU
SEQRES 19 a 334 THR TYR ASN ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG
SEQRES 20 a 334 LEU ILE PHE GLN TYR ALA SER PHE ASN ASN SER ARG SER
SEQRES 21 a 334 LEU HIS PHE PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL
SEQRES 22 a 334 TRP PHE ALA ALA LEU GLY ILE SER THR MET ALA PHE ASN
SEQRES 23 a 334 LEU ASN GLY PHE ASN PHE ASN HIS SER VAL ILE ASP ALA
SEQRES 24 a 334 LYS GLY ASN VAL ILE ASN THR TRP ALA ASP ILE ILE ASN
SEQRES 25 a 334 ARG ALA ASN LEU GLY MET GLU VAL MET HIS GLU ARG ASN
SEQRES 26 a 334 ALA HIS ASN PHE PRO LEU ASP LEU ALA
SEQRES 1 b 504 GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE ASN
SEQRES 2 b 504 ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS THR
SEQRES 3 b 504 ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU TYR
SEQRES 4 b 504 GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU ASN
SEQRES 5 b 504 PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE MET
SEQRES 6 b 504 ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP SER
SEQRES 7 b 504 ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP SER
SEQRES 8 b 504 PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER GLY
SEQRES 9 b 504 LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR TRP
SEQRES 10 b 504 ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU PRO
SEQRES 11 b 504 ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU PHE
SEQRES 12 b 504 LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE HIS
SEQRES 13 b 504 LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER ASP
SEQRES 14 b 504 PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA PRO
SEQRES 15 b 504 GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO GLY
SEQRES 16 b 504 GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL GLY
SEQRES 17 b 504 ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO PRO
SEQRES 18 b 504 GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE GLU
SEQRES 19 b 504 THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE ALA
SEQRES 20 b 504 ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER ALA
SEQRES 21 b 504 THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR GLN
SEQRES 22 b 504 TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG ARG
SEQRES 23 b 504 VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU GLU
SEQRES 24 b 504 ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR ASP
SEQRES 25 b 504 TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE ARG
SEQRES 26 b 504 THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN ALA
SEQRES 27 b 504 TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY GLU
SEQRES 28 b 504 GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU SER
SEQRES 29 b 504 PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL LYS
SEQRES 30 b 504 ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR SER
SEQRES 31 b 504 PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY GLY
SEQRES 32 b 504 GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR VAL
SEQRES 33 b 504 LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE PHE
SEQRES 34 b 504 GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE PHE
SEQRES 35 b 504 ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS ALA
SEQRES 36 b 504 VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP HIS
SEQRES 37 b 504 GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY ILE
SEQRES 38 b 504 ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY PHE
SEQRES 39 b 504 TYR GLN LYS VAL GLY ASP VAL THR THR ARG
SEQRES 1 c 455 ASN SER ILE PHE ALA THR ASN ARG ASP GLN GLU SER SER
SEQRES 2 c 455 GLY PHE ALA TRP TRP ALA GLY ASN ALA ARG LEU ILE ASN
SEQRES 3 c 455 LEU SER GLY LYS LEU LEU GLY ALA HIS VAL ALA HIS ALA
SEQRES 4 c 455 GLY LEU ILE VAL PHE TRP ALA GLY ALA MET THR LEU PHE
SEQRES 5 c 455 GLU LEU ALA HIS PHE ILE PRO GLU LYS PRO MET TYR GLU
SEQRES 6 c 455 GLN GLY LEU ILE LEU ILE PRO HIS ILE ALA THR LEU GLY
SEQRES 7 c 455 TRP GLY VAL GLY PRO GLY GLY GLU VAL VAL ASP THR PHE
SEQRES 8 c 455 PRO PHE PHE VAL VAL GLY VAL VAL HIS LEU ILE SER SER
SEQRES 9 c 455 ALA VAL LEU GLY PHE GLY GLY VAL TYR HIS ALA ILE ARG
SEQRES 10 c 455 GLY PRO GLU THR LEU GLU GLU TYR SER SER PHE PHE GLY
SEQRES 11 c 455 TYR ASP TRP LYS ASP LYS ASN LYS MET THR THR ILE LEU
SEQRES 12 c 455 GLY PHE HIS LEU ILE VAL LEU GLY ILE GLY ALA LEU LEU
SEQRES 13 c 455 LEU VAL ALA LYS ALA MET PHE PHE GLY GLY LEU TYR ASP
SEQRES 14 c 455 THR TRP ALA PRO GLY GLY GLY ASP VAL ARG VAL ILE THR
SEQRES 15 c 455 ASN PRO THR LEU ASP PRO ARG VAL ILE PHE GLY TYR LEU
SEQRES 16 c 455 LEU LYS SER PRO PHE GLY GLY GLU GLY TRP ILE VAL SER
SEQRES 17 c 455 VAL ASN ASN LEU GLU ASP VAL VAL GLY GLY HIS ILE TRP
SEQRES 18 c 455 ILE GLY LEU ILE CYS ILE ALA GLY GLY ILE TRP HIS ILE
SEQRES 19 c 455 LEU THR THR PRO PHE GLY TRP ALA ARG ARG ALA PHE ILE
SEQRES 20 c 455 TRP SER GLY GLU ALA TYR LEU SER TYR SER LEU GLY ALA
SEQRES 21 c 455 LEU SER MET MET GLY PHE ILE ALA THR CYS PHE VAL TRP
SEQRES 22 c 455 PHE ASN ASN THR VAL TYR PRO SER GLU PHE TYR GLY PRO
SEQRES 23 c 455 THR GLY PRO GLU ALA SER GLN ALA GLN ALA MET THR PHE
SEQRES 24 c 455 LEU ILE ARG ASP GLN LYS LEU GLY ALA ASN VAL GLY SER
SEQRES 25 c 455 ALA GLN GLY PRO THR GLY LEU GLY LYS TYR LEU MET ARG
SEQRES 26 c 455 SER PRO THR GLY GLU ILE ILE PHE GLY GLY GLU THR MET
SEQRES 27 c 455 ARG PHE TRP ASP PHE ARG GLY PRO TRP LEU GLU PRO LEU
SEQRES 28 c 455 ARG GLY PRO ASN GLY LEU ASP LEU ASN LYS ILE LYS ASN
SEQRES 29 c 455 ASP ILE GLN PRO TRP GLN GLU ARG ARG ALA ALA GLU TYR
SEQRES 30 c 455 MET THR HIS ALA PRO LEU GLY SER LEU ASN SER VAL GLY
SEQRES 31 c 455 GLY VAL ALA THR GLU ILE ASN SER VAL ASN PHE VAL SER
SEQRES 32 c 455 PRO ARG SER TRP LEU ALA THR SER HIS PHE VAL LEU ALA
SEQRES 33 c 455 PHE PHE PHE LEU VAL GLY HIS LEU TRP HIS ALA GLY ARG
SEQRES 34 c 455 ALA ARG ALA ALA ALA ALA GLY PHE GLU LYS GLY ILE ASP
SEQRES 35 c 455 ARG GLU SER GLU PRO VAL LEU SER MET PRO SER LEU ASP
SEQRES 1 d 342 GLU ARG GLY TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS
SEQRES 2 d 342 ARG ASP ARG PHE VAL PHE VAL GLY TRP SER GLY ILE LEU
SEQRES 3 d 342 LEU PHE PRO CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU
SEQRES 4 d 342 THR GLY THR THR PHE VAL THR SER TRP TYR THR HIS GLY
SEQRES 5 d 342 LEU ALA SER SER TYR LEU GLU GLY CYS ASN PHE LEU THR
SEQRES 6 d 342 VAL ALA VAL SER THR PRO ALA ASN SER MET GLY HIS SER
SEQRES 7 d 342 LEU LEU LEU LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE
SEQRES 8 d 342 THR ARG TRP CYS GLN LEU GLY GLY LEU TRP THR PHE ILE
SEQRES 9 d 342 ALA LEU HIS GLY ALA PHE GLY LEU ILE GLY PHE MET LEU
SEQRES 10 d 342 ARG GLN PHE GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO
SEQRES 11 d 342 TYR ASN ALA ILE ALA PHE SER ALA PRO ILE ALA VAL PHE
SEQRES 12 d 342 VAL SER VAL PHE LEU ILE TYR PRO LEU GLY GLN SER SER
SEQRES 13 d 342 TRP PHE PHE ALA PRO SER PHE GLY VAL ALA ALA ILE PHE
SEQRES 14 d 342 ARG PHE LEU LEU PHE PHE GLN GLY PHE HIS ASN TRP THR
SEQRES 15 d 342 LEU ASN PRO PHE HIS MET MET GLY VAL ALA GLY VAL LEU
SEQRES 16 d 342 GLY GLY ALA LEU LEU CYS ALA ILE HIS GLY ALA THR VAL
SEQRES 17 d 342 GLU ASN THR LEU PHE GLN ASP GLY GLU GLY ALA SER THR
SEQRES 18 d 342 PHE ARG ALA PHE ASN PRO THR GLN ALA GLU GLU THR TYR
SEQRES 19 d 342 SER MET VAL THR ALA ASN ARG PHE TRP SER GLN ILE PHE
SEQRES 20 d 342 GLY ILE ALA PHE SER ASN LYS ARG TRP LEU HIS PHE PHE
SEQRES 21 d 342 MET LEU PHE VAL PRO VAL THR GLY LEU TRP MET SER ALA
SEQRES 22 d 342 ILE GLY VAL VAL GLY LEU ALA LEU ASN LEU ARG SER TYR
SEQRES 23 d 342 ASP PHE ILE SER GLN GLU ILE ARG ALA ALA GLU ASP PRO
SEQRES 24 d 342 GLU PHE GLU THR PHE TYR THR LYS ASN LEU LEU LEU ASN
SEQRES 25 d 342 GLU GLY ILE ARG ALA TRP MET ALA PRO GLN ASP GLN PRO
SEQRES 26 d 342 HIS GLU ASN PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG
SEQRES 27 d 342 GLY ASN ALA LEU
SEQRES 1 e 81 THR THR GLY GLU ARG PRO PHE SER ASP ILE ILE THR SER
SEQRES 2 e 81 VAL ARG TYR TRP VAL ILE HIS SER ILE THR ILE PRO ALA
SEQRES 3 e 81 LEU PHE ILE ALA GLY TRP LEU PHE VAL SER THR GLY LEU
SEQRES 4 e 81 ALA TYR ASP VAL PHE GLY THR PRO ARG PRO ASP SER TYR
SEQRES 5 e 81 TYR ALA GLN GLU GLN ARG SER ILE PRO LEU VAL THR ASP
SEQRES 6 e 81 ARG PHE GLU ALA LYS GLN GLN VAL GLU THR PHE LEU GLU
SEQRES 7 e 81 GLN LEU LYS
SEQRES 1 f 34 SER TYR PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS
SEQRES 2 f 34 THR LEU ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE
SEQRES 3 f 34 ALA ALA MET GLN PHE ILE GLN ARG
SEQRES 1 h 65 ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO LEU
SEQRES 2 h 65 ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY THR
SEQRES 3 h 65 THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU VAL
SEQRES 4 h 65 PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR LEU
SEQRES 5 h 65 ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU GLY
SEQRES 1 i 38 MET GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR
SEQRES 2 i 38 PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY
SEQRES 3 i 38 ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP LEU GLU
SEQRES 1 j 40 MET MET SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL
SEQRES 2 j 40 ALA THR VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY
SEQRES 3 j 40 LEU PHE PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER
SEQRES 4 j 40 LEU
SEQRES 1 k 37 LYS LEU PRO GLU ALA TYR ALA ILE PHE ASP PRO LEU VAL
SEQRES 2 k 37 ASP VAL LEU PRO VAL ILE PRO VAL LEU PHE LEU ALA LEU
SEQRES 3 k 37 ALA PHE VAL TRP GLN ALA ALA VAL GLY PHE ARG
SEQRES 1 l 37 MET GLU PRO ASN PRO ASN ARG GLN PRO VAL GLU LEU ASN
SEQRES 2 l 37 ARG THR SER LEU TYR LEU GLY LEU LEU LEU ILE LEU VAL
SEQRES 3 l 37 LEU ALA LEU LEU PHE SER SER TYR PHE PHE ASN
SEQRES 1 m 34 MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU
SEQRES 2 m 34 PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR
SEQRES 3 m 34 VAL GLN THR GLU SER GLN GLN LYS
SEQRES 1 o 243 THR LEU THR TYR ASP ASP ILE VAL GLY THR GLY LEU ALA
SEQRES 2 o 243 ASN LYS CYS PRO THR LEU ASP ASP THR ALA ARG GLY ALA
SEQRES 3 o 243 TYR PRO ILE ASP SER SER GLN THR TYR ARG ILE ALA ARG
SEQRES 4 o 243 LEU CYS LEU GLN PRO THR THR PHE LEU VAL LYS GLU GLU
SEQRES 5 o 243 PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE VAL PRO THR
SEQRES 6 o 243 LYS LEU VAL THR ARG GLU THR THR SER LEU ASP GLN ILE
SEQRES 7 o 243 GLN GLY GLU LEU LYS VAL ASN SER ASP GLY SER LEU THR
SEQRES 8 o 243 PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN PRO VAL THR
SEQRES 9 o 243 VAL GLN MET ALA GLY GLY GLU ARG ILE PRO LEU LEU PHE
SEQRES 10 o 243 THR VAL LYS ASN LEU VAL ALA SER THR GLN PRO ASN VAL
SEQRES 11 o 243 THR SER ILE THR THR SER THR ASP PHE LYS GLY GLU PHE
SEQRES 12 o 243 ASN VAL PRO SER TYR ARG THR ALA ASN PHE LEU ASP PRO
SEQRES 13 o 243 LYS GLY ARG GLY LEU ALA SER GLY TYR ASP SER ALA ILE
SEQRES 14 o 243 ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU ALA ARG ALA
SEQRES 15 o 243 ASN VAL LYS ARG PHE SER LEU THR LYS GLY GLN ILE SER
SEQRES 16 o 243 LEU ASN VAL ALA LYS VAL ASP GLY ARG THR GLY GLU ILE
SEQRES 17 o 243 ALA GLY THR PHE GLU SER GLU GLN LEU SER ASP ASP ASP
SEQRES 18 o 243 MET GLY ALA HIS GLU PRO HIS GLU VAL LYS ILE GLN GLY
SEQRES 19 o 243 VAL PHE TYR ALA SER ILE GLU PRO ALA
SEQRES 1 t 30 MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE
SEQRES 2 t 30 ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO
SEQRES 3 t 30 PRO ARG ILE THR
SEQRES 1 u 97 GLU LEU VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA
SEQRES 2 u 97 TYR GLY GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA
SEQRES 3 u 97 ALA PHE ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA
SEQRES 4 u 97 LYS LEU ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU
SEQRES 5 u 97 ASP VAL LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS
SEQRES 6 u 97 GLN ILE LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR
SEQRES 7 u 97 GLU VAL GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR
SEQRES 8 u 97 ASN ASN GLY LEU TYR LYS
SEQRES 1 v 137 ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN
SEQRES 2 v 137 SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR
SEQRES 3 v 137 LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER
SEQRES 4 v 137 CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU
SEQRES 5 v 137 ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO
SEQRES 6 v 137 ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN
SEQRES 7 v 137 PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL
SEQRES 8 v 137 HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET
SEQRES 9 v 137 ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY
SEQRES 10 v 137 HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP
SEQRES 11 v 137 GLY GLY GLY LYS VAL TYR TYR
SEQRES 1 y 29 VAL ILE ALA GLN LEU THR MET ILE ALA MET ILE GLY ILE
SEQRES 2 y 29 ALA GLY PRO MET ILE ILE PHE LEU LEU ALA VAL ARG ARG
SEQRES 3 y 29 GLY ASN LEU
SEQRES 1 x 39 THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY LEU
SEQRES 2 x 39 LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA VAL
SEQRES 3 x 39 LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG SER
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 OEX A 601 10
HET FE2 A 602 1
HET CL A 603 1
HET CL A 604 1
HET BCT A 605 4
HET CLA A 606 65
HET CLA A 607 65
HET PHO A 608 64
HET CLA A 609 65
HET BCR A 610 40
HET PL9 A 611 55
HET SQD A 612 54
HET SQD A 613 54
HET CLA A 614 65
HET LHG A 615 42
HET CA B 601 1
HET CLA B 602 65
HET CLA B 603 65
HET CLA B 604 65
HET CLA B 605 65
HET CLA B 606 65
HET CLA B 607 65
HET CLA B 608 65
HET CLA B 609 65
HET CLA B 610 65
HET CLA B 611 65
HET CLA B 612 65
HET CLA B 613 65
HET CLA B 614 65
HET CLA B 615 65
HET CLA B 616 65
HET CLA B 617 65
HET BCR B 618 40
HET BCR B 619 40
HET BCR B 620 40
HET LHG B 621 49
HET BCR B 622 40
HET CLA C 501 65
HET CLA C 502 65
HET CLA C 503 65
HET CLA C 504 65
HET CLA C 505 65
HET CLA C 506 65
HET CLA C 507 65
HET CLA C 508 65
HET CLA C 509 65
HET CLA C 510 65
HET CLA C 511 65
HET CLA C 512 65
HET CLA C 513 65
HET BCR C 514 40
HET BCR C 515 40
HET DGD C 516 62
HET DGD C 517 62
HET DGD C 518 62
HET PHO D 401 64
HET CLA D 402 65
HET CLA D 403 65
HET BCR D 404 40
HET PL9 D 405 55
HET DGD D 406 62
HET LHG D 407 49
HET LHG D 408 49
HET LHG D 409 49
HET HEM E 101 43
HET SQD F 101 43
HET CA F 102 1
HET BCR H 101 40
HET DGD H 102 62
HET BCR K 101 40
HET SQD L 101 54
HET CA O 301 1
HET BCR T 101 40
HET BCR T 102 40
HET CL V 201 1
HET HEM V 202 43
HET BCR Y 101 40
HET OEX a 401 10
HET SQD a 402 54
HET FE2 a 403 1
HET CL a 404 1
HET CL a 405 1
HET CLA a 406 65
HET CLA a 407 65
HET CLA a 408 65
HET BCR a 409 40
HET PL9 a 410 55
HET SQD a 411 54
HET PHO a 412 64
HET LHG a 413 42
HET BCT a 414 4
HET CA b 601 1
HET CLA b 602 65
HET CLA b 603 65
HET CLA b 604 65
HET CLA b 605 65
HET CLA b 606 65
HET CLA b 607 65
HET CLA b 608 65
HET CLA b 609 65
HET CLA b 610 65
HET CLA b 611 65
HET CLA b 612 65
HET CLA b 613 65
HET CLA b 614 65
HET CLA b 615 65
HET CLA b 616 65
HET CLA b 617 65
HET BCR b 618 40
HET BCR b 619 40
HET LHG b 620 49
HET CA c 901 1
HET CLA c 902 65
HET CLA c 903 65
HET CLA c 904 65
HET CLA c 905 65
HET CLA c 906 65
HET CLA c 907 65
HET CLA c 908 65
HET CLA c 909 65
HET CLA c 910 65
HET CLA c 911 65
HET CLA c 912 65
HET CLA c 913 65
HET CLA c 914 65
HET BCR c 915 40
HET DGD c 916 62
HET DGD c 917 62
HET BCR c 918 40
HET CLA d 401 65
HET PHO d 402 64
HET CLA d 403 65
HET CLA d 404 65
HET PL9 d 405 55
HET DGD d 406 62
HET SQD d 407 43
HET LHG d 408 49
HET LHG d 409 49
HET LHG d 410 49
HET HEM e 101 43
HET BCR f 101 40
HET CA f 102 1
HET BCR h 101 40
HET DGD h 102 62
HET DGD j 101 62
HET MG j 102 1
HET BCR k 101 40
HET BCR k 102 40
HET SQD l 101 54
HET CA o 301 1
HET CL v 201 1
HET HEM v 202 43
HETNAM OEX CA-MN4-O5 CLUSTER
HETNAM FE2 FE (II) ION
HETNAM CL CHLORIDE ION
HETNAM BCT BICARBONATE ION
HETNAM CLA CHLOROPHYLL A
HETNAM PHO PHEOPHYTIN A
HETNAM BCR BETA-CAROTENE
HETNAM PL9 2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,
HETNAM 2 PL9 6,10,14,18,22,26,30,34-HEXATRIACONTANONAENYL-2,5-
HETNAM 3 PL9 CYCLOHEXADIENE-1,4-DIONE-2,3-DIMETHYL-5-SOLANESYL-1,4-
HETNAM 4 PL9 BENZOQUINONE
HETNAM SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-
HETNAM 2 SQD GLUCOPYRANOSYL]-SN-GLYCEROL
HETNAM LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE
HETNAM CA CALCIUM ION
HETNAM DGD DIGALACTOSYL DIACYL GLYCEROL (DGDG)
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM MG MAGNESIUM ION
HETSYN PL9 PLASTOQUINONE 9
HETSYN SQD SULFOQUINOVOSYLDIACYLGLYCEROL
HETSYN HEM HEME
FORMUL 39 OEX 2(CA MN4 O5)
FORMUL 40 FE2 2(FE 2+)
FORMUL 41 CL 6(CL 1-)
FORMUL 43 BCT 2(C H O3 1-)
FORMUL 44 CLA 70(C55 H72 MG N4 O5 2+)
FORMUL 46 PHO 4(C55 H74 N4 O5)
FORMUL 48 BCR 22(C40 H56)
FORMUL 49 PL9 4(C53 H80 O2)
FORMUL 50 SQD 8(C41 H78 O12 S)
FORMUL 53 LHG 10(C38 H75 O10 P)
FORMUL 54 CA 7(CA 2+)
FORMUL 91 DGD 10(C51 H96 O15)
FORMUL 03 HEM 4(C34 H32 FE N4 O4)
FORMUL 84 MG MG 2+
HELIX 1 AA1 ASN A 12 THR A 22 1 11
HELIX 2 AA2 VAL A 30 ALA A 55 1 26
HELIX 3 AA3 SER A 70 GLY A 74 5 5
HELIX 4 AA4 PRO A 95 ALA A 99 5 5
HELIX 5 AA5 SER A 101 ASN A 108 1 8
HELIX 6 AA6 GLY A 109 LEU A 137 1 29
HELIX 7 AA7 TRP A 142 LEU A 159 1 18
HELIX 8 AA8 LEU A 159 GLY A 166 1 8
HELIX 9 AA9 SER A 167 GLY A 171 5 5
HELIX 10 AB1 ILE A 176 ASN A 191 1 16
HELIX 11 AB2 ILE A 192 MET A 194 5 3
HELIX 12 AB3 HIS A 195 SER A 222 1 28
HELIX 13 AB4 SER A 232 TYR A 237 5 6
HELIX 14 AB5 ASN A 247 ILE A 259 1 13
HELIX 15 AB6 PHE A 260 SER A 264 5 5
HELIX 16 AB7 ASN A 267 ALA A 294 1 28
HELIX 17 AB8 THR A 316 HIS A 332 1 17
HELIX 18 AB9 PRO B 4 ILE B 13 5 10
HELIX 19 AC1 ASP B 15 PHE B 45 1 31
HELIX 20 AC2 PRO B 54 GLN B 58 5 5
HELIX 21 AC3 VAL B 62 LEU B 69 1 8
HELIX 22 AC4 SER B 92 TYR B 117 1 26
HELIX 23 AC5 LEU B 120 ARG B 124 5 5
HELIX 24 AC6 ASP B 134 PHE B 156 1 23
HELIX 25 AC7 GLY B 186 ASN B 191 5 6
HELIX 26 AC8 ASN B 194 VAL B 219 1 26
HELIX 27 AC9 PRO B 222 LEU B 229 1 8
HELIX 28 AD1 ASN B 233 GLY B 259 1 27
HELIX 29 AD2 PRO B 264 GLY B 269 1 6
HELIX 30 AD3 THR B 271 SER B 277 1 7
HELIX 31 AD4 SER B 278 SER B 294 1 17
HELIX 32 AD5 THR B 297 ALA B 304 1 8
HELIX 33 AD6 PRO B 306 ASP B 313 1 8
HELIX 34 AD7 TYR B 314 GLY B 322 5 9
HELIX 35 AD8 PRO B 329 GLY B 333 5 5
HELIX 36 AD9 SER B 391 GLY B 396 1 6
HELIX 37 AE1 ASP B 413 ILE B 425 1 13
HELIX 38 AE2 SER B 446 PHE B 475 1 30
HELIX 39 AE3 ARG B 476 PHE B 479 5 4
HELIX 40 AE4 SER B 487 VAL B 491 5 5
HELIX 41 AE5 ASP B 501 ARG B 505 5 5
HELIX 42 AE6 ASP C 27 GLY C 32 1 6
HELIX 43 AE7 ALA C 34 ILE C 43 5 10
HELIX 44 AE8 LEU C 45 PHE C 75 1 31
HELIX 45 AE9 PRO C 80 GLN C 84 5 5
HELIX 46 AF1 ILE C 87 LEU C 95 1 9
HELIX 47 AF2 GLY C 100 GLU C 104 5 5
HELIX 48 AF3 THR C 108 ARG C 135 1 28
HELIX 49 AF4 ASP C 153 PHE C 182 1 30
HELIX 50 AF5 ASP C 205 LEU C 214 1 10
HELIX 51 AF6 GLY C 222 VAL C 227 5 6
HELIX 52 AF7 ASN C 229 THR C 254 1 26
HELIX 53 AF8 PHE C 257 PHE C 264 1 8
HELIX 54 AF9 SER C 267 ASN C 293 1 27
HELIX 55 AG1 PRO C 298 GLY C 303 1 6
HELIX 56 AG2 THR C 305 LEU C 324 1 20
HELIX 57 AG3 GLY C 353 TRP C 359 5 7
HELIX 58 AG4 LEU C 366 PRO C 368 5 3
HELIX 59 AG5 ASP C 376 ASP C 383 1 8
HELIX 60 AG6 GLN C 385 THR C 397 1 13
HELIX 61 AG7 SER C 421 GLY C 454 1 34
HELIX 62 AG8 GLU C 464 MET C 469 5 6
HELIX 63 AG9 GLY D 13 LYS D 23 1 11
HELIX 64 AH1 VAL D 30 VAL D 55 1 26
HELIX 65 AH2 SER D 66 GLY D 70 5 5
HELIX 66 AH3 ALA D 82 GLY D 86 5 5
HELIX 67 AH4 ASP D 100 LEU D 107 1 8
HELIX 68 AH5 GLY D 108 GLY D 137 1 30
HELIX 69 AH6 PRO D 140 LEU D 158 1 19
HELIX 70 AH7 LEU D 158 GLN D 164 1 7
HELIX 71 AH8 SER D 166 ALA D 170 5 5
HELIX 72 AH9 VAL D 175 ASN D 190 1 16
HELIX 73 AI1 TRP D 191 LEU D 193 5 3
HELIX 74 AI2 ASN D 194 ASN D 220 1 27
HELIX 75 AI3 THR D 231 PHE D 235 5 5
HELIX 76 AI4 SER D 245 PHE D 257 1 13
HELIX 77 AI5 ASN D 263 ALA D 290 1 28
HELIX 78 AI6 PHE D 298 ASP D 308 1 11
HELIX 79 AI7 THR D 313 GLN D 334 1 22
HELIX 80 AI8 PRO D 335 ASN D 338 5 4
HELIX 81 AI9 PRO D 342 LEU D 346 5 5
HELIX 82 AJ1 PRO E 9 ILE E 14 1 6
HELIX 83 AJ2 SER E 16 THR E 40 1 25
HELIX 84 AJ3 GLY E 41 GLY E 48 1 8
HELIX 85 AJ4 GLU E 71 GLN E 82 1 12
HELIX 86 AJ5 THR F 17 GLN F 41 1 25
HELIX 87 AJ6 THR H 5 ARG H 12 1 8
HELIX 88 AJ7 PRO H 13 SER H 16 5 4
HELIX 89 AJ8 THR H 27 ASN H 50 1 24
HELIX 90 AJ9 GLU I 2 SER I 25 1 24
HELIX 91 AK1 GLY I 26 ARG I 30 5 5
HELIX 92 AK2 PRO J 9 TYR J 33 1 25
HELIX 93 AK3 PRO K 12 ILE K 17 5 6
HELIX 94 AK4 PHE K 18 LEU K 25 1 8
HELIX 95 AK5 VAL K 27 VAL K 43 1 17
HELIX 96 AK6 ASN L 13 ASN L 37 1 25
HELIX 97 AK7 LEU M 6 SER M 31 1 26
HELIX 98 AK8 THR O 6 VAL O 11 1 6
HELIX 99 AK9 GLY O 14 LYS O 18 5 5
HELIX 100 AL1 GLU O 179 GLU O 181 5 3
HELIX 101 AL2 LEU O 182 VAL O 187 1 6
HELIX 102 AL3 GLU T 2 PHE T 23 1 22
HELIX 103 AL4 ASN U 11 LEU U 17 1 7
HELIX 104 AL5 GLY U 18 GLU U 23 5 6
HELIX 105 AL6 ASN U 31 TYR U 38 5 8
HELIX 106 AL7 PRO U 43 ALA U 53 1 11
HELIX 107 AL8 SER U 57 ILE U 64 5 8
HELIX 108 AL9 THR U 68 ASN U 78 1 11
HELIX 109 AM1 GLU U 88 GLU U 93 1 6
HELIX 110 AM2 GLY U 94 ASP U 96 5 3
HELIX 111 AM3 THR V 22 CYS V 37 1 16
HELIX 112 AM4 CYS V 37 VAL V 42 1 6
HELIX 113 AM5 GLY V 43 ILE V 45 5 3
HELIX 114 AM6 ARG V 55 ALA V 62 1 8
HELIX 115 AM7 ASN V 68 ASN V 78 1 11
HELIX 116 AM8 PHE V 101 ARG V 105 5 5
HELIX 117 AM9 THR V 108 GLY V 127 1 20
HELIX 118 AN1 ASP V 128 TRP V 130 5 3
HELIX 119 AN2 GLY V 133 TYR V 137 5 5
HELIX 120 AN3 ILE Y 19 ARG Y 42 1 24
HELIX 121 AN4 THR X 4 ASP X 35 1 32
HELIX 122 AN5 THR Z 2 SER Z 29 1 28
HELIX 123 AN6 ASP Z 32 ASN Z 58 1 27
HELIX 124 AN7 PHE Z 59 VAL Z 61 5 3
HELIX 125 AN8 ASN a 12 THR a 22 1 11
HELIX 126 AN9 VAL a 30 ALA a 55 1 26
HELIX 127 AO1 PRO a 95 ALA a 99 5 5
HELIX 128 AO2 SER a 101 ASN a 108 1 8
HELIX 129 AO3 GLY a 109 LEU a 137 1 29
HELIX 130 AO4 TRP a 142 LEU a 159 1 18
HELIX 131 AO5 LEU a 159 GLY a 166 1 8
HELIX 132 AO6 SER a 167 GLY a 171 5 5
HELIX 133 AO7 ILE a 176 ASN a 191 1 16
HELIX 134 AO8 ILE a 192 MET a 194 5 3
HELIX 135 AO9 HIS a 195 SER a 222 1 28
HELIX 136 AP1 SER a 232 TYR a 237 5 6
HELIX 137 AP2 ASN a 247 ILE a 259 1 13
HELIX 138 AP3 PHE a 260 SER a 264 5 5
HELIX 139 AP4 ASN a 267 ALA a 294 1 28
HELIX 140 AP5 THR a 316 HIS a 332 1 17
HELIX 141 AP6 PRO b 4 ILE b 13 5 10
HELIX 142 AP7 ASP b 15 PHE b 45 1 31
HELIX 143 AP8 PRO b 54 GLN b 58 5 5
HELIX 144 AP9 VAL b 62 LEU b 69 1 8
HELIX 145 AQ1 SER b 92 TYR b 117 1 26
HELIX 146 AQ2 LEU b 120 ARG b 124 5 5
HELIX 147 AQ3 ASP b 134 PHE b 156 1 23
HELIX 148 AQ4 GLY b 186 ASN b 191 5 6
HELIX 149 AQ5 ASN b 194 VAL b 219 1 26
HELIX 150 AQ6 PRO b 222 LEU b 229 1 8
HELIX 151 AQ7 ASN b 233 GLY b 259 1 27
HELIX 152 AQ8 PRO b 264 GLY b 269 1 6
HELIX 153 AQ9 THR b 271 SER b 277 1 7
HELIX 154 AR1 SER b 278 SER b 294 1 17
HELIX 155 AR2 THR b 297 ALA b 304 1 8
HELIX 156 AR3 PRO b 306 ASP b 313 1 8
HELIX 157 AR4 TYR b 314 GLY b 322 5 9
HELIX 158 AR5 PRO b 329 GLY b 333 5 5
HELIX 159 AR6 SER b 391 GLY b 396 1 6
HELIX 160 AR7 ASP b 413 ILE b 425 1 13
HELIX 161 AR8 SER b 446 PHE b 475 1 30
HELIX 162 AR9 ARG b 476 PHE b 479 5 4
HELIX 163 AS1 ASP b 501 ARG b 505 5 5
HELIX 164 AS2 ASP c 27 GLY c 32 1 6
HELIX 165 AS3 ALA c 34 ILE c 43 5 10
HELIX 166 AS4 LEU c 45 PHE c 75 1 31
HELIX 167 AS5 PRO c 80 GLN c 84 5 5
HELIX 168 AS6 ILE c 87 LEU c 95 1 9
HELIX 169 AS7 GLY c 100 GLU c 104 5 5
HELIX 170 AS8 THR c 108 ARG c 135 1 28
HELIX 171 AS9 ASP c 153 PHE c 182 1 30
HELIX 172 AT1 ASP c 205 LEU c 214 1 10
HELIX 173 AT2 GLY c 222 VAL c 227 5 6
HELIX 174 AT3 ASN c 229 THR c 254 1 26
HELIX 175 AT4 PHE c 257 PHE c 264 1 8
HELIX 176 AT5 SER c 267 ASN c 293 1 27
HELIX 177 AT6 PRO c 298 GLY c 303 1 6
HELIX 178 AT7 THR c 305 GLY c 325 1 21
HELIX 179 AT8 GLY c 353 TRP c 359 5 7
HELIX 180 AT9 LEU c 366 PRO c 368 5 3
HELIX 181 AU1 ASP c 376 ASP c 383 1 8
HELIX 182 AU2 GLN c 385 THR c 397 1 13
HELIX 183 AU3 SER c 421 GLY c 454 1 34
HELIX 184 AU4 ASP c 460 MET c 469 5 10
HELIX 185 AU5 GLY d 13 LYS d 23 1 11
HELIX 186 AU6 VAL d 30 VAL d 55 1 26
HELIX 187 AU7 SER d 57 GLY d 62 1 6
HELIX 188 AU8 SER d 66 GLY d 70 5 5
HELIX 189 AU9 ALA d 82 GLY d 86 5 5
HELIX 190 AV1 ASP d 100 LEU d 107 1 8
HELIX 191 AV2 GLY d 108 GLY d 137 1 30
HELIX 192 AV3 PRO d 140 LEU d 158 1 19
HELIX 193 AV4 LEU d 158 GLN d 164 1 7
HELIX 194 AV5 SER d 166 ALA d 170 5 5
HELIX 195 AV6 VAL d 175 ASN d 190 1 16
HELIX 196 AV7 TRP d 191 LEU d 193 5 3
HELIX 197 AV8 ASN d 194 ASN d 220 1 27
HELIX 198 AV9 THR d 231 PHE d 235 5 5
HELIX 199 AW1 SER d 245 PHE d 257 1 13
HELIX 200 AW2 ASN d 263 ALA d 290 1 28
HELIX 201 AW3 PHE d 298 ASP d 308 1 11
HELIX 202 AW4 THR d 313 GLN d 334 1 22
HELIX 203 AW5 PRO d 335 ASN d 338 5 4
HELIX 204 AW6 PRO d 342 LEU d 346 5 5
HELIX 205 AW7 PRO e 9 ILE e 14 1 6
HELIX 206 AW8 SER e 16 THR e 40 1 25
HELIX 207 AW9 GLY e 41 GLY e 48 1 8
HELIX 208 AX1 GLU e 71 GLN e 82 1 12
HELIX 209 AX2 THR f 17 GLN f 41 1 25
HELIX 210 AX3 THR h 5 ARG h 12 1 8
HELIX 211 AX4 PRO h 13 SER h 16 5 4
HELIX 212 AX5 THR h 27 ASN h 50 1 24
HELIX 213 AX6 SER h 61 LEU h 65 5 5
HELIX 214 AX7 GLU i 2 SER i 25 1 24
HELIX 215 AX8 PRO j 9 ALA j 32 1 24
HELIX 216 AX9 PRO k 12 ILE k 17 5 6
HELIX 217 AY1 PHE k 18 LEU k 25 1 8
HELIX 218 AY2 VAL k 27 VAL k 43 1 17
HELIX 219 AY3 ASN l 13 ASN l 37 1 25
HELIX 220 AY4 LEU m 6 SER m 31 1 26
HELIX 221 AY5 THR o 6 VAL o 11 1 6
HELIX 222 AY6 GLY o 14 LYS o 18 5 5
HELIX 223 AY7 GLU o 179 GLU o 181 5 3
HELIX 224 AY8 LEU o 182 VAL o 187 1 6
HELIX 225 AY9 GLU t 2 PHE t 23 1 22
HELIX 226 AZ1 ASN u 11 LEU u 17 1 7
HELIX 227 AZ2 GLY u 18 GLU u 23 5 6
HELIX 228 AZ3 ASN u 31 TYR u 38 5 8
HELIX 229 AZ4 PRO u 43 ALA u 53 1 11
HELIX 230 AZ5 SER u 57 ILE u 64 5 8
HELIX 231 AZ6 THR u 68 LEU u 79 1 12
HELIX 232 AZ7 GLU u 88 GLU u 93 1 6
HELIX 233 AZ8 GLY u 94 ASP u 96 5 3
HELIX 234 AZ9 THR v 22 CYS v 37 1 16
HELIX 235 BA1 CYS v 37 VAL v 42 1 6
HELIX 236 BA2 GLY v 43 ILE v 45 5 3
HELIX 237 BA3 ARG v 55 ALA v 62 1 8
HELIX 238 BA4 ASN v 68 ASN v 78 1 11
HELIX 239 BA5 PHE v 101 ARG v 105 5 5
HELIX 240 BA6 THR v 108 GLY v 127 1 20
HELIX 241 BA7 ASP v 128 TRP v 130 5 3
HELIX 242 BA8 GLY v 133 TYR v 137 5 5
HELIX 243 BA9 ILE y 19 ARG y 42 1 24
HELIX 244 BB1 THR x 4 ASP x 35 1 32
HELIX 245 BB2 THR z 2 SER z 29 1 28
HELIX 246 BB3 ASP z 32 PHE z 59 1 28
SHEET 1 AA1 2 ALA A 81 VAL A 82 0
SHEET 2 AA1 2 LEU A 174 GLY A 175 -1 O LEU A 174 N VAL A 82
SHEET 1 AA2 2 LEU A 297 ASN A 298 0
SHEET 2 AA2 2 GLY C 402 SER C 403 1 O GLY C 402 N ASN A 298
SHEET 1 AA3 2 MET B 166 VAL B 168 0
SHEET 2 AA3 2 SER B 177 GLN B 179 -1 O GLN B 179 N MET B 166
SHEET 1 AA4 6 VAL B 377 ASP B 380 0
SHEET 2 AA4 6 ILE B 369 THR B 371 -1 N LEU B 370 O ALA B 379
SHEET 3 AA4 6 GLU B 353 VAL B 356 -1 N PHE B 355 O THR B 371
SHEET 4 AA4 6 ILE B 336 ARG B 347 -1 N PHE B 346 O LEU B 354
SHEET 5 AA4 6 THR B 398 TYR B 402 -1 O TYR B 402 N HIS B 343
SHEET 6 AA4 6 THR B 410 PHE B 411 -1 O PHE B 411 N VAL B 399
SHEET 1 AA5 5 VAL B 377 ASP B 380 0
SHEET 2 AA5 5 ILE B 369 THR B 371 -1 N LEU B 370 O ALA B 379
SHEET 3 AA5 5 GLU B 353 VAL B 356 -1 N PHE B 355 O THR B 371
SHEET 4 AA5 5 ILE B 336 ARG B 347 -1 N PHE B 346 O LEU B 354
SHEET 5 AA5 5 ILE B 429 ASP B 433 -1 O GLU B 431 N GLN B 338
SHEET 1 AA6 2 LEU C 185 ASP C 187 0
SHEET 2 AA6 2 ASP C 195 ARG C 197 -1 O ASP C 195 N ASP C 187
SHEET 1 AA7 2 LEU C 341 ARG C 343 0
SHEET 2 AA7 2 ILE C 349 PHE C 351 -1 O ILE C 350 N MET C 342
SHEET 1 AA8 2 ARG C 370 GLY C 371 0
SHEET 2 AA8 2 GLY C 374 LEU C 375 -1 O GLY C 374 N GLY C 371
SHEET 1 AA9 2 ALA D 77 VAL D 78 0
SHEET 2 AA9 2 PHE D 173 GLY D 174 -1 O PHE D 173 N VAL D 78
SHEET 1 AB1 2 TYR O 30 PRO O 31 0
SHEET 2 AB1 2 SER O 135 ILE O 136 -1 O ILE O 136 N TYR O 30
SHEET 1 AB210 PHE O 65 PRO O 67 0
SHEET 2 AB210 TYR O 38 LYS O 53 -1 N VAL O 52 O VAL O 66
SHEET 3 AB210 GLU O 232 PRO O 245 -1 O GLN O 236 N THR O 48
SHEET 4 AB210 GLU O 210 LEU O 220 -1 N ILE O 211 O ALA O 241
SHEET 5 AB210 LEU O 192 ASP O 205 -1 N ASN O 200 O THR O 214
SHEET 6 AB210 ASP O 141 PRO O 149 -1 N PHE O 142 O LEU O 199
SHEET 7 AB210 VAL O 126 SER O 128 -1 N SER O 128 O LYS O 143
SHEET 8 AB210 LEU O 93 ILE O 101 -1 N PHE O 95 O ALA O 127
SHEET 9 AB210 LEU O 78 VAL O 87 -1 N LYS O 86 O THR O 94
SHEET 10 AB210 TYR O 38 LYS O 53 -1 N LEU O 45 O LEU O 78
SHEET 1 AB3 3 LYS O 69 LEU O 70 0
SHEET 2 AB3 3 PHE O 103 GLN O 109 -1 O GLN O 109 N LYS O 69
SHEET 3 AB3 3 ARG O 115 THR O 121 -1 O ILE O 116 N VAL O 108
SHEET 1 AB4 2 ILE U 25 ASP U 26 0
SHEET 2 AB4 2 PHE U 82 THR U 83 1 O THR U 83 N ILE U 25
SHEET 1 AB5 2 THR V 9 PRO V 11 0
SHEET 2 AB5 2 THR V 18 THR V 20 -1 O ILE V 19 N VAL V 10
SHEET 1 AB6 2 ALA a 81 VAL a 82 0
SHEET 2 AB6 2 LEU a 174 GLY a 175 -1 O LEU a 174 N VAL a 82
SHEET 1 AB7 2 LEU a 297 ASN a 298 0
SHEET 2 AB7 2 GLY c 402 SER c 403 1 O GLY c 402 N ASN a 298
SHEET 1 AB8 2 MET b 166 VAL b 168 0
SHEET 2 AB8 2 SER b 177 GLN b 179 -1 O GLN b 179 N MET b 166
SHEET 1 AB9 6 VAL b 377 ASP b 380 0
SHEET 2 AB9 6 ILE b 369 THR b 371 -1 N LEU b 370 O ALA b 379
SHEET 3 AB9 6 GLU b 353 VAL b 356 -1 N PHE b 355 O THR b 371
SHEET 4 AB9 6 ILE b 336 ARG b 347 -1 N PHE b 346 O LEU b 354
SHEET 5 AB9 6 THR b 398 TYR b 402 -1 O TYR b 402 N HIS b 343
SHEET 6 AB9 6 THR b 410 PHE b 411 -1 O PHE b 411 N VAL b 399
SHEET 1 AC1 5 VAL b 377 ASP b 380 0
SHEET 2 AC1 5 ILE b 369 THR b 371 -1 N LEU b 370 O ALA b 379
SHEET 3 AC1 5 GLU b 353 VAL b 356 -1 N PHE b 355 O THR b 371
SHEET 4 AC1 5 ILE b 336 ARG b 347 -1 N PHE b 346 O LEU b 354
SHEET 5 AC1 5 ILE b 429 ASP b 433 -1 O GLU b 431 N GLN b 338
SHEET 1 AC2 2 LEU c 185 ASP c 187 0
SHEET 2 AC2 2 ASP c 195 ARG c 197 -1 O ASP c 195 N ASP c 187
SHEET 1 AC3 2 LEU c 341 ARG c 343 0
SHEET 2 AC3 2 ILE c 349 PHE c 351 -1 O ILE c 350 N MET c 342
SHEET 1 AC4 2 ARG c 370 GLY c 371 0
SHEET 2 AC4 2 GLY c 374 LEU c 375 -1 O GLY c 374 N GLY c 371
SHEET 1 AC5 2 ALA d 77 VAL d 78 0
SHEET 2 AC5 2 PHE d 173 GLY d 174 -1 O PHE d 173 N VAL d 78
SHEET 1 AC6 2 TYR o 30 PRO o 31 0
SHEET 2 AC6 2 SER o 135 ILE o 136 -1 O ILE o 136 N TYR o 30
SHEET 1 AC710 PHE o 65 PRO o 67 0
SHEET 2 AC710 TYR o 38 LYS o 53 -1 N VAL o 52 O VAL o 66
SHEET 3 AC710 GLU o 232 PRO o 245 -1 O GLN o 236 N THR o 48
SHEET 4 AC710 GLU o 210 LEU o 220 -1 N ILE o 211 O ALA o 241
SHEET 5 AC710 LEU o 192 ASP o 205 -1 N ASN o 200 O THR o 214
SHEET 6 AC710 ASP o 141 PRO o 149 -1 N PHE o 142 O LEU o 199
SHEET 7 AC710 VAL o 126 SER o 128 -1 N SER o 128 O LYS o 143
SHEET 8 AC710 LEU o 93 ILE o 101 -1 N PHE o 95 O ALA o 127
SHEET 9 AC710 LEU o 78 VAL o 87 -1 N LYS o 86 O THR o 94
SHEET 10 AC710 TYR o 38 LYS o 53 -1 N LEU o 45 O LEU o 78
SHEET 1 AC8 3 LYS o 69 LEU o 70 0
SHEET 2 AC8 3 PHE o 103 GLN o 109 -1 O GLN o 109 N LYS o 69
SHEET 3 AC8 3 ARG o 115 THR o 121 -1 O ILE o 116 N VAL o 108
SHEET 1 AC9 2 ILE u 25 ASP u 26 0
SHEET 2 AC9 2 PHE u 82 THR u 83 1 O THR u 83 N ILE u 25
SHEET 1 AD1 2 THR v 9 PRO v 11 0
SHEET 2 AD1 2 THR v 18 THR v 20 -1 O ILE v 19 N VAL v 10
SSBOND 1 CYS O 19 CYS O 44 1555 1555 2.05
SSBOND 2 CYS o 19 CYS o 44 1555 1555 2.03
LINK OD1 ASP A 170 MN4 OEX A 601 1555 1555 2.08
LINK OD2 ASP A 170 CA1 OEX A 601 1555 1555 2.44
LINK OE2 GLU A 189 MN1 OEX A 601 1555 1555 1.90
LINK NE2 HIS A 215 FE FE2 A 602 1555 1555 2.16
LINK NE2 HIS A 272 FE FE2 A 602 1555 1555 2.25
LINK NE2 HIS A 332 MN1 OEX A 601 1555 1555 2.14
LINK OE1 GLU A 333 MN3 OEX A 601 1555 1555 2.07
LINK OE2 GLU A 333 MN4 OEX A 601 1555 1555 2.17
LINK OD1 ASP A 342 MN2 OEX A 601 1555 1555 2.15
LINK OD2 ASP A 342 MN1 OEX A 601 1555 1555 2.26
LINK O ALA A 344 CA1 OEX A 601 1555 1555 2.54
LINK OXT ALA A 344 MN2 OEX A 601 1555 1555 1.99
LINK OD1 ASN B 438 CA CA B 601 1555 1555 2.65
LINK OD1 ASN C 39 MG CLA C 511 1555 1555 2.11
LINK OE1 GLU C 354 MN2 OEX A 601 1555 1555 1.85
LINK OE2 GLU C 354 MN3 OEX A 601 1555 1555 1.99
LINK NE2 HIS D 214 FE FE2 A 602 1555 1555 2.26
LINK NE2 HIS D 268 FE FE2 A 602 1555 1555 2.29
LINK NE2 HIS E 23 FE HEM E 101 1555 1555 2.10
LINK NE2 HIS F 24 FE HEM E 101 1555 1555 2.10
LINK O ARG F 45 CA CA F 102 1555 1555 2.97
LINK OXT ARG F 45 CA CA F 102 1555 1555 2.58
LINK O THR O 138 CA CA O 301 1555 1555 2.48
LINK OD1 ASN O 200 CA CA O 301 1555 1555 2.52
LINK O VAL O 201 CA CA O 301 1555 1555 2.51
LINK NE2 HIS V 41 FE HEM V 202 1555 1555 2.05
LINK NE2 HIS V 92 FE HEM V 202 1555 1555 2.13
LINK OD1 ASP a 170 MN4 OEX a 401 1555 1555 2.03
LINK OD2 ASP a 170 CA1 OEX a 401 1555 1555 2.37
LINK OE2 GLU a 189 MN1 OEX a 401 1555 1555 1.79
LINK NE2 HIS a 215 FE FE2 a 403 1555 1555 2.11
LINK NE2 HIS a 272 FE FE2 a 403 1555 1555 2.32
LINK NE2 HIS a 332 MN1 OEX a 401 1555 1555 2.19
LINK OE1 GLU a 333 MN3 OEX a 401 1555 1555 1.98
LINK OE2 GLU a 333 MN4 OEX a 401 1555 1555 2.13
LINK OD1 ASP a 342 MN2 OEX a 401 1555 1555 2.13
LINK OD2 ASP a 342 MN1 OEX a 401 1555 1555 2.26
LINK O ALA a 344 CA1 OEX a 401 1555 1555 2.46
LINK OXT ALA a 344 MN2 OEX a 401 1555 1555 1.89
LINK OD1 ASN b 438 CA CA b 601 1555 1555 2.58
LINK O PHE c 22 CA CA c 901 1555 1555 2.42
LINK O THR c 24 CA CA c 901 1555 1555 2.39
LINK OD1 ASP c 27 CA CA c 901 1555 1555 2.64
LINK OD2 ASP c 27 CA CA c 901 1555 1555 2.46
LINK OE1 GLU c 29 CA CA c 901 1555 1555 2.41
LINK OG SER c 30 CA CA c 901 1555 1555 2.41
LINK OD1 ASN c 39 MG CLA c 912 1555 1555 1.96
LINK OE1 GLU c 354 MN2 OEX a 401 1555 1555 1.85
LINK OE2 GLU c 354 MN3 OEX a 401 1555 1555 1.89
LINK NE2 HIS d 214 FE FE2 a 403 1555 1555 2.41
LINK NE2 HIS d 268 FE FE2 a 403 1555 1555 2.22
LINK NE2 HIS e 23 FE HEM e 101 1555 1555 2.13
LINK NE2 HIS f 24 FE HEM e 101 1555 1555 2.15
LINK O ARG f 45 CA CA f 102 1555 1555 3.01
LINK OXT ARG f 45 CA CA f 102 1555 1555 2.51
LINK O GLY j 31 MG MG j 102 1555 1555 2.25
LINK O ALA j 34 MG MG j 102 1555 1555 2.33
LINK O LEU j 36 MG MG j 102 1555 1555 2.28
LINK O THR o 138 CA CA o 301 1555 1555 2.28
LINK OD1 ASN o 200 CA CA o 301 1555 1555 2.59
LINK O VAL o 201 CA CA o 301 1555 1555 2.51
LINK NE2 HIS v 41 FE HEM v 202 1555 1555 2.05
LINK NE2 HIS v 92 FE HEM v 202 1555 1555 2.09
LINK FE FE2 A 602 O3 BCT A 605 1555 1555 2.26
LINK FE FE2 A 602 O2 BCT A 605 1555 1555 2.29
LINK FE FE2 a 403 O2 BCT a 414 1555 1555 2.18
LINK FE FE2 a 403 O3 BCT a 414 1555 1555 2.24
LINK CD GLN O 36 N SER c 20 1555 2455 1.33
LINK NE2 GLN O 36 N SER c 20 1555 2455 1.51
LINK CA THR O 37 OD1 ASN c 19 1555 2455 1.33
LINK C THR O 37 CG ASN c 19 1555 2455 1.29
LINK C THR O 37 ND2 ASN c 19 1555 2455 1.55
CISPEP 1 TYR U 42 PRO U 43 0 3.60
CISPEP 2 ALA U 53 PRO U 54 0 1.90
CISPEP 3 THR V 63 PRO V 64 0 -10.57
CISPEP 4 TYR u 42 PRO u 43 0 4.53
CISPEP 5 ALA u 53 PRO u 54 0 4.30
CISPEP 6 THR v 63 PRO v 64 0 -7.09
SITE 1 AC1 10 ASP A 170 VAL A 185 GLU A 189 HIS A 332
SITE 2 AC1 10 GLU A 333 HIS A 337 ASP A 342 ALA A 344
SITE 3 AC1 10 GLU C 354 ARG C 357
SITE 1 AC2 5 HIS A 215 HIS A 272 BCT A 605 HIS D 214
SITE 2 AC2 5 HIS D 268
SITE 1 AC3 4 ASN A 181 HIS A 332 GLU A 333 LYS D 317
SITE 1 AC4 4 ASN A 338 PHE A 339 GLY C 353 GLU C 354
SITE 1 AC5 8 HIS A 215 GLU A 244 TYR A 246 HIS A 272
SITE 2 AC5 8 FE2 A 602 HIS D 214 TYR D 244 HIS D 268
SITE 1 AC6 20 TYR A 147 PRO A 150 SER A 153 VAL A 157
SITE 2 AC6 20 MET A 183 PHE A 186 GLN A 187 ILE A 192
SITE 3 AC6 20 HIS A 198 GLY A 201 PHE A 206 ALA A 286
SITE 4 AC6 20 ALA A 287 ILE A 290 PHO A 608 CLA A 614
SITE 5 AC6 20 LEU D 182 LEU D 205 CLA D 402 PHE T 17
SITE 1 AC7 14 GLN A 199 VAL A 202 ALA A 203 PHE A 206
SITE 2 AC7 14 GLY A 207 LEU A 210 TRP A 278 PHE D 157
SITE 3 AC7 14 VAL D 175 ILE D 178 PHE D 179 LEU D 182
SITE 4 AC7 14 PHO D 401 CLA D 402
SITE 1 AC8 20 LEU A 41 ALA A 44 THR A 45 PHE A 48
SITE 2 AC8 20 TYR A 126 GLN A 130 ALA A 146 TYR A 147
SITE 3 AC8 20 PRO A 150 GLY A 175 PRO A 279 CLA A 606
SITE 4 AC8 20 CLA A 614 LEU D 205 ALA D 208 LEU D 209
SITE 5 AC8 20 ILE D 213 TRP D 253 PHE D 257 LHG D 408
SITE 1 AC9 15 ILE A 36 THR A 40 PHE A 93 PRO A 95
SITE 2 AC9 15 ILE A 96 TRP A 97 LEU A 114 HIS A 118
SITE 3 AC9 15 BCR A 610 CLA C 506 VAL I 8 TYR I 9
SITE 4 AC9 15 VAL I 11 VAL I 12 PHE I 15
SITE 1 AD1 4 ALA A 43 ILE A 96 CLA A 609 PHE I 15
SITE 1 AD2 18 PHE A 211 MET A 214 HIS A 215 LEU A 218
SITE 2 AD2 18 HIS A 252 PHE A 255 SER A 264 PHE A 265
SITE 3 AD2 18 LEU A 271 PHE A 274 LHG A 615 PHO D 401
SITE 4 AD2 18 VAL F 18 ALA F 22 THR F 25 LEU F 26
SITE 5 AD2 18 THR X 24 LEU X 28
SITE 1 AD3 16 LEU A 200 GLY A 204 ASN A 267 SER A 270
SITE 2 AD3 16 PHE A 273 PHE A 274 TRP A 278 GLN C 28
SITE 3 AD3 16 ALA C 34 TRP C 36 CLA C 508 PHE D 232
SITE 4 AD3 16 ARG D 233 LHG D 409 ILE J 22 PHE K 37
SITE 1 AD4 12 TRP A 20 ASN A 26 ARG A 27 LEU A 28
SITE 2 AD4 12 ILE A 38 THR A 45 CLA A 614 PHE T 22
SITE 3 AD4 12 BCR T 101 TRP b 113 TYR b 117 BCR b 619
SITE 1 AD5 18 VAL A 157 MET A 172 ILE A 176 THR A 179
SITE 2 AD5 18 PHE A 180 PHE A 182 MET A 183 CLA A 606
SITE 3 AD5 18 PHO A 608 SQD A 613 LHG B 621 MET D 198
SITE 4 AD5 18 VAL D 201 ALA D 202 LEU D 205 GLY D 206
SITE 5 AD5 18 CLA D 402 PL9 D 405
SITE 1 AD6 11 LEU A 258 PHE A 260 TYR A 262 PL9 A 611
SITE 2 AD6 11 PHE D 27 THR E 4 THR E 5 GLU E 7
SITE 3 AD6 11 PRO E 9 PHE E 10 SER E 11
SITE 1 AD7 1 ASN B 438
SITE 1 AD8 6 TRP B 185 GLY B 186 PHE B 190 CLA B 603
SITE 2 AD8 6 PHE H 41 BCR H 101
SITE 1 AD9 19 GLY B 189 PHE B 190 GLY B 197 ALA B 200
SITE 2 AD9 19 HIS B 201 ALA B 204 VAL B 208 PHE B 250
SITE 3 AD9 19 CLA B 602 CLA B 604 CLA B 606 LEU D 158
SITE 4 AD9 19 PHE H 38 PHE H 41 ILE H 45 LEU H 46
SITE 5 AD9 19 TYR H 49 BCR H 101 DGD H 102
SITE 1 AE1 16 ARG B 68 LEU B 69 ALA B 146 LEU B 149
SITE 2 AE1 16 PHE B 153 HIS B 201 HIS B 202 PHE B 247
SITE 3 AE1 16 ALA B 248 VAL B 252 THR B 262 CLA B 603
SITE 4 AE1 16 CLA B 605 CLA B 606 CLA B 607 CLA B 611
SITE 1 AE2 18 TRP B 33 PHE B 61 PHE B 65 ARG B 68
SITE 2 AE2 18 LEU B 149 VAL B 245 ALA B 248 ALA B 249
SITE 3 AE2 18 VAL B 252 PHE B 451 HIS B 455 PHE B 458
SITE 4 AE2 18 PHE B 462 CLA B 604 CLA B 606 CLA B 608
SITE 5 AE2 18 CLA B 613 CLA B 614
SITE 1 AE3 22 THR B 27 VAL B 30 TRP B 33 ALA B 34
SITE 2 AE3 22 VAL B 62 PHE B 65 MET B 66 ARG B 68
SITE 3 AE3 22 LEU B 69 VAL B 96 HIS B 100 LEU B 103
SITE 4 AE3 22 ALA B 205 CLA B 603 CLA B 604 CLA B 605
SITE 5 AE3 22 CLA B 607 CLA B 610 CLA B 611 CLA B 613
SITE 6 AE3 22 CLA B 616 BCR B 620
SITE 1 AE4 15 LEU B 69 GLY B 70 TRP B 91 HIS B 100
SITE 2 AE4 15 VAL B 102 GLY B 152 PHE B 153 HIS B 157
SITE 3 AE4 15 PHE B 162 GLY B 163 PRO B 164 CLA B 604
SITE 4 AE4 15 CLA B 606 BCR B 620 SQD a 402
SITE 1 AE5 20 TRP B 33 TYR B 40 GLN B 58 GLY B 59
SITE 2 AE5 20 PHE B 61 LEU B 324 PHE B 325 THR B 327
SITE 3 AE5 20 GLY B 328 PRO B 329 TRP B 450 ALA B 454
SITE 4 AE5 20 CLA B 605 CLA B 614 BCR B 619 BCR B 622
SITE 5 AE5 20 PL9 D 405 PHE L 31 PHE L 35 PHE M 14
SITE 1 AE6 17 LEU B 229 THR B 236 SER B 239 SER B 240
SITE 2 AE6 17 ALA B 243 PHE B 463 HIS B 466 ILE B 467
SITE 3 AE6 17 THR B 473 CLA B 611 LEU D 36 PHE D 120
SITE 4 AE6 17 ILE D 123 MET D 126 LEU D 127 ILE D 150
SITE 5 AE6 17 CLA D 403
SITE 1 AE7 16 PHE B 139 VAL B 208 ALA B 212 PHE B 215
SITE 2 AE7 16 HIS B 216 VAL B 219 PRO B 221 PRO B 222
SITE 3 AE7 16 LEU B 229 CLA B 606 CLA B 611 THR H 27
SITE 4 AE7 16 THR H 28 MET H 31 PHE H 34 BCR H 101
SITE 1 AE8 15 LEU B 135 PHE B 139 HIS B 142 LEU B 143
SITE 2 AE8 15 ALA B 146 MET B 231 VAL B 237 SER B 240
SITE 3 AE8 15 SER B 241 CLA B 604 CLA B 606 CLA B 609
SITE 4 AE8 15 CLA B 610 CLA B 613 CLA B 616
SITE 1 AE9 18 TRP B 5 TYR B 6 ARG B 7 VAL B 8
SITE 2 AE9 18 HIS B 9 THR B 10 ILE B 242 LEU B 461
SITE 3 AE9 18 PHE B 462 GLY B 465 TRP B 468 HIS B 469
SITE 4 AE9 18 ARG B 472 CLA B 613 CLA B 614 CLA B 615
SITE 5 AE9 18 LHG B 621 LHG D 407
SITE 1 AF1 16 HIS B 9 LEU B 19 HIS B 23 HIS B 26
SITE 2 AF1 16 THR B 27 ILE B 234 VAL B 237 LEU B 238
SITE 3 AF1 16 SER B 241 CLA B 605 CLA B 606 CLA B 611
SITE 4 AF1 16 CLA B 612 CLA B 614 CLA B 615 CLA B 616
SITE 1 AF2 13 HIS B 9 HIS B 26 VAL B 30 TRP B 33
SITE 2 AF2 13 PHE B 462 CLA B 605 CLA B 608 CLA B 612
SITE 3 AF2 13 CLA B 613 CLA B 615 BCR B 618 BCR B 619
SITE 4 AF2 13 LHG D 407
SITE 1 AF3 17 VAL B 8 HIS B 9 VAL B 11 ALA B 22
SITE 2 AF3 17 MET B 25 LEU B 29 TRP B 115 CLA B 612
SITE 3 AF3 17 CLA B 613 CLA B 614 BCR B 618 GLN L 8
SITE 4 AF3 17 VAL L 10 PHE M 21 LEU M 25 SQD l 101
SITE 5 AF3 17 PHE t 8
SITE 1 AF4 12 ILE B 20 HIS B 23 LEU B 24 MET B 138
SITE 2 AF4 12 HIS B 142 LEU B 145 CLA B 606 CLA B 611
SITE 3 AF4 12 CLA B 613 CLA B 617 LEU H 14 ASN H 15
SITE 1 AF5 8 LEU B 24 TRP B 113 HIS B 114 CLA B 616
SITE 2 AF5 8 BCR B 620 THR H 5 LEU H 7 GLY H 8
SITE 1 AF6 6 MET B 25 LEU B 29 CLA B 614 CLA B 615
SITE 2 AF6 6 BCR B 619 PHE t 19
SITE 1 AF7 10 LEU B 29 GLY B 32 TRP B 33 SER B 36
SITE 2 AF7 10 VAL B 102 GLY B 105 CLA B 608 CLA B 614
SITE 3 AF7 10 BCR B 618 BCR B 622
SITE 1 AF8 4 CLA B 606 CLA B 607 CLA B 617 PHE t 23
SITE 1 AF9 17 SER A 232 ASN A 234 CLA A 614 PRO B 4
SITE 2 AF9 17 TRP B 5 TYR B 6 CLA B 612 TRP D 266
SITE 3 AF9 17 PHE D 273 LHG D 407 LHG D 408 GLU L 11
SITE 4 AF9 17 LEU L 12 ASN L 13 SER L 16 GLY L 20
SITE 5 AF9 17 PHE M 21
SITE 1 AG1 9 TRP B 33 SER B 36 MET B 37 TYR B 40
SITE 2 AG1 9 CLA B 608 BCR B 619 SQD a 402 SQD l 101
SITE 3 AG1 9 PHE t 18
SITE 1 AG2 18 LEU C 95 LEU C 168 GLY C 171 ALA C 172
SITE 2 AG2 18 LEU C 175 ILE C 224 VAL C 233 HIS C 237
SITE 3 AG2 18 ILE C 240 ALA C 278 MET C 282 PHE C 289
SITE 4 AG2 18 TYR C 297 CLA C 502 CLA C 503 CLA C 506
SITE 5 AG2 18 CLA C 507 BCR C 515
SITE 1 AG3 14 TRP C 63 HIS C 91 LEU C 279 MET C 282
SITE 2 AG3 14 ALA C 286 VAL C 290 TYR C 297 HIS C 430
SITE 3 AG3 14 LEU C 433 PHE C 437 CLA C 501 CLA C 503
SITE 4 AG3 14 CLA C 504 CLA C 510
SITE 1 AG4 12 ILE C 60 VAL C 61 ALA C 64 THR C 68
SITE 2 AG4 12 LEU C 88 HIS C 91 VAL C 114 HIS C 118
SITE 3 AG4 12 CLA C 501 CLA C 502 CLA C 509 CLA C 512
SITE 1 AG5 17 TRP C 63 MET C 67 PHE C 70 GLN C 84
SITE 2 AG5 17 GLY C 85 ILE C 87 TRP C 425 SER C 429
SITE 3 AG5 17 PHE C 436 CLA C 502 CLA C 508 CLA C 510
SITE 4 AG5 17 DGD C 517 DGD C 518 LHG D 409 PRO K 26
SITE 5 AG5 17 VAL K 30
SITE 1 AG6 16 PHE A 33 MET A 127 GLY A 128 TRP A 131
SITE 2 AG6 16 PHE C 264 SER C 273 TYR C 274 GLY C 277
SITE 3 AG6 16 ALA C 278 HIS C 441 LEU C 442 ALA C 445
SITE 4 AG6 16 ARG C 449 CLA C 507 BCR C 515 PHE I 23
SITE 1 AG7 16 CLA A 609 LEU C 161 LEU C 165 ILE C 243
SITE 2 AG7 16 GLY C 247 TRP C 250 HIS C 251 THR C 254
SITE 3 AG7 16 THR C 255 PRO C 256 PHE C 257 TRP C 259
SITE 4 AG7 16 PHE C 264 CLA C 501 CLA C 507 BCR C 515
SITE 1 AG8 17 MET C 157 THR C 158 LEU C 161 HIS C 164
SITE 2 AG8 17 LEU C 168 TRP C 259 PHE C 264 TRP C 266
SITE 3 AG8 17 TYR C 271 TYR C 274 SER C 275 MET C 282
SITE 4 AG8 17 CLA C 501 CLA C 505 CLA C 506 CLA C 509
SITE 5 AG8 17 BCR C 515
SITE 1 AG9 20 SQD A 612 TRP C 36 ALA C 37 GLY C 38
SITE 2 AG9 20 ASN C 39 ALA C 40 GLU C 269 LEU C 272
SITE 3 AG9 20 LEU C 276 PHE C 436 PHE C 437 GLY C 440
SITE 4 AG9 20 TRP C 443 HIS C 444 ARG C 447 CLA C 504
SITE 5 AG9 20 CLA C 509 CLA C 510 CLA C 511 LHG D 409
SITE 1 AH1 16 ASN C 39 LEU C 49 ALA C 52 HIS C 53
SITE 2 AH1 16 HIS C 56 TYR C 149 GLY C 268 GLU C 269
SITE 3 AH1 16 TYR C 271 LEU C 272 SER C 275 CLA C 503
SITE 4 AH1 16 CLA C 507 CLA C 508 CLA C 510 CLA C 511
SITE 1 AH2 15 ASN C 39 HIS C 56 LEU C 59 TRP C 63
SITE 2 AH2 15 LEU C 279 PHE C 436 PHE C 437 CLA C 502
SITE 3 AH2 15 CLA C 504 CLA C 508 CLA C 509 CLA C 511
SITE 4 AH2 15 LHG D 409 PRO K 29 LEU K 33
SITE 1 AH3 27 THR C 24 ARG C 26 TRP C 35 GLY C 38
SITE 2 AH3 27 ASN C 39 ARG C 41 LEU C 42 LEU C 45
SITE 3 AH3 27 LYS C 48 ALA C 52 PHE C 127 ILE C 134
SITE 4 AH3 27 CLA C 508 CLA C 509 CLA C 510 PHE K 32
SITE 5 AH3 27 LEU K 33 ALA K 36 TRP K 39 GLN K 40
SITE 6 AH3 27 BCR K 101 LEU Y 39 ASN Y 45 LEU Y 46
SITE 7 AH3 27 VAL Z 20 VAL Z 23 ALA Z 28
SITE 1 AH4 12 HIS C 53 ALA C 57 LEU C 125 PHE C 146
SITE 2 AH4 12 PHE C 147 PHE C 163 HIS C 164 VAL C 167
SITE 3 AH4 12 GLY C 171 CLA C 503 CLA C 513 BCR C 514
SITE 1 AH5 10 LEU C 50 VAL C 124 GLY C 128 TYR C 131
SITE 2 AH5 10 HIS C 132 PRO C 137 TYR C 143 PHE C 147
SITE 3 AH5 10 CLA C 512 BCR C 514
SITE 1 AH6 10 PHE C 112 VAL C 116 SER C 121 VAL C 124
SITE 2 AH6 10 PHE C 147 CLA C 512 CLA C 513 TYR K 15
SITE 3 AH6 10 VAL Z 51 GLY Z 55
SITE 1 AH7 11 ILE C 209 LEU C 213 ILE C 224 GLY C 236
SITE 2 AH7 11 HIS C 237 PHE C 264 CLA C 501 CLA C 505
SITE 3 AH7 11 CLA C 506 CLA C 507 PHE I 23
SITE 1 AH8 19 LEU A 91 SER A 148 ILE A 163 PRO C 217
SITE 2 AH8 19 GLY C 219 GLY C 220 GLU C 221 GLY C 222
SITE 3 AH8 19 TRP C 223 VAL C 227 PHE C 284 CYS C 288
SITE 4 AH8 19 PHE C 292 ASN C 293 ASN C 294 THR C 295
SITE 5 AH8 19 ASP C 360 PHE C 361 ARG C 362
SITE 1 AH9 15 HIS A 195 PHE A 197 GLU C 83 GLN C 84
SITE 2 AH9 15 GLY C 85 LEU C 404 SER C 406 ASN C 418
SITE 3 AH9 15 PHE C 419 VAL C 420 TRP C 425 CLA C 504
SITE 4 AH9 15 DGD C 518 PHE J 29 TYR J 33
SITE 1 AI1 19 GLN A 199 PHE A 300 ASN A 301 PHE A 302
SITE 2 AI1 19 SER A 305 ASN C 405 VAL C 407 ASN C 415
SITE 3 AI1 19 SER C 416 ASN C 418 CLA C 504 DGD C 517
SITE 4 AI1 19 LHG D 409 PHE J 29 ALA J 32 TYR J 33
SITE 5 AI1 19 GLY J 37 SER J 38 SER J 39
SITE 1 AI2 21 PHE A 206 ALA A 209 LEU A 210 MET A 214
SITE 2 AI2 21 LEU A 258 CLA A 607 PL9 A 611 ALA D 41
SITE 3 AI2 21 LEU D 45 TRP D 48 ILE D 114 GLY D 121
SITE 4 AI2 21 LEU D 122 PHE D 125 GLN D 129 ASN D 142
SITE 5 AI2 21 PHE D 146 PRO D 149 GLY D 174 LEU D 279
SITE 6 AI2 21 CLA D 402
SITE 1 AI3 23 MET A 183 PHE A 206 CLA A 606 CLA A 607
SITE 2 AI3 23 CLA A 614 PRO D 149 VAL D 152 SER D 155
SITE 3 AI3 23 VAL D 156 PHE D 181 LEU D 182 PHE D 185
SITE 4 AI3 23 GLN D 186 TRP D 191 THR D 192 HIS D 197
SITE 5 AI3 23 GLY D 200 VAL D 204 LEU D 205 SER D 282
SITE 6 AI3 23 ALA D 283 VAL D 286 PHO D 401
SITE 1 AI4 18 CLA B 609 ILE D 35 LEU D 36 PRO D 39
SITE 2 AI4 18 CYS D 40 LEU D 43 LEU D 89 LEU D 90
SITE 3 AI4 18 LEU D 91 LEU D 92 TRP D 93 TRP D 104
SITE 4 AI4 18 THR D 112 PHE D 113 LEU D 116 HIS D 117
SITE 5 AI4 18 GLY X 13 ALA X 18
SITE 1 AI5 10 TYR D 42 LEU D 43 GLY D 46 GLY D 47
SITE 2 AI5 10 LEU D 49 THR D 50 PRO F 29 THR F 30
SITE 3 AI5 10 VAL J 21 VAL J 25
SITE 1 AI6 21 PHE A 52 ILE A 53 CLA A 614 CLA B 608
SITE 2 AI6 21 MET D 198 MET D 199 ALA D 202 HIS D 214
SITE 3 AI6 21 THR D 217 TRP D 253 ALA D 260 PHE D 261
SITE 4 AI6 21 LEU D 267 PHE D 270 PHE D 273 VAL D 274
SITE 5 AI6 21 LHG D 408 LEU L 23 VAL L 26 LEU L 29
SITE 6 AI6 21 PHE T 10
SITE 1 AI7 6 GLY D 99 ASP D 100 PHE D 101 THR D 102
SITE 2 AI7 6 PHE E 37 ASP E 45
SITE 1 AI8 18 SER A 232 ASN A 234 TRP B 5 TYR B 6
SITE 2 AI8 18 ARG B 7 LEU B 461 PHE B 464 TRP B 468
SITE 3 AI8 18 CLA B 612 CLA B 614 LHG B 621 TYR D 141
SITE 4 AI8 18 ILE D 144 TRP D 266 PHE D 269 THR D 277
SITE 5 AI8 18 LEU L 23 ILE L 24
SITE 1 AI9 20 MET A 37 PHO A 608 LHG B 621 ILE D 256
SITE 2 AI9 20 PHE D 257 ALA D 260 PHE D 261 SER D 262
SITE 3 AI9 20 ASN D 263 TRP D 266 PHE D 270 PL9 D 405
SITE 4 AI9 20 ASN L 13 THR L 15 SER L 16 TYR L 18
SITE 5 AI9 20 LEU L 19 PHE T 10 PHE T 17 ALA T 20
SITE 1 AJ1 18 ARG A 140 TRP A 142 PHE A 273 SQD A 612
SITE 2 AJ1 18 PHE C 33 TRP C 36 TRP C 443 ARG C 447
SITE 3 AJ1 18 CLA C 504 CLA C 508 CLA C 510 DGD C 518
SITE 4 AJ1 18 GLU D 219 ASN D 220 ALA D 229 SER D 230
SITE 5 AJ1 18 THR D 231 PHE D 232
SITE 1 AJ2 13 PHE E 10 ARG E 18 TYR E 19 HIS E 23
SITE 2 AJ2 13 THR E 26 ILE E 27 LEU E 30 ARG F 19
SITE 3 AJ2 13 TRP F 20 VAL F 23 HIS F 24 ALA F 27
SITE 4 AJ2 13 ILE F 31
SITE 1 AJ3 7 ARG D 24 ARG D 26 PHE F 16 THR F 17
SITE 2 AJ3 7 VAL F 18 ILE X 31 ASP X 35
SITE 1 AJ4 1 ARG F 45
SITE 1 AJ5 6 CLA B 602 CLA B 603 CLA B 610 PHE H 34
SITE 2 AJ5 6 MET H 35 PHE H 38
SITE 1 AJ6 18 TYR B 193 PHE B 250 TYR B 258 TYR B 273
SITE 2 AJ6 18 GLN B 274 SER B 277 TYR B 279 CLA B 603
SITE 3 AJ6 18 HIS D 87 LEU D 162 GLY D 163 LEU D 291
SITE 4 AJ6 18 LEU H 46 TYR H 49 ASN H 50 VAL H 60
SITE 5 AJ6 18 SER H 61 TRP H 62
SITE 1 AJ7 10 ALA C 55 GLY C 58 LEU C 59 SER C 122
SITE 2 AJ7 10 GLY C 126 CLA C 511 TYR K 15 PHE K 32
SITE 3 AJ7 10 BCR Y 101 SER Z 16
SITE 1 AJ8 12 ARG L 14 TYR L 18 LEU M 16 CYS T 12
SITE 2 AJ8 12 PHE T 19 PHE T 23 BCR T 102 ARG b 18
SITE 3 AJ8 12 SER b 104 PHE b 108 TRP b 115 ARG l 7
SITE 1 AJ9 3 THR O 138 ASN O 200 VAL O 201
SITE 1 AK1 6 SQD A 613 PHE T 18 TRP b 33 MET b 37
SITE 2 AK1 6 TYR b 40 BCR b 618
SITE 1 AK2 8 SQD L 101 PHE T 19 MET b 25 TRP b 115
SITE 2 AK2 8 CLA b 608 CLA b 614 CLA b 615 BCR b 618
SITE 1 AK3 20 ALA V 36 CYS V 37 CYS V 40 HIS V 41
SITE 2 AK3 20 THR V 46 THR V 48 LEU V 52 ASP V 53
SITE 3 AK3 20 LEU V 54 THR V 58 LEU V 59 ALA V 62
SITE 4 AK3 20 LEU V 72 TYR V 75 MET V 76 TYR V 82
SITE 5 AK3 20 ILE V 88 HIS V 92 PRO V 93 ILE V 115
SITE 1 AK4 14 PHE C 62 THR J 15 GLY J 18 MET J 19
SITE 2 AK4 14 LEU K 31 ALA K 34 PHE K 37 VAL K 38
SITE 3 AK4 14 BCR K 101 ILE Y 28 GLY Y 29 GLY Y 32
SITE 4 AK4 14 PRO Y 33 PHE Z 17
SITE 1 AK5 11 ASP a 61 ASP a 170 VAL a 185 GLU a 189
SITE 2 AK5 11 HIS a 332 GLU a 333 HIS a 337 ASP a 342
SITE 3 AK5 11 ALA a 344 GLU c 354 ARG c 357
SITE 1 AK6 11 TRP B 113 TYR B 117 CLA B 607 BCR B 622
SITE 2 AK6 11 TRP a 20 ASN a 26 ARG a 27 LEU a 28
SITE 3 AK6 11 LEU a 42 THR a 45 PHE t 22
SITE 1 AK7 5 HIS a 215 HIS a 272 BCT a 414 HIS d 214
SITE 2 AK7 5 HIS d 268
SITE 1 AK8 4 ASN a 181 HIS a 332 GLU a 333 LYS d 317
SITE 1 AK9 5 HIS a 337 ASN a 338 PHE a 339 GLY c 353
SITE 2 AK9 5 GLU c 354
SITE 1 AL1 19 TYR a 147 PRO a 150 SER a 153 VAL a 157
SITE 2 AL1 19 MET a 183 PHE a 186 GLN a 187 HIS a 198
SITE 3 AL1 19 GLY a 201 PHE a 206 ALA a 286 ALA a 287
SITE 4 AL1 19 ILE a 290 LEU d 182 LEU d 205 CLA d 401
SITE 5 AL1 19 PHO d 402 CLA d 403 PHE t 17
SITE 1 AL2 13 GLN a 199 VAL a 202 ALA a 203 PHE a 206
SITE 2 AL2 13 GLY a 207 LEU a 210 TRP a 278 PHO a 412
SITE 3 AL2 13 PHE d 157 VAL d 175 ILE d 178 PHE d 179
SITE 4 AL2 13 CLA d 403
SITE 1 AL3 20 ILE a 36 THR a 40 PHE a 93 PRO a 95
SITE 2 AL3 20 ILE a 96 TRP a 97 GLN a 113 LEU a 114
SITE 3 AL3 20 HIS a 118 LEU a 121 BCR a 409 CLA c 906
SITE 4 AL3 20 CLA c 907 VAL i 8 TYR i 9 VAL i 11
SITE 5 AL3 20 VAL i 12 THR i 13 PHE i 15 PHE i 19
SITE 1 AL4 4 ALA a 43 ILE a 50 ILE a 96 CLA a 408
SITE 1 AL5 19 PHE a 211 MET a 214 HIS a 215 LEU a 218
SITE 2 AL5 19 HIS a 252 PHE a 255 ALA a 263 SER a 264
SITE 3 AL5 19 PHE a 265 LEU a 271 PHE a 274 LHG a 413
SITE 4 AL5 19 TYR d 42 SQD d 407 VAL f 18 ALA f 22
SITE 5 AL5 19 THR f 25 THR x 24 LEU x 28
SITE 1 AL6 14 LEU a 200 GLY a 204 PHE a 265 ASN a 267
SITE 2 AL6 14 SER a 270 PHE a 273 TRP a 278 GLN c 28
SITE 3 AL6 14 ALA c 34 TRP c 36 CLA c 909 PHE d 232
SITE 4 AL6 14 ARG d 233 LHG d 410
SITE 1 AL7 21 PHE a 206 ALA a 209 LEU a 210 MET a 214
SITE 2 AL7 21 CLA a 407 ALA d 41 TRP d 48 ILE d 114
SITE 3 AL7 21 GLY d 121 LEU d 122 PHE d 125 GLN d 129
SITE 4 AL7 21 ASN d 142 ALA d 145 PHE d 146 PRO d 149
SITE 5 AL7 21 PHE d 153 GLY d 174 PRO d 275 LEU d 279
SITE 6 AL7 21 CLA d 403
SITE 1 AL8 13 LEU a 258 ILE a 259 PHE a 260 TYR a 262
SITE 2 AL8 13 PL9 a 410 PHE d 27 THR e 4 THR e 5
SITE 3 AL8 13 GLU e 7 PRO e 9 PHE e 10 SER e 11
SITE 4 AL8 13 ARG f 19
SITE 1 AL9 7 HIS a 215 GLU a 244 HIS a 272 FE2 a 403
SITE 2 AL9 7 HIS d 214 TYR d 244 HIS d 268
SITE 1 AM1 1 ASN b 438
SITE 1 AM2 6 TRP b 185 GLY b 186 PHE b 190 CLA b 603
SITE 2 AM2 6 PHE h 41 BCR h 101
SITE 1 AM3 19 GLY b 189 PHE b 190 PRO b 192 GLY b 197
SITE 2 AM3 19 HIS b 201 ALA b 204 VAL b 208 PHE b 246
SITE 3 AM3 19 PHE b 247 PHE b 250 VAL b 251 CLA b 602
SITE 4 AM3 19 CLA b 604 CLA b 606 PHE h 38 PHE h 41
SITE 5 AM3 19 ILE h 45 LEU h 46 TYR h 49
SITE 1 AM4 12 ARG b 68 LEU b 69 ALA b 146 PHE b 153
SITE 2 AM4 12 HIS b 201 HIS b 202 VAL b 252 THR b 262
SITE 3 AM4 12 CLA b 603 CLA b 605 CLA b 606 CLA b 607
SITE 1 AM5 21 TRP b 33 PHE b 61 PHE b 65 ARG b 68
SITE 2 AM5 21 LEU b 149 VAL b 245 ALA b 248 ALA b 249
SITE 3 AM5 21 VAL b 252 PHE b 451 HIS b 455 PHE b 458
SITE 4 AM5 21 PHE b 462 CLA b 604 CLA b 606 CLA b 607
SITE 5 AM5 21 CLA b 608 CLA b 612 CLA b 613 CLA b 614
SITE 6 AM5 21 CLA b 616
SITE 1 AM6 18 THR b 27 TRP b 33 ALA b 34 VAL b 62
SITE 2 AM6 18 PHE b 65 MET b 66 ARG b 68 LEU b 69
SITE 3 AM6 18 VAL b 96 HIS b 100 ALA b 205 CLA b 603
SITE 4 AM6 18 CLA b 604 CLA b 605 CLA b 607 CLA b 611
SITE 5 AM6 18 CLA b 616 BCR b 619
SITE 1 AM7 13 LEU b 69 GLY b 70 TRP b 91 VAL b 96
SITE 2 AM7 13 VAL b 102 HIS b 157 PHE b 162 GLY b 163
SITE 3 AM7 13 PRO b 164 CLA b 604 CLA b 605 CLA b 606
SITE 4 AM7 13 BCR b 619
SITE 1 AM8 21 BCR T 102 TRP b 33 MET b 37 TYR b 40
SITE 2 AM8 21 GLN b 58 GLY b 59 PHE b 61 LEU b 324
SITE 3 AM8 21 PHE b 325 THR b 327 GLY b 328 PRO b 329
SITE 4 AM8 21 TRP b 450 PHE b 451 ALA b 454 CLA b 605
SITE 5 AM8 21 CLA b 614 BCR b 618 PL9 d 405 PHE l 31
SITE 6 AM8 21 PHE m 14
SITE 1 AM9 16 THR b 236 SER b 239 SER b 240 ALA b 243
SITE 2 AM9 16 PHE b 463 HIS b 466 ILE b 467 THR b 473
SITE 3 AM9 16 LEU b 474 CLA b 611 PHE d 120 ILE d 123
SITE 4 AM9 16 MET d 126 LEU d 127 ILE d 150 CLA d 404
SITE 1 AN1 14 PHE b 139 VAL b 208 ALA b 212 PHE b 215
SITE 2 AN1 14 HIS b 216 VAL b 219 PRO b 221 PRO b 222
SITE 3 AN1 14 LEU b 229 CLA b 611 THR h 27 MET h 31
SITE 4 AN1 14 PHE h 34 BCR h 101
SITE 1 AN2 14 LEU b 135 MET b 138 PHE b 139 HIS b 142
SITE 2 AN2 14 LEU b 143 MET b 231 VAL b 237 SER b 240
SITE 3 AN2 14 SER b 241 CLA b 606 CLA b 609 CLA b 610
SITE 4 AN2 14 CLA b 613 CLA b 616
SITE 1 AN3 21 TRP b 5 TYR b 6 ARG b 7 VAL b 8
SITE 2 AN3 21 HIS b 9 THR b 10 LEU b 238 ILE b 242
SITE 3 AN3 21 LEU b 461 PHE b 462 GLY b 465 TRP b 468
SITE 4 AN3 21 HIS b 469 ARG b 472 CLA b 605 CLA b 613
SITE 5 AN3 21 CLA b 614 CLA b 615 LHG b 620 LHG d 408
SITE 6 AN3 21 PHE m 21
SITE 1 AN4 16 HIS b 9 LEU b 19 HIS b 23 HIS b 26
SITE 2 AN4 16 THR b 27 ILE b 234 VAL b 237 LEU b 238
SITE 3 AN4 16 SER b 241 ILE b 242 CLA b 605 CLA b 611
SITE 4 AN4 16 CLA b 612 CLA b 614 CLA b 615 CLA b 616
SITE 1 AN5 12 BCR T 102 HIS b 9 HIS b 26 VAL b 30
SITE 2 AN5 12 TRP b 33 PHE b 462 CLA b 605 CLA b 608
SITE 3 AN5 12 CLA b 612 CLA b 613 CLA b 615 LHG d 408
SITE 1 AN6 14 BCR T 102 VAL b 8 HIS b 9 VAL b 11
SITE 2 AN6 14 MET b 25 LEU b 29 TRP b 115 CLA b 612
SITE 3 AN6 14 CLA b 613 CLA b 614 VAL l 10 LEU m 13
SITE 4 AN6 14 PHE m 21 LEU m 25
SITE 1 AN7 13 ILE b 20 HIS b 23 MET b 138 HIS b 142
SITE 2 AN7 13 LEU b 145 CLA b 605 CLA b 606 CLA b 611
SITE 3 AN7 13 CLA b 613 CLA b 617 LEU h 7 LEU h 14
SITE 4 AN7 13 ASN h 15
SITE 1 AN8 9 LEU b 24 TRP b 113 HIS b 114 LEU b 120
SITE 2 AN8 9 CLA b 616 BCR b 619 THR h 5 LEU h 7
SITE 3 AN8 9 GLY h 8
SITE 1 AN9 9 BCR T 101 BCR T 102 LEU b 29 GLY b 32
SITE 2 AN9 9 TRP b 33 SER b 36 VAL b 102 GLY b 105
SITE 3 AN9 9 CLA b 608
SITE 1 AO1 6 SQD A 613 PHE T 18 PHE T 22 CLA b 606
SITE 2 AO1 6 CLA b 607 CLA b 617
SITE 1 AO2 18 SER a 232 ASN a 234 PRO b 4 TRP b 5
SITE 2 AO2 18 TYR b 6 CLA b 612 TRP d 266 PHE d 273
SITE 3 AO2 18 CLA d 401 LHG d 408 LHG d 409 GLU l 11
SITE 4 AO2 18 LEU l 12 ASN l 13 SER l 16 GLY l 20
SITE 5 AO2 18 PRO m 18 PHE m 21
SITE 1 AO3 5 PHE c 22 THR c 24 ASP c 27 GLU c 29
SITE 2 AO3 5 SER c 30
SITE 1 AO4 17 LEU c 95 LEU c 168 GLY c 171 ALA c 172
SITE 2 AO4 17 ILE c 224 VAL c 233 HIS c 237 ILE c 240
SITE 3 AO4 17 ALA c 278 MET c 282 PHE c 289 VAL c 296
SITE 4 AO4 17 TYR c 297 CLA c 903 CLA c 904 CLA c 907
SITE 5 AO4 17 BCR c 915
SITE 1 AO5 17 TRP c 63 ILE c 87 HIS c 91 LEU c 174
SITE 2 AO5 17 LEU c 279 MET c 282 ALA c 286 VAL c 290
SITE 3 AO5 17 TYR c 297 HIS c 430 LEU c 433 PHE c 437
SITE 4 AO5 17 CLA c 902 CLA c 904 CLA c 905 CLA c 911
SITE 5 AO5 17 CLA c 913
SITE 1 AO6 11 ILE c 60 VAL c 61 ALA c 64 THR c 68
SITE 2 AO6 11 LEU c 88 HIS c 91 VAL c 114 HIS c 118
SITE 3 AO6 11 CLA c 902 CLA c 903 CLA c 910
SITE 1 AO7 17 TRP c 63 MET c 67 PHE c 70 GLN c 84
SITE 2 AO7 17 GLY c 85 ILE c 87 TRP c 425 SER c 429
SITE 3 AO7 17 PHE c 436 CLA c 903 CLA c 909 CLA c 911
SITE 4 AO7 17 DGD c 917 LHG d 410 DGD j 101 PRO k 26
SITE 5 AO7 17 VAL k 30
SITE 1 AO8 21 PHE a 33 LEU a 121 SER a 124 CYS a 125
SITE 2 AO8 21 MET a 127 GLY a 128 TRP a 131 CLA a 408
SITE 3 AO8 21 PHE c 264 SER c 273 TYR c 274 GLY c 277
SITE 4 AO8 21 ALA c 278 MET c 281 HIS c 441 LEU c 442
SITE 5 AO8 21 ALA c 445 ARG c 449 CLA c 908 BCR c 915
SITE 6 AO8 21 PHE i 23
SITE 1 AO9 16 CLA a 408 LEU c 161 LEU c 165 ILE c 243
SITE 2 AO9 16 GLY c 247 TRP c 250 HIS c 251 THR c 254
SITE 3 AO9 16 THR c 255 PRO c 256 PHE c 257 TRP c 259
SITE 4 AO9 16 PHE c 264 CLA c 902 CLA c 908 BCR c 915
SITE 1 AP1 16 MET c 157 THR c 158 LEU c 161 HIS c 164
SITE 2 AP1 16 LEU c 168 PHE c 264 TRP c 266 TYR c 271
SITE 3 AP1 16 TYR c 274 SER c 275 LEU c 279 MET c 282
SITE 4 AP1 16 CLA c 906 CLA c 907 CLA c 910 BCR c 915
SITE 1 AP2 18 SQD a 411 TRP c 36 ALA c 37 GLY c 38
SITE 2 AP2 18 ASN c 39 ALA c 40 LEU c 276 PHE c 436
SITE 3 AP2 18 PHE c 437 GLY c 440 TRP c 443 HIS c 444
SITE 4 AP2 18 ARG c 447 CLA c 905 CLA c 910 CLA c 911
SITE 5 AP2 18 CLA c 912 LHG d 410
SITE 1 AP3 19 ASN c 39 LEU c 49 ALA c 52 HIS c 53
SITE 2 AP3 19 HIS c 56 TYR c 149 TRP c 151 GLY c 268
SITE 3 AP3 19 GLU c 269 TYR c 271 LEU c 272 SER c 275
SITE 4 AP3 19 LEU c 276 CLA c 904 CLA c 908 CLA c 909
SITE 5 AP3 19 CLA c 911 CLA c 912 CLA c 913
SITE 1 AP4 16 ASN c 39 HIS c 56 LEU c 59 TRP c 63
SITE 2 AP4 16 LEU c 279 PHE c 436 PHE c 437 CLA c 903
SITE 3 AP4 16 CLA c 905 CLA c 909 CLA c 910 CLA c 912
SITE 4 AP4 16 LHG d 410 PRO k 29 VAL k 30 LEU k 33
SITE 1 AP5 26 ARG c 26 TRP c 35 GLY c 38 ASN c 39
SITE 2 AP5 26 ARG c 41 LEU c 42 LEU c 45 LYS c 48
SITE 3 AP5 26 ALA c 52 ALA c 123 PHE c 127 ILE c 134
SITE 4 AP5 26 CLA c 909 CLA c 910 CLA c 911 PHE k 32
SITE 5 AP5 26 LEU k 33 ALA k 36 TRP k 39 GLN k 40
SITE 6 AP5 26 BCR k 102 ILE y 35 ILE y 36 LEU y 39
SITE 7 AP5 26 VAL z 20 ALA z 28
SITE 1 AP6 14 HIS c 53 ALA c 57 LEU c 125 PHE c 146
SITE 2 AP6 14 PHE c 147 TYR c 149 PHE c 163 HIS c 164
SITE 3 AP6 14 VAL c 167 GLY c 171 CLA c 903 CLA c 910
SITE 4 AP6 14 CLA c 914 BCR c 918
SITE 1 AP7 9 LEU c 50 VAL c 124 GLY c 128 TYR c 131
SITE 2 AP7 9 HIS c 132 TYR c 143 PHE c 147 CLA c 913
SITE 3 AP7 9 BCR c 918
SITE 1 AP8 12 ILE c 209 LEU c 213 GLY c 236 HIS c 237
SITE 2 AP8 12 ILE c 240 PHE c 264 CLA c 902 CLA c 906
SITE 3 AP8 12 CLA c 907 CLA c 908 PHE i 23 LEU i 24
SITE 1 AP9 21 LEU a 91 SER a 148 PHE a 155 ILE a 163
SITE 2 AP9 21 PRO c 217 PHE c 218 GLY c 219 GLY c 220
SITE 3 AP9 21 GLU c 221 GLY c 222 TRP c 223 VAL c 227
SITE 4 AP9 21 MET c 281 CYS c 288 PHE c 292 ASN c 293
SITE 5 AP9 21 ASN c 294 THR c 295 ASP c 360 PHE c 361
SITE 6 AP9 21 ARG c 362
SITE 1 AQ1 13 PHE a 197 GLU c 83 GLN c 84 GLY c 85
SITE 2 AQ1 13 SER c 406 ASN c 418 PHE c 419 VAL c 420
SITE 3 AQ1 13 TRP c 425 THR c 428 CLA c 905 TYR j 33
SITE 4 AQ1 13 DGD j 101
SITE 1 AQ2 12 PHE c 112 VAL c 116 ILE c 120 SER c 121
SITE 2 AQ2 12 VAL c 124 CLA c 913 CLA c 914 TYR k 15
SITE 3 AQ2 12 VAL z 51 GLY z 55 ASN z 58 PHE z 59
SITE 1 AQ3 17 VAL a 157 MET a 172 ILE a 176 THR a 179
SITE 2 AQ3 17 PHE a 180 MET a 183 CLA a 406 LHG b 620
SITE 3 AQ3 17 MET d 198 VAL d 201 ALA d 202 LEU d 205
SITE 4 AQ3 17 GLY d 206 PHO d 402 CLA d 403 PL9 d 405
SITE 5 AQ3 17 LEU l 30
SITE 1 AQ4 19 LEU a 41 ALA a 44 THR a 45 PHE a 48
SITE 2 AQ4 19 TYR a 126 GLN a 130 ALA a 146 TYR a 147
SITE 3 AQ4 19 PRO a 150 PRO a 279 CLA a 406 LEU d 205
SITE 4 AQ4 19 ALA d 208 LEU d 209 ILE d 213 TRP d 253
SITE 5 AQ4 19 PHE d 257 CLA d 401 LHG d 409
SITE 1 AQ5 23 MET a 183 PHE a 206 CLA a 406 CLA a 407
SITE 2 AQ5 23 PHO a 412 PRO d 149 VAL d 152 SER d 155
SITE 3 AQ5 23 VAL d 156 PHE d 181 LEU d 182 PHE d 185
SITE 4 AQ5 23 GLN d 186 TRP d 191 THR d 192 HIS d 197
SITE 5 AQ5 23 GLY d 200 VAL d 204 LEU d 205 SER d 282
SITE 6 AQ5 23 ALA d 283 VAL d 286 CLA d 401
SITE 1 AQ6 20 CLA b 609 ILE d 35 PRO d 39 CYS d 40
SITE 2 AQ6 20 LEU d 43 LEU d 89 LEU d 90 LEU d 91
SITE 3 AQ6 20 LEU d 92 TRP d 93 TRP d 104 THR d 112
SITE 4 AQ6 20 PHE d 113 LEU d 116 HIS d 117 VAL h 33
SITE 5 AQ6 20 GLY x 13 LEU x 14 GLY x 17 ALA x 18
SITE 1 AQ7 18 PHE a 52 ILE a 53 CLA b 608 MET d 198
SITE 2 AQ7 18 MET d 199 ALA d 202 HIS d 214 THR d 217
SITE 3 AQ7 18 TRP d 253 ALA d 260 PHE d 261 LEU d 267
SITE 4 AQ7 18 CLA d 401 LHG d 409 LEU l 23 VAL l 26
SITE 5 AQ7 18 LEU l 29 PHE t 10
SITE 1 AQ8 5 GLY d 99 PHE d 101 THR d 102 ASP e 45
SITE 2 AQ8 5 LEU e 80
SITE 1 AQ9 11 PL9 a 410 ARG d 24 ARG d 26 ILE f 15
SITE 2 AQ9 11 PHE f 16 THR f 17 VAL f 18 VAL f 21
SITE 3 AQ9 11 VAL x 27 ILE x 31 ASP x 35
SITE 1 AR1 16 SER a 232 ASN a 234 TRP b 5 TYR b 6
SITE 2 AR1 16 ARG b 7 LEU b 461 PHE b 464 TRP b 468
SITE 3 AR1 16 CLA b 612 CLA b 614 LHG b 620 TYR d 141
SITE 4 AR1 16 ILE d 144 TRP d 266 PHE d 269 THR d 277
SITE 1 AR2 19 MET a 37 LHG b 620 ILE d 256 PHE d 257
SITE 2 AR2 19 ALA d 260 PHE d 261 SER d 262 ASN d 263
SITE 3 AR2 19 TRP d 266 PHE d 270 PHO d 402 PL9 d 405
SITE 4 AR2 19 ASN l 13 THR l 15 SER l 16 TYR l 18
SITE 5 AR2 19 LEU l 19 PHE t 17 ALA t 20
SITE 1 AR3 20 ARG a 140 TRP a 142 PHE a 273 TRP a 284
SITE 2 AR3 20 PHE a 285 SQD a 411 PHE c 33 TRP c 36
SITE 3 AR3 20 TRP c 443 ARG c 447 CLA c 905 CLA c 909
SITE 4 AR3 20 CLA c 911 GLU d 219 ASN d 220 ALA d 229
SITE 5 AR3 20 SER d 230 THR d 231 PHE d 232 DGD j 101
SITE 1 AR4 13 ILE e 13 ARG e 18 TYR e 19 HIS e 23
SITE 2 AR4 13 THR e 26 ILE e 27 LEU e 30 ARG f 19
SITE 3 AR4 13 TRP f 20 VAL f 23 HIS f 24 ALA f 27
SITE 4 AR4 13 ILE f 31
SITE 1 AR5 12 TYR d 42 LEU d 43 GLY d 46 GLY d 47
SITE 2 AR5 12 LEU d 49 THR d 50 PHE d 101 PRO f 29
SITE 3 AR5 12 THR f 30 PHE f 33 VAL j 21 VAL j 25
SITE 1 AR6 2 ARG f 45 GLU v 23
SITE 1 AR7 7 CLA b 602 CLA b 610 PHE h 34 LEU h 37
SITE 2 AR7 7 PHE h 38 PHE h 41 ILE x 3
SITE 1 AR8 16 TYR b 193 PHE b 250 TYR b 258 TYR b 273
SITE 2 AR8 16 GLN b 274 SER b 277 TYR b 279 GLY d 86
SITE 3 AR8 16 HIS d 87 LEU d 162 GLY d 163 TYR h 49
SITE 4 AR8 16 ASN h 50 VAL h 60 SER h 61 TRP h 62
SITE 1 AR9 20 GLN a 199 LEU a 200 PHE a 300 ASN a 301
SITE 2 AR9 20 PHE a 302 SER a 305 ASN c 405 ASN c 415
SITE 3 AR9 20 SER c 416 ASN c 418 CLA c 905 DGD c 917
SITE 4 AR9 20 LHG d 410 PHE j 29 ALA j 32 TYR j 33
SITE 5 AR9 20 GLY j 37 SER j 38 SER j 39 GLN v 34
SITE 1 AS1 4 GLY j 31 ALA j 34 GLY j 35 LEU j 36
SITE 1 AS2 14 PHE c 62 LEU c 119 ALA j 14 THR j 15
SITE 2 AS2 14 MET j 19 ILE k 28 LEU k 31 PHE k 32
SITE 3 AS2 14 ALA k 34 PHE k 37 VAL k 38 BCR k 102
SITE 4 AS2 14 ILE y 28 GLY y 29
SITE 1 AS3 9 ALA c 55 GLY c 58 LEU c 59 SER c 122
SITE 2 AS3 9 CLA c 912 PHE k 32 TRP k 39 BCR k 101
SITE 3 AS3 9 SER z 16
SITE 1 AS4 13 ARG B 18 SER B 104 TRP B 115 CLA B 615
SITE 2 AS4 13 BCR B 622 ARG L 7 ARG l 14 TYR l 18
SITE 3 AS4 13 LEU l 21 VAL m 15 LEU m 16 TYR m 26
SITE 4 AS4 13 PHE t 23
SITE 1 AS5 3 THR o 138 ASN o 200 VAL o 201
SITE 1 AS6 19 ALA v 36 CYS v 37 CYS v 40 HIS v 41
SITE 2 AS6 19 THR v 46 THR v 48 LEU v 52 ASP v 53
SITE 3 AS6 19 LEU v 54 THR v 58 LEU v 59 LEU v 72
SITE 4 AS6 19 TYR v 75 MET v 76 TYR v 82 ILE v 88
SITE 5 AS6 19 HIS v 92 PRO v 93 MET v 104
SITE 1 AS7 6 GLN O 36 TYR O 38 PRO O 245 ALA O 246
SITE 2 AS7 6 ASN c 19 SER c 20
SITE 1 AS8 6 GLN O 36 TYR O 38 PRO O 245 ALA O 246
SITE 2 AS8 6 ASN c 19 SER c 20
SITE 1 AS9 6 GLN O 36 TYR O 38 PRO O 245 ALA O 246
SITE 2 AS9 6 ASN c 19 SER c 20
SITE 1 AT1 9 ASP O 33 SER O 34 SER O 35 THR O 37
SITE 2 AT1 9 TYR O 38 ALA O 246 ASN c 19 SER c 20
SITE 3 AT1 9 ALA c 23
SITE 1 AT2 9 ASP O 33 SER O 34 SER O 35 THR O 37
SITE 2 AT2 9 TYR O 38 ALA O 246 ASN c 19 SER c 20
SITE 3 AT2 9 ALA c 23
CRYST1 133.250 226.260 307.090 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 0.007505 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004420 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003256 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
