HEADER ELECTRON TRANSPORT,PHOTOSYNTHESIS 04-JUN-14 4TNK
TITLE RT XFEL STRUCTURE OF PHOTOSYSTEM II 250 MICROSEC AFTER THE THIRD
TITLE 2 ILLUMINATION AT 5.2 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOTOSYSTEM Q(B) PROTEIN 1;
COMPND 3 CHAIN: A, a;
COMPND 4 FRAGMENT: UNP RESIDUES 1-344;
COMPND 5 SYNONYM: 32 KDA THYLAKOID MEMBRANE PROTEIN 1,PHOTOSYSTEM II PROTEIN
COMPND 6 D1 1;
COMPND 7 EC: 1.10.3.9;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PHOTOSYSTEM II CORE LIGHT HARVESTING PROTEIN;
COMPND 10 CHAIN: B, b;
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;
COMPND 18 EC: 1.10.3.9;
COMPND 19 MOL_ID: 5;
COMPND 20 MOLECULE: CYTOCHROME B559 SUBUNIT ALPHA;
COMPND 21 CHAIN: E, e;
COMPND 22 SYNONYM: PSII REACTION CENTER SUBUNIT V;
COMPND 23 MOL_ID: 6;
COMPND 24 MOLECULE: CYTOCHROME B559 SUBUNIT BETA;
COMPND 25 CHAIN: F, f;
COMPND 26 SYNONYM: PSII REACTION CENTER SUBUNIT VI;
COMPND 27 MOL_ID: 7;
COMPND 28 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN H;
COMPND 29 CHAIN: H, h;
COMPND 30 SYNONYM: PSII-H;
COMPND 31 MOL_ID: 8;
COMPND 32 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN I;
COMPND 33 CHAIN: I, i;
COMPND 34 SYNONYM: PSII-I,PSII 4.4 KDA PROTEIN;
COMPND 35 MOL_ID: 9;
COMPND 36 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN J;
COMPND 37 CHAIN: J, j;
COMPND 38 SYNONYM: PSII-J;
COMPND 39 MOL_ID: 10;
COMPND 40 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN K;
COMPND 41 CHAIN: K, k;
COMPND 42 SYNONYM: PSII-K;
COMPND 43 MOL_ID: 11;
COMPND 44 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN L;
COMPND 45 CHAIN: L, l;
COMPND 46 SYNONYM: PSII-L,PSII 5 KDA PROTEIN;
COMPND 47 MOL_ID: 12;
COMPND 48 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN M;
COMPND 49 CHAIN: M, m;
COMPND 50 SYNONYM: PSII-M;
COMPND 51 MOL_ID: 13;
COMPND 52 MOLECULE: PHOTOSYSTEM II MANGANESE-STABILIZING POLYPEPTIDE;
COMPND 53 CHAIN: O, o;
COMPND 54 SYNONYM: MSP;
COMPND 55 MOL_ID: 14;
COMPND 56 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN T;
COMPND 57 CHAIN: T, t;
COMPND 58 SYNONYM: PSII-TC;
COMPND 59 MOL_ID: 15;
COMPND 60 MOLECULE: PHOTOSYSTEM II 12 KDA EXTRINSIC PROTEIN;
COMPND 61 CHAIN: U, u;
COMPND 62 SYNONYM: PS II COMPLEX 12 KDA EXTRINSIC PROTEIN,PSII-U;
COMPND 63 MOL_ID: 16;
COMPND 64 MOLECULE: CYTOCHROME C-550;
COMPND 65 CHAIN: V, v;
COMPND 66 SYNONYM: CYTOCHROME C-549,CYTOCHROME C550,LOW-POTENTIAL CYTOCHROME C;
COMPND 67 MOL_ID: 17;
COMPND 68 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN YCF12;
COMPND 69 CHAIN: y, g;
COMPND 70 MOL_ID: 18;
COMPND 71 MOLECULE: PHOTOSYSTEM II REACTION CENTER X PROTEIN;
COMPND 72 CHAIN: X, x;
COMPND 73 MOL_ID: 19;
COMPND 74 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN Y;
COMPND 75 CHAIN: Y, G;
COMPND 76 FRAGMENT: SEE REMARK 999;
COMPND 77 MOL_ID: 20;
COMPND 78 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN Z;
COMPND 79 CHAIN: Z, z;
COMPND 80 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;
SOURCE 77 MOL_ID: 20;
SOURCE 78 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 79 ORGANISM_TAXID: 197221;
SOURCE 80 STRAIN: BP-1
KEYWDS PHOTOSYNTHESIS, WATER OXIDATION, MEMBRANE PROTEIN, X-RAY FREE
KEYWDS 2 ELECTRON LASER, ELECTRON TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR J.KERN,R.TRAN,R.ALONSO-MORI,S.KOROIDOV,N.ECHOLS,J.HATTNE,M.IBRAHIM,
AUTHOR 2 S.GUL,H.LAKSMONO,R.G.SIERRA,R.J.GILDEA,G.HAN,J.HELLMICH,B.LASSALLE-
AUTHOR 3 KAISER,R.CHATTERJEE,A.BREWSTER,C.A.STAN,C.GLOECKNER,A.LAMPE,
AUTHOR 4 D.DIFIORE,D.MILATHIANAKI,A.R.FRY,M.M.SEIBERT,J.E.KOGLIN,E.GALLO,
AUTHOR 5 J.UHLIG,D.SOKARAS,T.-C.WENG,P.H.ZWART,D.E.SKINNER,M.J.BOGAN,
AUTHOR 6 M.MESSERSCHMIDT,P.GLATZEL,G.J.WILLIAMS,S.BOUTET,P.D.ADAMS,A.ZOUNI,
AUTHOR 7 J.MESSINGER,N.K.SAUTER,U.BERGMANN,J.YANO,V.K.YACHANDRA
REVDAT 4 04-DEC-19 4TNK 1 REMARK
REVDAT 3 27-SEP-17 4TNK 1 REMARK
REVDAT 2 23-JUL-14 4TNK 1 JRNL
REVDAT 1 09-JUL-14 4TNK 0
JRNL AUTH J.KERN,R.TRAN,R.ALONSO-MORI,S.KOROIDOV,N.ECHOLS,J.HATTNE,
JRNL AUTH 2 M.IBRAHIM,S.GUL,H.LAKSMONO,R.G.SIERRA,R.J.GILDEA,G.HAN,
JRNL AUTH 3 J.HELLMICH,B.LASSALLE-KAISER,R.CHATTERJEE,A.S.BREWSTER,
JRNL AUTH 4 C.A.STAN,C.GLOCKNER,A.LAMPE,D.DIFIORE,D.MILATHIANAKI,
JRNL AUTH 5 A.R.FRY,M.M.SEIBERT,J.E.KOGLIN,E.GALLO,J.UHLIG,D.SOKARAS,
JRNL AUTH 6 T.C.WENG,P.H.ZWART,D.E.SKINNER,M.J.BOGAN,M.MESSERSCHMIDT,
JRNL AUTH 7 P.GLATZEL,G.J.WILLIAMS,S.BOUTET,P.D.ADAMS,A.ZOUNI,
JRNL AUTH 8 J.MESSINGER,N.K.SAUTER,U.BERGMANN,J.YANO,V.K.YACHANDRA
JRNL TITL TAKING SNAPSHOTS OF PHOTOSYNTHETIC WATER OXIDATION USING
JRNL TITL 2 FEMTOSECOND X-RAY DIFFRACTION AND SPECTROSCOPY.
JRNL REF NAT COMMUN V. 5 4371 2014
JRNL REFN ESSN 2041-1723
JRNL PMID 25006873
JRNL DOI 10.1038/NCOMMS5371
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.V.AFONINE,R.W.GROSSE-KUNSTLEVE,N.ECHOLS,J.J.HEADD,
REMARK 1 AUTH 2 N.W.MORIARTY,M.MUSTYAKIMOV,T.C.TERWILLIGER,A.URZHUMTSEV,
REMARK 1 AUTH 3 P.H.ZWART,P.D.ADAMS
REMARK 1 TITL TOWARDS AUTOMATED CRYSTALLOGRAPHIC STRUCTURE REFINEMENT WITH
REMARK 1 TITL 2 PHENIX.REFINE.
REMARK 1 REF ACTA CRYSTALLOGR. D BIOL. V. 68 352 2012
REMARK 1 REF 2 CRYSTALLOGR.
REMARK 1 REFN ESSN 1399-0047
REMARK 1 PMID 22505256
REMARK 1 DOI 10.1107/S0907444912001308
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.D.ADAMS,P.V.AFONINE,G.BUNKOCZI,V.B.CHEN,I.W.DAVIS,
REMARK 1 AUTH 2 N.ECHOLS,J.J.HEADD,L.W.HUNG,G.J.KAPRAL,R.W.GROSSE-KUNSTLEVE,
REMARK 1 AUTH 3 A.J.MCCOY,N.W.MORIARTY,R.OEFFNER,R.J.READ,D.C.RICHARDSON,
REMARK 1 AUTH 4 J.S.RICHARDSON,T.C.TERWILLIGER,P.H.ZWART
REMARK 1 TITL PHENIX: A COMPREHENSIVE PYTHON-BASED SYSTEM FOR
REMARK 1 TITL 2 MACROMOLECULAR STRUCTURE SOLUTION.
REMARK 1 REF ACTA CRYSTALLOGR. D BIOL. V. 66 213 2010
REMARK 1 REF 2 CRYSTALLOGR.
REMARK 1 REFN ESSN 1399-0047
REMARK 1 PMID 20124702
REMARK 1 DOI 10.1107/S0907444909052925
REMARK 2
REMARK 2 RESOLUTION. 5.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1635+SVN)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 5.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 68.41
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.406
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 68083
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.272
REMARK 3 R VALUE (WORKING SET) : 0.271
REMARK 3 FREE R VALUE : 0.289
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.888
REMARK 3 FREE R VALUE TEST SET COUNT : 3328
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 68.4176 - 14.9500 1.00 2767 115 0.3377 0.3494
REMARK 3 2 14.9500 - 11.8865 1.00 2771 145 0.2402 0.2175
REMARK 3 3 11.8865 - 10.3899 1.00 2722 140 0.2159 0.2218
REMARK 3 4 10.3899 - 9.4426 1.00 2772 144 0.2310 0.2718
REMARK 3 5 9.4426 - 8.7673 1.00 2747 131 0.2239 0.2223
REMARK 3 6 8.7673 - 8.2513 1.00 2740 153 0.2305 0.2816
REMARK 3 7 8.2513 - 7.8387 1.00 2749 157 0.2401 0.2694
REMARK 3 8 7.8387 - 7.4979 1.00 2757 128 0.2423 0.2765
REMARK 3 9 7.4979 - 7.2096 1.00 2774 157 0.2491 0.2844
REMARK 3 10 7.2096 - 6.9610 1.00 2683 126 0.2534 0.3034
REMARK 3 11 6.9610 - 6.7436 1.00 2782 141 0.2608 0.2727
REMARK 3 12 6.7436 - 6.5510 1.00 2768 153 0.2757 0.2923
REMARK 3 13 6.5510 - 6.3786 1.00 2737 140 0.2860 0.2929
REMARK 3 14 6.3786 - 6.2231 1.00 2786 131 0.2719 0.2963
REMARK 3 15 6.2231 - 6.0817 1.00 2714 163 0.2936 0.3380
REMARK 3 16 6.0817 - 5.9524 1.00 2765 140 0.2966 0.3055
REMARK 3 17 5.9524 - 5.8334 1.00 2754 135 0.3138 0.3425
REMARK 3 18 5.8334 - 5.7233 0.99 2701 154 0.3095 0.3645
REMARK 3 19 5.7233 - 5.6212 0.98 2724 131 0.3294 0.3744
REMARK 3 20 5.6212 - 5.5259 0.98 2698 134 0.3359 0.3382
REMARK 3 21 5.5259 - 5.4368 0.94 2626 137 0.3434 0.3453
REMARK 3 22 5.4368 - 5.3532 0.90 2427 126 0.3487 0.3494
REMARK 3 23 5.3532 - 5.2745 0.88 2430 137 0.3448 0.3888
REMARK 3 24 5.2745 - 5.2003 0.86 2361 110 0.3560 0.3839
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) : 0.787
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.937
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 176.2
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 207.6
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 : 0.005 52088
REMARK 3 ANGLE : 0.776 71528
REMARK 3 CHIRALITY : 0.031 7238
REMARK 3 PLANARITY : 0.004 8510
REMARK 3 DIHEDRAL : 18.635 18206
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 'G'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'B'
REMARK 3 SELECTION : CHAIN 'N'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 3
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'C'
REMARK 3 SELECTION : CHAIN 'P'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 4
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'D'
REMARK 3 SELECTION : CHAIN 'Q'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 5
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'E'
REMARK 3 SELECTION : CHAIN 'R'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 6
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'F'
REMARK 3 SELECTION : CHAIN 'S'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 7
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'H'
REMARK 3 SELECTION : CHAIN 'W'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 8
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'I'
REMARK 3 SELECTION : CHAIN 'A'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 9
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'J'
REMARK 3 SELECTION : CHAIN 'B'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 10
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'K'
REMARK 3 SELECTION : CHAIN 'C'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 11
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'L'
REMARK 3 SELECTION : CHAIN 'D'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 12
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'M'
REMARK 3 SELECTION : CHAIN 'E'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 13
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'O'
REMARK 3 SELECTION : CHAIN 'F'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 14
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'T'
REMARK 3 SELECTION : CHAIN 'G'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 15
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'U'
REMARK 3 SELECTION : CHAIN 'H'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 16
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'V'
REMARK 3 SELECTION : CHAIN 'I'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 17
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'X'
REMARK 3 SELECTION : CHAIN 'J'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 18
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'Z'
REMARK 3 SELECTION : CHAIN 'L'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 19
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'M'
REMARK 3 SELECTION : CHAIN 'Y'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4TNK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1000201921.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 7850
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) : 1.77
REMARK 200 MONOCHROMATOR : NO MONOCHROMATOR, FEL BEAM WITH
REMARK 200 20-30 EV BANDWIDTH
REMARK 200 OPTICS : KB MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : CS-PAD DETECTOR
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CCTBX.XFEL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34679
REMARK 200 RESOLUTION RANGE HIGH (A) : 5.200
REMARK 200 RESOLUTION RANGE LOW (A) : 68.410
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 88.60
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 41.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 5.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 5.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 8.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 3BZ1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 4% PEG2000, 5 MM CALCIUM CHLORIDE, 100
REMARK 280 MM PIPES, PH 7.0, BATCH, TEMPERATURE 298K, BATCH MODE
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 66.30750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 153.41250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 114.64800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 153.41250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 66.30750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 114.64800
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: 40-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, Y,
REMARK 350 AND CHAINS: Z, a, b, c, d, e, f, h, i, j,
REMARK 350 AND CHAINS: k, l, m, o, t, u, v, g, x,
REMARK 350 AND CHAINS: G, z
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 THR A 3
REMARK 465 THR A 4
REMARK 465 LEU A 5
REMARK 465 GLN A 6
REMARK 465 ARG A 7
REMARK 465 ARG A 8
REMARK 465 GLU A 9
REMARK 465 MET B 1
REMARK 465 GLU B 492
REMARK 465 TRP B 493
REMARK 465 GLY B 494
REMARK 465 PHE B 495
REMARK 465 TYR B 496
REMARK 465 GLN B 497
REMARK 465 LYS B 498
REMARK 465 VAL B 499
REMARK 465 GLY B 500
REMARK 465 ASP B 501
REMARK 465 VAL B 502
REMARK 465 THR B 503
REMARK 465 THR B 504
REMARK 465 ARG B 505
REMARK 465 ARG B 506
REMARK 465 LYS B 507
REMARK 465 GLU B 508
REMARK 465 ALA B 509
REMARK 465 VAL B 510
REMARK 465 MET C 13
REMARK 465 VAL C 14
REMARK 465 THR C 15
REMARK 465 LEU C 16
REMARK 465 SER C 17
REMARK 465 SER C 18
REMARK 465 ASN C 19
REMARK 465 SER C 20
REMARK 465 ILE C 21
REMARK 465 PHE C 22
REMARK 465 ALA C 23
REMARK 465 THR C 24
REMARK 465 ASN C 25
REMARK 465 ARG C 26
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 ILE D 3
REMARK 465 ALA D 4
REMARK 465 ILE D 5
REMARK 465 GLY D 6
REMARK 465 ARG D 7
REMARK 465 ALA D 8
REMARK 465 PRO D 9
REMARK 465 ALA D 10
REMARK 465 GLU D 11
REMARK 465 ARG D 12
REMARK 465 MET E 1
REMARK 465 ALA E 2
REMARK 465 MET F 1
REMARK 465 THR F 2
REMARK 465 SER F 3
REMARK 465 ASN F 4
REMARK 465 THR F 5
REMARK 465 PRO F 6
REMARK 465 ASN F 7
REMARK 465 GLN F 8
REMARK 465 GLU F 9
REMARK 465 PRO F 10
REMARK 465 MET H 1
REMARK 465 ASP I 36
REMARK 465 LEU I 37
REMARK 465 GLU I 38
REMARK 465 MET J 1
REMARK 465 MET J 2
REMARK 465 SER J 3
REMARK 465 GLU J 4
REMARK 465 GLY J 5
REMARK 465 GLY J 6
REMARK 465 MET K 1
REMARK 465 ILE K 2
REMARK 465 ASP K 3
REMARK 465 ALA K 4
REMARK 465 LEU K 5
REMARK 465 VAL K 6
REMARK 465 LEU K 7
REMARK 465 VAL K 8
REMARK 465 ALA K 9
REMARK 465 SER M 35
REMARK 465 SER M 36
REMARK 465 MET O 1
REMARK 465 LYS O 2
REMARK 465 TYR O 3
REMARK 465 ARG O 4
REMARK 465 ILE O 5
REMARK 465 LEU O 6
REMARK 465 MET O 7
REMARK 465 ALA O 8
REMARK 465 THR O 9
REMARK 465 LEU O 10
REMARK 465 LEU O 11
REMARK 465 ALA O 12
REMARK 465 VAL O 13
REMARK 465 CYS O 14
REMARK 465 LEU O 15
REMARK 465 GLY O 16
REMARK 465 ILE O 17
REMARK 465 PHE O 18
REMARK 465 SER O 19
REMARK 465 LEU O 20
REMARK 465 SER O 21
REMARK 465 ALA O 22
REMARK 465 PRO O 23
REMARK 465 ALA O 24
REMARK 465 PHE O 25
REMARK 465 ALA O 26
REMARK 465 ALA O 27
REMARK 465 LYS O 28
REMARK 465 GLN O 29
REMARK 465 MET U 1
REMARK 465 GLN U 2
REMARK 465 ARG U 3
REMARK 465 LEU U 4
REMARK 465 GLY U 5
REMARK 465 ARG U 6
REMARK 465 TRP U 7
REMARK 465 LEU U 8
REMARK 465 ALA U 9
REMARK 465 LEU U 10
REMARK 465 ALA U 11
REMARK 465 TYR U 12
REMARK 465 PHE U 13
REMARK 465 VAL U 14
REMARK 465 GLY U 15
REMARK 465 VAL U 16
REMARK 465 SER U 17
REMARK 465 LEU U 18
REMARK 465 LEU U 19
REMARK 465 GLY U 20
REMARK 465 TRP U 21
REMARK 465 ILE U 22
REMARK 465 ASN U 23
REMARK 465 TRP U 24
REMARK 465 SER U 25
REMARK 465 ALA U 26
REMARK 465 PRO U 27
REMARK 465 THR U 28
REMARK 465 LEU U 29
REMARK 465 ALA U 30
REMARK 465 ALA U 31
REMARK 465 THR U 32
REMARK 465 ALA U 33
REMARK 465 SER U 34
REMARK 465 THR U 35
REMARK 465 GLU U 36
REMARK 465 GLU U 37
REMARK 465 MET V 1
REMARK 465 LEU V 2
REMARK 465 LYS V 3
REMARK 465 LYS V 4
REMARK 465 CYS V 5
REMARK 465 VAL V 6
REMARK 465 TRP V 7
REMARK 465 LEU V 8
REMARK 465 ALA V 9
REMARK 465 VAL V 10
REMARK 465 ALA V 11
REMARK 465 LEU V 12
REMARK 465 CYS V 13
REMARK 465 LEU V 14
REMARK 465 CYS V 15
REMARK 465 LEU V 16
REMARK 465 TRP V 17
REMARK 465 GLN V 18
REMARK 465 PHE V 19
REMARK 465 THR V 20
REMARK 465 MET V 21
REMARK 465 GLY V 22
REMARK 465 THR V 23
REMARK 465 ALA V 24
REMARK 465 LEU V 25
REMARK 465 ALA V 26
REMARK 465 MET y 1
REMARK 465 GLY y 2
REMARK 465 ILE y 3
REMARK 465 PHE y 4
REMARK 465 ASN y 5
REMARK 465 GLY y 6
REMARK 465 ILE y 7
REMARK 465 ILE y 8
REMARK 465 GLU y 9
REMARK 465 PHE y 10
REMARK 465 LEU y 11
REMARK 465 SER y 12
REMARK 465 ASN y 13
REMARK 465 ILE y 14
REMARK 465 ASN y 15
REMARK 465 PHE y 16
REMARK 465 GLU y 17
REMARK 465 VAL y 18
REMARK 465 MET X 10
REMARK 465 ARG X 48
REMARK 465 SER X 49
REMARK 465 LEU X 50
REMARK 465 MET a 1
REMARK 465 THR a 2
REMARK 465 THR a 3
REMARK 465 THR a 4
REMARK 465 LEU a 5
REMARK 465 GLN a 6
REMARK 465 ARG a 7
REMARK 465 ARG a 8
REMARK 465 GLU a 9
REMARK 465 MET b 1
REMARK 465 GLU b 492
REMARK 465 TRP b 493
REMARK 465 GLY b 494
REMARK 465 PHE b 495
REMARK 465 TYR b 496
REMARK 465 GLN b 497
REMARK 465 LYS b 498
REMARK 465 VAL b 499
REMARK 465 GLY b 500
REMARK 465 ASP b 501
REMARK 465 VAL b 502
REMARK 465 THR b 503
REMARK 465 THR b 504
REMARK 465 ARG b 505
REMARK 465 ARG b 506
REMARK 465 LYS b 507
REMARK 465 GLU b 508
REMARK 465 ALA b 509
REMARK 465 VAL b 510
REMARK 465 MET c 13
REMARK 465 VAL c 14
REMARK 465 THR c 15
REMARK 465 LEU c 16
REMARK 465 SER c 17
REMARK 465 SER c 18
REMARK 465 ASN c 19
REMARK 465 SER c 20
REMARK 465 ILE c 21
REMARK 465 PHE c 22
REMARK 465 ALA c 23
REMARK 465 THR c 24
REMARK 465 ASN c 25
REMARK 465 ARG c 26
REMARK 465 MET d 1
REMARK 465 THR d 2
REMARK 465 ILE d 3
REMARK 465 ALA d 4
REMARK 465 ILE d 5
REMARK 465 GLY d 6
REMARK 465 ARG d 7
REMARK 465 ALA d 8
REMARK 465 PRO d 9
REMARK 465 ALA d 10
REMARK 465 GLU d 11
REMARK 465 ARG d 12
REMARK 465 MET e 1
REMARK 465 ALA e 2
REMARK 465 MET f 1
REMARK 465 THR f 2
REMARK 465 SER f 3
REMARK 465 ASN f 4
REMARK 465 THR f 5
REMARK 465 PRO f 6
REMARK 465 ASN f 7
REMARK 465 GLN f 8
REMARK 465 GLU f 9
REMARK 465 PRO f 10
REMARK 465 MET h 1
REMARK 465 ASP i 36
REMARK 465 LEU i 37
REMARK 465 GLU i 38
REMARK 465 MET j 1
REMARK 465 MET j 2
REMARK 465 SER j 3
REMARK 465 GLU j 4
REMARK 465 GLY j 5
REMARK 465 GLY j 6
REMARK 465 MET k 1
REMARK 465 ILE k 2
REMARK 465 ASP k 3
REMARK 465 ALA k 4
REMARK 465 LEU k 5
REMARK 465 VAL k 6
REMARK 465 LEU k 7
REMARK 465 VAL k 8
REMARK 465 ALA k 9
REMARK 465 SER m 35
REMARK 465 SER m 36
REMARK 465 MET o 1
REMARK 465 LYS o 2
REMARK 465 TYR o 3
REMARK 465 ARG o 4
REMARK 465 ILE o 5
REMARK 465 LEU o 6
REMARK 465 MET o 7
REMARK 465 ALA o 8
REMARK 465 THR o 9
REMARK 465 LEU o 10
REMARK 465 LEU o 11
REMARK 465 ALA o 12
REMARK 465 VAL o 13
REMARK 465 CYS o 14
REMARK 465 LEU o 15
REMARK 465 GLY o 16
REMARK 465 ILE o 17
REMARK 465 PHE o 18
REMARK 465 SER o 19
REMARK 465 LEU o 20
REMARK 465 SER o 21
REMARK 465 ALA o 22
REMARK 465 PRO o 23
REMARK 465 ALA o 24
REMARK 465 PHE o 25
REMARK 465 ALA o 26
REMARK 465 ALA o 27
REMARK 465 LYS o 28
REMARK 465 GLN o 29
REMARK 465 MET u 1
REMARK 465 GLN u 2
REMARK 465 ARG u 3
REMARK 465 LEU u 4
REMARK 465 GLY u 5
REMARK 465 ARG u 6
REMARK 465 TRP u 7
REMARK 465 LEU u 8
REMARK 465 ALA u 9
REMARK 465 LEU u 10
REMARK 465 ALA u 11
REMARK 465 TYR u 12
REMARK 465 PHE u 13
REMARK 465 VAL u 14
REMARK 465 GLY u 15
REMARK 465 VAL u 16
REMARK 465 SER u 17
REMARK 465 LEU u 18
REMARK 465 LEU u 19
REMARK 465 GLY u 20
REMARK 465 TRP u 21
REMARK 465 ILE u 22
REMARK 465 ASN u 23
REMARK 465 TRP u 24
REMARK 465 SER u 25
REMARK 465 ALA u 26
REMARK 465 PRO u 27
REMARK 465 THR u 28
REMARK 465 LEU u 29
REMARK 465 ALA u 30
REMARK 465 ALA u 31
REMARK 465 THR u 32
REMARK 465 ALA u 33
REMARK 465 SER u 34
REMARK 465 THR u 35
REMARK 465 GLU u 36
REMARK 465 GLU u 37
REMARK 465 MET v 1
REMARK 465 LEU v 2
REMARK 465 LYS v 3
REMARK 465 LYS v 4
REMARK 465 CYS v 5
REMARK 465 VAL v 6
REMARK 465 TRP v 7
REMARK 465 LEU v 8
REMARK 465 ALA v 9
REMARK 465 VAL v 10
REMARK 465 ALA v 11
REMARK 465 LEU v 12
REMARK 465 CYS v 13
REMARK 465 LEU v 14
REMARK 465 CYS v 15
REMARK 465 LEU v 16
REMARK 465 TRP v 17
REMARK 465 GLN v 18
REMARK 465 PHE v 19
REMARK 465 THR v 20
REMARK 465 MET v 21
REMARK 465 GLY v 22
REMARK 465 THR v 23
REMARK 465 ALA v 24
REMARK 465 LEU v 25
REMARK 465 ALA v 26
REMARK 465 MET g 1
REMARK 465 GLY g 2
REMARK 465 ILE g 3
REMARK 465 PHE g 4
REMARK 465 ASN g 5
REMARK 465 GLY g 6
REMARK 465 ILE g 7
REMARK 465 ILE g 8
REMARK 465 GLU g 9
REMARK 465 PHE g 10
REMARK 465 LEU g 11
REMARK 465 SER g 12
REMARK 465 ASN g 13
REMARK 465 ILE g 14
REMARK 465 ASN g 15
REMARK 465 PHE g 16
REMARK 465 GLU g 17
REMARK 465 VAL g 18
REMARK 465 MET x 10
REMARK 465 ARG x 48
REMARK 465 SER x 49
REMARK 465 LEU x 50
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 TYR C 143 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU C 462 CG CD OE1 OE2
REMARK 470 LYS H 20 CG CD CE NZ
REMARK 470 ARG O 53 CG CD NE CZ NH1 NH2
REMARK 470 GLU O 80 CG CD OE1 OE2
REMARK 470 LYS O 85 CG CD CE NZ
REMARK 470 ARG O 233 CG CD NE CZ NH1 NH2
REMARK 470 GLU V 41 CG CD OE1 OE2
REMARK 470 ARG y 43 CG CD NE CZ NH1 NH2
REMARK 470 TYR c 143 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU c 462 CG CD OE1 OE2
REMARK 470 LYS h 20 CG CD CE NZ
REMARK 470 ARG o 53 CG CD NE CZ NH1 NH2
REMARK 470 GLU o 80 CG CD OE1 OE2
REMARK 470 LYS o 85 CG CD CE NZ
REMARK 470 ARG o 233 CG CD NE CZ NH1 NH2
REMARK 470 GLU v 41 CG CD OE1 OE2
REMARK 470 ARG g 43 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O TRP c 250 OG1 THR c 254 2.13
REMARK 500 O TRP C 250 OG1 THR C 254 2.13
REMARK 500 O TRP c 291 OG1 THR c 305 2.15
REMARK 500 O TRP C 291 OG1 THR C 305 2.16
REMARK 500 OD2 ASP u 56 OG1 THR u 115 2.17
REMARK 500 O ALA B 155 OG1 THR B 159 2.18
REMARK 500 OD2 ASP U 56 OG1 THR U 115 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO B 484 C - N - CA ANGL. DEV. = 13.9 DEGREES
REMARK 500 PRO b 484 C - N - CA ANGL. DEV. = 13.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 12 114.87 157.41
REMARK 500 PRO A 141 -128.53 -75.49
REMARK 500 TRP A 142 -11.06 58.64
REMARK 500 LEU A 159 -50.58 -131.85
REMARK 500 SER A 222 42.56 -109.57
REMARK 500 ILE A 259 -84.90 -104.06
REMARK 500 PHE A 302 32.41 -98.83
REMARK 500 SER A 305 -70.55 -77.34
REMARK 500 ARG A 334 -72.15 -27.25
REMARK 500 ASP B 119 54.86 -91.65
REMARK 500 ARG B 127 -72.10 -63.47
REMARK 500 PRO B 183 175.78 -59.24
REMARK 500 LEU B 218 -67.97 -95.25
REMARK 500 ARG B 230 53.27 31.45
REMARK 500 ASP B 313 42.32 -90.75
REMARK 500 LYS B 349 -39.98 -37.90
REMARK 500 THR B 436 -70.24 -33.81
REMARK 500 SER B 480 -13.16 70.35
REMARK 500 ILE B 482 -165.34 -118.17
REMARK 500 PRO B 484 -142.56 -7.45
REMARK 500 GLU B 485 162.24 62.58
REMARK 500 LEU B 486 69.38 -155.56
REMARK 500 PRO B 488 -109.59 6.89
REMARK 500 GLU B 489 57.02 -64.50
REMARK 500 GLN B 490 108.16 -166.86
REMARK 500 GLU C 29 -149.12 -148.60
REMARK 500 ARG C 135 -62.13 -122.68
REMARK 500 SER C 144 109.87 -179.18
REMARK 500 ASN C 201 59.39 -168.51
REMARK 500 TRP C 223 -145.87 60.93
REMARK 500 LEU C 253 30.92 -97.09
REMARK 500 PHE C 257 -144.84 -71.51
REMARK 500 ARG C 320 -71.46 -59.42
REMARK 500 THR C 355 2.95 -69.30
REMARK 500 PRO C 368 -9.84 -59.77
REMARK 500 LEU C 375 114.28 -34.48
REMARK 500 ASN C 382 12.48 -161.87
REMARK 500 HIS C 398 33.86 -142.14
REMARK 500 ALA C 411 -17.15 -49.74
REMARK 500 SER C 416 -59.62 -177.69
REMARK 500 PHE C 455 22.92 -150.08
REMARK 500 GLU C 462 -75.74 -68.70
REMARK 500 ARG D 26 -164.63 -102.29
REMARK 500 VAL D 30 -82.73 -89.29
REMARK 500 LEU D 37 -71.92 -56.30
REMARK 500 SER D 65 16.52 -141.23
REMARK 500 PRO D 140 37.37 -85.29
REMARK 500 LEU D 158 -64.67 -128.74
REMARK 500 ALA D 234 28.72 -76.02
REMARK 500 THR D 238 79.58 -100.40
REMARK 500
REMARK 500 THIS ENTRY HAS 250 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 PL9 A 407
REMARK 610 DGD A 409
REMARK 610 LHG A 410
REMARK 610 SQD A 413
REMARK 610 DGD B 620
REMARK 610 LMG B 621
REMARK 610 SQD B 622
REMARK 610 LMG B 625
REMARK 610 DGD B 626
REMARK 610 SQD B 627
REMARK 610 DGD C 514
REMARK 610 DGD C 515
REMARK 610 LMG C 517
REMARK 610 LHG C 518
REMARK 610 LMG C 521
REMARK 610 LMG D 406
REMARK 610 DGD D 407
REMARK 610 LMT D 408
REMARK 610 LMG D 409
REMARK 610 LMG E 101
REMARK 610 SQD F 103
REMARK 610 LMG I 101
REMARK 610 PL9 J 101
REMARK 610 LMG L 101
REMARK 610 LMG M 101
REMARK 610 LMG a 402
REMARK 610 PL9 a 407
REMARK 610 DGD a 408
REMARK 610 LHG a 409
REMARK 610 SQD a 412
REMARK 610 DGD b 601
REMARK 610 SQD b 602
REMARK 610 DGD b 625
REMARK 610 LMG b 626
REMARK 610 LMG b 627
REMARK 610 DGD c 515
REMARK 610 DGD c 516
REMARK 610 LMG c 518
REMARK 610 LHG c 519
REMARK 610 LMG c 522
REMARK 610 SQD d 403
REMARK 610 LMG d 408
REMARK 610 LMG d 409
REMARK 610 DGD d 410
REMARK 610 LMT d 411
REMARK 610 LMG d 412
REMARK 610 LMG e 101
REMARK 610 SQD f 103
REMARK 610 LMG i 102
REMARK 610 PL9 j 101
REMARK 610 LMG l 101
REMARK 610 LMG m 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 412 CA1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 170 OD1
REMARK 620 2 OEX A 412 O1 124.8
REMARK 620 3 OEX A 412 O2 61.2 63.6
REMARK 620 4 OEX A 412 O5 94.5 61.1 63.8
REMARK 620 5 GLU A 189 OE1 167.1 65.5 128.2 84.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX A 412 MN4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 170 OD2
REMARK 620 2 OEX A 412 O5 110.9
REMARK 620 3 OEX A 412 O4 68.4 87.2
REMARK 620 4 GLU A 333 OE2 125.0 107.3 75.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX A 412 MN1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 189 OE2
REMARK 620 2 OEX A 412 O1 81.8
REMARK 620 3 OEX A 412 O5 128.5 90.4
REMARK 620 4 OEX A 412 O3 142.5 89.7 87.7
REMARK 620 5 HIS A 332 NE2 77.6 157.5 109.5 101.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 A 401 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 215 NE2
REMARK 620 2 HIS A 272 NE2 98.8
REMARK 620 3 HIS D 214 NE2 122.0 109.7
REMARK 620 4 HIS D 268 NE2 79.5 157.4 89.6
REMARK 620 5 BCT D 402 O2 86.1 87.2 142.5 70.2
REMARK 620 6 BCT D 402 O3 131.9 93.6 96.2 72.2 48.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX A 412 MN3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 333 OE1
REMARK 620 2 OEX A 412 O2 136.6
REMARK 620 3 OEX A 412 O3 96.3 88.7
REMARK 620 4 OEX A 412 O4 83.6 92.2 178.9
REMARK 620 5 OEX A 412 O5 106.8 116.3 89.5 89.6
REMARK 620 6 GLU C 354 OE2 66.7 73.3 74.7 106.2 161.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX A 412 MN2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 342 OD1
REMARK 620 2 OEX A 412 O1 112.2
REMARK 620 3 OEX A 412 O2 157.6 89.9
REMARK 620 4 OEX A 412 O3 93.0 86.9 84.5
REMARK 620 5 ALA A 344 OXT 99.3 130.7 66.4 129.6
REMARK 620 6 GLU C 354 OE1 66.3 156.9 92.1 70.5 70.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C 510 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C 39 OD1
REMARK 620 2 CLA C 510 NA 96.1
REMARK 620 3 CLA C 510 NB 74.4 92.3
REMARK 620 4 CLA C 510 NC 84.2 176.8 90.9
REMARK 620 5 CLA C 510 ND 104.9 90.6 177.1 86.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM F 101 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 23 NE2
REMARK 620 2 HEM F 101 NA 87.8
REMARK 620 3 HEM F 101 NB 103.5 89.8
REMARK 620 4 HEM F 101 NC 88.9 176.0 88.6
REMARK 620 5 HEM F 101 ND 67.3 89.5 170.8 91.4
REMARK 620 6 HIS F 24 NE2 158.0 70.2 77.4 113.1 111.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA K 102 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP K 19 OD2
REMARK 620 2 ASP K 23 OD1 120.2
REMARK 620 3 ASP K 23 OD2 114.8 41.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM V 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS V 67 NE2
REMARK 620 2 HEM V 201 NA 86.9
REMARK 620 3 HEM V 201 NB 87.9 90.4
REMARK 620 4 HEM V 201 NC 88.1 175.0 90.0
REMARK 620 5 HEM V 201 ND 81.7 88.6 169.6 90.2
REMARK 620 6 HIS V 118 NE2 168.0 89.4 103.5 95.3 86.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 411 CA1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP a 170 OD1
REMARK 620 2 OEX a 411 O1 124.1
REMARK 620 3 OEX a 411 O2 60.8 63.4
REMARK 620 4 OEX a 411 O5 95.4 61.3 63.9
REMARK 620 5 GLU a 189 OE1 171.6 61.4 123.9 81.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 411 MN4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP a 170 OD2
REMARK 620 2 OEX a 411 O5 108.9
REMARK 620 3 OEX a 411 O4 68.2 87.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 411 MN1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU a 189 OE2
REMARK 620 2 OEX a 411 O1 84.6
REMARK 620 3 OEX a 411 O5 133.5 90.3
REMARK 620 4 OEX a 411 O3 138.3 89.6 87.7
REMARK 620 5 HIS a 332 NE2 74.1 157.5 109.5 101.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 a 413 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS a 215 NE2
REMARK 620 2 HIS a 272 NE2 93.7
REMARK 620 3 HIS d 214 NE2 120.8 110.2
REMARK 620 4 HIS d 268 NE2 77.1 155.8 93.6
REMARK 620 5 BCT d 404 O2 87.8 87.2 143.9 70.2
REMARK 620 6 BCT d 404 O3 133.9 97.5 96.7 74.5 48.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 411 MN3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU a 333 OE1
REMARK 620 2 OEX a 411 O2 135.4
REMARK 620 3 OEX a 411 O3 95.6 88.7
REMARK 620 4 OEX a 411 O4 84.1 92.2 179.0
REMARK 620 5 OEX a 411 O5 108.2 116.2 89.5 89.6
REMARK 620 6 GLU c 354 OE2 66.7 72.4 73.1 107.6 160.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 411 MN2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP a 342 OD1
REMARK 620 2 OEX a 411 O1 111.4
REMARK 620 3 OEX a 411 O2 158.6 89.8
REMARK 620 4 OEX a 411 O3 94.2 86.8 84.5
REMARK 620 5 ALA a 344 OXT 100.5 128.8 65.5 130.4
REMARK 620 6 GLU c 354 OE1 66.0 158.6 93.5 72.5 71.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA c 510 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN c 39 OD1
REMARK 620 2 CLA c 510 NA 96.8
REMARK 620 3 CLA c 510 NB 75.9 92.2
REMARK 620 4 CLA c 510 NC 83.4 176.7 91.0
REMARK 620 5 CLA c 510 ND 103.4 90.6 177.1 86.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM f 101 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS e 23 NE2
REMARK 620 2 HEM f 101 NA 87.0
REMARK 620 3 HEM f 101 NB 106.2 89.9
REMARK 620 4 HEM f 101 NC 91.0 176.7 88.1
REMARK 620 5 HEM f 101 ND 66.3 90.0 172.5 91.6
REMARK 620 6 HIS f 24 NE2 158.7 71.7 74.9 110.3 112.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA k 101 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP k 19 OD2
REMARK 620 2 ASP k 23 OD1 128.6
REMARK 620 3 ASP k 23 OD2 113.9 43.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM v 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS v 67 NE2
REMARK 620 2 HEM v 201 NA 85.2
REMARK 620 3 HEM v 201 NB 86.0 88.6
REMARK 620 4 HEM v 201 NC 89.6 174.8 90.9
REMARK 620 5 HEM v 201 ND 83.6 89.8 169.6 89.8
REMARK 620 6 HIS v 118 NE2 170.1 87.5 100.4 97.8 89.8
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 FE2 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OEX A 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD A 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD A 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD B 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD B 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT B 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT B 624
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 625
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD B 626
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD B 627
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT B 628
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT B 629
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG C 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 D 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG D 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD D 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT D 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG D 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG E 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM F 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR F 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD F 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA H 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR H 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG I 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT I 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 J 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR J 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR K 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA K 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG L 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG M 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT M 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT M 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA O 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM V 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR y 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD a 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG a 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 a 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD a 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG a 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OEX a 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD a 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE2 a 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD b 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD b 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT b 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT b 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 624
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD b 625
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG b 626
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG b 627
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT b 628
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT b 629
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG c 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 522
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO d 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO d 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD d 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT d 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 d 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG d 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG d 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD d 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT d 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG d 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG e 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM f 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR f 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD f 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR i 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG i 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT i 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 j 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR j 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA k 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG l 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG m 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AW1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA o 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AW2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM v 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AW3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR g 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AW4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR x 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4TNH RELATED DB: PDB
REMARK 900 PHOTOSYSTEM II IN THE DARK STATE AT 4.9 A RESOLUTION
REMARK 900 RELATED ID: 4TNI RELATED DB: PDB
REMARK 900 PHOTOSYSTEM II 500 MS AFTER THE THIRD ILLUMINATION (3F) AT 4.6 A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 4TNJ RELATED DB: PDB
REMARK 900 PHOTOSYSTEM II 500 MS AFTER THE SECOND ILLUMINATION (2F) AT 4.5 A
REMARK 900 RESOLUTION
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 MOLECULE 19 (PHOTOSYSTEM II PROTEIN Y): THE DEPOSITORS STATE THAT
REMARK 999 THE SAMPLE SEQUENCE IS MDWRVLVVLLPVLLAAGWAVRNILPYAVKQVQKLLQKAKAA
REMARK 999 (UNP Q8DKM3).
DBREF 4TNK A 1 344 UNP P0A444 PSBA1_THEEB 1 344
DBREF 4TNK B 1 510 UNP Q8DIQ1 Q8DIQ1_THEEB 1 510
DBREF 4TNK C 13 473 UNP Q8DIF8 Q8DIF8_THEEB 1 461
DBREF 4TNK D 1 352 UNP Q8CM25 PSBD_THEEB 1 352
DBREF 4TNK E 1 84 UNP Q8DIP0 PSBE_THEEB 1 84
DBREF 4TNK F 1 45 UNP Q8DIN9 PSBF_THEEB 1 45
DBREF 4TNK H 1 66 UNP Q8DJ43 PSBH_THEEB 1 66
DBREF 4TNK I 1 38 UNP Q8DJZ6 PSBI_THEEB 1 38
DBREF 4TNK J 1 40 UNP P59087 PSBJ_THEEB 1 40
DBREF 4TNK K 1 46 UNP Q9F1K9 PSBK_THEEB 1 46
DBREF 4TNK L 1 37 UNP Q8DIN8 PSBL_THEEB 1 37
DBREF 4TNK M 1 36 UNP Q8DHA7 PSBM_THEEB 1 36
DBREF 4TNK O 1 272 UNP P0A431 PSBO_THEEB 1 272
DBREF 4TNK T 1 32 UNP Q8DIQ0 PSBT_THEEB 1 32
DBREF 4TNK U 1 134 UNP Q9F1L5 PSBU_THEEB 1 134
DBREF 4TNK V 1 163 UNP P0A386 CY550_THEEB 1 163
DBREF 4TNK y 1 46 UNP Q8DJI1 YCF12_THEEB 1 46
DBREF 4TNK X 10 50 UNP Q9F1R6 PSBX_THEEB 1 41
DBREF 4TNK Y 1 28 PDB 4TNK 4TNK 1 28
DBREF 4TNK Z 1 62 UNP Q8DHJ2 PSBZ_THEEB 1 62
DBREF 4TNK a 1 344 UNP P0A444 PSBA1_THEEB 1 344
DBREF 4TNK b 1 510 UNP Q8DIQ1 Q8DIQ1_THEEB 1 510
DBREF 4TNK c 13 473 UNP Q8DIF8 Q8DIF8_THEEB 1 461
DBREF 4TNK d 1 352 UNP Q8CM25 PSBD_THEEB 1 352
DBREF 4TNK e 1 84 UNP Q8DIP0 PSBE_THEEB 1 84
DBREF 4TNK f 1 45 UNP Q8DIN9 PSBF_THEEB 1 45
DBREF 4TNK h 1 66 UNP Q8DJ43 PSBH_THEEB 1 66
DBREF 4TNK i 1 38 UNP Q8DJZ6 PSBI_THEEB 1 38
DBREF 4TNK j 1 40 UNP P59087 PSBJ_THEEB 1 40
DBREF 4TNK k 1 46 UNP Q9F1K9 PSBK_THEEB 1 46
DBREF 4TNK l 1 37 UNP Q8DIN8 PSBL_THEEB 1 37
DBREF 4TNK m 1 36 UNP Q8DHA7 PSBM_THEEB 1 36
DBREF 4TNK o 1 272 UNP P0A431 PSBO_THEEB 1 272
DBREF 4TNK t 1 32 UNP Q8DIQ0 PSBT_THEEB 1 32
DBREF 4TNK u 1 134 UNP Q9F1L5 PSBU_THEEB 1 134
DBREF 4TNK v 1 163 UNP P0A386 CY550_THEEB 1 163
DBREF 4TNK g 1 46 UNP Q8DJI1 YCF12_THEEB 1 46
DBREF 4TNK x 10 50 UNP Q9F1R6 PSBX_THEEB 1 41
DBREF 4TNK G 1 28 PDB 4TNK 4TNK 1 28
DBREF 4TNK z 1 62 UNP Q8DHJ2 PSBZ_THEEB 1 62
SEQRES 1 A 344 MET THR THR THR LEU GLN ARG ARG GLU SER ALA ASN LEU
SEQRES 2 A 344 TRP GLU ARG PHE CYS ASN TRP VAL THR SER THR ASP ASN
SEQRES 3 A 344 ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE MET ILE PRO
SEQRES 4 A 344 THR LEU LEU ALA ALA THR ILE CYS PHE VAL ILE ALA PHE
SEQRES 5 A 344 ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY ILE ARG GLU
SEQRES 6 A 344 PRO VAL SER GLY SER LEU LEU TYR GLY ASN ASN ILE ILE
SEQRES 7 A 344 THR GLY ALA VAL VAL PRO SER SER ASN ALA ILE GLY LEU
SEQRES 8 A 344 HIS PHE TYR PRO ILE TRP GLU ALA ALA SER LEU ASP GLU
SEQRES 9 A 344 TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU ILE ILE PHE
SEQRES 10 A 344 HIS PHE LEU LEU GLY ALA SER CYS TYR MET GLY ARG GLN
SEQRES 11 A 344 TRP GLU LEU SER TYR ARG LEU GLY MET ARG PRO TRP ILE
SEQRES 12 A 344 CYS VAL ALA TYR SER ALA PRO LEU ALA SER ALA PHE ALA
SEQRES 13 A 344 VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY SER PHE SER
SEQRES 14 A 344 ASP GLY MET PRO LEU GLY ILE SER GLY THR PHE ASN PHE
SEQRES 15 A 344 MET ILE VAL PHE GLN ALA GLU HIS ASN ILE LEU MET HIS
SEQRES 16 A 344 PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL PHE GLY GLY
SEQRES 17 A 344 ALA LEU PHE CYS ALA MET HIS GLY SER LEU VAL THR SER
SEQRES 18 A 344 SER LEU ILE ARG GLU THR THR GLU THR GLU SER ALA ASN
SEQRES 19 A 344 TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU THR TYR ASN
SEQRES 20 A 344 ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG LEU ILE PHE
SEQRES 21 A 344 GLN TYR ALA SER PHE ASN ASN SER ARG SER LEU HIS PHE
SEQRES 22 A 344 PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL TRP PHE THR
SEQRES 23 A 344 ALA LEU GLY ILE SER THR MET ALA PHE ASN LEU ASN GLY
SEQRES 24 A 344 PHE ASN PHE ASN HIS SER VAL ILE ASP ALA LYS GLY ASN
SEQRES 25 A 344 VAL ILE ASN THR TRP ALA ASP ILE ILE ASN ARG ALA ASN
SEQRES 26 A 344 LEU GLY MET GLU VAL MET HIS GLU ARG ASN ALA HIS ASN
SEQRES 27 A 344 PHE PRO LEU ASP LEU ALA
SEQRES 1 B 510 MET GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE
SEQRES 2 B 510 ASN ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS
SEQRES 3 B 510 THR ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU
SEQRES 4 B 510 TYR GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU
SEQRES 5 B 510 ASN PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE
SEQRES 6 B 510 MET ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP
SEQRES 7 B 510 SER ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP
SEQRES 8 B 510 SER PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER
SEQRES 9 B 510 GLY LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR
SEQRES 10 B 510 TRP ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU
SEQRES 11 B 510 PRO ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU
SEQRES 12 B 510 PHE LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE
SEQRES 13 B 510 HIS LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER
SEQRES 14 B 510 ASP PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA
SEQRES 15 B 510 PRO GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO
SEQRES 16 B 510 GLY GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL
SEQRES 17 B 510 GLY ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO
SEQRES 18 B 510 PRO GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE
SEQRES 19 B 510 GLU THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE
SEQRES 20 B 510 ALA ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER
SEQRES 21 B 510 ALA THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR
SEQRES 22 B 510 GLN TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG
SEQRES 23 B 510 ARG VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU
SEQRES 24 B 510 GLU ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR
SEQRES 25 B 510 ASP TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE
SEQRES 26 B 510 ARG THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN
SEQRES 27 B 510 ALA TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY
SEQRES 28 B 510 GLU GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU
SEQRES 29 B 510 SER PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL
SEQRES 30 B 510 LYS ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR
SEQRES 31 B 510 SER PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY
SEQRES 32 B 510 GLY GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR
SEQRES 33 B 510 VAL LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE
SEQRES 34 B 510 PHE GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE
SEQRES 35 B 510 PHE ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS
SEQRES 36 B 510 ALA VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP
SEQRES 37 B 510 HIS GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY
SEQRES 38 B 510 ILE ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY
SEQRES 39 B 510 PHE TYR GLN LYS VAL GLY ASP VAL THR THR ARG ARG LYS
SEQRES 40 B 510 GLU ALA VAL
SEQRES 1 C 461 MET VAL THR LEU SER SER ASN SER ILE PHE ALA THR ASN
SEQRES 2 C 461 ARG ASP GLN GLU SER SER GLY PHE ALA TRP TRP ALA GLY
SEQRES 3 C 461 ASN ALA ARG LEU ILE ASN LEU SER GLY LYS LEU LEU GLY
SEQRES 4 C 461 ALA HIS VAL ALA HIS ALA GLY LEU ILE VAL PHE TRP ALA
SEQRES 5 C 461 GLY ALA MET THR LEU PHE GLU LEU ALA HIS PHE ILE PRO
SEQRES 6 C 461 GLU LYS PRO MET TYR GLU GLN GLY LEU ILE LEU ILE PRO
SEQRES 7 C 461 HIS ILE ALA THR LEU GLY TRP GLY VAL GLY PRO GLY GLY
SEQRES 8 C 461 GLU VAL VAL ASP THR PHE PRO PHE PHE VAL VAL GLY VAL
SEQRES 9 C 461 VAL HIS LEU ILE SER SER ALA VAL LEU GLY PHE GLY GLY
SEQRES 10 C 461 VAL TYR HIS ALA ILE ARG GLY PRO GLU THR LEU GLU GLU
SEQRES 11 C 461 TYR SER SER PHE PHE GLY TYR ASP TRP LYS ASP LYS ASN
SEQRES 12 C 461 LYS MET THR THR ILE LEU GLY PHE HIS LEU ILE VAL LEU
SEQRES 13 C 461 GLY ILE GLY ALA LEU LEU LEU VAL ALA LYS ALA MET PHE
SEQRES 14 C 461 PHE GLY GLY LEU TYR ASP THR TRP ALA PRO GLY GLY GLY
SEQRES 15 C 461 ASP VAL ARG VAL ILE THR ASN PRO THR LEU ASP PRO ARG
SEQRES 16 C 461 VAL ILE PHE GLY TYR LEU LEU LYS SER PRO PHE GLY GLY
SEQRES 17 C 461 GLU GLY TRP ILE VAL SER VAL ASN ASN LEU GLU ASP VAL
SEQRES 18 C 461 VAL GLY GLY HIS ILE TRP ILE GLY LEU ILE CYS ILE ALA
SEQRES 19 C 461 GLY GLY ILE TRP HIS ILE LEU THR THR PRO PHE GLY TRP
SEQRES 20 C 461 ALA ARG ARG ALA PHE ILE TRP SER GLY GLU ALA TYR LEU
SEQRES 21 C 461 SER TYR SER LEU GLY ALA LEU SER MET MET GLY PHE ILE
SEQRES 22 C 461 ALA THR CYS PHE VAL TRP PHE ASN ASN THR VAL TYR PRO
SEQRES 23 C 461 SER GLU PHE TYR GLY PRO THR GLY PRO GLU ALA SER GLN
SEQRES 24 C 461 ALA GLN ALA MET THR PHE LEU ILE ARG ASP GLN LYS LEU
SEQRES 25 C 461 GLY ALA ASN VAL GLY SER ALA GLN GLY PRO THR GLY LEU
SEQRES 26 C 461 GLY LYS TYR LEU MET ARG SER PRO THR GLY GLU ILE ILE
SEQRES 27 C 461 PHE GLY GLY GLU THR MET ARG PHE TRP ASP PHE ARG GLY
SEQRES 28 C 461 PRO TRP LEU GLU PRO LEU ARG GLY PRO ASN GLY LEU ASP
SEQRES 29 C 461 LEU ASN LYS ILE LYS ASN ASP ILE GLN PRO TRP GLN GLU
SEQRES 30 C 461 ARG ARG ALA ALA GLU TYR MET THR HIS ALA PRO LEU GLY
SEQRES 31 C 461 SER LEU ASN SER VAL GLY GLY VAL ALA THR GLU ILE ASN
SEQRES 32 C 461 SER VAL ASN PHE VAL SER PRO ARG SER TRP LEU ALA THR
SEQRES 33 C 461 SER HIS PHE VAL LEU ALA PHE PHE PHE LEU VAL GLY HIS
SEQRES 34 C 461 LEU TRP HIS ALA GLY ARG ALA ARG ALA ALA ALA ALA GLY
SEQRES 35 C 461 PHE GLU LYS GLY ILE ASP ARG GLU SER GLU PRO VAL LEU
SEQRES 36 C 461 SER MET PRO SER LEU ASP
SEQRES 1 D 352 MET THR ILE ALA ILE GLY ARG ALA PRO ALA GLU ARG GLY
SEQRES 2 D 352 TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS ARG ASP ARG
SEQRES 3 D 352 PHE VAL PHE VAL GLY TRP SER GLY ILE LEU LEU PHE PRO
SEQRES 4 D 352 CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU THR GLY THR
SEQRES 5 D 352 THR PHE VAL THR SER TRP TYR THR HIS GLY LEU ALA SER
SEQRES 6 D 352 SER TYR LEU GLU GLY CYS ASN PHE LEU THR VAL ALA VAL
SEQRES 7 D 352 SER THR PRO ALA ASN SER MET GLY HIS SER LEU LEU LEU
SEQRES 8 D 352 LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE THR ARG TRP
SEQRES 9 D 352 CYS GLN LEU GLY GLY LEU TRP THR PHE ILE ALA LEU HIS
SEQRES 10 D 352 GLY ALA PHE GLY LEU ILE GLY PHE MET LEU ARG GLN PHE
SEQRES 11 D 352 GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO TYR ASN ALA
SEQRES 12 D 352 ILE ALA PHE SER ALA PRO ILE ALA VAL PHE VAL SER VAL
SEQRES 13 D 352 PHE LEU ILE TYR PRO LEU GLY GLN SER SER TRP PHE PHE
SEQRES 14 D 352 ALA PRO SER PHE GLY VAL ALA ALA ILE PHE ARG PHE LEU
SEQRES 15 D 352 LEU PHE PHE GLN GLY PHE HIS ASN TRP THR LEU ASN PRO
SEQRES 16 D 352 PHE HIS MET MET GLY VAL ALA GLY VAL LEU GLY GLY ALA
SEQRES 17 D 352 LEU LEU CYS ALA ILE HIS GLY ALA THR VAL GLU ASN THR
SEQRES 18 D 352 LEU PHE GLN ASP GLY GLU GLY ALA SER THR PHE ARG ALA
SEQRES 19 D 352 PHE ASN PRO THR GLN ALA GLU GLU THR TYR SER MET VAL
SEQRES 20 D 352 THR ALA ASN ARG PHE TRP SER GLN ILE PHE GLY ILE ALA
SEQRES 21 D 352 PHE SER ASN LYS ARG TRP LEU HIS PHE PHE MET LEU PHE
SEQRES 22 D 352 VAL PRO VAL THR GLY LEU TRP MET SER ALA ILE GLY VAL
SEQRES 23 D 352 VAL GLY LEU ALA LEU ASN LEU ARG SER TYR ASP PHE ILE
SEQRES 24 D 352 SER GLN GLU ILE ARG ALA ALA GLU ASP PRO GLU PHE GLU
SEQRES 25 D 352 THR PHE TYR THR LYS ASN LEU LEU LEU ASN GLU GLY ILE
SEQRES 26 D 352 ARG ALA TRP MET ALA PRO GLN ASP GLN PRO HIS GLU ASN
SEQRES 27 D 352 PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG GLY ASN ALA
SEQRES 28 D 352 LEU
SEQRES 1 E 84 MET ALA GLY THR THR GLY GLU ARG PRO PHE SER ASP ILE
SEQRES 2 E 84 ILE THR SER VAL ARG TYR TRP VAL ILE HIS SER ILE THR
SEQRES 3 E 84 ILE PRO ALA LEU PHE ILE ALA GLY TRP LEU PHE VAL SER
SEQRES 4 E 84 THR GLY LEU ALA TYR ASP VAL PHE GLY THR PRO ARG PRO
SEQRES 5 E 84 ASP SER TYR TYR ALA GLN GLU GLN ARG SER ILE PRO LEU
SEQRES 6 E 84 VAL THR ASP ARG PHE GLU ALA LYS GLN GLN VAL GLU THR
SEQRES 7 E 84 PHE LEU GLU GLN LEU LYS
SEQRES 1 F 45 MET THR SER ASN THR PRO ASN GLN GLU PRO VAL SER TYR
SEQRES 2 F 45 PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR LEU
SEQRES 3 F 45 ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA ALA
SEQRES 4 F 45 MET GLN PHE ILE GLN ARG
SEQRES 1 H 66 MET ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO
SEQRES 2 H 66 LEU ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY
SEQRES 3 H 66 THR THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU
SEQRES 4 H 66 VAL PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR
SEQRES 5 H 66 LEU ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU
SEQRES 6 H 66 GLY
SEQRES 1 I 38 MET GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR
SEQRES 2 I 38 PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY
SEQRES 3 I 38 ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP LEU GLU
SEQRES 1 J 40 MET MET SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL
SEQRES 2 J 40 ALA THR VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY
SEQRES 3 J 40 LEU PHE PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER
SEQRES 4 J 40 LEU
SEQRES 1 K 46 MET ILE ASP ALA LEU VAL LEU VAL ALA LYS LEU PRO GLU
SEQRES 2 K 46 ALA TYR ALA ILE PHE ASP PRO LEU VAL ASP VAL LEU PRO
SEQRES 3 K 46 VAL ILE PRO VAL LEU PHE LEU ALA LEU ALA PHE VAL TRP
SEQRES 4 K 46 GLN ALA ALA VAL GLY PHE ARG
SEQRES 1 L 37 MET GLU PRO ASN PRO ASN ARG GLN PRO VAL GLU LEU ASN
SEQRES 2 L 37 ARG THR SER LEU TYR LEU GLY LEU LEU LEU ILE LEU VAL
SEQRES 3 L 37 LEU ALA LEU LEU PHE SER SER TYR PHE PHE ASN
SEQRES 1 M 36 MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU
SEQRES 2 M 36 PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR
SEQRES 3 M 36 VAL GLN THR GLU SER GLN GLN LYS SER SER
SEQRES 1 O 272 MET LYS TYR ARG ILE LEU MET ALA THR LEU LEU ALA VAL
SEQRES 2 O 272 CYS LEU GLY ILE PHE SER LEU SER ALA PRO ALA PHE ALA
SEQRES 3 O 272 ALA LYS GLN THR LEU THR TYR ASP ASP ILE VAL GLY THR
SEQRES 4 O 272 GLY LEU ALA ASN LYS CYS PRO THR LEU ASP ASP THR ALA
SEQRES 5 O 272 ARG GLY ALA TYR PRO ILE ASP SER SER GLN THR TYR ARG
SEQRES 6 O 272 ILE ALA ARG LEU CYS LEU GLN PRO THR THR PHE LEU VAL
SEQRES 7 O 272 LYS GLU GLU PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE
SEQRES 8 O 272 VAL PRO THR LYS LEU VAL THR ARG GLU THR THR SER LEU
SEQRES 9 O 272 ASP GLN ILE GLN GLY GLU LEU LYS VAL ASN SER ASP GLY
SEQRES 10 O 272 SER LEU THR PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN
SEQRES 11 O 272 PRO VAL THR VAL GLN MET ALA GLY GLY GLU ARG ILE PRO
SEQRES 12 O 272 LEU LEU PHE THR VAL LYS ASN LEU VAL ALA SER THR GLN
SEQRES 13 O 272 PRO ASN VAL THR SER ILE THR THR SER THR ASP PHE LYS
SEQRES 14 O 272 GLY GLU PHE ASN VAL PRO SER TYR ARG THR ALA ASN PHE
SEQRES 15 O 272 LEU ASP PRO LYS GLY ARG GLY LEU ALA SER GLY TYR ASP
SEQRES 16 O 272 SER ALA ILE ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU
SEQRES 17 O 272 ALA ARG ALA ASN VAL LYS ARG PHE SER LEU THR LYS GLY
SEQRES 18 O 272 GLN ILE SER LEU ASN VAL ALA LYS VAL ASP GLY ARG THR
SEQRES 19 O 272 GLY GLU ILE ALA GLY THR PHE GLU SER GLU GLN LEU SER
SEQRES 20 O 272 ASP ASP ASP MET GLY ALA HIS GLU PRO HIS GLU VAL LYS
SEQRES 21 O 272 ILE GLN GLY VAL PHE TYR ALA SER ILE GLU PRO ALA
SEQRES 1 T 32 MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE
SEQRES 2 T 32 ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO
SEQRES 3 T 32 PRO ARG ILE THR LYS LYS
SEQRES 1 U 134 MET GLN ARG LEU GLY ARG TRP LEU ALA LEU ALA TYR PHE
SEQRES 2 U 134 VAL GLY VAL SER LEU LEU GLY TRP ILE ASN TRP SER ALA
SEQRES 3 U 134 PRO THR LEU ALA ALA THR ALA SER THR GLU GLU GLU LEU
SEQRES 4 U 134 VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA TYR GLY
SEQRES 5 U 134 GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA ALA PHE
SEQRES 6 U 134 ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA LYS LEU
SEQRES 7 U 134 ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU ASP VAL
SEQRES 8 U 134 LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS GLN ILE
SEQRES 9 U 134 LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR GLU VAL
SEQRES 10 U 134 GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR ASN ASN
SEQRES 11 U 134 GLY LEU TYR LYS
SEQRES 1 V 163 MET LEU LYS LYS CYS VAL TRP LEU ALA VAL ALA LEU CYS
SEQRES 2 V 163 LEU CYS LEU TRP GLN PHE THR MET GLY THR ALA LEU ALA
SEQRES 3 V 163 ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN
SEQRES 4 V 163 SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR
SEQRES 5 V 163 LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER
SEQRES 6 V 163 CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU
SEQRES 7 V 163 ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO
SEQRES 8 V 163 ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN
SEQRES 9 V 163 PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL
SEQRES 10 V 163 HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET
SEQRES 11 V 163 ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY
SEQRES 12 V 163 HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP
SEQRES 13 V 163 GLY GLY GLY LYS VAL TYR TYR
SEQRES 1 y 46 MET GLY ILE PHE ASN GLY ILE ILE GLU PHE LEU SER ASN
SEQRES 2 y 46 ILE ASN PHE GLU VAL ILE ALA GLN LEU THR MET ILE ALA
SEQRES 3 y 46 MET ILE GLY ILE ALA GLY PRO MET ILE ILE PHE LEU LEU
SEQRES 4 y 46 ALA VAL ARG ARG GLY ASN LEU
SEQRES 1 X 41 MET THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY
SEQRES 2 X 41 LEU LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA
SEQRES 3 X 41 VAL LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG
SEQRES 4 X 41 SER LEU
SEQRES 1 Y 28 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 2 Y 28 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 3 Y 28 UNK UNK
SEQRES 1 Z 62 MET THR ILE LEU PHE GLN LEU ALA LEU ALA ALA LEU VAL
SEQRES 2 Z 62 ILE LEU SER PHE VAL MET VAL ILE GLY VAL PRO VAL ALA
SEQRES 3 Z 62 TYR ALA SER PRO GLN ASP TRP ASP ARG SER LYS GLN LEU
SEQRES 4 Z 62 ILE PHE LEU GLY SER GLY LEU TRP ILE ALA LEU VAL LEU
SEQRES 5 Z 62 VAL VAL GLY VAL LEU ASN PHE PHE VAL VAL
SEQRES 1 a 344 MET THR THR THR LEU GLN ARG ARG GLU SER ALA ASN LEU
SEQRES 2 a 344 TRP GLU ARG PHE CYS ASN TRP VAL THR SER THR ASP ASN
SEQRES 3 a 344 ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE MET ILE PRO
SEQRES 4 a 344 THR LEU LEU ALA ALA THR ILE CYS PHE VAL ILE ALA PHE
SEQRES 5 a 344 ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY ILE ARG GLU
SEQRES 6 a 344 PRO VAL SER GLY SER LEU LEU TYR GLY ASN ASN ILE ILE
SEQRES 7 a 344 THR GLY ALA VAL VAL PRO SER SER ASN ALA ILE GLY LEU
SEQRES 8 a 344 HIS PHE TYR PRO ILE TRP GLU ALA ALA SER LEU ASP GLU
SEQRES 9 a 344 TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU ILE ILE PHE
SEQRES 10 a 344 HIS PHE LEU LEU GLY ALA SER CYS TYR MET GLY ARG GLN
SEQRES 11 a 344 TRP GLU LEU SER TYR ARG LEU GLY MET ARG PRO TRP ILE
SEQRES 12 a 344 CYS VAL ALA TYR SER ALA PRO LEU ALA SER ALA PHE ALA
SEQRES 13 a 344 VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY SER PHE SER
SEQRES 14 a 344 ASP GLY MET PRO LEU GLY ILE SER GLY THR PHE ASN PHE
SEQRES 15 a 344 MET ILE VAL PHE GLN ALA GLU HIS ASN ILE LEU MET HIS
SEQRES 16 a 344 PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL PHE GLY GLY
SEQRES 17 a 344 ALA LEU PHE CYS ALA MET HIS GLY SER LEU VAL THR SER
SEQRES 18 a 344 SER LEU ILE ARG GLU THR THR GLU THR GLU SER ALA ASN
SEQRES 19 a 344 TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU THR TYR ASN
SEQRES 20 a 344 ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG LEU ILE PHE
SEQRES 21 a 344 GLN TYR ALA SER PHE ASN ASN SER ARG SER LEU HIS PHE
SEQRES 22 a 344 PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL TRP PHE THR
SEQRES 23 a 344 ALA LEU GLY ILE SER THR MET ALA PHE ASN LEU ASN GLY
SEQRES 24 a 344 PHE ASN PHE ASN HIS SER VAL ILE ASP ALA LYS GLY ASN
SEQRES 25 a 344 VAL ILE ASN THR TRP ALA ASP ILE ILE ASN ARG ALA ASN
SEQRES 26 a 344 LEU GLY MET GLU VAL MET HIS GLU ARG ASN ALA HIS ASN
SEQRES 27 a 344 PHE PRO LEU ASP LEU ALA
SEQRES 1 b 510 MET GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE
SEQRES 2 b 510 ASN ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS
SEQRES 3 b 510 THR ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU
SEQRES 4 b 510 TYR GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU
SEQRES 5 b 510 ASN PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE
SEQRES 6 b 510 MET ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP
SEQRES 7 b 510 SER ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP
SEQRES 8 b 510 SER PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER
SEQRES 9 b 510 GLY LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR
SEQRES 10 b 510 TRP ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU
SEQRES 11 b 510 PRO ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU
SEQRES 12 b 510 PHE LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE
SEQRES 13 b 510 HIS LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER
SEQRES 14 b 510 ASP PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA
SEQRES 15 b 510 PRO GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO
SEQRES 16 b 510 GLY GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL
SEQRES 17 b 510 GLY ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO
SEQRES 18 b 510 PRO GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE
SEQRES 19 b 510 GLU THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE
SEQRES 20 b 510 ALA ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER
SEQRES 21 b 510 ALA THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR
SEQRES 22 b 510 GLN TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG
SEQRES 23 b 510 ARG VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU
SEQRES 24 b 510 GLU ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR
SEQRES 25 b 510 ASP TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE
SEQRES 26 b 510 ARG THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN
SEQRES 27 b 510 ALA TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY
SEQRES 28 b 510 GLU GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU
SEQRES 29 b 510 SER PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL
SEQRES 30 b 510 LYS ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR
SEQRES 31 b 510 SER PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY
SEQRES 32 b 510 GLY GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR
SEQRES 33 b 510 VAL LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE
SEQRES 34 b 510 PHE GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE
SEQRES 35 b 510 PHE ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS
SEQRES 36 b 510 ALA VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP
SEQRES 37 b 510 HIS GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY
SEQRES 38 b 510 ILE ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY
SEQRES 39 b 510 PHE TYR GLN LYS VAL GLY ASP VAL THR THR ARG ARG LYS
SEQRES 40 b 510 GLU ALA VAL
SEQRES 1 c 461 MET VAL THR LEU SER SER ASN SER ILE PHE ALA THR ASN
SEQRES 2 c 461 ARG ASP GLN GLU SER SER GLY PHE ALA TRP TRP ALA GLY
SEQRES 3 c 461 ASN ALA ARG LEU ILE ASN LEU SER GLY LYS LEU LEU GLY
SEQRES 4 c 461 ALA HIS VAL ALA HIS ALA GLY LEU ILE VAL PHE TRP ALA
SEQRES 5 c 461 GLY ALA MET THR LEU PHE GLU LEU ALA HIS PHE ILE PRO
SEQRES 6 c 461 GLU LYS PRO MET TYR GLU GLN GLY LEU ILE LEU ILE PRO
SEQRES 7 c 461 HIS ILE ALA THR LEU GLY TRP GLY VAL GLY PRO GLY GLY
SEQRES 8 c 461 GLU VAL VAL ASP THR PHE PRO PHE PHE VAL VAL GLY VAL
SEQRES 9 c 461 VAL HIS LEU ILE SER SER ALA VAL LEU GLY PHE GLY GLY
SEQRES 10 c 461 VAL TYR HIS ALA ILE ARG GLY PRO GLU THR LEU GLU GLU
SEQRES 11 c 461 TYR SER SER PHE PHE GLY TYR ASP TRP LYS ASP LYS ASN
SEQRES 12 c 461 LYS MET THR THR ILE LEU GLY PHE HIS LEU ILE VAL LEU
SEQRES 13 c 461 GLY ILE GLY ALA LEU LEU LEU VAL ALA LYS ALA MET PHE
SEQRES 14 c 461 PHE GLY GLY LEU TYR ASP THR TRP ALA PRO GLY GLY GLY
SEQRES 15 c 461 ASP VAL ARG VAL ILE THR ASN PRO THR LEU ASP PRO ARG
SEQRES 16 c 461 VAL ILE PHE GLY TYR LEU LEU LYS SER PRO PHE GLY GLY
SEQRES 17 c 461 GLU GLY TRP ILE VAL SER VAL ASN ASN LEU GLU ASP VAL
SEQRES 18 c 461 VAL GLY GLY HIS ILE TRP ILE GLY LEU ILE CYS ILE ALA
SEQRES 19 c 461 GLY GLY ILE TRP HIS ILE LEU THR THR PRO PHE GLY TRP
SEQRES 20 c 461 ALA ARG ARG ALA PHE ILE TRP SER GLY GLU ALA TYR LEU
SEQRES 21 c 461 SER TYR SER LEU GLY ALA LEU SER MET MET GLY PHE ILE
SEQRES 22 c 461 ALA THR CYS PHE VAL TRP PHE ASN ASN THR VAL TYR PRO
SEQRES 23 c 461 SER GLU PHE TYR GLY PRO THR GLY PRO GLU ALA SER GLN
SEQRES 24 c 461 ALA GLN ALA MET THR PHE LEU ILE ARG ASP GLN LYS LEU
SEQRES 25 c 461 GLY ALA ASN VAL GLY SER ALA GLN GLY PRO THR GLY LEU
SEQRES 26 c 461 GLY LYS TYR LEU MET ARG SER PRO THR GLY GLU ILE ILE
SEQRES 27 c 461 PHE GLY GLY GLU THR MET ARG PHE TRP ASP PHE ARG GLY
SEQRES 28 c 461 PRO TRP LEU GLU PRO LEU ARG GLY PRO ASN GLY LEU ASP
SEQRES 29 c 461 LEU ASN LYS ILE LYS ASN ASP ILE GLN PRO TRP GLN GLU
SEQRES 30 c 461 ARG ARG ALA ALA GLU TYR MET THR HIS ALA PRO LEU GLY
SEQRES 31 c 461 SER LEU ASN SER VAL GLY GLY VAL ALA THR GLU ILE ASN
SEQRES 32 c 461 SER VAL ASN PHE VAL SER PRO ARG SER TRP LEU ALA THR
SEQRES 33 c 461 SER HIS PHE VAL LEU ALA PHE PHE PHE LEU VAL GLY HIS
SEQRES 34 c 461 LEU TRP HIS ALA GLY ARG ALA ARG ALA ALA ALA ALA GLY
SEQRES 35 c 461 PHE GLU LYS GLY ILE ASP ARG GLU SER GLU PRO VAL LEU
SEQRES 36 c 461 SER MET PRO SER LEU ASP
SEQRES 1 d 352 MET THR ILE ALA ILE GLY ARG ALA PRO ALA GLU ARG GLY
SEQRES 2 d 352 TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS ARG ASP ARG
SEQRES 3 d 352 PHE VAL PHE VAL GLY TRP SER GLY ILE LEU LEU PHE PRO
SEQRES 4 d 352 CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU THR GLY THR
SEQRES 5 d 352 THR PHE VAL THR SER TRP TYR THR HIS GLY LEU ALA SER
SEQRES 6 d 352 SER TYR LEU GLU GLY CYS ASN PHE LEU THR VAL ALA VAL
SEQRES 7 d 352 SER THR PRO ALA ASN SER MET GLY HIS SER LEU LEU LEU
SEQRES 8 d 352 LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE THR ARG TRP
SEQRES 9 d 352 CYS GLN LEU GLY GLY LEU TRP THR PHE ILE ALA LEU HIS
SEQRES 10 d 352 GLY ALA PHE GLY LEU ILE GLY PHE MET LEU ARG GLN PHE
SEQRES 11 d 352 GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO TYR ASN ALA
SEQRES 12 d 352 ILE ALA PHE SER ALA PRO ILE ALA VAL PHE VAL SER VAL
SEQRES 13 d 352 PHE LEU ILE TYR PRO LEU GLY GLN SER SER TRP PHE PHE
SEQRES 14 d 352 ALA PRO SER PHE GLY VAL ALA ALA ILE PHE ARG PHE LEU
SEQRES 15 d 352 LEU PHE PHE GLN GLY PHE HIS ASN TRP THR LEU ASN PRO
SEQRES 16 d 352 PHE HIS MET MET GLY VAL ALA GLY VAL LEU GLY GLY ALA
SEQRES 17 d 352 LEU LEU CYS ALA ILE HIS GLY ALA THR VAL GLU ASN THR
SEQRES 18 d 352 LEU PHE GLN ASP GLY GLU GLY ALA SER THR PHE ARG ALA
SEQRES 19 d 352 PHE ASN PRO THR GLN ALA GLU GLU THR TYR SER MET VAL
SEQRES 20 d 352 THR ALA ASN ARG PHE TRP SER GLN ILE PHE GLY ILE ALA
SEQRES 21 d 352 PHE SER ASN LYS ARG TRP LEU HIS PHE PHE MET LEU PHE
SEQRES 22 d 352 VAL PRO VAL THR GLY LEU TRP MET SER ALA ILE GLY VAL
SEQRES 23 d 352 VAL GLY LEU ALA LEU ASN LEU ARG SER TYR ASP PHE ILE
SEQRES 24 d 352 SER GLN GLU ILE ARG ALA ALA GLU ASP PRO GLU PHE GLU
SEQRES 25 d 352 THR PHE TYR THR LYS ASN LEU LEU LEU ASN GLU GLY ILE
SEQRES 26 d 352 ARG ALA TRP MET ALA PRO GLN ASP GLN PRO HIS GLU ASN
SEQRES 27 d 352 PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG GLY ASN ALA
SEQRES 28 d 352 LEU
SEQRES 1 e 84 MET ALA GLY THR THR GLY GLU ARG PRO PHE SER ASP ILE
SEQRES 2 e 84 ILE THR SER VAL ARG TYR TRP VAL ILE HIS SER ILE THR
SEQRES 3 e 84 ILE PRO ALA LEU PHE ILE ALA GLY TRP LEU PHE VAL SER
SEQRES 4 e 84 THR GLY LEU ALA TYR ASP VAL PHE GLY THR PRO ARG PRO
SEQRES 5 e 84 ASP SER TYR TYR ALA GLN GLU GLN ARG SER ILE PRO LEU
SEQRES 6 e 84 VAL THR ASP ARG PHE GLU ALA LYS GLN GLN VAL GLU THR
SEQRES 7 e 84 PHE LEU GLU GLN LEU LYS
SEQRES 1 f 45 MET THR SER ASN THR PRO ASN GLN GLU PRO VAL SER TYR
SEQRES 2 f 45 PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR LEU
SEQRES 3 f 45 ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA ALA
SEQRES 4 f 45 MET GLN PHE ILE GLN ARG
SEQRES 1 h 66 MET ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO
SEQRES 2 h 66 LEU ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY
SEQRES 3 h 66 THR THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU
SEQRES 4 h 66 VAL PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR
SEQRES 5 h 66 LEU ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU
SEQRES 6 h 66 GLY
SEQRES 1 i 38 MET GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR
SEQRES 2 i 38 PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY
SEQRES 3 i 38 ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP LEU GLU
SEQRES 1 j 40 MET MET SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL
SEQRES 2 j 40 ALA THR VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY
SEQRES 3 j 40 LEU PHE PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER
SEQRES 4 j 40 LEU
SEQRES 1 k 46 MET ILE ASP ALA LEU VAL LEU VAL ALA LYS LEU PRO GLU
SEQRES 2 k 46 ALA TYR ALA ILE PHE ASP PRO LEU VAL ASP VAL LEU PRO
SEQRES 3 k 46 VAL ILE PRO VAL LEU PHE LEU ALA LEU ALA PHE VAL TRP
SEQRES 4 k 46 GLN ALA ALA VAL GLY PHE ARG
SEQRES 1 l 37 MET GLU PRO ASN PRO ASN ARG GLN PRO VAL GLU LEU ASN
SEQRES 2 l 37 ARG THR SER LEU TYR LEU GLY LEU LEU LEU ILE LEU VAL
SEQRES 3 l 37 LEU ALA LEU LEU PHE SER SER TYR PHE PHE ASN
SEQRES 1 m 36 MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU
SEQRES 2 m 36 PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR
SEQRES 3 m 36 VAL GLN THR GLU SER GLN GLN LYS SER SER
SEQRES 1 o 272 MET LYS TYR ARG ILE LEU MET ALA THR LEU LEU ALA VAL
SEQRES 2 o 272 CYS LEU GLY ILE PHE SER LEU SER ALA PRO ALA PHE ALA
SEQRES 3 o 272 ALA LYS GLN THR LEU THR TYR ASP ASP ILE VAL GLY THR
SEQRES 4 o 272 GLY LEU ALA ASN LYS CYS PRO THR LEU ASP ASP THR ALA
SEQRES 5 o 272 ARG GLY ALA TYR PRO ILE ASP SER SER GLN THR TYR ARG
SEQRES 6 o 272 ILE ALA ARG LEU CYS LEU GLN PRO THR THR PHE LEU VAL
SEQRES 7 o 272 LYS GLU GLU PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE
SEQRES 8 o 272 VAL PRO THR LYS LEU VAL THR ARG GLU THR THR SER LEU
SEQRES 9 o 272 ASP GLN ILE GLN GLY GLU LEU LYS VAL ASN SER ASP GLY
SEQRES 10 o 272 SER LEU THR PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN
SEQRES 11 o 272 PRO VAL THR VAL GLN MET ALA GLY GLY GLU ARG ILE PRO
SEQRES 12 o 272 LEU LEU PHE THR VAL LYS ASN LEU VAL ALA SER THR GLN
SEQRES 13 o 272 PRO ASN VAL THR SER ILE THR THR SER THR ASP PHE LYS
SEQRES 14 o 272 GLY GLU PHE ASN VAL PRO SER TYR ARG THR ALA ASN PHE
SEQRES 15 o 272 LEU ASP PRO LYS GLY ARG GLY LEU ALA SER GLY TYR ASP
SEQRES 16 o 272 SER ALA ILE ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU
SEQRES 17 o 272 ALA ARG ALA ASN VAL LYS ARG PHE SER LEU THR LYS GLY
SEQRES 18 o 272 GLN ILE SER LEU ASN VAL ALA LYS VAL ASP GLY ARG THR
SEQRES 19 o 272 GLY GLU ILE ALA GLY THR PHE GLU SER GLU GLN LEU SER
SEQRES 20 o 272 ASP ASP ASP MET GLY ALA HIS GLU PRO HIS GLU VAL LYS
SEQRES 21 o 272 ILE GLN GLY VAL PHE TYR ALA SER ILE GLU PRO ALA
SEQRES 1 t 32 MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE
SEQRES 2 t 32 ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO
SEQRES 3 t 32 PRO ARG ILE THR LYS LYS
SEQRES 1 u 134 MET GLN ARG LEU GLY ARG TRP LEU ALA LEU ALA TYR PHE
SEQRES 2 u 134 VAL GLY VAL SER LEU LEU GLY TRP ILE ASN TRP SER ALA
SEQRES 3 u 134 PRO THR LEU ALA ALA THR ALA SER THR GLU GLU GLU LEU
SEQRES 4 u 134 VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA TYR GLY
SEQRES 5 u 134 GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA ALA PHE
SEQRES 6 u 134 ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA LYS LEU
SEQRES 7 u 134 ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU ASP VAL
SEQRES 8 u 134 LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS GLN ILE
SEQRES 9 u 134 LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR GLU VAL
SEQRES 10 u 134 GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR ASN ASN
SEQRES 11 u 134 GLY LEU TYR LYS
SEQRES 1 v 163 MET LEU LYS LYS CYS VAL TRP LEU ALA VAL ALA LEU CYS
SEQRES 2 v 163 LEU CYS LEU TRP GLN PHE THR MET GLY THR ALA LEU ALA
SEQRES 3 v 163 ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN
SEQRES 4 v 163 SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR
SEQRES 5 v 163 LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER
SEQRES 6 v 163 CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU
SEQRES 7 v 163 ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO
SEQRES 8 v 163 ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN
SEQRES 9 v 163 PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL
SEQRES 10 v 163 HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET
SEQRES 11 v 163 ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY
SEQRES 12 v 163 HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP
SEQRES 13 v 163 GLY GLY GLY LYS VAL TYR TYR
SEQRES 1 g 46 MET GLY ILE PHE ASN GLY ILE ILE GLU PHE LEU SER ASN
SEQRES 2 g 46 ILE ASN PHE GLU VAL ILE ALA GLN LEU THR MET ILE ALA
SEQRES 3 g 46 MET ILE GLY ILE ALA GLY PRO MET ILE ILE PHE LEU LEU
SEQRES 4 g 46 ALA VAL ARG ARG GLY ASN LEU
SEQRES 1 x 41 MET THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY
SEQRES 2 x 41 LEU LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA
SEQRES 3 x 41 VAL LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG
SEQRES 4 x 41 SER LEU
SEQRES 1 G 28 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 2 G 28 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 3 G 28 UNK UNK
SEQRES 1 z 62 MET THR ILE LEU PHE GLN LEU ALA LEU ALA ALA LEU VAL
SEQRES 2 z 62 ILE LEU SER PHE VAL MET VAL ILE GLY VAL PRO VAL ALA
SEQRES 3 z 62 TYR ALA SER PRO GLN ASP TRP ASP ARG SER LYS GLN LEU
SEQRES 4 z 62 ILE PHE LEU GLY SER GLY LEU TRP ILE ALA LEU VAL LEU
SEQRES 5 z 62 VAL VAL GLY VAL LEU ASN PHE PHE VAL VAL
HET FE2 A 401 1
HET CLA A 402 65
HET CLA A 403 65
HET CLA A 404 65
HET PHO A 405 64
HET CLA A 406 65
HET PL9 A 407 45
HET BCR A 408 40
HET DGD A 409 56
HET LHG A 410 39
HET CL A 411 1
HET OEX A 412 10
HET SQD A 413 51
HET SQD A 414 54
HET CLA B 601 65
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 BCR B 616 40
HET BCR B 617 40
HET BCR B 618 40
HET BCR B 619 40
HET DGD B 620 58
HET LMG B 621 49
HET SQD B 622 43
HET LMT B 623 35
HET LMT B 624 35
HET LMG B 625 49
HET DGD B 626 52
HET SQD B 627 47
HET LMT B 628 35
HET LMT B 629 35
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 BCR C 513 40
HET DGD C 514 53
HET DGD C 515 62
HET DGD C 516 66
HET LMG C 517 45
HET LHG C 518 37
HET CLA C 519 65
HET BCR C 520 40
HET LMG C 521 48
HET PHO D 401 64
HET BCT D 402 4
HET CLA D 403 65
HET CLA D 404 65
HET PL9 D 405 55
HET LMG D 406 48
HET DGD D 407 63
HET LMT D 408 31
HET LMG D 409 46
HET LMG E 101 44
HET HEM F 101 43
HET BCR F 102 40
HET SQD F 103 45
HET CLA H 101 65
HET BCR H 102 40
HET LMG I 101 43
HET LMT I 102 35
HET PL9 J 101 35
HET BCR J 102 40
HET BCR K 101 40
HET CA K 102 1
HET LMG L 101 51
HET LMG M 101 42
HET LMT M 102 35
HET LMT M 103 35
HET CA O 301 1
HET HEM V 201 43
HET BCR y 101 40
HET SQD a 401 54
HET LMG a 402 42
HET CLA a 403 65
HET CLA a 404 65
HET CLA a 405 65
HET CLA a 406 65
HET PL9 a 407 45
HET DGD a 408 56
HET LHG a 409 39
HET CL a 410 1
HET OEX a 411 10
HET SQD a 412 51
HET FE2 a 413 1
HET DGD b 601 52
HET SQD b 602 47
HET LMT b 603 35
HET LMT b 604 35
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 CLA b 618 65
HET CLA b 619 65
HET CLA b 620 65
HET BCR b 621 40
HET BCR b 622 40
HET BCR b 623 40
HET BCR b 624 40
HET DGD b 625 58
HET LMG b 626 49
HET LMG b 627 42
HET LMT b 628 35
HET LMT b 629 35
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 BCR c 513 40
HET BCR c 514 40
HET DGD c 515 53
HET DGD c 516 62
HET DGD c 517 66
HET LMG c 518 45
HET LHG c 519 37
HET CLA c 520 65
HET BCR c 521 40
HET LMG c 522 48
HET PHO d 401 64
HET PHO d 402 64
HET SQD d 403 43
HET BCT d 404 4
HET CLA d 405 65
HET CLA d 406 65
HET PL9 d 407 55
HET LMG d 408 49
HET LMG d 409 48
HET DGD d 410 63
HET LMT d 411 31
HET LMG d 412 46
HET LMG e 101 44
HET HEM f 101 43
HET BCR f 102 40
HET SQD f 103 45
HET BCR i 101 40
HET LMG i 102 43
HET LMT i 103 35
HET PL9 j 101 35
HET BCR j 102 40
HET CA k 101 1
HET LMG l 101 51
HET LMG m 101 42
HET CA o 301 1
HET HEM v 201 43
HET BCR g 101 40
HET BCR x 101 40
HETNAM FE2 FE (II) ION
HETNAM CLA CHLOROPHYLL A
HETNAM PHO PHEOPHYTIN A
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 BCR BETA-CAROTENE
HETNAM DGD DIGALACTOSYL DIACYL GLYCEROL (DGDG)
HETNAM LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE
HETNAM CL CHLORIDE ION
HETNAM OEX CA-MN4-O5 CLUSTER
HETNAM SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-
HETNAM 2 SQD GLUCOPYRANOSYL]-SN-GLYCEROL
HETNAM LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE
HETNAM LMT DODECYL-BETA-D-MALTOSIDE
HETNAM BCT BICARBONATE ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM CA CALCIUM ION
HETSYN PL9 PLASTOQUINONE 9
HETSYN SQD SULFOQUINOVOSYLDIACYLGLYCEROL
HETSYN HEM HEME
FORMUL 41 FE2 2(FE 2+)
FORMUL 42 CLA 70(C55 H72 MG N4 O5 2+)
FORMUL 45 PHO 4(C55 H74 N4 O5)
FORMUL 47 PL9 6(C53 H80 O2)
FORMUL 48 BCR 24(C40 H56)
FORMUL 49 DGD 14(C51 H96 O15)
FORMUL 50 LHG 4(C38 H75 O10 P)
FORMUL 51 CL 2(CL 1-)
FORMUL 52 OEX 2(CA MN4 O5)
FORMUL 53 SQD 10(C41 H78 O12 S)
FORMUL 75 LMG 22(C45 H86 O10)
FORMUL 77 LMT 14(C24 H46 O11)
FORMUL 06 BCT 2(C H O3 1-)
FORMUL 15 HEM 4(C34 H32 FE N4 O4)
FORMUL 25 CA 4(CA 2+)
HELIX 1 AA1 ASN A 12 THR A 22 1 11
HELIX 2 AA2 PHE A 33 ALA A 55 1 23
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 MET A 293 1 27
HELIX 17 AB8 THR A 316 HIS A 332 1 17
HELIX 18 AB9 GLU A 333 HIS A 337 5 5
HELIX 19 AC1 PRO B 4 ILE B 13 5 10
HELIX 20 AC2 ASP B 15 ALA B 43 1 29
HELIX 21 AC3 PRO B 54 GLN B 58 5 5
HELIX 22 AC4 VAL B 62 ARG B 68 1 7
HELIX 23 AC5 SER B 92 TYR B 117 1 26
HELIX 24 AC6 LEU B 120 ARG B 124 5 5
HELIX 25 AC7 ASP B 134 PHE B 156 1 23
HELIX 26 AC8 GLY B 186 ASN B 191 5 6
HELIX 27 AC9 ASN B 194 VAL B 219 1 26
HELIX 28 AD1 PRO B 222 LEU B 229 1 8
HELIX 29 AD2 ASN B 233 GLU B 235 5 3
HELIX 30 AD3 THR B 236 TYR B 258 1 23
HELIX 31 AD4 PRO B 264 GLY B 269 1 6
HELIX 32 AD5 THR B 271 SER B 277 1 7
HELIX 33 AD6 SER B 278 SER B 294 1 17
HELIX 34 AD7 THR B 297 ILE B 305 1 9
HELIX 35 AD8 PRO B 306 TYR B 312 1 7
HELIX 36 AD9 ASP B 313 ASN B 318 5 6
HELIX 37 AE1 PRO B 329 GLY B 333 5 5
HELIX 38 AE2 ARG B 384 SER B 388 5 5
HELIX 39 AE3 SER B 391 GLY B 396 1 6
HELIX 40 AE4 ASP B 413 ILE B 425 1 13
HELIX 41 AE5 SER B 446 PHE B 475 1 30
HELIX 42 AE6 ALA C 34 ILE C 43 5 10
HELIX 43 AE7 LEU C 45 PHE C 75 1 31
HELIX 44 AE8 PRO C 80 GLN C 84 5 5
HELIX 45 AE9 LEU C 88 LEU C 95 1 8
HELIX 46 AF1 GLY C 100 GLU C 104 5 5
HELIX 47 AF2 THR C 108 ARG C 135 1 28
HELIX 48 AF3 ASP C 153 PHE C 181 1 29
HELIX 49 AF4 ASP C 205 PHE C 210 1 6
HELIX 50 AF5 GLY C 211 LYS C 215 5 5
HELIX 51 AF6 GLY C 222 VAL C 227 5 6
HELIX 52 AF7 ASN C 229 LEU C 253 1 25
HELIX 53 AF8 GLY C 258 PHE C 264 1 7
HELIX 54 AF9 SER C 267 ASN C 293 1 27
HELIX 55 AG1 THR C 305 LEU C 324 1 20
HELIX 56 AG2 ASN C 327 ALA C 331 5 5
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 TRP D 14 LYS D 23 1 10
HELIX 64 AH1 VAL D 30 PHE D 54 1 25
HELIX 65 AH2 SER D 57 GLY D 62 1 6
HELIX 66 AH3 SER D 66 GLY D 70 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 PHE D 146 1 7
HELIX 70 AH7 PHE D 146 LEU D 158 1 13
HELIX 71 AH8 LEU D 158 GLN D 164 1 7
HELIX 72 AH9 SER D 166 ALA D 170 5 5
HELIX 73 AI1 VAL D 175 ASN D 190 1 16
HELIX 74 AI2 TRP D 191 LEU D 193 5 3
HELIX 75 AI3 ASN D 194 ASN D 220 1 27
HELIX 76 AI4 SER D 245 PHE D 257 1 13
HELIX 77 AI5 ASN D 263 LEU D 291 1 29
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 SER E 16 1 8
HELIX 83 AJ2 SER E 16 THR E 40 1 25
HELIX 84 AJ3 GLY E 41 PHE E 47 1 7
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 THR H 27 ASN H 50 1 24
HELIX 89 AJ8 GLU I 2 SER I 25 1 24
HELIX 90 AJ9 PRO J 9 ALA J 32 1 24
HELIX 91 AK1 PRO K 12 ILE K 17 5 6
HELIX 92 AK2 PHE K 18 ASP K 23 1 6
HELIX 93 AK3 VAL K 24 PRO K 26 5 3
HELIX 94 AK4 VAL K 27 VAL K 43 1 17
HELIX 95 AK5 ASN L 13 ASN L 37 1 25
HELIX 96 AK6 LEU M 6 SER M 31 1 26
HELIX 97 AK7 GLY O 40 LYS O 44 5 5
HELIX 98 AK8 LEU O 208 VAL O 213 1 6
HELIX 99 AK9 GLU T 2 PHE T 23 1 22
HELIX 100 AL1 ASN U 41 LEU U 47 1 7
HELIX 101 AL2 ASN U 61 TYR U 68 5 8
HELIX 102 AL3 PRO U 73 ASN U 82 1 10
HELIX 103 AL4 SER U 87 ILE U 94 5 8
HELIX 104 AL5 THR U 98 LEU U 109 1 12
HELIX 105 AL6 GLU U 118 GLU U 123 1 6
HELIX 106 AL7 GLY U 124 ASP U 126 5 3
HELIX 107 AL8 THR V 48 CYS V 63 1 16
HELIX 108 AL9 CYS V 63 VAL V 68 1 6
HELIX 109 AM1 GLY V 69 ILE V 71 5 3
HELIX 110 AM2 ARG V 81 LEU V 87 1 7
HELIX 111 AM3 ASN V 94 MET V 102 1 9
HELIX 112 AM4 SER V 120 ALA V 124 5 5
HELIX 113 AM5 PRO V 128 LEU V 133 1 6
HELIX 114 AM6 THR V 134 GLY V 153 1 20
HELIX 115 AM7 GLY V 153 GLY V 158 1 6
HELIX 116 AM8 GLY V 159 TYR V 163 5 5
HELIX 117 AM9 GLN y 21 ARG y 42 1 22
HELIX 118 AN1 THR X 13 GLN X 42 1 30
HELIX 119 AN2 UNK Y 2 UNK Y 12 1 11
HELIX 120 AN3 UNK Y 14 UNK Y 25 1 12
HELIX 121 AN4 THR Z 2 SER Z 29 1 28
HELIX 122 AN5 ARG Z 35 VAL Z 62 1 28
HELIX 123 AN6 ASN a 12 THR a 22 1 11
HELIX 124 AN7 PHE a 33 ALA a 55 1 23
HELIX 125 AN8 SER a 70 GLY a 74 5 5
HELIX 126 AN9 PRO a 95 ALA a 99 5 5
HELIX 127 AO1 SER a 101 ASN a 108 1 8
HELIX 128 AO2 GLY a 109 LEU a 137 1 29
HELIX 129 AO3 TRP a 142 TYR a 147 1 6
HELIX 130 AO4 TYR a 147 LEU a 159 1 13
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 ASN a 247 ILE a 259 1 13
HELIX 137 AP2 PHE a 260 SER a 264 5 5
HELIX 138 AP3 ASN a 267 MET a 293 1 27
HELIX 139 AP4 THR a 316 HIS a 332 1 17
HELIX 140 AP5 GLU a 333 HIS a 337 5 5
HELIX 141 AP6 PRO b 4 ILE b 13 5 10
HELIX 142 AP7 ASP b 15 ALA b 43 1 29
HELIX 143 AP8 PRO b 54 GLN b 58 5 5
HELIX 144 AP9 VAL b 62 ARG b 68 1 7
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 GLU b 235 5 3
HELIX 152 AQ8 THR b 236 TYR b 258 1 23
HELIX 153 AQ9 PRO b 264 GLY b 269 1 6
HELIX 154 AR1 THR b 271 SER b 277 1 7
HELIX 155 AR2 SER b 278 SER b 294 1 17
HELIX 156 AR3 THR b 297 ILE b 305 1 9
HELIX 157 AR4 PRO b 306 TYR b 312 1 7
HELIX 158 AR5 ASP b 313 ASN b 318 5 6
HELIX 159 AR6 PRO b 329 GLY b 333 5 5
HELIX 160 AR7 ARG b 384 SER b 388 5 5
HELIX 161 AR8 SER b 391 GLY b 396 1 6
HELIX 162 AR9 ASP b 413 ILE b 425 1 13
HELIX 163 AS1 SER b 446 PHE b 475 1 30
HELIX 164 AS2 ALA c 34 ILE c 43 5 10
HELIX 165 AS3 LEU c 45 PHE c 75 1 31
HELIX 166 AS4 PRO c 80 GLN c 84 5 5
HELIX 167 AS5 LEU c 88 LEU c 95 1 8
HELIX 168 AS6 GLY c 100 GLU c 104 5 5
HELIX 169 AS7 THR c 108 ARG c 135 1 28
HELIX 170 AS8 ASP c 153 PHE c 181 1 29
HELIX 171 AS9 ASP c 205 PHE c 210 1 6
HELIX 172 AT1 GLY c 211 LYS c 215 5 5
HELIX 173 AT2 GLY c 222 VAL c 227 5 6
HELIX 174 AT3 ASN c 229 LEU c 253 1 25
HELIX 175 AT4 GLY c 258 PHE c 264 1 7
HELIX 176 AT5 SER c 267 ASN c 293 1 27
HELIX 177 AT6 THR c 305 LEU c 324 1 20
HELIX 178 AT7 ASN c 327 ALA c 331 5 5
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 GLU c 464 MET c 469 5 6
HELIX 185 AU5 TRP d 14 LYS d 23 1 10
HELIX 186 AU6 VAL d 30 PHE d 54 1 25
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 ASP d 100 LEU d 107 1 8
HELIX 190 AV1 GLY d 108 GLY d 137 1 30
HELIX 191 AV2 PRO d 140 PHE d 146 1 7
HELIX 192 AV3 PHE d 146 LEU d 158 1 13
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 SER d 245 PHE d 257 1 13
HELIX 199 AW1 ASN d 263 LEU d 291 1 29
HELIX 200 AW2 PHE d 298 ASP d 308 1 11
HELIX 201 AW3 THR d 313 GLN d 334 1 22
HELIX 202 AW4 PRO d 335 ASN d 338 5 4
HELIX 203 AW5 PRO d 342 LEU d 346 5 5
HELIX 204 AW6 PRO e 9 SER e 16 1 8
HELIX 205 AW7 SER e 16 THR e 40 1 25
HELIX 206 AW8 GLY e 41 PHE e 47 1 7
HELIX 207 AW9 GLU e 71 GLN e 82 1 12
HELIX 208 AX1 THR f 17 GLN f 41 1 25
HELIX 209 AX2 THR h 5 LEU h 11 1 7
HELIX 210 AX3 THR h 27 ASN h 50 1 24
HELIX 211 AX4 GLU i 2 SER i 25 1 24
HELIX 212 AX5 PRO j 9 ALA j 32 1 24
HELIX 213 AX6 PRO k 12 ILE k 17 5 6
HELIX 214 AX7 PHE k 18 ASP k 23 1 6
HELIX 215 AX8 VAL k 24 PRO k 26 5 3
HELIX 216 AX9 VAL k 27 VAL k 43 1 17
HELIX 217 AY1 ASN l 13 ASN l 37 1 25
HELIX 218 AY2 LEU m 6 SER m 31 1 26
HELIX 219 AY3 THR o 32 ILE o 36 5 5
HELIX 220 AY4 GLY o 40 LYS o 44 5 5
HELIX 221 AY5 LEU o 208 VAL o 213 1 6
HELIX 222 AY6 GLU t 2 PHE t 23 1 22
HELIX 223 AY7 ASN u 41 LEU u 47 1 7
HELIX 224 AY8 ASN u 61 TYR u 68 5 8
HELIX 225 AY9 PRO u 73 ASN u 82 1 10
HELIX 226 AZ1 SER u 87 ILE u 94 5 8
HELIX 227 AZ2 THR u 98 LEU u 109 1 12
HELIX 228 AZ3 GLU u 118 GLU u 123 1 6
HELIX 229 AZ4 GLY u 124 ASP u 126 5 3
HELIX 230 AZ5 THR v 48 CYS v 63 1 16
HELIX 231 AZ6 CYS v 63 VAL v 68 1 6
HELIX 232 AZ7 GLY v 69 ILE v 71 5 3
HELIX 233 AZ8 ARG v 81 LEU v 87 1 7
HELIX 234 AZ9 ASN v 94 MET v 102 1 9
HELIX 235 BA1 SER v 120 ALA v 124 5 5
HELIX 236 BA2 PHE v 127 ARG v 131 5 5
HELIX 237 BA3 THR v 134 GLY v 153 1 20
HELIX 238 BA4 GLY v 153 GLY v 158 1 6
HELIX 239 BA5 GLN g 21 ARG g 42 1 22
HELIX 240 BA6 THR x 13 GLN x 42 1 30
HELIX 241 BA7 UNK G 2 UNK G 12 1 11
HELIX 242 BA8 UNK G 14 UNK G 25 1 12
HELIX 243 BA9 THR z 2 SER z 29 1 28
HELIX 244 BB1 ARG z 35 VAL z 62 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 SER B 177 N VAL B 168
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 THR B 398 N ARG B 347
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 ARG C 197 N LEU C 185
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 56 PRO O 57 0
SHEET 2 AB1 2 SER O 161 ILE O 162 -1 O ILE O 162 N TYR O 56
SHEET 1 AB210 PHE O 91 PRO O 93 0
SHEET 2 AB210 ARG O 65 LYS O 79 -1 N VAL O 78 O VAL O 92
SHEET 3 AB210 GLU O 258 GLU O 270 -1 O GLN O 262 N THR O 74
SHEET 4 AB210 GLU O 236 LEU O 246 -1 N SER O 243 O ILE O 261
SHEET 5 AB210 LEU O 218 LYS O 229 -1 N ALA O 228 O ALA O 238
SHEET 6 AB210 PHE O 168 PRO O 175 -1 N VAL O 174 O THR O 219
SHEET 7 AB210 VAL O 152 SER O 154 -1 N SER O 154 O LYS O 169
SHEET 8 AB210 LEU O 119 ILE O 127 -1 N PHE O 121 O ALA O 153
SHEET 9 AB210 LEU O 104 VAL O 113 -1 N GLN O 108 O GLU O 124
SHEET 10 AB210 ARG O 65 LYS O 79 -1 N LEU O 71 O LEU O 104
SHEET 1 AB3 3 LYS O 95 LEU O 96 0
SHEET 2 AB3 3 PHE O 129 GLN O 135 -1 O GLN O 135 N LYS O 95
SHEET 3 AB3 3 ARG O 141 THR O 147 -1 O ILE O 142 N VAL O 134
SHEET 1 AB4 2 ILE U 55 ASP U 56 0
SHEET 2 AB4 2 PHE U 112 THR U 113 1 O THR U 113 N ILE U 55
SHEET 1 AB5 2 THR V 35 PRO V 37 0
SHEET 2 AB5 2 THR V 44 THR V 46 -1 O ILE V 45 N VAL V 36
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 SER b 177 N VAL b 168
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 SER b 400 N VAL b 345
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 ARG c 197 N LEU c 185
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 56 PRO o 57 0
SHEET 2 AC6 2 SER o 161 ILE o 162 -1 O ILE o 162 N TYR o 56
SHEET 1 AC710 PHE o 91 PRO o 93 0
SHEET 2 AC710 ARG o 65 LYS o 79 -1 N VAL o 78 O VAL o 92
SHEET 3 AC710 GLU o 258 GLU o 270 -1 O LYS o 260 N LEU o 77
SHEET 4 AC710 GLU o 236 LEU o 246 -1 N SER o 243 O ILE o 261
SHEET 5 AC710 LEU o 218 LYS o 229 -1 N GLN o 222 O GLU o 244
SHEET 6 AC710 PHE o 168 PRO o 175 -1 N VAL o 174 O THR o 219
SHEET 7 AC710 LYS o 149 SER o 154 -1 N LYS o 149 O ASN o 173
SHEET 8 AC710 LEU o 119 ILE o 127 -1 N PHE o 121 O ALA o 153
SHEET 9 AC710 LEU o 104 VAL o 113 -1 N GLN o 108 O GLU o 124
SHEET 10 AC710 ARG o 65 LYS o 79 -1 N LEU o 71 O LEU o 104
SHEET 1 AC8 3 LYS o 95 LEU o 96 0
SHEET 2 AC8 3 PHE o 129 GLN o 135 -1 O GLN o 135 N LYS o 95
SHEET 3 AC8 3 ARG o 141 THR o 147 -1 O ILE o 142 N VAL o 134
SHEET 1 AC9 2 ILE u 55 ASP u 56 0
SHEET 2 AC9 2 PHE u 112 THR u 113 1 O THR u 113 N ILE u 55
SHEET 1 AD1 2 THR v 35 PRO v 37 0
SHEET 2 AD1 2 THR v 44 THR v 46 -1 O ILE v 45 N VAL v 36
SSBOND 1 CYS O 45 CYS O 70 1555 1555 2.03
SSBOND 2 CYS o 45 CYS o 70 1555 1555 2.03
LINK OD1 ASP A 170 CA1 OEX A 412 1555 1555 3.03
LINK OD2 ASP A 170 MN4 OEX A 412 1555 1555 2.67
LINK OE1 GLU A 189 CA1 OEX A 412 1555 1555 3.04
LINK OE2 GLU A 189 MN1 OEX A 412 1555 1555 2.49
LINK NE2 HIS A 215 FE FE2 A 401 1555 1555 2.57
LINK NE2 HIS A 272 FE FE2 A 401 1555 1555 2.56
LINK NE2 HIS A 332 MN1 OEX A 412 1555 1555 2.57
LINK OE1 GLU A 333 MN3 OEX A 412 1555 1555 2.56
LINK OE2 GLU A 333 MN4 OEX A 412 1555 1555 2.77
LINK OD1 ASP A 342 MN2 OEX A 412 1555 1555 2.59
LINK OXT ALA A 344 MN2 OEX A 412 1555 1555 2.62
LINK OD1 ASN C 39 MG CLA C 510 1555 1555 2.95
LINK OE1 GLU C 354 MN2 OEX A 412 1555 1555 2.77
LINK OE2 GLU C 354 MN3 OEX A 412 1555 1555 2.65
LINK NE2 HIS D 214 FE FE2 A 401 1555 1555 2.50
LINK NE2 HIS D 268 FE FE2 A 401 1555 1555 2.73
LINK NE2 HIS E 23 FE HEM F 101 1555 1555 2.58
LINK NE2 HIS F 24 FE HEM F 101 1555 1555 2.62
LINK OD2 ASP K 19 CA CA K 102 1555 1555 2.55
LINK OD1 ASP K 23 CA CA K 102 1555 1555 3.16
LINK OD2 ASP K 23 CA CA K 102 1555 1555 2.98
LINK OE1 GLU O 140 CA CA O 301 1555 1555 2.67
LINK NE2 HIS V 67 FE HEM V 201 1555 1555 2.47
LINK NE2 HIS V 118 FE HEM V 201 1555 1555 2.57
LINK C UNK Y 1 N UNK Y 2 1555 1555 1.33
LINK C UNK Y 2 N UNK Y 3 1555 1555 1.33
LINK C UNK Y 3 N UNK Y 4 1555 1555 1.33
LINK C UNK Y 4 N UNK Y 5 1555 1555 1.33
LINK C UNK Y 5 N UNK Y 6 1555 1555 1.33
LINK C UNK Y 6 N UNK Y 7 1555 1555 1.33
LINK C UNK Y 7 N UNK Y 8 1555 1555 1.33
LINK C UNK Y 8 N UNK Y 9 1555 1555 1.33
LINK C UNK Y 9 N UNK Y 10 1555 1555 1.33
LINK C UNK Y 10 N UNK Y 11 1555 1555 1.33
LINK C UNK Y 11 N UNK Y 12 1555 1555 1.33
LINK C UNK Y 12 N UNK Y 13 1555 1555 1.33
LINK C UNK Y 13 N UNK Y 14 1555 1555 1.33
LINK C UNK Y 14 N UNK Y 15 1555 1555 1.33
LINK C UNK Y 15 N UNK Y 16 1555 1555 1.33
LINK C UNK Y 16 N UNK Y 17 1555 1555 1.33
LINK C UNK Y 17 N UNK Y 18 1555 1555 1.33
LINK C UNK Y 18 N UNK Y 19 1555 1555 1.33
LINK C UNK Y 19 N UNK Y 20 1555 1555 1.33
LINK C UNK Y 20 N UNK Y 21 1555 1555 1.33
LINK C UNK Y 21 N UNK Y 22 1555 1555 1.33
LINK C UNK Y 22 N UNK Y 23 1555 1555 1.33
LINK C UNK Y 23 N UNK Y 24 1555 1555 1.33
LINK C UNK Y 24 N UNK Y 25 1555 1555 1.33
LINK C UNK Y 25 N UNK Y 26 1555 1555 1.33
LINK C UNK Y 26 N UNK Y 27 1555 1555 1.33
LINK C UNK Y 27 N UNK Y 28 1555 1555 1.33
LINK OD1 ASP a 170 CA1 OEX a 411 1555 1555 3.04
LINK OD2 ASP a 170 MN4 OEX a 411 1555 1555 2.65
LINK OE1 GLU a 189 CA1 OEX a 411 1555 1555 3.09
LINK OE2 GLU a 189 MN1 OEX a 411 1555 1555 2.54
LINK NE2 HIS a 215 FE FE2 a 413 1555 1555 2.61
LINK NE2 HIS a 272 FE FE2 a 413 1555 1555 2.55
LINK NE2 HIS a 332 MN1 OEX a 411 1555 1555 2.57
LINK OE1 GLU a 333 MN3 OEX a 411 1555 1555 2.57
LINK OD1 ASP a 342 MN2 OEX a 411 1555 1555 2.62
LINK OXT ALA a 344 MN2 OEX a 411 1555 1555 2.67
LINK OD1 ASN c 39 MG CLA c 510 1555 1555 2.98
LINK OE1 GLU c 354 MN2 OEX a 411 1555 1555 2.80
LINK OE2 GLU c 354 MN3 OEX a 411 1555 1555 2.71
LINK NE2 HIS d 214 FE FE2 a 413 1555 1555 2.54
LINK NE2 HIS d 268 FE FE2 a 413 1555 1555 2.71
LINK NE2 HIS e 23 FE HEM f 101 1555 1555 2.61
LINK NE2 HIS f 24 FE HEM f 101 1555 1555 2.63
LINK OD2 ASP k 19 CA CA k 101 1555 1555 2.67
LINK OD1 ASP k 23 CA CA k 101 1555 1555 2.97
LINK OD2 ASP k 23 CA CA k 101 1555 1555 2.91
LINK OE1 GLU o 140 CA CA o 301 1555 1555 2.68
LINK NE2 HIS v 67 FE HEM v 201 1555 1555 2.51
LINK NE2 HIS v 118 FE HEM v 201 1555 1555 2.67
LINK C UNK G 1 N UNK G 2 1555 1555 1.33
LINK C UNK G 2 N UNK G 3 1555 1555 1.33
LINK C UNK G 3 N UNK G 4 1555 1555 1.33
LINK C UNK G 4 N UNK G 5 1555 1555 1.33
LINK C UNK G 5 N UNK G 6 1555 1555 1.33
LINK C UNK G 6 N UNK G 7 1555 1555 1.33
LINK C UNK G 7 N UNK G 8 1555 1555 1.33
LINK C UNK G 8 N UNK G 9 1555 1555 1.33
LINK C UNK G 9 N UNK G 10 1555 1555 1.33
LINK C UNK G 10 N UNK G 11 1555 1555 1.33
LINK C UNK G 11 N UNK G 12 1555 1555 1.33
LINK C UNK G 12 N UNK G 13 1555 1555 1.33
LINK C UNK G 13 N UNK G 14 1555 1555 1.33
LINK C UNK G 14 N UNK G 15 1555 1555 1.33
LINK C UNK G 15 N UNK G 16 1555 1555 1.33
LINK C UNK G 16 N UNK G 17 1555 1555 1.33
LINK C UNK G 17 N UNK G 18 1555 1555 1.33
LINK C UNK G 18 N UNK G 19 1555 1555 1.33
LINK C UNK G 19 N UNK G 20 1555 1555 1.33
LINK C UNK G 20 N UNK G 21 1555 1555 1.33
LINK C UNK G 21 N UNK G 22 1555 1555 1.33
LINK C UNK G 22 N UNK G 23 1555 1555 1.33
LINK C UNK G 23 N UNK G 24 1555 1555 1.33
LINK C UNK G 24 N UNK G 25 1555 1555 1.33
LINK C UNK G 25 N UNK G 26 1555 1555 1.33
LINK C UNK G 26 N UNK G 27 1555 1555 1.33
LINK C UNK G 27 N UNK G 28 1555 1555 1.33
LINK FE FE2 A 401 O2 BCT D 402 1555 1555 2.70
LINK FE FE2 A 401 O3 BCT D 402 1555 1555 2.67
LINK FE FE2 a 413 O2 BCT d 404 1555 1555 2.64
LINK FE FE2 a 413 O3 BCT d 404 1555 1555 2.68
CISPEP 1 THR V 89 PRO V 90 0 -0.84
CISPEP 2 THR v 89 PRO v 90 0 -0.93
SITE 1 AC1 5 HIS A 215 HIS A 272 HIS D 214 HIS D 268
SITE 2 AC1 5 BCT D 402
SITE 1 AC2 24 PHE A 119 TYR A 147 PRO A 150 SER A 153
SITE 2 AC2 24 VAL A 157 MET A 183 PHE A 186 GLN A 187
SITE 3 AC2 24 ILE A 192 LEU A 193 HIS A 198 GLY A 201
SITE 4 AC2 24 VAL A 205 PHE A 206 VAL A 283 THR A 286
SITE 5 AC2 24 ILE A 290 CLA A 403 CLA A 404 PHO A 405
SITE 6 AC2 24 LEU D 182 LEU D 205 CLA D 403 PHE T 17
SITE 1 AC3 14 THR A 45 VAL A 157 PHE A 158 MET A 172
SITE 2 AC3 14 ILE A 176 THR A 179 MET A 183 CLA A 402
SITE 3 AC3 14 PHO A 405 MET D 198 VAL D 201 ALA D 202
SITE 4 AC3 14 CLA D 403 PL9 D 405
SITE 1 AC4 14 GLN A 199 VAL A 202 ALA A 203 TRP A 278
SITE 2 AC4 14 CLA A 402 PL9 A 407 PHE D 157 VAL D 175
SITE 3 AC4 14 ILE D 178 PHE D 179 PHE D 181 LEU D 182
SITE 4 AC4 14 PHO D 401 CLA D 403
SITE 1 AC5 17 ALA A 44 THR A 45 ILE A 115 TYR A 126
SITE 2 AC5 17 GLN A 130 TYR A 147 VAL A 283 CLA A 402
SITE 3 AC5 17 CLA A 403 SQD A 414 LEU D 205 ALA D 208
SITE 4 AC5 17 LEU D 209 ALA D 212 ILE D 213 TRP D 253
SITE 5 AC5 17 PHE D 257
SITE 1 AC6 14 ILE A 36 PRO A 39 THR A 40 PHE A 93
SITE 2 AC6 14 PRO A 95 ILE A 96 TRP A 97 LEU A 114
SITE 3 AC6 14 HIS A 118 LEU A 121 BCR A 408 VAL I 8
SITE 4 AC6 14 TYR I 9 PHE I 15
SITE 1 AC7 15 HIS A 215 LEU A 218 HIS A 252 PHE A 255
SITE 2 AC7 15 SER A 264 PHE A 265 LEU A 271 PHE A 274
SITE 3 AC7 15 CLA A 404 PHE D 38 ALA D 41 TYR D 42
SITE 4 AC7 15 LEU D 45 THR F 25 PL9 J 101
SITE 1 AC8 8 LEU A 42 ALA A 43 TRP A 105 LEU A 106
SITE 2 AC8 8 CLA A 406 SQD A 414 PHE I 15 LMT b 603
SITE 1 AC9 14 PHE A 93 TRP A 97 GLU A 98 PHE A 155
SITE 2 AC9 14 LEU C 214 LYS C 215 SER C 216 PRO C 217
SITE 3 AC9 14 PHE C 218 TRP C 223 PHE C 284 LYS I 5
SITE 4 AC9 14 TYR I 9 GLY O 38
SITE 1 AD1 15 ARG A 140 TRP A 142 PHE A 273 SQD A 413
SITE 2 AD1 15 TRP C 36 TRP C 443 ARG C 447 CLA C 507
SITE 3 AD1 15 CLA C 509 CLA C 519 ASN D 220 ALA D 229
SITE 4 AD1 15 SER D 230 THR D 231 PHE D 232
SITE 1 AD2 2 ASN A 181 LYS D 317
SITE 1 AD3 9 ASP A 170 GLU A 189 HIS A 332 GLU A 333
SITE 2 AD3 9 HIS A 337 ASP A 342 ALA A 344 GLU C 354
SITE 3 AD3 9 ARG C 357
SITE 1 AD4 15 ASN A 267 SER A 270 PHE A 273 PHE A 274
SITE 2 AD4 15 TRP A 278 LHG A 410 TRP C 35 TRP C 36
SITE 3 AD4 15 DGD C 515 DGD C 516 LHG C 518 PHE D 232
SITE 4 AD4 15 ARG D 233 BCR J 102 PHE K 37
SITE 1 AD5 13 TRP A 20 ASN A 26 ARG A 27 LEU A 28
SITE 2 AD5 13 THR A 45 PHO A 405 BCR A 408 TRP b 113
SITE 3 AD5 13 TYR b 117 CLA b 610 CLA b 620 BCR b 622
SITE 4 AD5 13 BCR b 624
SITE 1 AD6 9 TRP B 185 PRO B 187 PHE B 190 ILE B 207
SITE 2 AD6 9 VAL B 208 PHE H 41 ILE H 44 CLA H 101
SITE 3 AD6 9 BCR H 102
SITE 1 AD7 19 ARG B 68 LEU B 69 ALA B 146 LEU B 149
SITE 2 AD7 19 CYS B 150 PHE B 153 VAL B 198 HIS B 201
SITE 3 AD7 19 HIS B 202 ALA B 248 VAL B 252 THR B 262
SITE 4 AD7 19 CLA B 603 CLA B 604 CLA B 605 CLA B 608
SITE 5 AD7 19 PHE H 38 LEU H 42 CLA H 101
SITE 1 AD8 20 TRP B 33 PHE B 61 PHE B 65 ARG B 68
SITE 2 AD8 20 LEU B 149 VAL B 245 ALA B 248 ALA B 249
SITE 3 AD8 20 VAL B 252 PHE B 451 HIS B 455 PHE B 458
SITE 4 AD8 20 ALA B 459 PHE B 462 CLA B 602 CLA B 604
SITE 5 AD8 20 CLA B 606 CLA B 611 CLA B 612 CLA B 614
SITE 1 AD9 20 THR B 27 VAL B 30 ALA B 31 TRP B 33
SITE 2 AD9 20 ALA B 34 VAL B 62 PHE B 65 MET B 66
SITE 3 AD9 20 ARG B 68 LEU B 69 VAL B 96 HIS B 100
SITE 4 AD9 20 LEU B 103 GLY B 147 ALA B 205 CLA B 602
SITE 5 AD9 20 CLA B 603 CLA B 605 CLA B 609 CLA B 611
SITE 1 AE1 17 LEU B 69 TRP B 91 ALA B 99 LEU B 103
SITE 2 AE1 17 LEU B 106 GLY B 152 PHE B 153 PHE B 156
SITE 3 AE1 17 HIS B 157 PHE B 162 PRO B 164 CLA B 602
SITE 4 AE1 17 CLA B 604 CLA B 615 BCR B 619 LMT B 623
SITE 5 AE1 17 SQD a 401
SITE 1 AE2 20 TRP B 33 MET B 37 TYR B 40 GLN B 58
SITE 2 AE2 20 GLY B 59 PHE B 61 THR B 327 GLY B 328
SITE 3 AE2 20 PRO B 329 TRP B 450 ALA B 454 CLA B 603
SITE 4 AE2 20 BCR B 616 BCR B 617 BCR B 618 LMG B 621
SITE 5 AE2 20 LMG B 625 MET D 281 LEU L 27 PHE M 14
SITE 1 AE3 15 THR B 236 SER B 239 ALA B 243 PHE B 246
SITE 2 AE3 15 PHE B 247 HIS B 466 LEU B 474 CLA B 608
SITE 3 AE3 15 CLA B 609 SQD B 622 PHE D 120 ILE D 123
SITE 4 AE3 15 MET D 126 LEU D 127 PHE D 130
SITE 1 AE4 15 PHE B 139 ALA B 212 PHE B 215 HIS B 216
SITE 2 AE4 15 PRO B 221 PRO B 222 LEU B 229 CLA B 602
SITE 3 AE4 15 CLA B 607 CLA B 609 THR H 27 MET H 31
SITE 4 AE4 15 PHE H 34 MET H 35 BCR H 102
SITE 1 AE5 15 HIS B 23 LEU B 135 PHE B 139 HIS B 142
SITE 2 AE5 15 LEU B 143 ALA B 146 VAL B 237 SER B 240
SITE 3 AE5 15 SER B 241 CLA B 604 CLA B 607 CLA B 608
SITE 4 AE5 15 CLA B 611 CLA B 614 BCR H 102
SITE 1 AE6 18 TRP B 5 TYR B 6 ARG B 7 VAL B 8
SITE 2 AE6 18 HIS B 9 THR B 10 LEU B 238 ILE B 242
SITE 3 AE6 18 LEU B 461 PHE B 462 GLY B 465 TRP B 468
SITE 4 AE6 18 HIS B 469 ARG B 472 CLA B 611 CLA B 612
SITE 5 AE6 18 CLA B 613 LMG B 625
SITE 1 AE7 18 HIS B 9 LEU B 19 ALA B 22 HIS B 23
SITE 2 AE7 18 HIS B 26 THR B 27 ILE B 234 VAL B 237
SITE 3 AE7 18 LEU B 238 SER B 241 VAL B 245 CLA B 603
SITE 4 AE7 18 CLA B 604 CLA B 609 CLA B 610 CLA B 612
SITE 5 AE7 18 CLA B 613 CLA B 614
SITE 1 AE8 9 HIS B 9 HIS B 26 VAL B 30 PHE B 462
SITE 2 AE8 9 CLA B 603 CLA B 610 CLA B 611 CLA B 613
SITE 3 AE8 9 LMG B 625
SITE 1 AE9 11 VAL B 8 HIS B 9 VAL B 11 TRP B 115
SITE 2 AE9 11 CLA B 610 CLA B 611 CLA B 612 BCR B 616
SITE 3 AE9 11 SQD B 627 VAL L 10 LMG m 101
SITE 1 AF1 11 HIS B 23 MET B 138 ILE B 141 HIS B 142
SITE 2 AF1 11 LEU B 145 CLA B 603 CLA B 609 CLA B 611
SITE 3 AF1 11 CLA B 615 BCR B 619 LEU H 14
SITE 1 AF2 11 LEU B 24 ALA B 110 TRP B 113 HIS B 114
SITE 2 AF2 11 LEU B 120 CLA B 605 CLA B 614 BCR B 619
SITE 3 AF2 11 THR H 5 LEU H 7 SQD a 401
SITE 1 AF3 9 MET B 25 LEU B 29 TRP B 115 CLA B 606
SITE 2 AF3 9 CLA B 613 BCR B 617 BCR B 618 LEU M 13
SITE 3 AF3 9 PHE t 19
SITE 1 AF4 10 TRP B 33 SER B 36 MET B 37 CLA B 606
SITE 2 AF4 10 BCR B 616 BCR B 618 LMT B 629 ILE t 4
SITE 3 AF4 10 ALA t 11 PHE t 17
SITE 1 AF5 6 GLY B 32 TRP B 33 GLY B 105 CLA B 606
SITE 2 AF5 6 BCR B 616 BCR B 617
SITE 1 AF6 9 LEU B 109 CYS B 112 TYR B 117 CLA B 605
SITE 2 AF6 9 CLA B 614 CLA B 615 LMT B 623 SQD a 401
SITE 3 AF6 9 PHE t 18
SITE 1 AF7 13 TYR B 193 PHE B 250 TYR B 258 TYR B 273
SITE 2 AF7 13 SER B 277 HIS D 87 LEU D 162 TYR H 49
SITE 3 AF7 13 ASN H 50 VAL H 60 SER H 61 TRP H 62
SITE 4 AF7 13 CLA H 101
SITE 1 AF8 11 TYR B 40 THR B 327 GLY B 328 PRO B 329
SITE 2 AF8 11 LYS B 332 CLA B 606 ILE D 284 PHE L 35
SITE 3 AF8 11 ASN M 4 LEU M 6 LMT M 103
SITE 1 AF9 10 LYS B 227 ALA B 228 ARG B 230 LEU B 474
SITE 2 AF9 10 CLA B 607 LMT B 624 LYS D 23 TRP D 32
SITE 3 AF9 10 ARG D 134 LEU D 135
SITE 1 AG1 4 TRP B 91 PHE B 162 CLA B 605 BCR B 619
SITE 1 AG2 7 ARG B 224 LYS B 227 SQD B 622 ASP D 16
SITE 2 AG2 7 ASP D 19 ALA H 32 MET H 35
SITE 1 AG3 14 ASN A 234 TRP B 5 TYR B 6 ARG B 7
SITE 2 AG3 14 PHE B 464 TRP B 468 CLA B 606 CLA B 610
SITE 3 AG3 14 CLA B 612 ARG D 139 TYR D 141 PHE D 269
SITE 4 AG3 14 PHE D 273 LMG L 101
SITE 1 AG4 7 TRP B 75 ASP B 87 GLY B 89 PHE B 90
SITE 2 AG4 7 LMT B 628 ILE a 46 LMG i 102
SITE 1 AG5 12 ARG B 18 LEU B 29 SER B 104 PHE B 108
SITE 2 AG5 12 CLA B 613 ASN L 4 ARG l 14 TYR l 18
SITE 3 AG5 12 TYR m 26 LMG m 101 PHE t 19 PHE t 23
SITE 1 AG6 8 ASP B 87 DGD B 626 ALA a 100 MET i 1
SITE 2 AG6 8 LEU i 4 BCR i 101 LMG i 102 LYS o 95
SITE 1 AG7 4 ALA B 43 BCR B 617 LMG a 402 VAL t 7
SITE 1 AG8 17 LEU C 95 LEU C 168 GLY C 171 ALA C 172
SITE 2 AG8 17 ILE C 224 VAL C 233 HIS C 237 ILE C 240
SITE 3 AG8 17 ALA C 278 MET C 282 VAL C 296 TYR C 297
SITE 4 AG8 17 CLA C 502 CLA C 503 CLA C 505 CLA C 506
SITE 5 AG8 17 BCR C 513
SITE 1 AG9 17 TRP C 63 HIS C 91 TRP C 97 LEU C 174
SITE 2 AG9 17 LYS C 178 PHE C 182 LEU C 279 MET C 282
SITE 3 AG9 17 ALA C 286 TYR C 297 HIS C 430 LEU C 433
SITE 4 AG9 17 PHE C 437 CLA C 501 CLA C 503 CLA C 508
SITE 5 AG9 17 CLA C 509
SITE 1 AH1 14 ILE C 60 VAL C 61 ALA C 64 THR C 68
SITE 2 AH1 14 LEU C 88 HIS C 91 ILE C 92 VAL C 114
SITE 3 AH1 14 HIS C 118 CLA C 501 CLA C 502 CLA C 509
SITE 4 AH1 14 CLA C 511 LMG C 517
SITE 1 AH2 16 PHE A 33 MET A 127 TRP A 131 PHE C 264
SITE 2 AH2 16 ILE C 265 TYR C 274 GLY C 277 ALA C 278
SITE 3 AH2 16 MET C 281 HIS C 441 LEU C 442 ALA C 445
SITE 4 AH2 16 ARG C 449 CLA C 506 BCR C 513 PHE I 23
SITE 1 AH3 14 LEU C 165 LEU C 213 ILE C 243 GLY C 247
SITE 2 AH3 14 TRP C 250 HIS C 251 THR C 255 PRO C 256
SITE 3 AH3 14 PHE C 257 TRP C 259 ALA C 260 PHE C 264
SITE 4 AH3 14 CLA C 501 CLA C 506
SITE 1 AH4 15 MET C 157 LEU C 161 HIS C 164 ILE C 240
SITE 2 AH4 15 PHE C 264 TRP C 266 TYR C 271 TYR C 274
SITE 3 AH4 15 SER C 275 LEU C 279 CLA C 501 CLA C 504
SITE 4 AH4 15 CLA C 505 CLA C 508 BCR C 513
SITE 1 AH5 17 LHG A 410 TRP C 36 ALA C 37 ASN C 39
SITE 2 AH5 17 ALA C 40 GLU C 269 LEU C 276 PHE C 436
SITE 3 AH5 17 PHE C 437 GLY C 440 TRP C 443 HIS C 444
SITE 4 AH5 17 ARG C 447 CLA C 508 CLA C 509 DGD C 515
SITE 5 AH5 17 CLA C 519
SITE 1 AH6 19 ASN C 39 LEU C 42 LEU C 49 ALA C 52
SITE 2 AH6 19 HIS C 53 HIS C 56 TYR C 149 TRP C 151
SITE 3 AH6 19 GLY C 268 TYR C 271 LEU C 272 SER C 275
SITE 4 AH6 19 LEU C 279 CLA C 502 CLA C 506 CLA C 507
SITE 5 AH6 19 CLA C 509 CLA C 510 CLA C 511
SITE 1 AH7 16 LHG A 410 ASN C 39 HIS C 56 LEU C 59
SITE 2 AH7 16 LEU C 279 PHE C 436 PHE C 437 CLA C 502
SITE 3 AH7 16 CLA C 503 CLA C 507 CLA C 508 CLA C 510
SITE 4 AH7 16 CLA C 519 PRO K 29 VAL K 30 LEU K 33
SITE 1 AH8 22 GLN C 28 TRP C 35 GLY C 38 ASN C 39
SITE 2 AH8 22 ARG C 41 LEU C 42 LYS C 48 ALA C 52
SITE 3 AH8 22 PHE C 127 ILE C 134 CLA C 508 CLA C 509
SITE 4 AH8 22 PHE K 32 TRP K 39 GLN K 40 BCR K 101
SITE 5 AH8 22 MET Z 19 VAL Z 20 VAL Z 23 PRO Z 24
SITE 6 AH8 22 ILE y 35 LEU y 46
SITE 1 AH9 11 HIS C 53 ALA C 57 PHE C 147 PHE C 163
SITE 2 AH9 11 HIS C 164 VAL C 167 LEU C 174 CLA C 503
SITE 3 AH9 11 CLA C 508 CLA C 512 BCR C 520
SITE 1 AI1 9 VAL C 54 VAL C 124 GLY C 128 TYR C 131
SITE 2 AI1 9 HIS C 132 PRO C 137 PHE C 147 CLA C 511
SITE 3 AI1 9 BCR C 520
SITE 1 AI2 12 ILE C 209 TYR C 212 LEU C 213 VAL C 227
SITE 2 AI2 12 ASP C 232 VAL C 233 GLY C 236 ILE C 240
SITE 3 AI2 12 PHE C 264 CLA C 501 CLA C 504 CLA C 506
SITE 1 AI3 16 LEU A 91 PHE A 155 ILE A 163 PRO C 217
SITE 2 AI3 16 PHE C 218 GLY C 219 GLY C 220 GLY C 222
SITE 3 AI3 16 VAL C 225 SER C 226 PHE C 284 CYS C 288
SITE 4 AI3 16 PHE C 292 ASN C 294 PHE C 361 ARG C 362
SITE 1 AI4 20 PHE A 197 LEU A 297 SQD A 413 TYR C 82
SITE 2 AI4 20 GLU C 83 GLN C 84 GLY C 85 LEU C 404
SITE 3 AI4 20 SER C 406 ASN C 418 PHE C 419 VAL C 420
SITE 4 AI4 20 TRP C 425 SER C 429 CLA C 507 DGD C 516
SITE 5 AI4 20 CLA C 519 LMG C 521 TYR J 33 BCR J 102
SITE 1 AI5 22 LEU A 200 TRP A 278 PHE A 300 ASN A 301
SITE 2 AI5 22 SER A 305 SQD A 413 ASN C 405 SER C 406
SITE 3 AI5 22 VAL C 407 ASN C 415 SER C 416 ASN C 418
SITE 4 AI5 22 DGD C 515 CLA C 519 LMG D 409 PHE J 29
SITE 5 AI5 22 ALA J 32 TYR J 33 GLY J 37 SER J 38
SITE 6 AI5 22 SER J 39 GLN V 60
SITE 1 AI6 8 TRP C 97 PHE C 109 VAL C 113 VAL C 114
SITE 2 AI6 8 VAL C 117 HIS C 118 CLA C 503 PHE Z 59
SITE 1 AI7 7 TYR A 262 ASN A 266 SQD A 413 TRP C 35
SITE 2 AI7 7 LMG E 101 BCR J 102 PHE K 45
SITE 1 AI8 18 PHE A 285 LHG A 410 TRP C 63 MET C 67
SITE 2 AI8 18 PHE C 70 GLN C 84 GLY C 85 ILE C 87
SITE 3 AI8 18 LEU C 404 TRP C 425 SER C 429 CLA C 507
SITE 4 AI8 18 CLA C 509 DGD C 515 DGD C 516 LMG C 521
SITE 5 AI8 18 PRO K 26 VAL K 30
SITE 1 AI9 9 PHE C 112 VAL C 116 SER C 121 VAL C 124
SITE 2 AI9 9 CLA C 511 CLA C 512 TYR K 15 GLY Z 55
SITE 3 AI9 9 ASN Z 58
SITE 1 AJ1 7 HIS C 74 DGD C 515 CLA C 519 BCR J 102
SITE 2 AJ1 7 ASP K 23 VAL K 27 ILE y 25
SITE 1 AJ2 23 PHE A 206 ALA A 209 LEU A 210 MET A 214
SITE 2 AJ2 23 LEU A 258 CLA A 404 ALA D 41 TRP D 48
SITE 3 AJ2 23 ILE D 114 GLY D 118 LEU D 122 PHE D 125
SITE 4 AJ2 23 GLN D 129 ASN D 142 ALA D 145 PHE D 146
SITE 5 AJ2 23 ALA D 148 PRO D 149 PHE D 153 PHE D 173
SITE 6 AJ2 23 PRO D 275 LEU D 279 CLA D 403
SITE 1 AJ3 8 HIS A 215 GLU A 244 TYR A 246 HIS A 272
SITE 2 AJ3 8 FE2 A 401 TYR D 244 LYS D 264 HIS D 268
SITE 1 AJ4 24 PHE A 206 CLA A 402 CLA A 403 CLA A 404
SITE 2 AJ4 24 TRP D 48 LEU D 122 VAL D 152 PHE D 153
SITE 3 AJ4 24 SER D 155 VAL D 156 LEU D 182 PHE D 185
SITE 4 AJ4 24 GLN D 186 TRP D 191 THR D 192 HIS D 197
SITE 5 AJ4 24 GLY D 200 VAL D 201 VAL D 204 LEU D 279
SITE 6 AJ4 24 SER D 282 ALA D 283 VAL D 286 PHO D 401
SITE 1 AJ5 14 LEU D 43 LEU D 89 LEU D 90 LEU D 91
SITE 2 AJ5 14 LEU D 92 TRP D 93 THR D 112 PHE D 113
SITE 3 AJ5 14 HIS D 117 PHE D 120 LMT D 408 GLY X 22
SITE 4 AJ5 14 LEU X 23 GLY X 26
SITE 1 AJ6 14 CLA A 403 MET D 199 HIS D 214 THR D 217
SITE 2 AJ6 14 TRP D 253 ALA D 260 PHE D 261 LEU D 267
SITE 3 AJ6 14 PHE D 270 PHE D 273 LMG D 406 VAL L 26
SITE 4 AJ6 14 LMG L 101 PHE T 10
SITE 1 AJ7 11 PHE D 257 ALA D 260 PHE D 261 SER D 262
SITE 2 AJ7 11 ASN D 263 TRP D 266 PL9 D 405 THR L 15
SITE 3 AJ7 11 TYR L 18 LEU L 19 PHE T 17
SITE 1 AJ8 6 ASP D 100 PHE D 101 THR D 102 LMT D 408
SITE 2 AJ8 6 ASP E 45 VAL E 46
SITE 1 AJ9 8 LEU D 92 TRP D 93 GLY D 99 CLA D 404
SITE 2 AJ9 8 DGD D 407 ILE X 21 SER X 25 GLY X 26
SITE 1 AK1 13 DGD C 516 TYR D 67 GLY D 70 ASN D 72
SITE 2 AK1 13 PHE D 73 ILE F 37 MET F 40 GLN F 41
SITE 3 AK1 13 BCR F 102 PHE J 28 GLY J 31 ALA J 32
SITE 4 AK1 13 GLY J 37
SITE 1 AK2 7 TYR A 262 LHG C 518 PHE D 27 PRO E 9
SITE 2 AK2 7 PHE E 10 SER E 11 PL9 J 101
SITE 1 AK3 15 ARG E 8 PHE E 10 ILE E 13 ARG E 18
SITE 2 AK3 15 TYR E 19 HIS E 23 THR E 26 LEU E 30
SITE 3 AK3 15 ILE F 15 ARG F 19 TRP F 20 VAL F 23
SITE 4 AK3 15 HIS F 24 ALA F 27 ILE F 31
SITE 1 AK4 10 TYR D 42 GLY D 47 LEU D 49 THR D 50
SITE 2 AK4 10 PHE D 101 LMG D 409 PRO F 29 PHE F 33
SITE 3 AK4 10 VAL J 25 PL9 J 101
SITE 1 AK5 9 TRP D 21 ARG D 24 ARG D 26 GLU E 7
SITE 2 AK5 9 PHE F 16 THR F 17 VAL F 18 THR X 33
SITE 3 AK5 9 ASP X 44
SITE 1 AK6 17 GLU B 184 GLY B 189 PHE B 190 GLY B 197
SITE 2 AK6 17 HIS B 201 ALA B 205 VAL B 208 PHE B 247
SITE 3 AK6 17 CLA B 601 CLA B 602 DGD B 620 VAL D 154
SITE 4 AK6 17 PHE H 38 PHE H 41 ILE H 45 LEU H 46
SITE 5 AK6 17 TYR H 49
SITE 1 AK7 10 CLA B 601 CLA B 608 CLA B 609 PHE H 34
SITE 2 AK7 10 MET H 35 LEU H 37 PHE H 38 PHE H 41
SITE 3 AK7 10 THR X 11 LEU X 16
SITE 1 AK8 6 MET I 1 THR I 3 LEU I 4 LMT I 102
SITE 2 AK8 6 DGD b 601 LMT b 603
SITE 1 AK9 4 THR I 3 ILE I 6 ILE I 10 LMG I 101
SITE 1 AL1 3 PL9 A 407 LMG E 101 BCR F 102
SITE 1 AL2 7 SQD A 413 DGD C 515 LHG C 518 LMG C 521
SITE 2 AL2 7 ILE J 22 PHE J 29 TYR J 33
SITE 1 AL3 10 ALA C 55 LEU C 59 VAL C 116 LEU C 119
SITE 2 AL3 10 SER C 122 ALA C 123 CLA C 510 PHE K 32
SITE 3 AL3 10 VAL Z 13 BCR y 101
SITE 1 AL4 2 ASP K 19 ASP K 23
SITE 1 AL5 14 SER A 232 ASN A 234 TRP B 5 TYR B 6
SITE 2 AL5 14 LMG B 625 TRP D 266 PHE D 269 PHE D 270
SITE 3 AL5 14 PHE D 273 PL9 D 405 GLU L 11 ASN L 13
SITE 4 AL5 14 SER L 16 ILE L 24
SITE 1 AL6 10 ILE M 23 GLU M 30 SER M 31 SQD b 602
SITE 2 AL6 10 CLA b 618 PRO l 9 VAL l 10 ILE m 24
SITE 3 AL6 10 GLN m 28 GLN m 32
SITE 1 AL7 4 MET M 1 GLU M 2 TYR b 40 GLN m 5
SITE 1 AL8 7 TYR B 40 LMG B 621 GLN M 5 LEU M 6
SITE 2 AL8 7 MET m 1 GLU m 2 MET t 1
SITE 1 AL9 2 GLU O 140 HIS O 257
SITE 1 AM1 14 ALA V 62 CYS V 63 CYS V 66 HIS V 67
SITE 2 AM1 14 THR V 74 LEU V 78 ASP V 79 LEU V 80
SITE 3 AM1 14 THR V 84 LEU V 85 TYR V 101 MET V 102
SITE 4 AM1 14 TYR V 108 HIS V 118
SITE 1 AM2 15 ALA J 14 THR J 15 LEU K 25 ILE K 28
SITE 2 AM2 15 LEU K 31 ALA K 34 PHE K 37 VAL K 38
SITE 3 AM2 15 ALA K 41 BCR K 101 VAL Z 13 PHE Z 17
SITE 4 AM2 15 ILE y 28 GLY y 29 GLY y 32
SITE 1 AM3 12 TRP B 113 TYR B 117 CLA B 605 CLA B 615
SITE 2 AM3 12 BCR B 619 TRP a 20 ASN a 26 ARG a 27
SITE 3 AM3 12 LEU a 28 THR a 45 BCR i 101 LMG i 102
SITE 1 AM4 9 ALA B 43 TRP B 75 SER B 76 LEU B 98
SITE 2 AM4 9 LMT B 629 LEU a 72 ASP a 103 ARG d 304
SITE 3 AM4 9 GLY o 138
SITE 1 AM5 23 PHE a 119 TYR a 147 PRO a 150 SER a 153
SITE 2 AM5 23 VAL a 157 MET a 183 PHE a 186 GLN a 187
SITE 3 AM5 23 HIS a 198 GLY a 201 VAL a 205 PHE a 206
SITE 4 AM5 23 VAL a 283 THR a 286 ILE a 290 CLA a 404
SITE 5 AM5 23 CLA a 405 LEU d 182 LEU d 205 PHO d 401
SITE 6 AM5 23 CLA d 405 LMG d 409 PHE t 17
SITE 1 AM6 14 THR a 45 VAL a 157 PHE a 158 MET a 172
SITE 2 AM6 14 ILE a 176 THR a 179 PHE a 180 MET a 183
SITE 3 AM6 14 CLA a 403 MET d 198 VAL d 201 PHO d 401
SITE 4 AM6 14 CLA d 405 PL9 d 407
SITE 1 AM7 15 GLN a 199 VAL a 202 ALA a 203 LEU a 210
SITE 2 AM7 15 CLA a 403 PL9 a 407 PHE d 157 VAL d 175
SITE 3 AM7 15 ILE d 178 PHE d 179 PHE d 181 LEU d 182
SITE 4 AM7 15 PHO d 402 CLA d 405 PL9 j 101
SITE 1 AM8 14 ILE a 36 PRO a 39 THR a 40 PHE a 93
SITE 2 AM8 14 PRO a 95 ILE a 96 TRP a 97 LEU a 114
SITE 3 AM8 14 HIS a 118 LEU a 121 DGD a 408 TYR i 9
SITE 4 AM8 14 PHE i 15 BCR i 101
SITE 1 AM9 14 HIS a 215 LEU a 218 HIS a 252 PHE a 255
SITE 2 AM9 14 SER a 264 PHE a 265 LEU a 271 PHE a 274
SITE 3 AM9 14 CLA a 405 PHE d 38 ALA d 41 TYR d 42
SITE 4 AM9 14 THR f 25 PL9 j 101
SITE 1 AN1 14 PHE a 93 TRP a 97 GLU a 98 LEU a 121
SITE 2 AN1 14 CLA a 406 LEU c 214 LYS c 215 SER c 216
SITE 3 AN1 14 PRO c 217 PHE c 218 TRP c 223 LYS i 5
SITE 4 AN1 14 TYR i 9 GLY o 38
SITE 1 AN2 15 ARG a 140 TRP a 142 PHE a 273 SQD a 412
SITE 2 AN2 15 TRP c 36 PHE c 436 TRP c 443 ARG c 447
SITE 3 AN2 15 CLA c 507 CLA c 520 ASN d 220 ALA d 229
SITE 4 AN2 15 SER d 230 THR d 231 PHE d 232
SITE 1 AN3 3 HIS a 332 GLU a 333 LYS d 317
SITE 1 AN4 10 GLN a 165 ASP a 170 GLU a 189 HIS a 332
SITE 2 AN4 10 GLU a 333 HIS a 337 ASP a 342 ALA a 344
SITE 3 AN4 10 GLU c 354 ARG c 357
SITE 1 AN5 14 ASN a 267 SER a 270 PHE a 273 PHE a 274
SITE 2 AN5 14 TRP a 278 LHG a 409 TRP c 36 CLA c 507
SITE 3 AN5 14 DGD c 517 LHG c 519 PHE d 232 ARG d 233
SITE 4 AN5 14 BCR j 102 PHE k 37
SITE 1 AN6 5 HIS a 215 HIS a 272 HIS d 214 HIS d 268
SITE 2 AN6 5 BCT d 404
SITE 1 AN7 7 ILE A 46 LMG I 101 TRP b 75 ASP b 87
SITE 2 AN7 7 PHE b 90 LMT b 603 LMT b 628
SITE 1 AN8 11 ARG L 14 TYR L 18 TYR M 26 LMG M 101
SITE 2 AN8 11 PHE T 19 PHE T 23 ARG b 18 SER b 104
SITE 3 AN8 11 CLA b 618 BCR b 621 ASN l 4
SITE 1 AN9 6 BCR A 408 LMG I 101 LYS O 95 GLY b 85
SITE 2 AN9 6 ASP b 87 DGD b 601
SITE 1 AO1 5 ILE T 4 VAL T 7 ALA b 43 LEU b 437
SITE 2 AO1 5 BCR b 622
SITE 1 AO2 8 TRP b 185 PRO b 187 PHE b 190 ILE b 207
SITE 2 AO2 8 CLA b 606 PHE h 41 ILE h 44 BCR x 101
SITE 1 AO3 17 GLU b 184 GLY b 189 PHE b 190 GLY b 197
SITE 2 AO3 17 HIS b 201 ALA b 204 ALA b 205 VAL b 208
SITE 3 AO3 17 PHE b 247 CLA b 605 CLA b 607 VAL d 154
SITE 4 AO3 17 PHE h 38 PHE h 41 ILE h 45 LEU h 46
SITE 5 AO3 17 TYR h 49
SITE 1 AO4 20 ARG b 68 LEU b 69 ALA b 146 LEU b 149
SITE 2 AO4 20 CYS b 150 PHE b 153 VAL b 198 HIS b 201
SITE 3 AO4 20 HIS b 202 PHE b 247 ALA b 248 VAL b 252
SITE 4 AO4 20 THR b 262 CLA b 606 CLA b 608 CLA b 609
SITE 5 AO4 20 CLA b 610 CLA b 613 PHE h 38 LEU h 42
SITE 1 AO5 21 TRP b 33 PHE b 61 PHE b 65 ARG b 68
SITE 2 AO5 21 LEU b 149 VAL b 245 ALA b 248 ALA b 249
SITE 3 AO5 21 VAL b 252 PHE b 451 HIS b 455 PHE b 458
SITE 4 AO5 21 ALA b 459 PHE b 462 CLA b 607 CLA b 609
SITE 5 AO5 21 CLA b 611 CLA b 615 CLA b 616 CLA b 617
SITE 6 AO5 21 CLA b 619
SITE 1 AO6 20 THR b 27 VAL b 30 ALA b 31 TRP b 33
SITE 2 AO6 20 ALA b 34 VAL b 62 PHE b 65 MET b 66
SITE 3 AO6 20 ARG b 68 LEU b 69 VAL b 96 HIS b 100
SITE 4 AO6 20 LEU b 103 ALA b 205 CLA b 607 CLA b 608
SITE 5 AO6 20 CLA b 610 CLA b 613 CLA b 614 CLA b 616
SITE 1 AO7 17 SQD A 414 LEU b 69 TRP b 91 ALA b 99
SITE 2 AO7 17 LEU b 103 LEU b 106 GLY b 152 PHE b 153
SITE 3 AO7 17 PHE b 156 HIS b 157 PHE b 162 PRO b 164
SITE 4 AO7 17 CLA b 607 CLA b 609 CLA b 620 BCR b 624
SITE 5 AO7 17 LMT b 628
SITE 1 AO8 17 TRP b 33 TYR b 40 GLN b 58 GLY b 59
SITE 2 AO8 17 PHE b 61 THR b 327 GLY b 328 PRO b 329
SITE 3 AO8 17 TRP b 450 ALA b 454 CLA b 608 CLA b 617
SITE 4 AO8 17 BCR b 622 BCR b 623 LMG b 626 MET d 281
SITE 5 AO8 17 LEU l 27
SITE 1 AO9 17 THR b 236 SER b 239 ALA b 243 PHE b 246
SITE 2 AO9 17 PHE b 247 PHE b 463 HIS b 466 LEU b 474
SITE 3 AO9 17 CLA b 613 CLA b 614 PHE d 120 ILE d 123
SITE 4 AO9 17 MET d 126 LEU d 127 PHE d 130 SQD d 403
SITE 5 AO9 17 LEU h 43
SITE 1 AP1 18 PHE b 139 ALA b 212 PHE b 215 HIS b 216
SITE 2 AP1 18 PRO b 221 PRO b 222 LEU b 229 CLA b 607
SITE 3 AP1 18 CLA b 609 CLA b 612 CLA b 614 SQD d 403
SITE 4 AP1 18 THR h 27 THR h 28 MET h 31 PHE h 34
SITE 5 AP1 18 MET h 35 BCR x 101
SITE 1 AP2 14 HIS b 23 LEU b 135 PHE b 139 HIS b 142
SITE 2 AP2 14 LEU b 143 THR b 236 VAL b 237 SER b 240
SITE 3 AP2 14 CLA b 609 CLA b 612 CLA b 613 CLA b 616
SITE 4 AP2 14 CLA b 619 BCR x 101
SITE 1 AP3 19 TRP b 5 TYR b 6 ARG b 7 VAL b 8
SITE 2 AP3 19 HIS b 9 THR b 10 ILE b 242 LEU b 461
SITE 3 AP3 19 PHE b 462 GLY b 465 TRP b 468 HIS b 469
SITE 4 AP3 19 ARG b 472 CLA b 608 CLA b 616 CLA b 617
SITE 5 AP3 19 CLA b 618 LMG d 408 LMG l 101
SITE 1 AP4 16 HIS b 9 LEU b 19 HIS b 23 HIS b 26
SITE 2 AP4 16 THR b 27 ILE b 234 VAL b 237 LEU b 238
SITE 3 AP4 16 SER b 241 CLA b 608 CLA b 609 CLA b 614
SITE 4 AP4 16 CLA b 615 CLA b 617 CLA b 618 CLA b 619
SITE 1 AP5 9 HIS b 9 HIS b 26 PHE b 462 CLA b 608
SITE 2 AP5 9 CLA b 611 CLA b 615 CLA b 616 CLA b 618
SITE 3 AP5 9 LMG d 408
SITE 1 AP6 13 LMG M 101 VAL b 8 HIS b 9 VAL b 11
SITE 2 AP6 13 LEU b 12 LEU b 29 TRP b 115 SQD b 602
SITE 3 AP6 13 CLA b 615 CLA b 616 CLA b 617 BCR b 621
SITE 4 AP6 13 VAL l 10
SITE 1 AP7 13 HIS b 23 MET b 138 ILE b 141 HIS b 142
SITE 2 AP7 13 LEU b 145 CLA b 608 CLA b 614 CLA b 616
SITE 3 AP7 13 CLA b 620 BCR b 624 LEU h 7 LEU h 14
SITE 4 AP7 13 ASN h 15
SITE 1 AP8 10 SQD A 414 LEU b 24 ALA b 110 TRP b 113
SITE 2 AP8 10 HIS b 114 LEU b 122 CLA b 610 CLA b 619
SITE 3 AP8 10 THR h 5 LEU h 7
SITE 1 AP9 8 PHE T 19 MET b 25 TRP b 115 SQD b 602
SITE 2 AP9 8 CLA b 618 BCR b 622 BCR b 623 LEU m 13
SITE 1 AQ1 15 SQD A 414 ILE T 4 PHE T 8 ALA T 11
SITE 2 AQ1 15 PHE T 17 PHE T 18 ILE T 21 PHE T 22
SITE 3 AQ1 15 TRP b 33 SER b 36 MET b 37 LMT b 604
SITE 4 AQ1 15 CLA b 611 BCR b 621 BCR b 623
SITE 1 AQ2 8 LEU b 29 GLY b 32 TRP b 33 ILE b 101
SITE 2 AQ2 8 GLY b 105 CLA b 611 BCR b 621 BCR b 622
SITE 1 AQ3 9 SQD A 414 PHE T 18 PHE T 22 LEU b 109
SITE 2 AQ3 9 ALA b 110 CYS b 112 TYR b 117 CLA b 610
SITE 3 AQ3 9 CLA b 619
SITE 1 AQ4 12 TYR b 193 PHE b 250 TYR b 258 TYR b 273
SITE 2 AQ4 12 SER b 277 HIS d 87 LEU d 162 TYR h 49
SITE 3 AQ4 12 ASN h 50 VAL h 60 SER h 61 TRP h 62
SITE 1 AQ5 11 TYR b 40 THR b 327 GLY b 328 PRO b 329
SITE 2 AQ5 11 LYS b 332 PHE b 453 CLA b 611 ILE d 284
SITE 3 AQ5 11 PHE l 35 ASN m 4 LEU m 6
SITE 1 AQ6 8 LEU A 72 ASP A 103 ARG D 304 GLY O 138
SITE 2 AQ6 8 ALA b 43 TRP b 75 SER b 76 LEU b 98
SITE 1 AQ7 4 TRP b 91 PHE b 162 DGD b 601 CLA b 610
SITE 1 AQ8 7 ARG b 224 LYS b 227 ASP d 16 ASP d 19
SITE 2 AQ8 7 SQD d 403 ALA h 32 MET h 35
SITE 1 AQ9 17 LEU c 95 LEU c 168 GLY c 171 ALA c 172
SITE 2 AQ9 17 LEU c 175 ILE c 224 VAL c 233 HIS c 237
SITE 3 AQ9 17 ILE c 240 ALA c 278 MET c 282 VAL c 296
SITE 4 AQ9 17 TYR c 297 CLA c 502 CLA c 503 CLA c 506
SITE 5 AQ9 17 BCR c 514
SITE 1 AR1 16 TRP c 63 HIS c 91 TRP c 97 GLY c 171
SITE 2 AR1 16 LYS c 178 PHE c 182 LEU c 279 MET c 282
SITE 3 AR1 16 ALA c 286 TYR c 297 HIS c 430 LEU c 433
SITE 4 AR1 16 PHE c 437 CLA c 501 CLA c 503 CLA c 508
SITE 1 AR2 14 ILE c 60 VAL c 61 ALA c 64 THR c 68
SITE 2 AR2 14 LEU c 88 HIS c 91 ILE c 92 VAL c 114
SITE 3 AR2 14 HIS c 118 CLA c 501 CLA c 502 CLA c 509
SITE 4 AR2 14 CLA c 511 LMG c 518
SITE 1 AR3 18 PHE a 33 MET a 127 GLY a 128 TRP a 131
SITE 2 AR3 18 PHE c 264 ILE c 265 TYR c 274 GLY c 277
SITE 3 AR3 18 ALA c 278 MET c 281 HIS c 441 LEU c 442
SITE 4 AR3 18 ALA c 445 ARG c 449 CLA c 506 BCR c 514
SITE 5 AR3 18 VAL i 12 PHE i 23
SITE 1 AR4 12 LEU c 165 ILE c 243 GLY c 247 TRP c 250
SITE 2 AR4 12 HIS c 251 THR c 255 PRO c 256 PHE c 257
SITE 3 AR4 12 TRP c 259 ALA c 260 PHE c 264 CLA c 506
SITE 1 AR5 13 MET c 157 LEU c 161 HIS c 164 PHE c 264
SITE 2 AR5 13 TRP c 266 TYR c 271 TYR c 274 SER c 275
SITE 3 AR5 13 LEU c 279 CLA c 501 CLA c 504 CLA c 505
SITE 4 AR5 13 CLA c 508
SITE 1 AR6 17 LHG a 409 SQD a 412 TRP c 36 ALA c 37
SITE 2 AR6 17 ASN c 39 ALA c 40 GLU c 269 LEU c 276
SITE 3 AR6 17 PHE c 436 PHE c 437 GLY c 440 TRP c 443
SITE 4 AR6 17 HIS c 444 ARG c 447 CLA c 508 CLA c 509
SITE 5 AR6 17 DGD c 516
SITE 1 AR7 18 ASN c 39 LEU c 42 LEU c 49 ALA c 52
SITE 2 AR7 18 HIS c 53 HIS c 56 TYR c 149 TRP c 151
SITE 3 AR7 18 GLY c 268 TYR c 271 LEU c 272 SER c 275
SITE 4 AR7 18 LEU c 279 CLA c 502 CLA c 506 CLA c 507
SITE 5 AR7 18 CLA c 509 CLA c 511
SITE 1 AR8 15 ASN c 39 HIS c 56 LEU c 59 TRP c 63
SITE 2 AR8 15 LEU c 279 PHE c 436 PHE c 437 CLA c 503
SITE 3 AR8 15 CLA c 507 CLA c 508 CLA c 510 CLA c 520
SITE 4 AR8 15 PRO k 29 VAL k 30 LEU k 33
SITE 1 AR9 20 TRP c 35 GLY c 38 ASN c 39 ARG c 41
SITE 2 AR9 20 LEU c 42 LEU c 45 LYS c 48 ALA c 52
SITE 3 AR9 20 PHE c 127 ILE c 134 CLA c 509 BCR c 513
SITE 4 AR9 20 ILE g 35 LEU g 46 PHE k 32 TRP k 39
SITE 5 AR9 20 GLN k 40 MET z 19 VAL z 20 PRO z 24
SITE 1 AS1 13 HIS c 53 ALA c 57 PHE c 147 PHE c 163
SITE 2 AS1 13 HIS c 164 VAL c 167 ILE c 170 GLY c 171
SITE 3 AS1 13 LEU c 174 CLA c 503 CLA c 508 CLA c 512
SITE 4 AS1 13 BCR c 521
SITE 1 AS2 10 LEU c 50 VAL c 54 VAL c 124 GLY c 128
SITE 2 AS2 10 TYR c 131 HIS c 132 PRO c 137 PHE c 147
SITE 3 AS2 10 CLA c 511 BCR c 521
SITE 1 AS3 12 ALA c 55 VAL c 116 LEU c 119 ILE c 120
SITE 2 AS3 12 SER c 122 ALA c 123 CLA c 510 BCR c 521
SITE 3 AS3 12 BCR g 101 PHE k 18 PHE k 32 VAL z 13
SITE 1 AS4 11 ILE c 209 TYR c 212 LEU c 213 VAL c 227
SITE 2 AS4 11 ASP c 232 VAL c 233 GLY c 236 ILE c 240
SITE 3 AS4 11 PHE c 264 CLA c 501 CLA c 504
SITE 1 AS5 16 LEU a 91 PHE a 155 ILE a 163 PRO c 217
SITE 2 AS5 16 PHE c 218 GLY c 219 GLY c 220 GLY c 222
SITE 3 AS5 16 VAL c 225 SER c 226 PHE c 284 CYS c 288
SITE 4 AS5 16 PHE c 292 ASN c 294 PHE c 361 ARG c 362
SITE 1 AS6 18 PHE a 197 TYR c 82 GLU c 83 GLN c 84
SITE 2 AS6 18 GLY c 85 LEU c 404 SER c 406 ASN c 418
SITE 3 AS6 18 PHE c 419 VAL c 420 TRP c 425 CLA c 507
SITE 4 AS6 18 DGD c 517 LHG c 519 CLA c 520 LMG c 522
SITE 5 AS6 18 TYR j 33 BCR j 102
SITE 1 AS7 21 TRP a 278 PHE a 300 ASN a 301 PHE a 302
SITE 2 AS7 21 SER a 305 SQD a 412 ASN c 405 SER c 406
SITE 3 AS7 21 VAL c 407 ASN c 415 SER c 416 ASN c 418
SITE 4 AS7 21 DGD c 516 CLA c 520 PHE j 29 ALA j 32
SITE 5 AS7 21 TYR j 33 GLY j 37 SER j 38 SER j 39
SITE 6 AS7 21 GLN v 60
SITE 1 AS8 7 TRP c 97 PHE c 109 VAL c 113 VAL c 117
SITE 2 AS8 7 HIS c 118 CLA c 503 PHE z 59
SITE 1 AS9 8 TYR a 262 ASN a 266 SQD a 412 TRP c 35
SITE 2 AS9 8 DGD c 516 LMG e 101 BCR j 102 PHE k 45
SITE 1 AT1 17 PHE a 285 LHG a 409 TRP c 63 MET c 67
SITE 2 AT1 17 PHE c 70 GLN c 84 GLY c 85 ILE c 87
SITE 3 AT1 17 LEU c 404 TRP c 425 SER c 429 CLA c 509
SITE 4 AT1 17 DGD c 516 DGD c 517 LMG c 522 PRO k 26
SITE 5 AT1 17 VAL k 30
SITE 1 AT2 9 PHE c 112 VAL c 116 SER c 121 VAL c 124
SITE 2 AT2 9 CLA c 511 CLA c 512 BCR c 513 TYR k 15
SITE 3 AT2 9 GLY z 55
SITE 1 AT3 6 HIS c 74 DGD c 516 CLA c 520 ILE g 25
SITE 2 AT3 6 BCR j 102 ASP k 23
SITE 1 AT4 18 LEU a 41 ALA a 44 THR a 45 ILE a 115
SITE 2 AT4 18 TYR a 126 GLN a 130 TYR a 147 LEU a 174
SITE 3 AT4 18 VAL a 283 CLA a 403 CLA a 404 LEU d 205
SITE 4 AT4 18 ALA d 208 LEU d 209 ALA d 212 ILE d 213
SITE 5 AT4 18 TRP d 253 PHE d 257
SITE 1 AT5 19 PHE a 206 ALA a 209 LEU a 210 MET a 214
SITE 2 AT5 19 LEU a 258 CLA a 405 ALA d 41 TRP d 48
SITE 3 AT5 19 GLY d 118 LEU d 122 PHE d 125 GLN d 129
SITE 4 AT5 19 ASN d 142 PHE d 146 PHE d 153 PHE d 173
SITE 5 AT5 19 PRO d 275 LEU d 279 CLA d 405
SITE 1 AT6 10 ALA b 228 ARG b 230 LEU b 474 CLA b 612
SITE 2 AT6 10 CLA b 613 LMT b 629 LYS d 23 TRP d 32
SITE 3 AT6 10 ARG d 134 LEU d 135
SITE 1 AT7 8 HIS a 215 GLU a 244 TYR a 246 HIS a 272
SITE 2 AT7 8 FE2 a 413 TYR d 244 LYS d 264 HIS d 268
SITE 1 AT8 23 PHE a 206 CLA a 403 CLA a 404 CLA a 405
SITE 2 AT8 23 TRP d 48 LEU d 122 VAL d 152 PHE d 153
SITE 3 AT8 23 VAL d 156 LEU d 182 PHE d 185 GLN d 186
SITE 4 AT8 23 TRP d 191 THR d 192 HIS d 197 GLY d 200
SITE 5 AT8 23 VAL d 201 VAL d 204 LEU d 279 SER d 282
SITE 6 AT8 23 ALA d 283 VAL d 286 PHO d 402
SITE 1 AT9 14 LEU d 43 LEU d 89 LEU d 90 LEU d 91
SITE 2 AT9 14 LEU d 92 TRP d 93 THR d 112 PHE d 113
SITE 3 AT9 14 HIS d 117 PHE d 120 LMT d 411 GLY x 22
SITE 4 AT9 14 LEU x 23 GLY x 26
SITE 1 AU1 12 PHE a 52 CLA a 404 MET d 199 HIS d 214
SITE 2 AU1 12 THR d 217 TRP d 253 ALA d 260 PHE d 261
SITE 3 AU1 12 LEU d 267 VAL l 26 LMG l 101 PHE t 10
SITE 1 AU2 13 ASN a 234 TRP b 5 TYR b 6 ARG b 7
SITE 2 AU2 13 PHE b 464 TRP b 468 CLA b 615 CLA b 617
SITE 3 AU2 13 ARG d 139 TYR d 141 PHE d 269 PHE d 273
SITE 4 AU2 13 LMG l 101
SITE 1 AU3 13 CLA a 403 PHE d 257 ILE d 259 ALA d 260
SITE 2 AU3 13 PHE d 261 SER d 262 ASN d 263 TRP d 266
SITE 3 AU3 13 THR l 15 TYR l 18 LEU l 19 PHE t 17
SITE 4 AU3 13 ALA t 20
SITE 1 AU4 7 ASP d 100 PHE d 101 THR d 102 LMT d 411
SITE 2 AU4 7 LEU e 42 ASP e 45 VAL e 46
SITE 1 AU5 8 LEU d 92 TRP d 93 GLY d 99 CLA d 406
SITE 2 AU5 8 DGD d 410 ILE x 21 SER x 25 GLY x 26
SITE 1 AU6 12 TYR d 67 GLY d 70 ASN d 72 PHE d 73
SITE 2 AU6 12 ILE f 37 MET f 40 GLN f 41 PHE j 28
SITE 3 AU6 12 GLY j 31 ALA j 32 GLY j 37 PL9 j 101
SITE 1 AU7 7 TYR a 262 LHG c 519 PHE d 27 PRO e 9
SITE 2 AU7 7 PHE e 10 SER e 11 PL9 j 101
SITE 1 AU8 15 ARG e 8 PHE e 10 ILE e 13 ARG e 18
SITE 2 AU8 15 TYR e 19 HIS e 23 THR e 26 LEU e 30
SITE 3 AU8 15 ILE f 15 ARG f 19 TRP f 20 VAL f 23
SITE 4 AU8 15 HIS f 24 ALA f 27 ILE f 31
SITE 1 AU9 9 TYR d 42 LEU d 49 THR d 50 PHE d 101
SITE 2 AU9 9 PRO f 29 PHE f 33 VAL j 21 VAL j 25
SITE 3 AU9 9 PL9 j 101
SITE 1 AV1 8 TRP d 21 ARG d 24 ARG d 26 GLU e 7
SITE 2 AV1 8 PHE f 16 THR f 17 VAL f 18 THR x 33
SITE 1 AV2 7 LMT B 628 ILE a 38 LEU a 42 ALA a 43
SITE 2 AV2 7 SQD a 401 CLA a 406 PHE i 15
SITE 1 AV3 7 DGD B 626 LMT B 628 SQD a 401 MET i 1
SITE 2 AV3 7 THR i 3 LEU i 4 LMT i 103
SITE 1 AV4 5 THR i 3 ILE i 6 ILE i 10 PHE i 14
SITE 2 AV4 5 LMG i 102
SITE 1 AV5 6 CLA a 405 PL9 a 407 LMG d 412 LMG e 101
SITE 2 AV5 6 BCR f 102 VAL j 16
SITE 1 AV6 7 SQD a 412 DGD c 516 LHG c 519 LMG c 522
SITE 2 AV6 7 BCR g 101 PHE j 29 TYR j 33
SITE 1 AV7 2 ASP k 19 ASP k 23
SITE 1 AV8 14 SER a 232 ASN a 234 TRP b 5 TYR b 6
SITE 2 AV8 14 CLA b 615 TRP d 266 PHE d 269 PL9 d 407
SITE 3 AV8 14 LMG d 408 GLU l 11 LEU l 12 ASN l 13
SITE 4 AV8 14 SER l 16 ILE l 24
SITE 1 AV9 9 CLA B 613 SQD B 627 VAL L 10 ILE M 24
SITE 2 AV9 9 GLN M 28 GLN M 32 ILE m 23 GLU m 30
SITE 3 AV9 9 SER m 31
SITE 1 AW1 2 GLU o 140 HIS o 257
SITE 1 AW2 15 ALA v 62 CYS v 63 CYS v 66 HIS v 67
SITE 2 AW2 15 THR v 74 LEU v 78 ASP v 79 LEU v 80
SITE 3 AW2 15 THR v 84 LEU v 85 TYR v 101 MET v 102
SITE 4 AW2 15 TYR v 108 HIS v 118 PRO v 119
SITE 1 AW3 16 BCR c 513 ILE g 28 GLY g 29 GLY g 32
SITE 2 AW3 16 ALA j 14 THR j 15 BCR j 102 LEU k 25
SITE 3 AW3 16 ILE k 28 LEU k 31 ALA k 34 PHE k 37
SITE 4 AW3 16 VAL k 38 ALA k 41 VAL z 13 PHE z 17
SITE 1 AW4 9 CLA b 605 CLA b 613 CLA b 614 MET h 35
SITE 2 AW4 9 LEU h 37 PHE h 38 PHE h 41 THR x 11
SITE 3 AW4 9 LEU x 16
CRYST1 132.615 229.296 306.825 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 0.007541 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004361 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003259 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
