HEADER ELECTRON TRANSPORT,PHOTOSYNTHESIS 04-JUN-14 4TNJ
TITLE RT XFEL STRUCTURE OF PHOTOSYSTEM II 500 MS AFTER THE 2ND ILLUMINATION
TITLE 2 (2F) AT 4.5 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 5 27-SEP-23 4TNJ 1 FORMUL LINK
REVDAT 4 04-DEC-19 4TNJ 1 REMARK
REVDAT 3 27-SEP-17 4TNJ 1 REMARK
REVDAT 2 23-JUL-14 4TNJ 1 JRNL
REVDAT 1 09-JUL-14 4TNJ 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. 4.50 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) : 4.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 72.97
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.364
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 103594
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.276
REMARK 3 R VALUE (WORKING SET) : 0.276
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.896
REMARK 3 FREE R VALUE TEST SET COUNT : 5072
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 72.9798 - 13.9511 1.00 3411 149 0.3138 0.3032
REMARK 3 2 13.9511 - 11.0859 1.00 3387 176 0.2272 0.2217
REMARK 3 3 11.0859 - 9.6882 1.00 3394 169 0.2200 0.2138
REMARK 3 4 9.6882 - 8.8040 1.00 3379 168 0.2079 0.2239
REMARK 3 5 8.8040 - 8.1739 1.00 3403 192 0.2234 0.2128
REMARK 3 6 8.1739 - 7.6925 1.00 3409 185 0.2346 0.2807
REMARK 3 7 7.6925 - 7.3077 1.00 3393 170 0.2384 0.2545
REMARK 3 8 7.3077 - 6.9898 1.00 3347 175 0.2458 0.2869
REMARK 3 9 6.9898 - 6.7209 1.00 3424 177 0.2569 0.2718
REMARK 3 10 6.7209 - 6.4892 1.00 3417 173 0.2707 0.3124
REMARK 3 11 6.4892 - 6.2864 1.00 3351 172 0.2636 0.2590
REMARK 3 12 6.2864 - 6.1068 1.00 3428 174 0.2777 0.2912
REMARK 3 13 6.1068 - 5.9461 1.00 3392 188 0.2801 0.3347
REMARK 3 14 5.9461 - 5.8011 1.00 3404 162 0.2907 0.2844
REMARK 3 15 5.8011 - 5.6692 1.00 3386 199 0.2995 0.3075
REMARK 3 16 5.6692 - 5.5486 1.00 3382 157 0.2873 0.3259
REMARK 3 17 5.5486 - 5.4377 1.00 3429 182 0.3082 0.3028
REMARK 3 18 5.4377 - 5.3351 1.00 3335 181 0.3038 0.3356
REMARK 3 19 5.3351 - 5.2398 1.00 3425 164 0.3126 0.3522
REMARK 3 20 5.2398 - 5.1510 1.00 3374 177 0.3080 0.3008
REMARK 3 21 5.1510 - 5.0680 0.99 3307 167 0.3202 0.2995
REMARK 3 22 5.0680 - 4.9900 0.99 3393 198 0.3254 0.3408
REMARK 3 23 4.9900 - 4.9167 0.98 3334 175 0.3196 0.3218
REMARK 3 24 4.9167 - 4.8474 0.96 3276 163 0.3395 0.2994
REMARK 3 25 4.8474 - 4.7819 0.95 3242 161 0.3352 0.3406
REMARK 3 26 4.7819 - 4.7198 0.92 3052 155 0.3489 0.3529
REMARK 3 27 4.7198 - 4.6608 0.86 2971 143 0.3623 0.3655
REMARK 3 28 4.6608 - 4.6047 0.86 2948 161 0.3564 0.3870
REMARK 3 29 4.6047 - 4.5512 0.81 2736 148 0.3683 0.3759
REMARK 3 30 4.5512 - 4.5000 0.70 2393 111 0.3779 0.4248
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) : 0.648
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.666
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 152.7
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 174.0
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 : 0.757 71528
REMARK 3 CHIRALITY : 0.029 7238
REMARK 3 PLANARITY : 0.004 8510
REMARK 3 DIHEDRAL : 18.658 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 4TNJ 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_1000201918.
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 : 16973
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 : 52965
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.500
REMARK 200 RESOLUTION RANGE LOW (A) : 72.970
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 131.4
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 52.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8
REMARK 200 DATA REDUNDANCY IN SHELL : 7.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
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 66.14900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 153.98800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 114.35650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 153.98800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 66.14900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 114.35650
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 2.11
REMARK 500 O TRP c 250 OG1 THR c 254 2.12
REMARK 500 O TRP C 291 OG1 THR C 305 2.13
REMARK 500 O TRP c 291 OG1 THR c 305 2.17
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. = 13.8 DEGREES
REMARK 500 PRO b 484 C - N - CA ANGL. DEV. = 13.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 12 113.55 156.68
REMARK 500 PRO A 141 -129.69 -74.18
REMARK 500 TRP A 142 -10.47 57.87
REMARK 500 LEU A 159 -50.96 -132.18
REMARK 500 SER A 222 43.06 -109.78
REMARK 500 GLU A 226 10.06 -147.12
REMARK 500 ILE A 259 -84.54 -103.94
REMARK 500 PHE A 302 32.40 -98.39
REMARK 500 ARG A 334 -71.03 -27.38
REMARK 500 ASP B 119 55.12 -91.78
REMARK 500 ARG B 127 -71.75 -63.31
REMARK 500 PRO B 183 175.19 -59.24
REMARK 500 LEU B 218 -67.61 -95.18
REMARK 500 ARG B 230 53.37 31.50
REMARK 500 SER B 294 27.72 -79.83
REMARK 500 ASP B 313 41.82 -91.60
REMARK 500 THR B 436 -70.31 -33.73
REMARK 500 SER B 480 -12.56 70.07
REMARK 500 ILE B 482 -165.91 -117.54
REMARK 500 PRO B 484 -143.81 -7.86
REMARK 500 GLU B 485 164.38 62.54
REMARK 500 LEU B 486 68.84 -155.03
REMARK 500 PRO B 488 -108.51 5.33
REMARK 500 GLU B 489 56.92 -65.19
REMARK 500 GLN B 490 107.87 -167.15
REMARK 500 GLU C 29 -149.64 -148.47
REMARK 500 ARG C 135 -62.72 -121.66
REMARK 500 SER C 144 112.05 -179.97
REMARK 500 ASN C 201 59.14 -168.57
REMARK 500 ILE C 209 -70.11 -53.63
REMARK 500 TRP C 223 -145.28 61.06
REMARK 500 LEU C 253 30.21 -96.38
REMARK 500 PHE C 257 -145.97 -71.51
REMARK 500 ARG C 320 -71.40 -59.53
REMARK 500 PRO C 368 -9.54 -59.70
REMARK 500 LEU C 375 114.06 -34.69
REMARK 500 ASN C 382 12.46 -161.40
REMARK 500 HIS C 398 33.97 -142.05
REMARK 500 SER C 406 65.49 60.08
REMARK 500 ALA C 411 -17.37 -49.62
REMARK 500 SER C 416 -60.84 -176.83
REMARK 500 PHE C 455 23.38 -150.16
REMARK 500 GLU C 462 -76.04 -68.52
REMARK 500 ARG D 26 -165.46 -102.53
REMARK 500 VAL D 30 -83.56 -89.78
REMARK 500 LEU D 37 -71.44 -56.83
REMARK 500 SER D 65 16.45 -141.31
REMARK 500 PRO D 140 37.12 -84.86
REMARK 500 LEU D 158 -65.10 -128.95
REMARK 500 ALA D 234 28.82 -76.04
REMARK 500
REMARK 500 THIS ENTRY HAS 248 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 406
REMARK 610 DGD A 408
REMARK 610 LHG A 409
REMARK 610 LMG A 410
REMARK 610 SQD A 413
REMARK 610 LMG A 415
REMARK 610 DGD B 620
REMARK 610 LMG B 621
REMARK 610 LMG B 624
REMARK 610 DGD B 625
REMARK 610 SQD B 626
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 DGD D 409
REMARK 610 LMT D 410
REMARK 610 LMG D 412
REMARK 610 LMG E 101
REMARK 610 SQD F 102
REMARK 610 LMG I 101
REMARK 610 PL9 J 101
REMARK 610 LMG M 101
REMARK 610 LMG a 402
REMARK 610 PL9 a 409
REMARK 610 DGD a 411
REMARK 610 LHG a 412
REMARK 610 LMG a 413
REMARK 610 SQD a 415
REMARK 610 DGD b 601
REMARK 610 SQD b 602
REMARK 610 DGD b 624
REMARK 610 LMG b 625
REMARK 610 LMG b 628
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 402
REMARK 610 LMG d 407
REMARK 610 DGD d 408
REMARK 610 LMT d 409
REMARK 610 LMG d 410
REMARK 610 LMG e 101
REMARK 610 SQD f 103
REMARK 610 LMG i 101
REMARK 610 PL9 j 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 124.3
REMARK 620 3 OEX A 412 O2 60.4 63.8
REMARK 620 4 OEX A 412 O5 94.8 60.5 64.3
REMARK 620 5 GLU A 189 OE1 169.0 63.7 126.7 82.8
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 106.7
REMARK 620 3 OEX A 412 O4 68.1 87.4
REMARK 620 4 GLU A 333 OE2 127.5 107.3 74.7
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 83.1
REMARK 620 3 OEX A 412 O5 127.5 90.7
REMARK 620 4 OEX A 412 O3 143.8 89.5 87.8
REMARK 620 5 HIS A 332 NE2 74.7 157.2 106.8 105.4
REMARK 620 6 ASP A 342 OD2 66.2 89.8 166.2 78.5 76.8
REMARK 620 N 1 2 3 4 5
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 96.4
REMARK 620 3 HIS D 214 NE2 125.2 113.8
REMARK 620 4 HIS D 268 NE2 79.8 154.9 87.8
REMARK 620 5 BCT D 404 O3 129.9 91.6 95.2 73.0
REMARK 620 6 BCT D 404 O2 84.0 81.5 142.4 73.5 48.5
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 96.8 88.6
REMARK 620 4 OEX A 412 O4 83.9 92.0 178.2
REMARK 620 5 OEX A 412 O5 107.3 115.9 89.0 89.2
REMARK 620 6 GLU C 354 OE2 67.1 74.1 71.4 110.3 158.2
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 111.4
REMARK 620 3 OEX A 412 O2 159.1 89.3
REMARK 620 4 OEX A 412 O3 93.3 87.0 85.3
REMARK 620 5 ALA A 344 OXT 98.9 130.1 67.4 130.9
REMARK 620 N 1 2 3 4
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 96.2
REMARK 620 3 CLA C 510 NB 75.2 92.2
REMARK 620 4 CLA C 510 NC 84.2 176.7 91.0
REMARK 620 5 CLA C 510 ND 104.1 90.7 177.0 86.0
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 87.3
REMARK 620 3 HEM F 101 NB 104.3 89.3
REMARK 620 4 HEM F 101 NC 89.3 175.5 88.7
REMARK 620 5 HEM F 101 ND 67.2 90.4 171.6 90.9
REMARK 620 6 HIS F 24 NE2 157.7 70.4 75.3 112.9 112.5
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 132.5
REMARK 620 3 ASP K 23 OD2 124.7 46.4
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 88.6 89.8
REMARK 620 4 HEM V 201 NC 88.5 175.4 90.1
REMARK 620 5 HEM V 201 ND 81.5 88.6 170.0 90.7
REMARK 620 6 HIS V 118 NE2 169.4 87.3 100.3 97.2 89.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 414 CA1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP a 170 OD1
REMARK 620 2 OEX a 414 O1 126.1
REMARK 620 3 OEX a 414 O2 62.6 63.6
REMARK 620 4 OEX a 414 O5 97.5 61.0 63.9
REMARK 620 5 GLU a 189 OE1 170.0 62.7 125.4 82.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 414 MN4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP a 170 OD2
REMARK 620 2 OEX a 414 O5 110.5
REMARK 620 3 OEX a 414 O4 66.9 87.6
REMARK 620 4 GLU a 333 OE2 123.1 107.7 74.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 414 MN1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU a 189 OE2
REMARK 620 2 OEX a 414 O1 85.0
REMARK 620 3 OEX a 414 O5 129.2 90.6
REMARK 620 4 OEX a 414 O3 142.5 89.4 87.7
REMARK 620 5 HIS a 332 NE2 70.8 155.4 107.6 107.2
REMARK 620 6 ASP a 342 OD2 63.0 89.8 167.7 80.0 75.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 a 403 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS a 215 NE2
REMARK 620 2 HIS a 272 NE2 96.3
REMARK 620 3 HIS d 214 NE2 120.4 112.2
REMARK 620 4 HIS d 268 NE2 78.4 156.6 89.7
REMARK 620 5 BCT d 403 O2 87.1 85.3 143.5 71.7
REMARK 620 6 BCT d 403 O3 133.4 94.5 96.5 74.1 48.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 414 MN3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU a 333 OE1
REMARK 620 2 OEX a 414 O2 136.8
REMARK 620 3 OEX a 414 O3 98.0 88.7
REMARK 620 4 OEX a 414 O4 82.3 92.0 178.6
REMARK 620 5 OEX a 414 O5 107.6 115.2 89.1 89.5
REMARK 620 6 GLU c 354 OE2 68.4 73.2 73.0 108.4 160.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 414 MN2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP a 342 OD1
REMARK 620 2 OEX a 414 O1 109.3
REMARK 620 3 OEX a 414 O2 161.2 89.3
REMARK 620 4 OEX a 414 O3 93.0 87.1 85.4
REMARK 620 5 ALA a 344 OXT 101.6 129.0 66.6 131.3
REMARK 620 6 GLU c 354 OE1 66.9 158.2 95.0 72.0 71.8
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 95.8
REMARK 620 3 CLA c 510 NB 75.2 92.2
REMARK 620 4 CLA c 510 NC 84.5 176.7 91.0
REMARK 620 5 CLA c 510 ND 104.2 90.7 177.1 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 87.6
REMARK 620 3 HEM f 101 NB 103.5 89.5
REMARK 620 4 HEM f 101 NC 88.5 175.0 88.4
REMARK 620 5 HEM f 101 ND 67.4 90.2 170.8 91.2
REMARK 620 6 HIS f 24 NE2 157.7 70.2 78.1 113.7 110.3
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 124.2
REMARK 620 3 ASP k 23 OD2 115.3 41.7
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 86.2
REMARK 620 3 HEM v 201 NB 86.5 89.3
REMARK 620 4 HEM v 201 NC 89.3 175.5 90.2
REMARK 620 5 HEM v 201 ND 83.7 89.8 170.2 90.0
REMARK 620 6 HIS v 118 NE2 170.4 86.9 100.2 97.6 89.6
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 CLA A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG 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 LMG A 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD B 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT B 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT B 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 624
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD B 625
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD B 626
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT B 627
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT B 628
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 BCR 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 DGD C 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG C 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 522
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 D 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG D 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD D 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT D 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR D 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG D 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG E 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM F 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD F 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA H 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR H 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG I 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT I 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 J 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR J 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA K 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG M 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT M 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT M 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA O 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM V 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR y 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD a 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG a 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE2 a 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO a 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 a 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR a 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD a 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG a 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG a 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OEX a 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD a 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD b 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD b 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT b 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT b 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD b 624
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG b 625
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT b 626
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT b 627
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG b 628
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG c 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 522
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO d 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD d 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT d 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 d 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG d 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD d 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT d 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG d 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG e 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM f 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR f 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD f 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA h 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG i 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT i 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 j 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR j 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA k 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 RT STRUCTURE OF THE DARK STATE OF PHOTOSYSTEM II
REMARK 900 RELATED ID: 4TNI RELATED DB: PDB
REMARK 900 RELATED ID: 4TNK RELATED DB: PDB
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 4TNJ A 1 344 UNP P0A444 PSBA1_THEEB 1 344
DBREF 4TNJ B 1 510 UNP Q8DIQ1 Q8DIQ1_THEEB 1 510
DBREF 4TNJ C 13 473 UNP Q8DIF8 Q8DIF8_THEEB 1 461
DBREF 4TNJ D 1 352 UNP Q8CM25 PSBD_THEEB 1 352
DBREF 4TNJ E 1 84 UNP Q8DIP0 PSBE_THEEB 1 84
DBREF 4TNJ F 1 45 UNP Q8DIN9 PSBF_THEEB 1 45
DBREF 4TNJ H 1 66 UNP Q8DJ43 PSBH_THEEB 1 66
DBREF 4TNJ I 1 38 UNP Q8DJZ6 PSBI_THEEB 1 38
DBREF 4TNJ J 1 40 UNP P59087 PSBJ_THEEB 1 40
DBREF 4TNJ K 1 46 UNP Q9F1K9 PSBK_THEEB 1 46
DBREF 4TNJ L 1 37 UNP Q8DIN8 PSBL_THEEB 1 37
DBREF 4TNJ M 1 36 UNP Q8DHA7 PSBM_THEEB 1 36
DBREF 4TNJ O 1 272 UNP P0A431 PSBO_THEEB 1 272
DBREF 4TNJ T 1 32 UNP Q8DIQ0 PSBT_THEEB 1 32
DBREF 4TNJ U 1 134 UNP Q9F1L5 PSBU_THEEB 1 134
DBREF 4TNJ V 1 163 UNP P0A386 CY550_THEEB 1 163
DBREF 4TNJ y 1 46 UNP Q8DJI1 YCF12_THEEB 1 46
DBREF 4TNJ X 10 50 UNP Q9F1R6 PSBX_THEEB 1 41
DBREF 4TNJ Y 1 28 PDB 4TNJ 4TNJ 1 28
DBREF 4TNJ Z 1 62 UNP Q8DHJ2 PSBZ_THEEB 1 62
DBREF 4TNJ a 1 344 UNP P0A444 PSBA1_THEEB 1 344
DBREF 4TNJ b 1 510 UNP Q8DIQ1 Q8DIQ1_THEEB 1 510
DBREF 4TNJ c 13 473 UNP Q8DIF8 Q8DIF8_THEEB 1 461
DBREF 4TNJ d 1 352 UNP Q8CM25 PSBD_THEEB 1 352
DBREF 4TNJ e 1 84 UNP Q8DIP0 PSBE_THEEB 1 84
DBREF 4TNJ f 1 45 UNP Q8DIN9 PSBF_THEEB 1 45
DBREF 4TNJ h 1 66 UNP Q8DJ43 PSBH_THEEB 1 66
DBREF 4TNJ i 1 38 UNP Q8DJZ6 PSBI_THEEB 1 38
DBREF 4TNJ j 1 40 UNP P59087 PSBJ_THEEB 1 40
DBREF 4TNJ k 1 46 UNP Q9F1K9 PSBK_THEEB 1 46
DBREF 4TNJ l 1 37 UNP Q8DIN8 PSBL_THEEB 1 37
DBREF 4TNJ m 1 36 UNP Q8DHA7 PSBM_THEEB 1 36
DBREF 4TNJ o 1 272 UNP P0A431 PSBO_THEEB 1 272
DBREF 4TNJ t 1 32 UNP Q8DIQ0 PSBT_THEEB 1 32
DBREF 4TNJ u 1 134 UNP Q9F1L5 PSBU_THEEB 1 134
DBREF 4TNJ v 1 163 UNP P0A386 CY550_THEEB 1 163
DBREF 4TNJ g 1 46 UNP Q8DJI1 YCF12_THEEB 1 46
DBREF 4TNJ x 10 50 UNP Q9F1R6 PSBX_THEEB 1 41
DBREF 4TNJ G 1 28 PDB 4TNJ 4TNJ 1 28
DBREF 4TNJ 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 CLA A 405 65
HET PL9 A 406 45
HET BCR A 407 40
HET DGD A 408 56
HET LHG A 409 39
HET LMG A 410 51
HET CL A 411 1
HET OEX A 412 10
HET SQD A 413 51
HET SQD A 414 54
HET LMG A 415 42
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 LMT B 622 35
HET LMT B 623 35
HET LMG B 624 49
HET DGD B 625 52
HET SQD B 626 47
HET LMT B 627 35
HET LMT B 628 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 48
HET DGD D 409 63
HET LMT D 410 31
HET BCR D 411 40
HET LMG D 412 46
HET LMG E 101 44
HET HEM F 101 43
HET SQD F 102 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 CA K 101 1
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 FE2 a 403 1
HET CLA a 404 65
HET CLA a 405 65
HET CLA a 406 65
HET PHO a 407 64
HET CLA a 408 65
HET PL9 a 409 45
HET BCR a 410 40
HET DGD a 411 56
HET LHG a 412 39
HET LMG a 413 51
HET OEX a 414 10
HET SQD a 415 51
HET CL a 416 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 BCR b 620 40
HET BCR b 621 40
HET BCR b 622 40
HET BCR b 623 40
HET DGD b 624 58
HET LMG b 625 49
HET LMT b 626 35
HET LMT b 627 35
HET LMG b 628 49
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 SQD d 402 43
HET BCT d 403 4
HET CLA d 404 65
HET CLA d 405 65
HET PL9 d 406 55
HET LMG d 407 48
HET DGD d 408 63
HET LMT d 409 31
HET LMG d 410 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 LMG i 101 43
HET LMT i 102 35
HET PL9 j 101 35
HET BCR j 102 40
HET CA k 101 1
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 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 LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE
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 LMT DODECYL-BETA-D-MALTOSIDE
HETNAM PHO PHEOPHYTIN A
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)
FORMUL 46 PL9 6(C53 H80 O2)
FORMUL 47 BCR 24(C40 H56)
FORMUL 48 DGD 14(C51 H96 O15)
FORMUL 49 LHG 4(C38 H75 O10 P)
FORMUL 50 LMG 22(C45 H86 O10)
FORMUL 51 CL 2(CL 1-)
FORMUL 52 OEX 2(CA MN4 O5)
FORMUL 53 SQD 10(C41 H78 O12 S)
FORMUL 77 LMT 14(C24 H46 O11)
FORMUL 06 PHO 4(C55 H74 N4 O5)
FORMUL 09 BCT 2(C H O3 1-)
FORMUL 19 HEM 4(C34 H32 FE N4 O4)
FORMUL 27 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 TYR A 147 1 6
HELIX 8 AA8 TYR A 147 LEU A 159 1 13
HELIX 9 AA9 LEU A 159 GLY A 166 1 8
HELIX 10 AB1 SER A 167 GLY A 171 5 5
HELIX 11 AB2 ILE A 176 ASN A 191 1 16
HELIX 12 AB3 ILE A 192 MET A 194 5 3
HELIX 13 AB4 HIS A 195 SER A 222 1 28
HELIX 14 AB5 SER A 232 TYR A 237 5 6
HELIX 15 AB6 ASN A 247 ILE A 259 1 13
HELIX 16 AB7 PHE A 260 SER A 264 5 5
HELIX 17 AB8 ASN A 267 MET A 293 1 27
HELIX 18 AB9 THR A 316 HIS A 332 1 17
HELIX 19 AC1 GLU A 333 HIS A 337 5 5
HELIX 20 AC2 PRO B 4 ILE B 13 5 10
HELIX 21 AC3 ASP B 15 ALA B 43 1 29
HELIX 22 AC4 PRO B 54 GLN B 58 5 5
HELIX 23 AC5 VAL B 62 ARG B 68 1 7
HELIX 24 AC6 SER B 92 TYR B 117 1 26
HELIX 25 AC7 LEU B 120 ARG B 124 5 5
HELIX 26 AC8 ASP B 134 PHE B 156 1 23
HELIX 27 AC9 GLY B 186 ASN B 191 5 6
HELIX 28 AD1 ASN B 194 VAL B 219 1 26
HELIX 29 AD2 PRO B 222 LEU B 229 1 8
HELIX 30 AD3 ASN B 233 GLU B 235 5 3
HELIX 31 AD4 THR B 236 TYR B 258 1 23
HELIX 32 AD5 PRO B 264 GLY B 269 1 6
HELIX 33 AD6 THR B 271 SER B 277 1 7
HELIX 34 AD7 SER B 278 SER B 294 1 17
HELIX 35 AD8 THR B 297 ILE B 305 1 9
HELIX 36 AD9 PRO B 306 TYR B 312 1 7
HELIX 37 AE1 ASP B 313 ASN B 318 5 6
HELIX 38 AE2 PRO B 329 GLY B 333 5 5
HELIX 39 AE3 ARG B 384 SER B 388 5 5
HELIX 40 AE4 SER B 391 GLY B 396 1 6
HELIX 41 AE5 ASP B 413 ILE B 425 1 13
HELIX 42 AE6 SER B 446 PHE B 475 1 30
HELIX 43 AE7 ALA C 34 ILE C 43 5 10
HELIX 44 AE8 LEU C 45 PHE C 75 1 31
HELIX 45 AE9 PRO C 80 GLN C 84 5 5
HELIX 46 AF1 LEU C 88 LEU C 95 1 8
HELIX 47 AF2 GLY C 100 GLU C 104 5 5
HELIX 48 AF3 THR C 108 ARG C 135 1 28
HELIX 49 AF4 ASP C 153 PHE C 181 1 29
HELIX 50 AF5 ASP C 205 PHE C 210 1 6
HELIX 51 AF6 GLY C 211 LYS C 215 5 5
HELIX 52 AF7 GLY C 222 VAL C 227 5 6
HELIX 53 AF8 ASN C 229 LEU C 253 1 25
HELIX 54 AF9 GLY C 258 PHE C 264 1 7
HELIX 55 AG1 SER C 267 ASN C 293 1 27
HELIX 56 AG2 THR C 305 LEU C 324 1 20
HELIX 57 AG3 ASN C 327 ALA C 331 5 5
HELIX 58 AG4 GLY C 353 TRP C 359 5 7
HELIX 59 AG5 LEU C 366 PRO C 368 5 3
HELIX 60 AG6 ASP C 376 ASP C 383 1 8
HELIX 61 AG7 GLN C 385 THR C 397 1 13
HELIX 62 AG8 SER C 421 GLY C 454 1 34
HELIX 63 AG9 GLU C 464 MET C 469 5 6
HELIX 64 AH1 TRP D 14 LYS D 23 1 10
HELIX 65 AH2 VAL D 30 PHE D 54 1 25
HELIX 66 AH3 SER D 57 GLY D 62 1 6
HELIX 67 AH4 SER D 66 GLY D 70 5 5
HELIX 68 AH5 ASP D 100 LEU D 107 1 8
HELIX 69 AH6 GLY D 108 GLY D 137 1 30
HELIX 70 AH7 PRO D 140 PHE D 146 1 7
HELIX 71 AH8 PHE D 146 LEU D 158 1 13
HELIX 72 AH9 LEU D 158 GLN D 164 1 7
HELIX 73 AI1 SER D 166 ALA D 170 5 5
HELIX 74 AI2 VAL D 175 ASN D 190 1 16
HELIX 75 AI3 TRP D 191 LEU D 193 5 3
HELIX 76 AI4 ASN D 194 ASN D 220 1 27
HELIX 77 AI5 SER D 245 PHE D 257 1 13
HELIX 78 AI6 ASN D 263 LEU D 291 1 29
HELIX 79 AI7 PHE D 298 ASP D 308 1 11
HELIX 80 AI8 THR D 313 GLN D 334 1 22
HELIX 81 AI9 PRO D 335 ASN D 338 5 4
HELIX 82 AJ1 PRO D 342 LEU D 346 5 5
HELIX 83 AJ2 PRO E 9 SER E 16 1 8
HELIX 84 AJ3 SER E 16 THR E 40 1 25
HELIX 85 AJ4 GLY E 41 PHE E 47 1 7
HELIX 86 AJ5 GLU E 71 GLN E 82 1 12
HELIX 87 AJ6 THR F 17 GLN F 41 1 25
HELIX 88 AJ7 THR H 5 LEU H 11 1 7
HELIX 89 AJ8 THR H 27 ASN H 50 1 24
HELIX 90 AJ9 GLU I 2 SER I 25 1 24
HELIX 91 AK1 PRO J 9 ALA J 32 1 24
HELIX 92 AK2 ALA K 14 ILE K 17 5 4
HELIX 93 AK3 PHE K 18 ASP K 23 1 6
HELIX 94 AK4 VAL K 24 PRO K 26 5 3
HELIX 95 AK5 VAL K 27 VAL K 43 1 17
HELIX 96 AK6 ASN L 13 ASN L 37 1 25
HELIX 97 AK7 LEU M 6 SER M 31 1 26
HELIX 98 AK8 GLY O 40 LYS O 44 5 5
HELIX 99 AK9 LEU O 208 VAL O 213 1 6
HELIX 100 AL1 GLU T 2 PHE T 23 1 22
HELIX 101 AL2 ASN U 41 LEU U 47 1 7
HELIX 102 AL3 ASN U 61 TYR U 68 5 8
HELIX 103 AL4 PRO U 73 ASN U 82 1 10
HELIX 104 AL5 SER U 87 ILE U 94 5 8
HELIX 105 AL6 THR U 98 LEU U 109 1 12
HELIX 106 AL7 GLU U 118 GLU U 123 1 6
HELIX 107 AL8 GLY U 124 ASP U 126 5 3
HELIX 108 AL9 THR V 48 CYS V 63 1 16
HELIX 109 AM1 CYS V 63 VAL V 68 1 6
HELIX 110 AM2 GLY V 69 ILE V 71 5 3
HELIX 111 AM3 ARG V 81 LEU V 87 1 7
HELIX 112 AM4 ASN V 94 MET V 102 1 9
HELIX 113 AM5 SER V 120 ALA V 124 5 5
HELIX 114 AM6 PRO V 128 LEU V 133 1 6
HELIX 115 AM7 THR V 134 GLY V 153 1 20
HELIX 116 AM8 GLY V 153 GLY V 158 1 6
HELIX 117 AM9 GLY V 159 TYR V 163 5 5
HELIX 118 AN1 GLN y 21 ARG y 42 1 22
HELIX 119 AN2 THR X 13 GLN X 42 1 30
HELIX 120 AN3 UNK Y 2 UNK Y 13 1 12
HELIX 121 AN4 UNK Y 14 UNK Y 25 1 12
HELIX 122 AN5 THR Z 2 SER Z 29 1 28
HELIX 123 AN6 ARG Z 35 VAL Z 62 1 28
HELIX 124 AN7 ASN a 12 THR a 22 1 11
HELIX 125 AN8 PHE a 33 ALA a 55 1 23
HELIX 126 AN9 SER a 70 GLY a 74 5 5
HELIX 127 AO1 PRO a 95 ALA a 99 5 5
HELIX 128 AO2 SER a 101 ASN a 108 1 8
HELIX 129 AO3 GLY a 109 LEU a 137 1 29
HELIX 130 AO4 TRP a 142 TYR a 147 1 6
HELIX 131 AO5 TYR a 147 LEU a 159 1 13
HELIX 132 AO6 LEU a 159 GLY a 166 1 8
HELIX 133 AO7 SER a 167 GLY a 171 5 5
HELIX 134 AO8 ILE a 176 ASN a 191 1 16
HELIX 135 AO9 ILE a 192 MET a 194 5 3
HELIX 136 AP1 HIS a 195 SER a 222 1 28
HELIX 137 AP2 SER a 232 TYR a 237 5 6
HELIX 138 AP3 ASN a 247 ILE a 259 1 13
HELIX 139 AP4 PHE a 260 SER a 264 5 5
HELIX 140 AP5 ASN a 267 MET a 293 1 27
HELIX 141 AP6 THR a 316 HIS a 332 1 17
HELIX 142 AP7 GLU a 333 HIS a 337 5 5
HELIX 143 AP8 PRO b 4 ILE b 13 5 10
HELIX 144 AP9 ASP b 15 ALA b 43 1 29
HELIX 145 AQ1 PRO b 54 GLN b 58 5 5
HELIX 146 AQ2 VAL b 62 ARG b 68 1 7
HELIX 147 AQ3 SER b 92 TYR b 117 1 26
HELIX 148 AQ4 LEU b 120 ARG b 124 5 5
HELIX 149 AQ5 ASP b 134 PHE b 156 1 23
HELIX 150 AQ6 GLY b 186 ASN b 191 5 6
HELIX 151 AQ7 ASN b 194 VAL b 219 1 26
HELIX 152 AQ8 PRO b 222 LEU b 229 1 8
HELIX 153 AQ9 ASN b 233 GLU b 235 5 3
HELIX 154 AR1 THR b 236 TYR b 258 1 23
HELIX 155 AR2 PRO b 264 GLY b 269 1 6
HELIX 156 AR3 THR b 271 SER b 277 1 7
HELIX 157 AR4 SER b 278 SER b 294 1 17
HELIX 158 AR5 THR b 297 ILE b 305 1 9
HELIX 159 AR6 PRO b 306 TYR b 312 1 7
HELIX 160 AR7 ASP b 313 ASN b 318 5 6
HELIX 161 AR8 PRO b 329 GLY b 333 5 5
HELIX 162 AR9 ARG b 384 SER b 388 5 5
HELIX 163 AS1 SER b 391 GLY b 396 1 6
HELIX 164 AS2 ASP b 413 ILE b 425 1 13
HELIX 165 AS3 SER b 446 PHE b 475 1 30
HELIX 166 AS4 ALA c 34 ILE c 43 5 10
HELIX 167 AS5 LEU c 45 PHE c 75 1 31
HELIX 168 AS6 PRO c 80 GLN c 84 5 5
HELIX 169 AS7 LEU c 88 LEU c 95 1 8
HELIX 170 AS8 GLY c 100 GLU c 104 5 5
HELIX 171 AS9 THR c 108 ARG c 135 1 28
HELIX 172 AT1 ASP c 153 PHE c 181 1 29
HELIX 173 AT2 ASP c 205 PHE c 210 1 6
HELIX 174 AT3 GLY c 211 LYS c 215 5 5
HELIX 175 AT4 GLY c 222 VAL c 227 5 6
HELIX 176 AT5 ASN c 229 LEU c 253 1 25
HELIX 177 AT6 GLY c 258 PHE c 264 1 7
HELIX 178 AT7 SER c 267 ASN c 293 1 27
HELIX 179 AT8 THR c 305 LEU c 324 1 20
HELIX 180 AT9 ASN c 327 ALA c 331 5 5
HELIX 181 AU1 GLY c 353 TRP c 359 5 7
HELIX 182 AU2 LEU c 366 PRO c 368 5 3
HELIX 183 AU3 ASP c 376 ASP c 383 1 8
HELIX 184 AU4 GLN c 385 THR c 397 1 13
HELIX 185 AU5 SER c 421 GLY c 454 1 34
HELIX 186 AU6 GLU c 464 MET c 469 5 6
HELIX 187 AU7 TRP d 14 LYS d 23 1 10
HELIX 188 AU8 VAL d 30 PHE d 54 1 25
HELIX 189 AU9 SER d 57 GLY d 62 1 6
HELIX 190 AV1 SER d 66 GLY d 70 5 5
HELIX 191 AV2 ASP d 100 LEU d 107 1 8
HELIX 192 AV3 GLY d 108 GLY d 137 1 30
HELIX 193 AV4 PRO d 140 PHE d 146 1 7
HELIX 194 AV5 PHE d 146 LEU d 158 1 13
HELIX 195 AV6 LEU d 158 GLN d 164 1 7
HELIX 196 AV7 SER d 166 ALA d 170 5 5
HELIX 197 AV8 VAL d 175 ASN d 190 1 16
HELIX 198 AV9 TRP d 191 LEU d 193 5 3
HELIX 199 AW1 ASN d 194 ASN d 220 1 27
HELIX 200 AW2 SER d 245 PHE d 257 1 13
HELIX 201 AW3 ASN d 263 LEU d 291 1 29
HELIX 202 AW4 PHE d 298 ASP d 308 1 11
HELIX 203 AW5 THR d 313 GLN d 334 1 22
HELIX 204 AW6 PRO d 335 ASN d 338 5 4
HELIX 205 AW7 PRO d 342 LEU d 346 5 5
HELIX 206 AW8 PRO e 9 SER e 16 1 8
HELIX 207 AW9 SER e 16 THR e 40 1 25
HELIX 208 AX1 GLY e 41 PHE e 47 1 7
HELIX 209 AX2 GLU e 71 GLN e 82 1 12
HELIX 210 AX3 THR f 17 GLN f 41 1 25
HELIX 211 AX4 THR h 5 LEU h 11 1 7
HELIX 212 AX5 THR h 27 ASN h 50 1 24
HELIX 213 AX6 GLU i 2 SER i 25 1 24
HELIX 214 AX7 PRO j 9 ALA j 32 1 24
HELIX 215 AX8 ALA k 14 ILE k 17 5 4
HELIX 216 AX9 PHE k 18 ASP k 23 1 6
HELIX 217 AY1 VAL k 24 PRO k 26 5 3
HELIX 218 AY2 VAL k 27 VAL k 43 1 17
HELIX 219 AY3 ASN l 13 ASN l 37 1 25
HELIX 220 AY4 LEU m 6 SER m 31 1 26
HELIX 221 AY5 GLY o 40 LYS o 44 5 5
HELIX 222 AY6 LEU o 208 VAL o 213 1 6
HELIX 223 AY7 GLU t 2 PHE t 23 1 22
HELIX 224 AY8 ASN u 41 LEU u 47 1 7
HELIX 225 AY9 ASN u 61 TYR u 68 5 8
HELIX 226 AZ1 PRO u 73 ASN u 82 1 10
HELIX 227 AZ2 SER u 87 ILE u 94 5 8
HELIX 228 AZ3 THR u 98 LEU u 109 1 12
HELIX 229 AZ4 GLU u 118 GLU u 123 1 6
HELIX 230 AZ5 GLY u 124 ASP u 126 5 3
HELIX 231 AZ6 THR v 48 CYS v 63 1 16
HELIX 232 AZ7 CYS v 63 VAL v 68 1 6
HELIX 233 AZ8 GLY v 69 ILE v 71 5 3
HELIX 234 AZ9 ARG v 81 LEU v 87 1 7
HELIX 235 BA1 ASN v 94 MET v 102 1 9
HELIX 236 BA2 SER v 120 ALA v 124 5 5
HELIX 237 BA3 PRO v 128 LEU v 133 1 6
HELIX 238 BA4 THR v 134 GLY v 153 1 20
HELIX 239 BA5 GLY v 153 GLY v 158 1 6
HELIX 240 BA6 GLY v 159 TYR v 163 5 5
HELIX 241 BA7 GLN g 21 ARG g 42 1 22
HELIX 242 BA8 THR x 13 GLN x 42 1 30
HELIX 243 BA9 UNK G 2 UNK G 12 1 11
HELIX 244 BB1 UNK G 14 UNK G 25 1 12
HELIX 245 BB2 THR z 2 SER z 29 1 28
HELIX 246 BB3 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 LYS O 260 N LEU O 77
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 THR b 398 N ARG b 347
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 ALA o 228 O ALA o 238
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 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 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 OD1 ASP A 170 CA1 OEX A 412 1555 1555 3.20
LINK OD2 ASP A 170 MN4 OEX A 412 1555 1555 2.75
LINK OE1 GLU A 189 CA1 OEX A 412 1555 1555 3.08
LINK OE2 GLU A 189 MN1 OEX A 412 1555 1555 2.48
LINK NE2 HIS A 215 FE FE2 A 401 1555 1555 2.53
LINK NE2 HIS A 272 FE FE2 A 401 1555 1555 2.54
LINK NE2 HIS A 332 MN1 OEX A 412 1555 1555 2.54
LINK OE1 GLU A 333 MN3 OEX A 412 1555 1555 2.51
LINK OE2 GLU A 333 MN4 OEX A 412 1555 1555 2.73
LINK OD1 ASP A 342 MN2 OEX A 412 1555 1555 2.60
LINK OD2 ASP A 342 MN1 OEX A 412 1555 1555 2.78
LINK OXT ALA A 344 MN2 OEX A 412 1555 1555 2.58
LINK FE FE2 A 401 NE2 HIS D 214 1555 1555 2.51
LINK FE FE2 A 401 NE2 HIS D 268 1555 1555 2.67
LINK FE FE2 A 401 O3 BCT D 404 1555 1555 2.67
LINK FE FE2 A 401 O2 BCT D 404 1555 1555 2.68
LINK MN3 OEX A 412 OE2 GLU C 354 1555 1555 2.70
LINK OD1 ASN C 39 MG CLA C 510 1555 1555 2.88
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 2.59
LINK OD1 ASP K 23 CA CA K 101 1555 1555 2.88
LINK OD2 ASP K 23 CA CA K 101 1555 1555 2.67
LINK OE1 GLU O 140 CA CA O 301 1555 1555 2.60
LINK NE2 HIS V 67 FE HEM V 201 1555 1555 2.50
LINK NE2 HIS V 118 FE HEM V 201 1555 1555 2.58
LINK OD1 ASP a 170 CA1 OEX a 414 1555 1555 3.00
LINK OD2 ASP a 170 MN4 OEX a 414 1555 1555 2.74
LINK OE1 GLU a 189 CA1 OEX a 414 1555 1555 3.06
LINK OE2 GLU a 189 MN1 OEX a 414 1555 1555 2.52
LINK NE2 HIS a 215 FE FE2 a 403 1555 1555 2.58
LINK NE2 HIS a 272 FE FE2 a 403 1555 1555 2.57
LINK NE2 HIS a 332 MN1 OEX a 414 1555 1555 2.53
LINK OE1 GLU a 333 MN3 OEX a 414 1555 1555 2.53
LINK OE2 GLU a 333 MN4 OEX a 414 1555 1555 2.79
LINK OD1 ASP a 342 MN2 OEX a 414 1555 1555 2.59
LINK OD2 ASP a 342 MN1 OEX a 414 1555 1555 2.79
LINK OXT ALA a 344 MN2 OEX a 414 1555 1555 2.59
LINK FE FE2 a 403 NE2 HIS d 214 1555 1555 2.55
LINK FE FE2 a 403 NE2 HIS d 268 1555 1555 2.68
LINK FE FE2 a 403 O2 BCT d 403 1555 1555 2.65
LINK FE FE2 a 403 O3 BCT d 403 1555 1555 2.67
LINK MN2 OEX a 414 OE1 GLU c 354 1555 1555 2.72
LINK MN3 OEX a 414 OE2 GLU c 354 1555 1555 2.65
LINK OD1 ASN c 39 MG CLA c 510 1555 1555 2.94
LINK NE2 HIS e 23 FE HEM f 101 1555 1555 2.60
LINK NE2 HIS f 24 FE HEM f 101 1555 1555 2.64
LINK OD2 ASP k 19 CA CA k 101 1555 1555 2.56
LINK OD1 ASP k 23 CA CA k 101 1555 1555 3.17
LINK OD2 ASP k 23 CA CA k 101 1555 1555 2.99
LINK OE1 GLU o 140 CA CA o 301 1555 1555 2.57
LINK NE2 HIS v 67 FE HEM v 201 1555 1555 2.53
LINK NE2 HIS v 118 FE HEM v 201 1555 1555 2.62
CISPEP 1 THR V 89 PRO V 90 0 -0.74
CISPEP 2 THR v 89 PRO v 90 0 -0.81
SITE 1 AC1 5 HIS A 215 HIS A 272 HIS D 214 HIS D 268
SITE 2 AC1 5 BCT D 404
SITE 1 AC2 23 PHE A 119 TYR A 147 PRO A 150 SER A 153
SITE 2 AC2 23 VAL A 157 MET A 183 PHE A 186 GLN A 187
SITE 3 AC2 23 LEU A 193 HIS A 198 GLY A 201 VAL A 205
SITE 4 AC2 23 PHE A 206 VAL A 283 THR A 286 ILE A 290
SITE 5 AC2 23 CLA A 403 CLA A 404 LEU D 182 LEU D 205
SITE 6 AC2 23 PHO D 401 CLA D 405 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 MET D 198 VAL D 201 ALA D 202 PHO D 401
SITE 4 AC3 14 CLA D 405 PL9 D 407
SITE 1 AC4 15 GLN A 199 VAL A 202 ALA A 203 LEU A 210
SITE 2 AC4 15 TRP A 278 CLA A 402 PL9 A 406 PHE D 157
SITE 3 AC4 15 VAL D 175 ILE D 178 PHE D 179 PHE D 181
SITE 4 AC4 15 LEU D 182 PHO D 402 CLA D 405
SITE 1 AC5 14 ILE A 36 PRO A 39 THR A 40 PHE A 93
SITE 2 AC5 14 PRO A 95 ILE A 96 TRP A 97 LEU A 114
SITE 3 AC5 14 HIS A 118 LEU A 121 BCR A 407 DGD A 408
SITE 4 AC5 14 TYR I 9 PHE I 15
SITE 1 AC6 15 HIS A 215 LEU A 218 HIS A 252 PHE A 255
SITE 2 AC6 15 SER A 264 PHE A 265 LEU A 271 PHE A 274
SITE 3 AC6 15 CLA A 404 PHE D 38 ALA D 41 TYR D 42
SITE 4 AC6 15 ALA F 22 THR F 25 PL9 J 101
SITE 1 AC7 8 ILE A 38 LEU A 42 ALA A 43 TRP A 105
SITE 2 AC7 8 CLA A 405 SQD A 414 PHE I 15 LMT b 603
SITE 1 AC8 13 PHE A 93 TRP A 97 GLU A 98 CLA A 405
SITE 2 AC8 13 LEU C 214 LYS C 215 SER C 216 PRO C 217
SITE 3 AC8 13 TRP C 223 PHE C 284 LYS I 5 TYR I 9
SITE 4 AC8 13 GLY O 38
SITE 1 AC9 14 ARG A 140 TRP A 142 PHE A 273 SQD A 413
SITE 2 AC9 14 TRP C 36 TRP C 443 ARG C 447 CLA C 507
SITE 3 AC9 14 CLA C 520 ASN D 220 ALA D 229 SER D 230
SITE 4 AC9 14 THR D 231 PHE D 232
SITE 1 AD1 12 SER A 232 ASN A 234 TRP B 5 TYR B 6
SITE 2 AD1 12 LMG B 624 TRP D 266 PHE D 269 PHE D 273
SITE 3 AD1 12 PL9 D 407 GLU L 11 ASN L 13 SER L 16
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 14 ASN A 267 SER A 270 PHE A 273 PHE A 274
SITE 2 AD4 14 TRP A 278 LHG A 409 TRP C 36 DGD C 516
SITE 3 AD4 14 DGD C 517 LHG C 519 PHE D 232 ARG D 233
SITE 4 AD4 14 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 VAL A 30 THR A 45 BCR A 407 PHO D 401
SITE 3 AD5 13 TRP b 113 TYR b 117 CLA b 609 CLA b 619
SITE 4 AD5 13 BCR b 623
SITE 1 AD6 9 LEU A 72 LEU A 102 ASP A 103 ARG D 304
SITE 2 AD6 9 GLY O 138 ALA b 43 TRP b 75 SER b 76
SITE 3 AD6 9 LEU b 98
SITE 1 AD7 9 TRP B 185 PRO B 187 PHE B 190 ILE B 207
SITE 2 AD7 9 VAL B 208 PHE H 41 ILE H 44 CLA H 101
SITE 3 AD7 9 BCR H 102
SITE 1 AD8 20 ARG B 68 LEU B 69 ALA B 146 LEU B 149
SITE 2 AD8 20 CYS B 150 PHE B 153 VAL B 198 HIS B 201
SITE 3 AD8 20 HIS B 202 PHE B 247 ALA B 248 VAL B 252
SITE 4 AD8 20 THR B 262 CLA B 603 CLA B 604 CLA B 605
SITE 5 AD8 20 CLA B 608 PHE H 38 LEU H 42 CLA H 101
SITE 1 AD9 20 TRP B 33 PHE B 61 PHE B 65 ARG B 68
SITE 2 AD9 20 VAL B 245 ALA B 248 ALA B 249 VAL B 252
SITE 3 AD9 20 PHE B 451 HIS B 455 PHE B 458 ALA B 459
SITE 4 AD9 20 PHE B 462 CLA B 602 CLA B 604 CLA B 606
SITE 5 AD9 20 CLA B 610 CLA B 611 CLA B 612 CLA B 614
SITE 1 AE1 18 THR B 27 VAL B 30 ALA B 31 TRP B 33
SITE 2 AE1 18 ALA B 34 VAL B 62 PHE B 65 MET B 66
SITE 3 AE1 18 ARG B 68 LEU B 69 HIS B 100 LEU B 103
SITE 4 AE1 18 ALA B 205 CLA B 602 CLA B 603 CLA B 605
SITE 5 AE1 18 CLA B 609 CLA B 611
SITE 1 AE2 17 LEU B 69 TRP B 91 ALA B 99 LEU B 103
SITE 2 AE2 17 LEU B 106 GLY B 152 PHE B 153 PHE B 156
SITE 3 AE2 17 HIS B 157 PHE B 162 PRO B 164 CLA B 602
SITE 4 AE2 17 CLA B 604 CLA B 615 BCR B 619 LMT B 622
SITE 5 AE2 17 SQD a 401
SITE 1 AE3 20 TRP B 33 MET B 37 TYR B 40 GLN B 58
SITE 2 AE3 20 GLY B 59 PHE B 61 THR B 327 GLY B 328
SITE 3 AE3 20 PRO B 329 TRP B 450 ALA B 454 CLA B 603
SITE 4 AE3 20 BCR B 616 BCR B 617 BCR B 618 LMG B 621
SITE 5 AE3 20 LMG B 624 MET D 281 LEU L 27 PHE M 14
SITE 1 AE4 17 THR B 236 SER B 239 ALA B 243 PHE B 246
SITE 2 AE4 17 PHE B 247 PHE B 463 HIS B 466 LEU B 474
SITE 3 AE4 17 CLA B 608 CLA B 609 PHE D 120 ILE D 123
SITE 4 AE4 17 MET D 126 LEU D 127 PHE D 130 SQD D 403
SITE 5 AE4 17 LEU H 43
SITE 1 AE5 16 PHE B 139 ALA B 212 PHE B 215 HIS B 216
SITE 2 AE5 16 PRO B 221 PRO B 222 LEU B 229 CLA B 602
SITE 3 AE5 16 CLA B 607 CLA B 609 THR H 27 THR H 28
SITE 4 AE5 16 MET H 31 PHE H 34 MET H 35 BCR H 102
SITE 1 AE6 12 PHE B 139 HIS B 142 LEU B 143 ALA B 146
SITE 2 AE6 12 VAL B 237 SER B 240 CLA B 604 CLA B 607
SITE 3 AE6 12 CLA B 608 CLA B 611 CLA B 614 BCR H 102
SITE 1 AE7 17 TRP B 5 TYR B 6 ARG B 7 VAL B 8
SITE 2 AE7 17 HIS B 9 ILE B 242 LEU B 461 PHE B 462
SITE 3 AE7 17 GLY B 465 TRP B 468 HIS B 469 ARG B 472
SITE 4 AE7 17 CLA B 603 CLA B 611 CLA B 612 CLA B 613
SITE 5 AE7 17 LMG B 624
SITE 1 AE8 17 HIS B 9 LEU B 19 HIS B 23 HIS B 26
SITE 2 AE8 17 THR B 27 ILE B 234 VAL B 237 LEU B 238
SITE 3 AE8 17 SER B 241 VAL B 245 CLA B 603 CLA B 604
SITE 4 AE8 17 CLA B 609 CLA B 610 CLA B 612 CLA B 613
SITE 5 AE8 17 CLA B 614
SITE 1 AE9 10 HIS B 9 HIS B 26 VAL B 30 PHE B 462
SITE 2 AE9 10 CLA B 603 CLA B 610 CLA B 611 CLA B 613
SITE 3 AE9 10 BCR B 618 LMG B 624
SITE 1 AF1 14 VAL B 8 HIS B 9 VAL B 11 LEU B 12
SITE 2 AF1 14 LEU B 29 TRP B 115 CLA B 610 CLA B 611
SITE 3 AF1 14 CLA B 612 BCR B 616 SQD B 626 VAL L 10
SITE 4 AF1 14 LMG m 101 PHE t 8
SITE 1 AF2 12 HIS B 23 MET B 138 ILE B 141 HIS B 142
SITE 2 AF2 12 LEU B 145 CLA B 603 CLA B 609 CLA B 611
SITE 3 AF2 12 CLA B 615 BCR B 619 LEU H 14 ASN H 15
SITE 1 AF3 9 LEU B 24 ALA B 110 TRP B 113 HIS B 114
SITE 2 AF3 9 CLA B 605 CLA B 614 THR H 5 LEU H 7
SITE 3 AF3 9 SQD a 401
SITE 1 AF4 10 MET B 25 LEU B 29 TRP B 115 CLA B 606
SITE 2 AF4 10 CLA B 613 BCR B 617 BCR B 618 SQD B 626
SITE 3 AF4 10 LEU M 13 PHE t 19
SITE 1 AF5 12 TRP B 33 SER B 36 MET B 37 CLA B 606
SITE 2 AF5 12 BCR B 616 BCR B 618 LMT B 628 ILE t 4
SITE 3 AF5 12 PHE t 8 ALA t 11 PHE t 17 ILE t 21
SITE 1 AF6 9 LEU B 29 GLY B 32 TRP B 33 GLY B 105
SITE 2 AF6 9 CLA B 606 CLA B 612 BCR B 616 BCR B 617
SITE 3 AF6 9 DGD B 625
SITE 1 AF7 8 LEU B 109 CYS B 112 TYR B 117 CLA B 605
SITE 2 AF7 8 CLA B 614 SQD a 401 PHE t 18 PHE t 22
SITE 1 AF8 13 TYR B 193 PHE B 250 TYR B 258 TYR B 273
SITE 2 AF8 13 SER B 277 HIS D 87 LEU D 162 TYR H 49
SITE 3 AF8 13 ASN H 50 VAL H 60 SER H 61 TRP H 62
SITE 4 AF8 13 CLA H 101
SITE 1 AF9 10 THR B 327 GLY B 328 PRO B 329 LYS B 332
SITE 2 AF9 10 CLA B 606 ILE D 284 PHE L 35 ASN M 4
SITE 3 AF9 10 LEU M 6 LMT M 103
SITE 1 AG1 4 TRP B 91 PHE B 162 CLA B 605 DGD B 625
SITE 1 AG2 7 ARG B 224 LYS B 227 ASP D 16 ASP D 19
SITE 2 AG2 7 SQD D 403 ALA H 32 MET H 35
SITE 1 AG3 14 ASN A 234 LMG A 410 TRP B 5 TYR B 6
SITE 2 AG3 14 ARG B 7 PHE B 464 TRP B 468 CLA B 606
SITE 3 AG3 14 CLA B 610 CLA B 612 ARG D 139 TYR D 141
SITE 4 AG3 14 PHE D 269 PHE D 273
SITE 1 AG4 9 TRP B 75 ASP B 87 GLY B 89 PHE B 90
SITE 2 AG4 9 BCR B 618 LMT B 622 LMT B 627 ILE a 46
SITE 3 AG4 9 LMG i 101
SITE 1 AG5 13 ARG B 18 LEU B 29 SER B 104 PHE B 108
SITE 2 AG5 13 TRP B 115 CLA B 613 BCR B 616 ASN L 4
SITE 3 AG5 13 ARG l 14 TYR l 18 TYR m 26 PHE t 19
SITE 4 AG5 13 PHE t 23
SITE 1 AG6 8 GLY B 85 ASP B 87 DGD B 625 ALA a 100
SITE 2 AG6 8 BCR a 410 MET i 1 LMG i 101 LYS o 95
SITE 1 AG7 4 ALA B 43 LEU B 437 BCR B 617 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 PHE C 289 VAL C 296
SITE 4 AG8 17 TYR C 297 CLA C 502 CLA C 503 CLA C 506
SITE 5 AG8 17 BCR C 514
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 518
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 514 PHE I 23
SITE 1 AH3 13 LEU C 165 LEU C 213 ILE C 243 GLY C 247
SITE 2 AH3 13 TRP C 250 HIS C 251 THR C 255 PRO C 256
SITE 3 AH3 13 PHE C 257 TRP C 259 ALA C 260 PHE C 264
SITE 4 AH3 13 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 514
SITE 1 AH5 18 LHG A 409 TRP C 36 ALA C 37 ASN C 39
SITE 2 AH5 18 ALA C 40 GLU C 269 LEU C 276 PHE C 436
SITE 3 AH5 18 PHE C 437 GLY C 440 TRP C 443 HIS C 444
SITE 4 AH5 18 ARG C 447 CLA C 508 CLA C 509 DGD C 516
SITE 5 AH5 18 CLA C 520 VAL K 30
SITE 1 AH6 18 ASN C 39 LEU C 42 LEU C 49 ALA C 52
SITE 2 AH6 18 HIS C 53 HIS C 56 TYR C 149 GLY C 268
SITE 3 AH6 18 TYR C 271 LEU C 272 SER C 275 LEU C 279
SITE 4 AH6 18 CLA C 502 CLA C 506 CLA C 507 CLA C 509
SITE 5 AH6 18 CLA C 510 CLA C 511
SITE 1 AH7 15 ASN C 39 HIS C 56 LEU C 59 LEU C 279
SITE 2 AH7 15 PHE C 436 PHE C 437 CLA C 502 CLA C 503
SITE 3 AH7 15 CLA C 507 CLA C 508 CLA C 510 CLA C 520
SITE 4 AH7 15 PRO K 29 VAL K 30 LEU K 33
SITE 1 AH8 21 GLN C 28 TRP C 35 GLY C 38 ASN C 39
SITE 2 AH8 21 ARG C 41 LEU C 42 LYS C 48 ALA C 52
SITE 3 AH8 21 PHE C 127 ILE C 134 CLA C 508 CLA C 509
SITE 4 AH8 21 BCR C 513 PHE K 32 TRP K 39 GLN K 40
SITE 5 AH8 21 MET Z 19 VAL Z 20 PRO Z 24 ILE y 35
SITE 6 AH8 21 LEU y 46
SITE 1 AH9 12 HIS C 53 ALA C 57 PHE C 147 PHE C 163
SITE 2 AH9 12 HIS C 164 VAL C 167 ILE C 170 LEU C 174
SITE 3 AH9 12 CLA C 503 CLA C 508 CLA C 512 BCR C 521
SITE 1 AI1 9 LEU C 50 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 521
SITE 1 AI2 11 ALA C 55 LEU C 59 VAL C 116 LEU C 119
SITE 2 AI2 11 SER C 122 ALA C 123 CLA C 510 BCR C 521
SITE 3 AI2 11 PHE K 32 VAL Z 13 BCR y 101
SITE 1 AI3 11 ILE C 209 TYR C 212 LEU C 213 VAL C 227
SITE 2 AI3 11 ASP C 232 VAL C 233 ILE C 240 PHE C 264
SITE 3 AI3 11 CLA C 501 CLA C 504 CLA C 506
SITE 1 AI4 16 LEU A 91 PHE A 155 ILE A 163 PRO C 217
SITE 2 AI4 16 PHE C 218 GLY C 219 GLY C 220 VAL C 225
SITE 3 AI4 16 SER C 226 PHE C 284 CYS C 288 PHE C 292
SITE 4 AI4 16 ASN C 294 PRO C 307 PHE C 361 ARG C 362
SITE 1 AI5 20 PHE A 197 SQD A 413 TYR C 82 GLU C 83
SITE 2 AI5 20 GLN C 84 GLY C 85 LEU C 404 SER C 406
SITE 3 AI5 20 ASN C 418 PHE C 419 VAL C 420 TRP C 425
SITE 4 AI5 20 SER C 429 CLA C 507 DGD C 517 LHG C 519
SITE 5 AI5 20 CLA C 520 LMG C 522 TYR J 33 BCR J 102
SITE 1 AI6 20 LEU A 200 TRP A 278 PHE A 300 ASN A 301
SITE 2 AI6 20 SER A 305 SQD A 413 ASN C 405 VAL C 407
SITE 3 AI6 20 ASN C 415 SER C 416 ASN C 418 DGD C 516
SITE 4 AI6 20 CLA C 520 PHE J 29 ALA J 32 TYR J 33
SITE 5 AI6 20 GLY J 37 SER J 38 SER J 39 GLN V 60
SITE 1 AI7 7 TRP C 97 PHE C 109 VAL C 113 VAL C 117
SITE 2 AI7 7 HIS C 118 CLA C 503 PHE Z 59
SITE 1 AI8 8 TYR A 262 ASN A 266 SQD A 413 TRP C 35
SITE 2 AI8 8 DGD C 516 LMG E 101 BCR J 102 PHE K 45
SITE 1 AI9 17 PHE A 285 LHG A 409 TRP C 63 MET C 67
SITE 2 AI9 17 PHE C 70 GLN C 84 GLY C 85 ILE C 87
SITE 3 AI9 17 TRP C 425 SER C 429 CLA C 507 CLA C 509
SITE 4 AI9 17 DGD C 516 DGD C 517 LMG C 522 PRO K 26
SITE 5 AI9 17 VAL K 30
SITE 1 AJ1 11 PHE C 112 VAL C 116 SER C 121 VAL C 124
SITE 2 AJ1 11 CLA C 511 CLA C 512 BCR C 513 TYR K 15
SITE 3 AJ1 11 VAL Z 54 GLY Z 55 ASN Z 58
SITE 1 AJ2 7 HIS C 74 DGD C 516 CLA C 520 BCR J 102
SITE 2 AJ2 7 ASP K 23 VAL K 27 ILE y 25
SITE 1 AJ3 19 LEU A 41 ALA A 44 THR A 45 ILE A 115
SITE 2 AJ3 19 TYR A 126 GLN A 130 ALA A 146 TYR A 147
SITE 3 AJ3 19 VAL A 283 CLA A 402 CLA A 403 SQD A 414
SITE 4 AJ3 19 LEU D 205 ALA D 208 LEU D 209 ALA D 212
SITE 5 AJ3 19 ILE D 213 TRP D 253 PHE D 257
SITE 1 AJ4 20 PHE A 206 ALA A 209 LEU A 210 MET A 214
SITE 2 AJ4 20 LEU A 258 CLA A 404 ALA D 41 LEU D 45
SITE 3 AJ4 20 TRP D 48 GLY D 118 LEU D 122 PHE D 125
SITE 4 AJ4 20 GLN D 129 ASN D 142 PHE D 146 PHE D 153
SITE 5 AJ4 20 PHE D 173 PRO D 275 LEU D 279 CLA D 405
SITE 1 AJ5 10 LYS B 227 ALA B 228 ARG B 230 LEU B 474
SITE 2 AJ5 10 CLA B 607 LMT B 623 LYS D 23 TRP D 32
SITE 3 AJ5 10 ARG D 134 LEU D 135
SITE 1 AJ6 8 HIS A 215 GLU A 244 TYR A 246 HIS A 272
SITE 2 AJ6 8 FE2 A 401 TYR D 244 LYS D 264 HIS D 268
SITE 1 AJ7 22 PHE A 206 CLA A 402 CLA A 403 CLA A 404
SITE 2 AJ7 22 LEU D 122 VAL D 152 PHE D 153 VAL D 156
SITE 3 AJ7 22 LEU D 182 PHE D 185 GLN D 186 TRP D 191
SITE 4 AJ7 22 THR D 192 HIS D 197 GLY D 200 VAL D 201
SITE 5 AJ7 22 VAL D 204 LEU D 279 SER D 282 ALA D 283
SITE 6 AJ7 22 VAL D 286 PHO D 402
SITE 1 AJ8 14 LEU D 43 LEU D 89 LEU D 90 LEU D 91
SITE 2 AJ8 14 LEU D 92 TRP D 93 THR D 112 PHE D 113
SITE 3 AJ8 14 HIS D 117 PHE D 120 LMT D 410 GLY X 22
SITE 4 AJ8 14 LEU X 23 GLY X 26
SITE 1 AJ9 18 PHE A 52 ILE A 77 CLA A 403 LMG A 410
SITE 2 AJ9 18 MET D 199 LEU D 209 HIS D 214 THR D 217
SITE 3 AJ9 18 TRP D 253 ALA D 260 PHE D 261 LEU D 267
SITE 4 AJ9 18 PHE D 270 PHE D 273 VAL D 274 LMG D 408
SITE 5 AJ9 18 VAL L 26 PHE T 10
SITE 1 AK1 13 PHE D 257 ILE D 259 ALA D 260 PHE D 261
SITE 2 AK1 13 SER D 262 ASN D 263 TRP D 266 PL9 D 407
SITE 3 AK1 13 THR L 15 TYR L 18 LEU L 19 PHE T 17
SITE 4 AK1 13 ALA T 20
SITE 1 AK2 6 ASP D 100 PHE D 101 THR D 102 LMT D 410
SITE 2 AK2 6 ASP E 45 VAL E 46
SITE 1 AK3 8 LEU D 92 TRP D 93 GLY D 99 CLA D 406
SITE 2 AK3 8 DGD D 409 ILE X 21 SER X 25 GLY X 26
SITE 1 AK4 11 TYR D 42 GLY D 47 LEU D 49 THR D 50
SITE 2 AK4 11 PHE D 101 LMG D 412 PRO F 29 PHE F 33
SITE 3 AK4 11 VAL J 21 VAL J 25 PL9 J 101
SITE 1 AK5 13 TYR D 67 GLY D 70 CYS D 71 ASN D 72
SITE 2 AK5 13 PHE D 73 BCR D 411 ILE F 37 MET F 40
SITE 3 AK5 13 GLN F 41 PHE J 28 GLY J 31 ALA J 32
SITE 4 AK5 13 GLY J 37
SITE 1 AK6 7 TYR A 262 LHG C 519 PHE D 27 PRO E 9
SITE 2 AK6 7 PHE E 10 SER E 11 PL9 J 101
SITE 1 AK7 15 ARG E 8 PHE E 10 ILE E 13 ARG E 18
SITE 2 AK7 15 TYR E 19 HIS E 23 THR E 26 LEU E 30
SITE 3 AK7 15 ILE F 15 ARG F 19 TRP F 20 VAL F 23
SITE 4 AK7 15 HIS F 24 ALA F 27 ILE F 31
SITE 1 AK8 9 TRP D 21 ARG D 24 ARG D 26 GLU E 7
SITE 2 AK8 9 PHE F 16 THR F 17 VAL F 18 THR X 33
SITE 3 AK8 9 ASP X 44
SITE 1 AK9 16 GLU B 184 GLY B 189 GLY B 197 HIS B 201
SITE 2 AK9 16 ALA B 204 ALA B 205 VAL B 208 PHE B 247
SITE 3 AK9 16 CLA B 601 CLA B 602 DGD B 620 VAL D 154
SITE 4 AK9 16 PHE H 38 PHE H 41 ILE H 45 TYR H 49
SITE 1 AL1 10 CLA B 601 CLA B 608 CLA B 609 PHE H 34
SITE 2 AL1 10 MET H 35 LEU H 37 PHE H 38 PHE H 41
SITE 3 AL1 10 THR X 11 LEU X 16
SITE 1 AL2 6 MET I 1 THR I 3 LEU I 4 LMT I 102
SITE 2 AL2 6 DGD b 601 LMT b 603
SITE 1 AL3 4 THR I 3 ILE I 6 ILE I 10 LMG I 101
SITE 1 AL4 4 PL9 A 406 BCR D 411 LMG E 101 VAL J 16
SITE 1 AL5 6 SQD A 413 DGD C 516 LHG C 519 LMG C 522
SITE 2 AL5 6 PHE J 29 TYR J 33
SITE 1 AL6 2 ASP K 19 ASP K 23
SITE 1 AL7 9 GLU M 30 SER M 31 SQD b 602 CLA b 617
SITE 2 AL7 9 PRO l 9 VAL l 10 ILE m 24 GLN m 28
SITE 3 AL7 9 GLN m 32
SITE 1 AL8 7 MET M 1 GLU M 2 MET T 1 ILE T 4
SITE 2 AL8 7 TYR b 40 LMG b 625 GLN m 5
SITE 1 AL9 6 TYR B 40 LMG B 621 GLN M 5 MET m 1
SITE 2 AL9 6 GLU m 2 MET t 1
SITE 1 AM1 2 GLU O 140 HIS O 257
SITE 1 AM2 14 ALA V 62 CYS V 63 CYS V 66 HIS V 67
SITE 2 AM2 14 THR V 74 LEU V 78 ASP V 79 THR V 84
SITE 3 AM2 14 LEU V 85 TYR V 101 MET V 102 TYR V 108
SITE 4 AM2 14 HIS V 118 PRO V 119
SITE 1 AM3 14 BCR C 513 ALA J 14 THR J 15 MET J 19
SITE 2 AM3 14 ILE K 28 LEU K 31 ALA K 34 PHE K 37
SITE 3 AM3 14 VAL K 38 VAL Z 13 PHE Z 17 ILE y 28
SITE 4 AM3 14 GLY y 29 GLY y 32
SITE 1 AM4 13 TRP B 113 TYR B 117 CLA B 605 CLA B 615
SITE 2 AM4 13 BCR B 619 TRP a 20 ASN a 26 ARG a 27
SITE 3 AM4 13 LEU a 28 VAL a 30 THR a 45 BCR a 410
SITE 4 AM4 13 PHO d 401
SITE 1 AM5 8 ALA B 43 TRP B 75 SER B 76 LEU B 98
SITE 2 AM5 8 LEU a 72 ASP a 103 ARG d 304 GLY o 138
SITE 1 AM6 5 HIS a 215 HIS a 272 HIS d 214 HIS d 268
SITE 2 AM6 5 BCT d 403
SITE 1 AM7 24 PHE a 119 TYR a 147 PRO a 150 SER a 153
SITE 2 AM7 24 VAL a 157 MET a 183 PHE a 186 GLN a 187
SITE 3 AM7 24 LEU a 193 HIS a 198 GLY a 201 VAL a 205
SITE 4 AM7 24 PHE a 206 VAL a 283 THR a 286 ILE a 290
SITE 5 AM7 24 CLA a 405 CLA a 406 LEU d 182 LEU d 205
SITE 6 AM7 24 PHO d 401 CLA d 404 LMG d 407 PHE t 17
SITE 1 AM8 14 THR a 45 VAL a 157 PHE a 158 MET a 172
SITE 2 AM8 14 ILE a 176 THR a 179 PHE a 180 MET a 183
SITE 3 AM8 14 CLA a 404 MET d 198 VAL d 201 PHO d 401
SITE 4 AM8 14 CLA d 404 PL9 d 406
SITE 1 AM9 13 GLN a 199 VAL a 202 ALA a 203 TRP a 278
SITE 2 AM9 13 CLA a 404 PHO a 407 PHE d 157 VAL d 175
SITE 3 AM9 13 ILE d 178 PHE d 179 PHE d 181 LEU d 182
SITE 4 AM9 13 CLA d 404
SITE 1 AN1 21 PHE a 206 ALA a 209 LEU a 210 MET a 214
SITE 2 AN1 21 LEU a 258 CLA a 406 ALA d 41 TRP d 48
SITE 3 AN1 21 GLY d 118 LEU d 122 PHE d 125 GLN d 129
SITE 4 AN1 21 ASN d 142 ALA d 145 PHE d 146 ALA d 148
SITE 5 AN1 21 PHE d 153 PHE d 173 PRO d 275 LEU d 279
SITE 6 AN1 21 CLA d 404
SITE 1 AN2 14 ILE a 36 PRO a 39 THR a 40 PHE a 93
SITE 2 AN2 14 PRO a 95 ILE a 96 TRP a 97 LEU a 114
SITE 3 AN2 14 HIS a 118 LEU a 121 BCR a 410 DGD a 411
SITE 4 AN2 14 TYR i 9 PHE i 15
SITE 1 AN3 13 HIS a 215 LEU a 218 HIS a 252 PHE a 255
SITE 2 AN3 13 SER a 264 PHE a 265 LEU a 271 PHE a 274
SITE 3 AN3 13 PHE d 38 ALA d 41 TYR d 42 THR f 25
SITE 4 AN3 13 PL9 j 101
SITE 1 AN4 8 LMT B 627 LEU a 42 ALA a 43 TRP a 105
SITE 2 AN4 8 LEU a 106 SQD a 401 CLA a 408 PHE i 15
SITE 1 AN5 13 PHE a 93 TRP a 97 GLU a 98 CLA a 408
SITE 2 AN5 13 LEU c 214 LYS c 215 SER c 216 PRO c 217
SITE 3 AN5 13 TRP c 223 PHE c 284 LYS i 5 TYR i 9
SITE 4 AN5 13 GLY o 38
SITE 1 AN6 15 ARG a 140 TRP a 142 PHE a 273 SQD a 415
SITE 2 AN6 15 TRP c 36 PHE c 436 TRP c 443 ARG c 447
SITE 3 AN6 15 CLA c 507 CLA c 520 ASN d 220 ALA d 229
SITE 4 AN6 15 SER d 230 THR d 231 PHE d 232
SITE 1 AN7 13 SER a 232 ASN a 234 TRP b 5 TYR b 6
SITE 2 AN7 13 LMG b 628 TRP d 266 PHE d 269 PHE d 273
SITE 3 AN7 13 PL9 d 406 GLU l 11 ASN l 13 SER l 16
SITE 4 AN7 13 VAL l 26
SITE 1 AN8 9 ASP a 170 GLU a 189 HIS a 332 GLU a 333
SITE 2 AN8 9 HIS a 337 ASP a 342 ALA a 344 GLU c 354
SITE 3 AN8 9 ARG c 357
SITE 1 AN9 14 ASN a 267 SER a 270 PHE a 273 PHE a 274
SITE 2 AN9 14 TRP a 278 LHG a 412 TRP c 36 DGD c 516
SITE 3 AN9 14 DGD c 517 LHG c 519 PHE d 232 ARG d 233
SITE 4 AN9 14 BCR j 102 PHE k 37
SITE 1 AO1 3 ASN a 181 GLU a 333 LYS d 317
SITE 1 AO2 8 ILE A 46 LMG I 101 TRP b 75 ASP b 87
SITE 2 AO2 8 GLY b 89 PHE b 90 LMT b 603 LMT b 626
SITE 1 AO3 13 ARG L 14 TYR L 18 TYR M 26 LMG M 101
SITE 2 AO3 13 PHE T 19 PHE T 23 ARG b 18 LEU b 29
SITE 3 AO3 13 SER b 104 TRP b 115 CLA b 617 BCR b 620
SITE 4 AO3 13 ASN l 4
SITE 1 AO4 7 BCR A 407 MET I 1 LMG I 101 LYS O 95
SITE 2 AO4 7 GLY b 85 ASP b 87 DGD b 601
SITE 1 AO5 4 VAL T 7 ALA b 43 LEU b 437 BCR b 621
SITE 1 AO6 8 TRP b 185 PRO b 187 PHE b 190 ILE b 207
SITE 2 AO6 8 PHE h 41 ILE h 44 CLA h 101 BCR x 101
SITE 1 AO7 19 ARG b 68 LEU b 69 ALA b 146 LEU b 149
SITE 2 AO7 19 CYS b 150 PHE b 153 VAL b 198 HIS b 201
SITE 3 AO7 19 HIS b 202 PHE b 247 ALA b 248 VAL b 252
SITE 4 AO7 19 THR b 262 CLA b 607 CLA b 608 CLA b 609
SITE 5 AO7 19 CLA b 612 PHE h 38 CLA h 101
SITE 1 AO8 20 TRP b 33 PHE b 61 PHE b 65 ARG b 68
SITE 2 AO8 20 VAL b 245 ALA b 248 ALA b 249 VAL b 252
SITE 3 AO8 20 PHE b 451 HIS b 455 PHE b 458 ALA b 459
SITE 4 AO8 20 PHE b 462 CLA b 606 CLA b 608 CLA b 610
SITE 5 AO8 20 CLA b 614 CLA b 615 CLA b 616 CLA b 618
SITE 1 AO9 20 THR b 27 VAL b 30 ALA b 31 TRP b 33
SITE 2 AO9 20 ALA b 34 VAL b 62 PHE b 65 MET b 66
SITE 3 AO9 20 ARG b 68 LEU b 69 VAL b 96 HIS b 100
SITE 4 AO9 20 LEU b 103 ALA b 205 CLA b 606 CLA b 607
SITE 5 AO9 20 CLA b 609 CLA b 612 CLA b 613 CLA b 615
SITE 1 AP1 16 SQD A 414 LEU b 69 TRP b 91 ALA b 99
SITE 2 AP1 16 LEU b 103 LEU b 106 GLY b 152 PHE b 153
SITE 3 AP1 16 PHE b 156 HIS b 157 PHE b 162 PRO b 164
SITE 4 AP1 16 CLA b 606 CLA b 608 BCR b 623 LMT b 626
SITE 1 AP2 18 TRP b 33 TYR b 40 GLN b 58 GLY b 59
SITE 2 AP2 18 PHE b 61 THR b 327 GLY b 328 PRO b 329
SITE 3 AP2 18 TRP b 450 ALA b 454 CLA b 607 BCR b 620
SITE 4 AP2 18 BCR b 621 BCR b 622 LMG b 625 LMG b 628
SITE 5 AP2 18 MET d 281 LEU l 27
SITE 1 AP3 15 THR b 236 SER b 239 ALA b 243 PHE b 246
SITE 2 AP3 15 PHE b 247 HIS b 466 LEU b 474 CLA b 612
SITE 3 AP3 15 CLA b 613 PHE d 120 ILE d 123 MET d 126
SITE 4 AP3 15 LEU d 127 PHE d 130 SQD d 402
SITE 1 AP4 17 PHE b 139 ALA b 212 PHE b 215 HIS b 216
SITE 2 AP4 17 PRO b 221 PRO b 222 LEU b 229 CLA b 606
SITE 3 AP4 17 CLA b 608 CLA b 611 CLA b 613 THR h 27
SITE 4 AP4 17 THR h 28 MET h 31 PHE h 34 MET h 35
SITE 5 AP4 17 BCR x 101
SITE 1 AP5 13 LEU b 135 PHE b 139 HIS b 142 LEU b 143
SITE 2 AP5 13 THR b 236 VAL b 237 SER b 240 CLA b 608
SITE 3 AP5 13 CLA b 611 CLA b 612 CLA b 615 CLA b 618
SITE 4 AP5 13 BCR x 101
SITE 1 AP6 18 TRP b 5 TYR b 6 ARG b 7 VAL b 8
SITE 2 AP6 18 HIS b 9 THR b 10 ILE b 242 LEU b 461
SITE 3 AP6 18 PHE b 462 GLY b 465 TRP b 468 HIS b 469
SITE 4 AP6 18 ARG b 472 CLA b 607 CLA b 615 CLA b 616
SITE 5 AP6 18 CLA b 617 LMG b 628
SITE 1 AP7 17 HIS b 9 LEU b 19 HIS b 23 HIS b 26
SITE 2 AP7 17 THR b 27 ILE b 234 VAL b 237 LEU b 238
SITE 3 AP7 17 SER b 241 VAL b 245 CLA b 607 CLA b 608
SITE 4 AP7 17 CLA b 613 CLA b 614 CLA b 616 CLA b 617
SITE 5 AP7 17 CLA b 618
SITE 1 AP8 8 HIS b 9 HIS b 26 PHE b 462 CLA b 607
SITE 2 AP8 8 CLA b 614 CLA b 615 CLA b 617 LMG b 628
SITE 1 AP9 12 LMG M 101 PHE T 8 VAL b 8 HIS b 9
SITE 2 AP9 12 VAL b 11 TRP b 115 SQD b 602 CLA b 614
SITE 3 AP9 12 CLA b 615 CLA b 616 BCR b 620 VAL l 10
SITE 1 AQ1 11 HIS b 23 MET b 138 ILE b 141 HIS b 142
SITE 2 AQ1 11 LEU b 145 CLA b 607 CLA b 613 CLA b 615
SITE 3 AQ1 11 CLA b 619 BCR b 623 LEU h 14
SITE 1 AQ2 8 SQD A 414 LEU b 24 ALA b 110 TRP b 113
SITE 2 AQ2 8 HIS b 114 CLA b 618 THR h 5 LEU h 7
SITE 1 AQ3 11 PHE T 19 MET b 25 LEU b 29 TRP b 115
SITE 2 AQ3 11 SQD b 602 CLA b 610 CLA b 617 BCR b 621
SITE 3 AQ3 11 BCR b 622 ALA m 10 LEU m 13
SITE 1 AQ4 14 ILE T 4 PHE T 8 ALA T 11 PHE T 17
SITE 2 AQ4 14 PHE T 18 ILE T 21 PHE T 22 TRP b 33
SITE 3 AQ4 14 SER b 36 MET b 37 LMT b 604 CLA b 610
SITE 4 AQ4 14 BCR b 620 BCR b 622
SITE 1 AQ5 6 GLY b 32 TRP b 33 GLY b 105 CLA b 610
SITE 2 AQ5 6 BCR b 620 BCR b 621
SITE 1 AQ6 9 SQD A 414 PHE T 22 LEU b 106 LEU b 109
SITE 2 AQ6 9 ALA b 110 CYS b 112 TYR b 117 CLA b 609
SITE 3 AQ6 9 CLA b 618
SITE 1 AQ7 13 TYR b 193 PHE b 250 TYR b 258 TYR b 273
SITE 2 AQ7 13 SER b 277 HIS d 87 LEU d 162 TYR h 49
SITE 3 AQ7 13 ASN h 50 VAL h 60 SER h 61 TRP h 62
SITE 4 AQ7 13 CLA h 101
SITE 1 AQ8 11 LMT M 102 THR b 327 GLY b 328 PRO b 329
SITE 2 AQ8 11 LYS b 332 PHE b 453 CLA b 610 ILE d 284
SITE 3 AQ8 11 PHE l 35 ASN m 4 LEU m 6
SITE 1 AQ9 4 TRP b 91 PHE b 162 DGD b 601 CLA b 609
SITE 1 AR1 7 ARG b 224 LYS b 227 ASP d 16 ASP d 19
SITE 2 AR1 7 SQD d 402 ALA h 32 MET h 35
SITE 1 AR2 13 ASN a 234 LMG a 413 TRP b 5 TYR b 6
SITE 2 AR2 13 ARG b 7 PHE b 464 TRP b 468 CLA b 610
SITE 3 AR2 13 CLA b 614 CLA b 616 ARG d 139 TYR d 141
SITE 4 AR2 13 PHE d 269
SITE 1 AR3 16 LEU c 95 LEU c 168 GLY c 171 ALA c 172
SITE 2 AR3 16 ILE c 224 VAL c 233 HIS c 237 ILE c 240
SITE 3 AR3 16 MET c 282 PHE c 289 VAL c 296 TYR c 297
SITE 4 AR3 16 CLA c 502 CLA c 503 CLA c 506 BCR c 514
SITE 1 AR4 15 TRP c 63 HIS c 91 TRP c 97 LYS c 178
SITE 2 AR4 15 PHE c 182 LEU c 279 MET c 282 ALA c 286
SITE 3 AR4 15 TYR c 297 HIS c 430 LEU c 433 PHE c 437
SITE 4 AR4 15 CLA c 501 CLA c 503 CLA c 508
SITE 1 AR5 14 ILE c 60 VAL c 61 ALA c 64 THR c 68
SITE 2 AR5 14 LEU c 88 HIS c 91 ILE c 92 VAL c 114
SITE 3 AR5 14 HIS c 118 CLA c 501 CLA c 502 CLA c 509
SITE 4 AR5 14 CLA c 511 LMG c 518
SITE 1 AR6 17 PHE a 33 MET a 127 TRP a 131 PHE c 264
SITE 2 AR6 17 ILE c 265 TYR c 274 GLY c 277 ALA c 278
SITE 3 AR6 17 MET c 281 HIS c 441 LEU c 442 ALA c 445
SITE 4 AR6 17 ARG c 449 CLA c 506 BCR c 514 VAL i 12
SITE 5 AR6 17 PHE i 23
SITE 1 AR7 13 LEU c 165 LEU c 213 ILE c 243 GLY c 247
SITE 2 AR7 13 TRP c 250 HIS c 251 THR c 255 PRO c 256
SITE 3 AR7 13 PHE c 257 TRP c 259 ALA c 260 PHE c 264
SITE 4 AR7 13 CLA c 506
SITE 1 AR8 13 MET c 157 LEU c 161 HIS c 164 PHE c 264
SITE 2 AR8 13 TRP c 266 TYR c 271 TYR c 274 SER c 275
SITE 3 AR8 13 LEU c 279 CLA c 501 CLA c 504 CLA c 505
SITE 4 AR8 13 CLA c 508
SITE 1 AR9 16 LHG a 412 TRP c 36 ALA c 37 ASN c 39
SITE 2 AR9 16 ALA c 40 GLU c 269 LEU c 276 PHE c 436
SITE 3 AR9 16 PHE c 437 GLY c 440 TRP c 443 HIS c 444
SITE 4 AR9 16 ARG c 447 CLA c 508 CLA c 509 DGD c 516
SITE 1 AS1 19 ASN c 39 LEU c 42 LEU c 49 ALA c 52
SITE 2 AS1 19 HIS c 53 HIS c 56 TYR c 149 TRP c 151
SITE 3 AS1 19 GLY c 268 TYR c 271 LEU c 272 SER c 275
SITE 4 AS1 19 LEU c 279 CLA c 502 CLA c 506 CLA c 507
SITE 5 AS1 19 CLA c 509 CLA c 510 CLA c 511
SITE 1 AS2 14 ASN c 39 HIS c 56 LEU c 59 LEU c 279
SITE 2 AS2 14 PHE c 436 PHE c 437 CLA c 503 CLA c 507
SITE 3 AS2 14 CLA c 508 CLA c 510 CLA c 520 PRO k 29
SITE 4 AS2 14 VAL k 30 LEU k 33
SITE 1 AS3 21 GLN c 28 TRP c 35 GLY c 38 ASN c 39
SITE 2 AS3 21 ARG c 41 LEU c 42 LYS c 48 ALA c 52
SITE 3 AS3 21 PHE c 127 ILE c 134 CLA c 508 CLA c 509
SITE 4 AS3 21 BCR c 513 ILE g 35 LEU g 46 PHE k 32
SITE 5 AS3 21 TRP k 39 GLN k 40 MET z 19 VAL z 20
SITE 6 AS3 21 PRO z 24
SITE 1 AS4 12 HIS c 53 ALA c 57 PHE c 147 PHE c 163
SITE 2 AS4 12 HIS c 164 VAL c 167 ILE c 170 LEU c 174
SITE 3 AS4 12 CLA c 503 CLA c 508 CLA c 512 BCR c 521
SITE 1 AS5 9 LEU c 50 VAL c 124 GLY c 128 TYR c 131
SITE 2 AS5 9 HIS c 132 PRO c 137 PHE c 147 CLA c 511
SITE 3 AS5 9 BCR c 521
SITE 1 AS6 10 ALA c 55 VAL c 116 LEU c 119 SER c 122
SITE 2 AS6 10 ALA c 123 CLA c 510 BCR c 521 BCR g 101
SITE 3 AS6 10 PHE k 32 VAL z 13
SITE 1 AS7 11 ILE c 209 TYR c 212 LEU c 213 VAL c 227
SITE 2 AS7 11 ASP c 232 VAL c 233 GLY c 236 ILE c 240
SITE 3 AS7 11 PHE c 264 CLA c 501 CLA c 504
SITE 1 AS8 16 LEU a 91 PHE a 155 ILE a 163 PRO c 217
SITE 2 AS8 16 PHE c 218 GLY c 219 GLY c 220 VAL c 225
SITE 3 AS8 16 SER c 226 PHE c 284 CYS c 288 PHE c 292
SITE 4 AS8 16 ASN c 294 PRO c 307 PHE c 361 ARG c 362
SITE 1 AS9 19 PHE a 197 SQD a 415 TYR c 82 GLU c 83
SITE 2 AS9 19 GLN c 84 GLY c 85 SER c 406 ASN c 418
SITE 3 AS9 19 PHE c 419 VAL c 420 TRP c 425 SER c 429
SITE 4 AS9 19 CLA c 507 DGD c 517 LHG c 519 CLA c 520
SITE 5 AS9 19 LMG c 522 TYR j 33 BCR j 102
SITE 1 AT1 22 LEU a 200 TRP a 278 PHE a 300 ASN a 301
SITE 2 AT1 22 SER a 305 SQD a 415 ASN c 405 SER c 406
SITE 3 AT1 22 VAL c 407 ASN c 415 SER c 416 ASN c 418
SITE 4 AT1 22 DGD c 516 CLA c 520 LMG d 410 PHE j 29
SITE 5 AT1 22 ALA j 32 TYR j 33 GLY j 37 SER j 38
SITE 6 AT1 22 SER j 39 GLN v 60
SITE 1 AT2 7 TRP c 97 PHE c 109 VAL c 113 VAL c 117
SITE 2 AT2 7 HIS c 118 CLA c 503 PHE z 59
SITE 1 AT3 8 TYR a 262 ASN a 266 SQD a 415 TRP c 35
SITE 2 AT3 8 DGD c 516 LMG e 101 BCR j 102 PHE k 45
SITE 1 AT4 16 PHE a 285 LHG a 412 TRP c 63 MET c 67
SITE 2 AT4 16 PHE c 70 GLN c 84 GLY c 85 ILE c 87
SITE 3 AT4 16 TRP c 425 SER c 429 CLA c 509 DGD c 516
SITE 4 AT4 16 DGD c 517 LMG c 522 PRO k 26 VAL k 30
SITE 1 AT5 10 VAL c 116 SER c 121 VAL c 124 CLA c 511
SITE 2 AT5 10 CLA c 512 BCR c 513 TYR k 15 VAL z 54
SITE 3 AT5 10 GLY z 55 ASN z 58
SITE 1 AT6 8 PHE c 70 HIS c 74 DGD c 516 CLA c 520
SITE 2 AT6 8 ILE g 25 BCR j 102 ASP k 23 VAL k 27
SITE 1 AT7 19 ALA a 44 THR a 45 ILE a 115 TYR a 126
SITE 2 AT7 19 GLN a 130 TYR a 147 PRO a 150 LEU a 174
SITE 3 AT7 19 GLY a 175 VAL a 283 SQD a 401 CLA a 404
SITE 4 AT7 19 CLA a 405 LEU d 205 ALA d 208 LEU d 209
SITE 5 AT7 19 ILE d 213 TRP d 253 PHE d 257
SITE 1 AT8 10 LYS b 227 ALA b 228 ARG b 230 LEU b 474
SITE 2 AT8 10 CLA b 611 LMT b 627 LYS d 23 TRP d 32
SITE 3 AT8 10 ARG d 134 LEU d 135
SITE 1 AT9 8 HIS a 215 GLU a 244 TYR a 246 HIS a 272
SITE 2 AT9 8 FE2 a 403 TYR d 244 LYS d 264 HIS d 268
SITE 1 AU1 22 PHE a 206 CLA a 404 CLA a 405 CLA a 406
SITE 2 AU1 22 PHO a 407 TRP d 48 VAL d 152 PHE d 153
SITE 3 AU1 22 VAL d 156 LEU d 182 PHE d 185 GLN d 186
SITE 4 AU1 22 TRP d 191 THR d 192 HIS d 197 GLY d 200
SITE 5 AU1 22 VAL d 201 VAL d 204 LEU d 279 SER d 282
SITE 6 AU1 22 ALA d 283 VAL d 286
SITE 1 AU2 14 LEU d 43 LEU d 89 LEU d 90 LEU d 91
SITE 2 AU2 14 LEU d 92 TRP d 93 THR d 112 PHE d 113
SITE 3 AU2 14 HIS d 117 PHE d 120 LMT d 409 GLY x 22
SITE 4 AU2 14 LEU x 23 GLY x 26
SITE 1 AU3 14 CLA a 405 LMG a 413 MET d 199 HIS d 214
SITE 2 AU3 14 THR d 217 TRP d 253 ILE d 259 ALA d 260
SITE 3 AU3 14 PHE d 261 LEU d 267 PHE d 273 VAL d 274
SITE 4 AU3 14 VAL l 26 PHE t 10
SITE 1 AU4 13 CLA a 404 PHE d 257 ILE d 259 ALA d 260
SITE 2 AU4 13 PHE d 261 SER d 262 ASN d 263 TRP d 266
SITE 3 AU4 13 THR l 15 TYR l 18 LEU l 19 PHE t 17
SITE 4 AU4 13 ALA t 20
SITE 1 AU5 6 ASP d 100 PHE d 101 THR d 102 LMT d 409
SITE 2 AU5 6 ASP e 45 VAL e 46
SITE 1 AU6 8 LEU d 92 TRP d 93 GLY d 99 CLA d 405
SITE 2 AU6 8 DGD d 408 ILE x 21 SER x 25 GLY x 26
SITE 1 AU7 13 DGD c 517 TYR d 67 GLY d 70 ASN d 72
SITE 2 AU7 13 PHE d 73 ILE f 37 MET f 40 GLN f 41
SITE 3 AU7 13 BCR f 102 PHE j 28 GLY j 31 ALA j 32
SITE 4 AU7 13 GLY j 37
SITE 1 AU8 7 TYR a 262 LHG c 519 PHE d 27 PRO e 9
SITE 2 AU8 7 PHE e 10 SER e 11 PL9 j 101
SITE 1 AU9 14 ARG e 8 PHE e 10 ILE e 13 ARG e 18
SITE 2 AU9 14 TYR e 19 HIS e 23 THR e 26 LEU e 30
SITE 3 AU9 14 ILE f 15 ARG f 19 TRP f 20 HIS f 24
SITE 4 AU9 14 ALA f 27 ILE f 31
SITE 1 AV1 12 TYR d 42 GLY d 46 GLY d 47 LEU d 49
SITE 2 AV1 12 THR d 50 PHE d 101 LMG d 410 PRO f 29
SITE 3 AV1 12 PHE f 33 VAL j 21 VAL j 25 PL9 j 101
SITE 1 AV2 9 TRP d 21 ARG d 24 ARG d 26 GLU e 7
SITE 2 AV2 9 PHE f 16 THR f 17 VAL f 18 THR x 33
SITE 3 AV2 9 VAL x 36
SITE 1 AV3 15 GLU b 184 GLY b 189 GLY b 197 HIS b 201
SITE 2 AV3 15 ALA b 204 VAL b 208 PHE b 247 CLA b 605
SITE 3 AV3 15 CLA b 606 DGD b 624 VAL d 154 PHE h 38
SITE 4 AV3 15 PHE h 41 ILE h 45 TYR h 49
SITE 1 AV4 6 DGD B 625 LMT B 627 MET i 1 THR i 3
SITE 2 AV4 6 LEU i 4 LMT i 102
SITE 1 AV5 5 THR i 3 ILE i 6 THR i 7 ILE i 10
SITE 2 AV5 5 LMG i 101
SITE 1 AV6 3 PL9 a 409 LMG e 101 BCR f 102
SITE 1 AV7 8 SQD a 415 DGD c 516 LHG c 519 LMG c 522
SITE 2 AV7 8 BCR g 101 PHE j 29 TYR j 30 TYR j 33
SITE 1 AV8 2 ASP k 19 ASP k 23
SITE 1 AV9 7 CLA B 613 VAL L 10 GLN M 28 GLN M 32
SITE 2 AV9 7 VAL m 27 GLU m 30 SER m 31
SITE 1 AW1 2 GLU o 140 HIS o 257
SITE 1 AW2 14 ALA v 62 CYS v 63 CYS v 66 HIS v 67
SITE 2 AW2 14 THR v 74 LEU v 78 ASP v 79 THR v 84
SITE 3 AW2 14 LEU v 85 TYR v 101 MET v 102 TYR v 108
SITE 4 AW2 14 HIS v 118 PRO v 119
SITE 1 AW3 13 BCR c 513 ILE g 28 GLY g 29 GLY g 32
SITE 2 AW3 13 ALA j 14 THR j 15 BCR j 102 ILE k 28
SITE 3 AW3 13 LEU k 31 ALA k 34 PHE k 37 VAL k 38
SITE 4 AW3 13 VAL z 13
SITE 1 AW4 10 CLA b 605 CLA b 612 CLA b 613 PHE h 34
SITE 2 AW4 10 MET h 35 LEU h 37 PHE h 38 PHE h 41
SITE 3 AW4 10 THR x 11 LEU x 16
CRYST1 132.298 228.713 307.976 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 0.007559 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004372 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003247 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
