HEADER PHOTOSYNTHESIS 03-OCT-16 5TIS
TITLE ROOM TEMPERATURE XFEL STRUCTURE OF THE NATIVE, DOUBLY-ILLUMINATED
TITLE 2 PHOTOSYSTEM II COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOTOSYSTEM II PROTEIN D1 1;
COMPND 3 CHAIN: A, a;
COMPND 4 FRAGMENT: UNP RESIDUES 1-344;
COMPND 5 SYNONYM: PSII D1 PROTEIN 1,PHOTOSYSTEM II Q(B) PROTEIN 1;
COMPND 6 EC: 1.10.3.9;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PHOTOSYSTEM II CP47 REACTION CENTER PROTEIN;
COMPND 9 CHAIN: B, b;
COMPND 10 SYNONYM: PSII 47 KDA PROTEIN,PROTEIN CP-47;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: PHOTOSYSTEM II CP43 REACTION CENTER PROTEIN;
COMPND 13 CHAIN: C, c;
COMPND 14 SYNONYM: PSII 43 KDA PROTEIN,PROTEIN CP-43;
COMPND 15 MOL_ID: 4;
COMPND 16 MOLECULE: PHOTOSYSTEM II D2 PROTEIN;
COMPND 17 CHAIN: D, d;
COMPND 18 SYNONYM: PSII D2 PROTEIN,PHOTOSYSTEM II Q(A) PROTEIN;
COMPND 19 EC: 1.10.3.9;
COMPND 20 MOL_ID: 5;
COMPND 21 MOLECULE: CYTOCHROME B559 SUBUNIT ALPHA;
COMPND 22 CHAIN: E, e;
COMPND 23 SYNONYM: PSII REACTION CENTER SUBUNIT V;
COMPND 24 MOL_ID: 6;
COMPND 25 MOLECULE: CYTOCHROME B559 SUBUNIT BETA;
COMPND 26 CHAIN: F, f;
COMPND 27 SYNONYM: PSII REACTION CENTER SUBUNIT VI;
COMPND 28 MOL_ID: 7;
COMPND 29 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN H;
COMPND 30 CHAIN: H, h;
COMPND 31 SYNONYM: PSII-H;
COMPND 32 MOL_ID: 8;
COMPND 33 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN I;
COMPND 34 CHAIN: I, i;
COMPND 35 SYNONYM: PSII-I,PSII 4.4 KDA PROTEIN;
COMPND 36 MOL_ID: 9;
COMPND 37 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN J;
COMPND 38 CHAIN: J, j;
COMPND 39 SYNONYM: PSII-J;
COMPND 40 MOL_ID: 10;
COMPND 41 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN K;
COMPND 42 CHAIN: K, k;
COMPND 43 SYNONYM: PSII-K;
COMPND 44 MOL_ID: 11;
COMPND 45 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN L;
COMPND 46 CHAIN: L, l;
COMPND 47 SYNONYM: PSII-L;
COMPND 48 MOL_ID: 12;
COMPND 49 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN M;
COMPND 50 CHAIN: M, m;
COMPND 51 SYNONYM: PSII-M;
COMPND 52 MOL_ID: 13;
COMPND 53 MOLECULE: PHOTOSYSTEM II MANGANESE-STABILIZING POLYPEPTIDE;
COMPND 54 CHAIN: O, o;
COMPND 55 SYNONYM: MSP;
COMPND 56 MOL_ID: 14;
COMPND 57 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN T;
COMPND 58 CHAIN: T, t;
COMPND 59 SYNONYM: PSII-TC;
COMPND 60 MOL_ID: 15;
COMPND 61 MOLECULE: PHOTOSYSTEM II 12 KDA EXTRINSIC PROTEIN;
COMPND 62 CHAIN: U, u;
COMPND 63 SYNONYM: PS II COMPLEX 12 KDA EXTRINSIC PROTEIN,PSII-U;
COMPND 64 MOL_ID: 16;
COMPND 65 MOLECULE: CYTOCHROME C-550;
COMPND 66 CHAIN: V, v;
COMPND 67 SYNONYM: CYTOCHROME C-549,CYTOCHROME C550,LOW-POTENTIAL CYTOCHROME C;
COMPND 68 MOL_ID: 17;
COMPND 69 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN YCF12;
COMPND 70 CHAIN: Y, y;
COMPND 71 MOL_ID: 18;
COMPND 72 MOLECULE: PHOTOSYSTEM II REACTION CENTER X PROTEIN;
COMPND 73 CHAIN: X, x;
COMPND 74 MOL_ID: 19;
COMPND 75 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN Z;
COMPND 76 CHAIN: Z, z;
COMPND 77 SYNONYM: PSII-Z;
COMPND 78 MOL_ID: 20;
COMPND 79 MOLECULE: PHOTOSYSTEM II PROTEIN Y;
COMPND 80 CHAIN: R, r
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 3 ORGANISM_TAXID: 197221;
SOURCE 4 STRAIN: BP-1;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 7 ORGANISM_TAXID: 197221;
SOURCE 8 STRAIN: BP-1;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 11 ORGANISM_TAXID: 197221;
SOURCE 12 STRAIN: BP-1;
SOURCE 13 MOL_ID: 4;
SOURCE 14 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 15 ORGANISM_TAXID: 197221;
SOURCE 16 STRAIN: BP-1;
SOURCE 17 MOL_ID: 5;
SOURCE 18 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 19 ORGANISM_TAXID: 197221;
SOURCE 20 STRAIN: BP-1;
SOURCE 21 MOL_ID: 6;
SOURCE 22 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 23 ORGANISM_TAXID: 197221;
SOURCE 24 STRAIN: BP-1;
SOURCE 25 MOL_ID: 7;
SOURCE 26 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
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 (STRAIN BP-1);
SOURCE 35 ORGANISM_TAXID: 197221;
SOURCE 36 STRAIN: BP-1;
SOURCE 37 MOL_ID: 10;
SOURCE 38 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 39 ORGANISM_TAXID: 197221;
SOURCE 40 STRAIN: BP-1;
SOURCE 41 MOL_ID: 11;
SOURCE 42 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
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 (STRAIN BP-1);
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 (STRAIN BP-1);
SOURCE 59 ORGANISM_TAXID: 197221;
SOURCE 60 STRAIN: BP-1;
SOURCE 61 MOL_ID: 16;
SOURCE 62 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 63 ORGANISM_TAXID: 197221;
SOURCE 64 STRAIN: BP-1;
SOURCE 65 MOL_ID: 17;
SOURCE 66 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 67 ORGANISM_TAXID: 197221;
SOURCE 68 STRAIN: BP-1;
SOURCE 69 MOL_ID: 18;
SOURCE 70 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 71 ORGANISM_TAXID: 197221;
SOURCE 72 STRAIN: BP-1;
SOURCE 73 MOL_ID: 19;
SOURCE 74 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 75 ORGANISM_TAXID: 197221;
SOURCE 76 STRAIN: BP-1;
SOURCE 77 MOL_ID: 20;
SOURCE 78 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 79 ORGANISM_TAXID: 197221;
SOURCE 80 STRAIN: BP-1
KEYWDS PHOTOSYSTEMS, TRANSMEMBRANE, ROOM TEMPERATURE, ELECTRON TRANSPORT,
KEYWDS 2 PHOTOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR I.D.YOUNG,M.IBRAHIM,R.CHATTERJEE,S.GUL,F.FULLER,S.KOROIDOV,
AUTHOR 2 A.S.BREWSTER,R.TRAN,R.ALONSO-MORI,T.KROLL,T.MICHELS-CLARK,
AUTHOR 3 H.LAKSMONO,R.G.SIERRA,C.A.STAN,R.HUSSEIN,M.ZHANG,L.DOUTHIT,M.KUBIN,
AUTHOR 4 C.DE LICHTENBERG,L.V.PHAM,H.NILSSON,M.H.CHEAH,D.SHEVELA,C.SARACINI,
AUTHOR 5 M.A.BEAN,I.SEUFFERT,D.SOKARAS,T.-C.WENG,E.PASTOR,C.WENINGER,
AUTHOR 6 T.FRANSSON,L.LASSALLE,P.BRAEUER,P.ALLER,P.T.DOCKER,B.ANDI,
AUTHOR 7 A.M.ORVILLE,J.M.GLOWNIA,S.NELSON,M.SIKORSKI,D.ZHU,M.S.HUNTER,
AUTHOR 8 A.AQUILA,J.E.KOGLIN,J.ROBINSON,M.LIANG,S.BOUTET,A.Y.LYUBIMOV,
AUTHOR 9 M.UERVIROJNANGKOORN,N.W.MORIARTY,D.LIEBSCHNER,P.V.AFONINE,
AUTHOR 10 D.G.WATERMANN,G.EVANS,P.WERNET,H.DOBBEK,W.I.WEIS,A.T.BRUNGER,
AUTHOR 11 P.H.ZWART,P.D.ADAMS,A.ZOUNI,J.MESSINGER,U.BERGMANN,N.K.SAUTER,
AUTHOR 12 J.KERN,V.K.YACHANDRA,J.YANO
REVDAT 6 01-JAN-20 5TIS 1 REMARK
REVDAT 5 20-NOV-19 5TIS 1 REMARK
REVDAT 4 27-SEP-17 5TIS 1 REMARK
REVDAT 3 28-DEC-16 5TIS 1 JRNL
REVDAT 2 14-DEC-16 5TIS 1 JRNL
REVDAT 1 23-NOV-16 5TIS 0
JRNL AUTH I.D.YOUNG,M.IBRAHIM,R.CHATTERJEE,S.GUL,F.D.FULLER,
JRNL AUTH 2 S.KOROIDOV,A.S.BREWSTER,R.TRAN,R.ALONSO-MORI,T.KROLL,
JRNL AUTH 3 T.MICHELS-CLARK,H.LAKSMONO,R.G.SIERRA,C.A.STAN,R.HUSSEIN,
JRNL AUTH 4 M.ZHANG,L.DOUTHIT,M.KUBIN,C.DE LICHTENBERG,L.VO PHAM,
JRNL AUTH 5 H.NILSSON,M.H.CHEAH,D.SHEVELA,C.SARACINI,M.A.BEAN,
JRNL AUTH 6 I.SEUFFERT,D.SOKARAS,T.C.WENG,E.PASTOR,C.WENINGER,
JRNL AUTH 7 T.FRANSSON,L.LASSALLE,P.BRAUER,P.ALLER,P.T.DOCKER,B.ANDI,
JRNL AUTH 8 A.M.ORVILLE,J.M.GLOWNIA,S.NELSON,M.SIKORSKI,D.ZHU,
JRNL AUTH 9 M.S.HUNTER,T.J.LANE,A.AQUILA,J.E.KOGLIN,J.ROBINSON,M.LIANG,
JRNL AUTH10 S.BOUTET,A.Y.LYUBIMOV,M.UERVIROJNANGKOORN,N.W.MORIARTY,
JRNL AUTH11 D.LIEBSCHNER,P.V.AFONINE,D.G.WATERMAN,G.EVANS,P.WERNET,
JRNL AUTH12 H.DOBBEK,W.I.WEIS,A.T.BRUNGER,P.H.ZWART,P.D.ADAMS,A.ZOUNI,
JRNL AUTH13 J.MESSINGER,U.BERGMANN,N.K.SAUTER,J.KERN,V.K.YACHANDRA,
JRNL AUTH14 J.YANO
JRNL TITL STRUCTURE OF PHOTOSYSTEM II AND SUBSTRATE BINDING AT ROOM
JRNL TITL 2 TEMPERATURE.
JRNL REF NATURE V. 540 453 2016
JRNL REFN ESSN 1476-4687
JRNL PMID 27871088
JRNL DOI 10.1038/NATURE20161
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.,SECT.D V. 68 352 2012
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.,SECT.D V. 66 213 2010
REMARK 1 REFN ESSN 1399-0047
REMARK 1 PMID 20124702
REMARK 1 DOI 10.1107/S0907444909052925
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_2481
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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.28
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.325
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 385545
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.889
REMARK 3 FREE R VALUE TEST SET COUNT : 3426
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 44.2852 - 6.4836 1.00 16669 150 0.1671 0.1996
REMARK 3 2 6.4836 - 5.1487 1.00 16221 145 0.1753 0.2027
REMARK 3 3 5.1487 - 4.4986 1.00 16104 144 0.1539 0.1954
REMARK 3 4 4.4986 - 4.0876 1.00 16055 145 0.1520 0.1764
REMARK 3 5 4.0876 - 3.7948 1.00 16011 141 0.1600 0.1879
REMARK 3 6 3.7948 - 3.5712 1.00 15927 144 0.1681 0.1990
REMARK 3 7 3.5712 - 3.3924 1.00 15987 143 0.1788 0.2289
REMARK 3 8 3.3924 - 3.2448 1.00 15940 143 0.1824 0.2412
REMARK 3 9 3.2448 - 3.1199 1.00 15884 143 0.1955 0.2441
REMARK 3 10 3.1199 - 3.0123 1.00 15888 141 0.2002 0.2329
REMARK 3 11 3.0123 - 2.9181 1.00 15905 142 0.2007 0.2332
REMARK 3 12 2.9181 - 2.8347 1.00 15860 144 0.2065 0.2724
REMARK 3 13 2.8347 - 2.7601 1.00 15879 143 0.2105 0.2596
REMARK 3 14 2.7601 - 2.6928 1.00 15846 143 0.2234 0.2686
REMARK 3 15 2.6928 - 2.6315 1.00 15827 137 0.2368 0.2965
REMARK 3 16 2.6315 - 2.5756 1.00 15809 146 0.2509 0.2910
REMARK 3 17 2.5756 - 2.5240 1.00 15859 145 0.2572 0.3153
REMARK 3 18 2.5240 - 2.4764 1.00 15823 140 0.2679 0.2714
REMARK 3 19 2.4764 - 2.4322 1.00 15850 139 0.2870 0.3425
REMARK 3 20 2.4322 - 2.3910 1.00 15764 140 0.3005 0.3175
REMARK 3 21 2.3910 - 2.3524 1.00 15735 146 0.3157 0.3893
REMARK 3 22 2.3524 - 2.3162 1.00 15806 141 0.3249 0.3876
REMARK 3 23 2.3162 - 2.2821 1.00 15786 141 0.3369 0.3493
REMARK 3 24 2.2821 - 2.2500 0.99 15684 140 0.3474 0.3924
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.339
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.408
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.98
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.76
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 : 0.006 52552
REMARK 3 ANGLE : 0.503 71877
REMARK 3 CHIRALITY : 0.038 7085
REMARK 3 PLANARITY : 0.004 8681
REMARK 3 DIHEDRAL : 14.902 28166
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 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: INDEXED AND INTEGRATED IMAGES FROM THE
REMARK 3 TWO DIFFRACTION EXPERIMENTS WERE MERGED TO GENERATE THE SINGLE
REMARK 3 DIFFRACTION DATASET DESCRIBED HERE.
REMARK 4
REMARK 4 5TIS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1000223850.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-NOV-15; 14-JUL-16
REMARK 200 TEMPERATURE (KELVIN) : 293; 293
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N; N
REMARK 200 RADIATION SOURCE : FREE ELECTRON LASER; FREE
REMARK 200 ELECTRON LASER
REMARK 200 BEAMLINE : XPP; MFX
REMARK 200 X-RAY GENERATOR MODEL : SLAC LCLS BEAMLINE XPP; SLAC
REMARK 200 LCLS BEAMLINE MFX
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.3051; 1.3051
REMARK 200 MONOCHROMATOR : NONE; NONE
REMARK 200 OPTICS : COMPOUND REFRACTIVE LENSES;
REMARK 200 COMPOUND REFRACTIVE LENSES
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX170-HS; RAYONIX MX170
REMARK 200 -HS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CCTBX.XFEL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 385545
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 44.280
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 158.4
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.8340
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 6.11
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 44.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 649.0
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 120.7
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 5KAI
REMARK 200
REMARK 200 REMARK: OBLONG CRYSTALS 10-20 MICROMETERS IN LENGTH
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTAL GROWTH WAS AS DESCRIBED IN
REMARK 280 KERN ET AL. 2005, BIOCHIM. BIOPHYS. ACTA-BIOENERGETICS AND
REMARK 280 IBRAHIM ET AL. 2015, STRUCT. DYN. 2 (4), 041705, SUBSTITUTING
REMARK 280 C12E8 FOR BETA-DM AND BETAINE FOR GLYCEROL, PH 6.5, BATCH MODE,
REMARK 280 TEMPERATURE 293K
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 58.93500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 155.35500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 111.57000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 155.35500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 58.93500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 111.57000
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, Z,
REMARK 350 AND CHAINS: R, a, b, c, d, e, f, h, i, j,
REMARK 350 AND CHAINS: k, l, m, o, t, u, v, y, x,
REMARK 350 AND CHAINS: z, r
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 SER A 10
REMARK 465 MET B 1
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 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 MET E 1
REMARK 465 ALA E 2
REMARK 465 GLY E 3
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 VAL F 11
REMARK 465 MET H 1
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 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 LYS M 34
REMARK 465 SER M 35
REMARK 465 SER M 36
REMARK 465 MET O -25
REMARK 465 LYS O -24
REMARK 465 TYR O -23
REMARK 465 ARG O -22
REMARK 465 ILE O -21
REMARK 465 LEU O -20
REMARK 465 MET O -19
REMARK 465 ALA O -18
REMARK 465 THR O -17
REMARK 465 LEU O -16
REMARK 465 LEU O -15
REMARK 465 ALA O -14
REMARK 465 VAL O -13
REMARK 465 CYS O -12
REMARK 465 LEU O -11
REMARK 465 GLY O -10
REMARK 465 ILE O -9
REMARK 465 PHE O -8
REMARK 465 SER O -7
REMARK 465 LEU O -6
REMARK 465 SER O -5
REMARK 465 ALA O -4
REMARK 465 PRO O -3
REMARK 465 ALA O -2
REMARK 465 PHE O -1
REMARK 465 ALA O 0
REMARK 465 ALA O 1
REMARK 465 LYS O 2
REMARK 465 LYS T 31
REMARK 465 LYS T 32
REMARK 465 MET U -29
REMARK 465 GLN U -28
REMARK 465 ARG U -27
REMARK 465 LEU U -26
REMARK 465 GLY U -25
REMARK 465 ARG U -24
REMARK 465 TRP U -23
REMARK 465 LEU U -22
REMARK 465 ALA U -21
REMARK 465 LEU U -20
REMARK 465 ALA U -19
REMARK 465 TYR U -18
REMARK 465 PHE U -17
REMARK 465 VAL U -16
REMARK 465 GLY U -15
REMARK 465 VAL U -14
REMARK 465 SER U -13
REMARK 465 LEU U -12
REMARK 465 LEU U -11
REMARK 465 GLY U -10
REMARK 465 TRP U -9
REMARK 465 ILE U -8
REMARK 465 ASN U -7
REMARK 465 TRP U -6
REMARK 465 SER U -5
REMARK 465 ALA U -4
REMARK 465 PRO U -3
REMARK 465 THR U -2
REMARK 465 LEU U -1
REMARK 465 ALA U 0
REMARK 465 ALA U 1
REMARK 465 THR U 2
REMARK 465 ALA U 3
REMARK 465 SER U 4
REMARK 465 THR U 5
REMARK 465 GLU U 6
REMARK 465 GLU U 7
REMARK 465 MET V -25
REMARK 465 LEU V -24
REMARK 465 LYS V -23
REMARK 465 LYS V -22
REMARK 465 CYS V -21
REMARK 465 VAL V -20
REMARK 465 TRP V -19
REMARK 465 LEU V -18
REMARK 465 ALA V -17
REMARK 465 VAL V -16
REMARK 465 ALA V -15
REMARK 465 LEU V -14
REMARK 465 CYS V -13
REMARK 465 LEU V -12
REMARK 465 CYS V -11
REMARK 465 LEU V -10
REMARK 465 TRP V -9
REMARK 465 GLN V -8
REMARK 465 PHE V -7
REMARK 465 THR V -6
REMARK 465 MET V -5
REMARK 465 GLY V -4
REMARK 465 THR V -3
REMARK 465 ALA V -2
REMARK 465 LEU V -1
REMARK 465 ALA V 0
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 ILE Y 19
REMARK 465 MET X 1
REMARK 465 SER X 40
REMARK 465 LEU X 41
REMARK 465 MET R 1
REMARK 465 GLN R 36
REMARK 465 LYS R 37
REMARK 465 ALA R 38
REMARK 465 LYS R 39
REMARK 465 ALA R 40
REMARK 465 ALA R 41
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 SER a 10
REMARK 465 MET b 1
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 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 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 VAL f 11
REMARK 465 MET h 1
REMARK 465 LEU h 65
REMARK 465 GLY h 66
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 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 LYS m 34
REMARK 465 SER m 35
REMARK 465 SER m 36
REMARK 465 MET o -25
REMARK 465 LYS o -24
REMARK 465 TYR o -23
REMARK 465 ARG o -22
REMARK 465 ILE o -21
REMARK 465 LEU o -20
REMARK 465 MET o -19
REMARK 465 ALA o -18
REMARK 465 THR o -17
REMARK 465 LEU o -16
REMARK 465 LEU o -15
REMARK 465 ALA o -14
REMARK 465 VAL o -13
REMARK 465 CYS o -12
REMARK 465 LEU o -11
REMARK 465 GLY o -10
REMARK 465 ILE o -9
REMARK 465 PHE o -8
REMARK 465 SER o -7
REMARK 465 LEU o -6
REMARK 465 SER o -5
REMARK 465 ALA o -4
REMARK 465 PRO o -3
REMARK 465 ALA o -2
REMARK 465 PHE o -1
REMARK 465 ALA o 0
REMARK 465 ALA o 1
REMARK 465 LYS o 2
REMARK 465 LYS t 31
REMARK 465 LYS t 32
REMARK 465 MET u -29
REMARK 465 GLN u -28
REMARK 465 ARG u -27
REMARK 465 LEU u -26
REMARK 465 GLY u -25
REMARK 465 ARG u -24
REMARK 465 TRP u -23
REMARK 465 LEU u -22
REMARK 465 ALA u -21
REMARK 465 LEU u -20
REMARK 465 ALA u -19
REMARK 465 TYR u -18
REMARK 465 PHE u -17
REMARK 465 VAL u -16
REMARK 465 GLY u -15
REMARK 465 VAL u -14
REMARK 465 SER u -13
REMARK 465 LEU u -12
REMARK 465 LEU u -11
REMARK 465 GLY u -10
REMARK 465 TRP u -9
REMARK 465 ILE u -8
REMARK 465 ASN u -7
REMARK 465 TRP u -6
REMARK 465 SER u -5
REMARK 465 ALA u -4
REMARK 465 PRO u -3
REMARK 465 THR u -2
REMARK 465 LEU u -1
REMARK 465 ALA u 0
REMARK 465 ALA u 1
REMARK 465 THR u 2
REMARK 465 ALA u 3
REMARK 465 SER u 4
REMARK 465 THR u 5
REMARK 465 GLU u 6
REMARK 465 GLU u 7
REMARK 465 MET v -25
REMARK 465 LEU v -24
REMARK 465 LYS v -23
REMARK 465 LYS v -22
REMARK 465 CYS v -21
REMARK 465 VAL v -20
REMARK 465 TRP v -19
REMARK 465 LEU v -18
REMARK 465 ALA v -17
REMARK 465 VAL v -16
REMARK 465 ALA v -15
REMARK 465 LEU v -14
REMARK 465 CYS v -13
REMARK 465 LEU v -12
REMARK 465 CYS v -11
REMARK 465 LEU v -10
REMARK 465 TRP v -9
REMARK 465 GLN v -8
REMARK 465 PHE v -7
REMARK 465 THR v -6
REMARK 465 MET v -5
REMARK 465 GLY v -4
REMARK 465 THR v -3
REMARK 465 ALA v -2
REMARK 465 LEU v -1
REMARK 465 ALA v 0
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 MET x 1
REMARK 465 SER x 40
REMARK 465 LEU x 41
REMARK 465 MET r 1
REMARK 465 GLN r 36
REMARK 465 LYS r 37
REMARK 465 ALA r 38
REMARK 465 LYS r 39
REMARK 465 ALA r 40
REMARK 465 ALA r 41
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 GLU b 489 CG CD OE1 OE2
REMARK 470 HIS d 336 O
REMARK 470 THR x 2 OG1 CG2
REMARK 470 LEU r 6 CG CD1 CD2
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 OE2 GLU A 189 MN1 OEX A 601 1.68
REMARK 500 SG CYS v 40 CBC HEM v 201 2.00
REMARK 500 SG CYS V 40 CBC HEM V 201 2.02
REMARK 500 OH TYR u 55 O HOH u 201 2.07
REMARK 500 O ILE u 49 O HOH u 201 2.07
REMARK 500 O GLY J 31 O HOH J 201 2.17
REMARK 500 O LEU I 37 O HOH I 201 2.17
REMARK 500 O HOH b 740 O HOH b 770 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 VAL A 30 -81.03 -93.74
REMARK 500 ILE A 259 -97.28 -114.12
REMARK 500 ASP B 49 79.36 -155.98
REMARK 500 PHE B 162 67.45 -151.91
REMARK 500 ASP B 313 53.42 -90.96
REMARK 500 PRO B 488 35.24 -72.95
REMARK 500 THR B 504 74.76 -110.23
REMARK 500 ASN C 25 -114.24 55.92
REMARK 500 ASP C 107 111.74 -160.57
REMARK 500 TRP C 223 -135.39 57.19
REMARK 500 THR C 295 -64.36 -98.93
REMARK 500 THR C 355 2.25 -68.70
REMARK 500 ASN C 382 -24.42 -140.08
REMARK 500 SER C 416 -56.73 179.90
REMARK 500 VAL D 30 -80.68 -102.64
REMARK 500 SER D 65 15.60 -159.33
REMARK 500 PRO D 140 40.84 -92.16
REMARK 500 SER D 295 73.10 -102.55
REMARK 500 ALA D 351 -57.10 67.67
REMARK 500 THR E 5 -75.32 -87.85
REMARK 500 ASN H 15 58.54 -118.66
REMARK 500 LYS I 33 -91.34 -116.35
REMARK 500 LYS I 35 79.93 -113.91
REMARK 500 ASP I 36 -40.73 -157.00
REMARK 500 GLN M 32 -82.81 -72.78
REMARK 500 LYS O 59 -74.45 61.18
REMARK 500 ARG O 73 -156.21 64.05
REMARK 500 ASN O 132 75.41 58.61
REMARK 500 LEU O 164 -70.22 -87.16
REMARK 500 THR U 19 -168.45 -104.10
REMARK 500 ASN U 99 104.72 -160.76
REMARK 500 TYR U 103 -103.56 -121.91
REMARK 500 ILE V 45 -167.57 -100.11
REMARK 500 ASN V 49 78.05 -161.21
REMARK 500 ASP V 67 35.98 -89.41
REMARK 500 LEU Y 22 30.06 -99.93
REMARK 500 ILE X 3 86.37 58.75
REMARK 500 ASP X 35 79.23 -107.22
REMARK 500 VAL a 30 -85.56 -89.40
REMARK 500 LEU a 159 -54.23 -129.09
REMARK 500 ILE a 259 -91.70 -116.40
REMARK 500 ARG b 127 -73.13 -73.21
REMARK 500 PHE b 162 67.68 -150.61
REMARK 500 GLU b 485 44.31 -88.67
REMARK 500 THR b 504 42.18 -95.96
REMARK 500 ILE c 134 -57.95 -121.49
REMARK 500 GLU c 221 -57.84 -120.57
REMARK 500 TRP c 223 -134.01 58.20
REMARK 500 THR c 295 -61.05 -104.24
REMARK 500 THR c 355 3.33 -68.02
REMARK 500
REMARK 500 THIS ENTRY HAS 85 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH E 214 DISTANCE = 5.97 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 CLA A 609
REMARK 610 SQD A 612
REMARK 610 LHG A 614
REMARK 610 LMG B 620
REMARK 610 LMG B 621
REMARK 610 LMG B 626
REMARK 610 LMG C 501
REMARK 610 DGD C 517
REMARK 610 DGD C 518
REMARK 610 DGD C 519
REMARK 610 LMG C 520
REMARK 610 LMG C 521
REMARK 610 LMG D 407
REMARK 610 SQD D 408
REMARK 610 SQD D 409
REMARK 610 DGD H 102
REMARK 610 SQD L 101
REMARK 610 LMG a 614
REMARK 610 LHG a 616
REMARK 610 LHG a 617
REMARK 610 CLA b 616
REMARK 610 LMG b 620
REMARK 610 SQD b 621
REMARK 610 CLA c 504
REMARK 610 CLA c 508
REMARK 610 DGD c 516
REMARK 610 DGD c 517
REMARK 610 DGD c 518
REMARK 610 LMG c 519
REMARK 610 LMG c 520
REMARK 610 LMG d 407
REMARK 610 LMG d 408
REMARK 610 SQD f 101
REMARK 610 DGD h 102
REMARK 610 LMG m 102
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX A 601 CA1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 170 OD1
REMARK 620 2 OEX A 601 O1 139.7
REMARK 620 3 OEX A 601 O2 78.0 63.3
REMARK 620 4 OEX A 601 O5 95.9 81.4 69.4
REMARK 620 5 GLU A 189 OE1 152.1 68.2 129.1 89.2
REMARK 620 6 ALA A 344 O 81.8 75.7 71.2 140.1 111.2
REMARK 620 7 HOH A 772 O 83.5 132.0 135.1 72.4 71.9 145.4
REMARK 620 8 HOH A 714 O 91.4 114.7 147.2 143.3 69.1 76.6 72.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX A 601 MN4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 170 OD2
REMARK 620 2 OEX A 601 O5 98.2
REMARK 620 3 OEX A 601 O4 97.2 88.5
REMARK 620 4 GLU A 333 OE2 167.0 85.6 95.4
REMARK 620 5 HOH A 738 O 92.9 166.3 98.0 81.9
REMARK 620 6 HOH A 723 O 79.7 85.2 172.5 88.2 89.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 A 602 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 215 NE2
REMARK 620 2 HIS A 272 NE2 94.9
REMARK 620 3 HIS D 214 NE2 102.4 90.4
REMARK 620 4 HIS D 268 NE2 85.3 175.3 94.2
REMARK 620 5 BCT A 605 O2 99.2 89.8 158.2 85.5
REMARK 620 6 BCT A 605 O1 159.6 90.9 97.1 87.3 61.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX A 601 MN1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 332 NE2
REMARK 620 2 OEX A 601 O1 164.6
REMARK 620 3 OEX A 601 O5 101.6 90.0
REMARK 620 4 OEX A 601 O3 84.4 88.5 77.0
REMARK 620 5 ASP A 342 OD2 81.5 83.9 157.1 80.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX A 601 MN3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 333 OE1
REMARK 620 2 OEX A 601 O2 157.6
REMARK 620 3 OEX A 601 O3 76.2 89.6
REMARK 620 4 OEX A 601 O4 103.4 89.9 177.0
REMARK 620 5 OEX A 601 O5 94.9 102.1 88.8 94.2
REMARK 620 6 GLU C 354 OE2 84.9 77.0 86.8 90.2 175.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX A 601 MN2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 342 OD1
REMARK 620 2 OEX A 601 O1 88.7
REMARK 620 3 OEX A 601 O2 167.7 100.5
REMARK 620 4 OEX A 601 O3 94.6 90.5 93.5
REMARK 620 5 ALA A 344 OXT 88.8 82.1 84.5 171.8
REMARK 620 6 GLU C 354 OE1 83.5 172.1 87.0 91.8 96.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C 512 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C 39 OD1
REMARK 620 2 CLA C 512 NA 96.2
REMARK 620 3 CLA C 512 NB 95.1 91.7
REMARK 620 4 CLA C 512 NC 88.5 174.3 91.1
REMARK 620 5 CLA C 512 ND 89.6 90.5 174.6 86.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM E 101 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 23 NE2
REMARK 620 2 HEM E 101 NA 93.7
REMARK 620 3 HEM E 101 NB 106.7 89.3
REMARK 620 4 HEM E 101 NC 89.9 176.3 89.3
REMARK 620 5 HEM E 101 ND 68.2 91.4 174.9 90.3
REMARK 620 6 HIS F 24 NE2 155.4 72.6 93.8 104.2 91.2
REMARK 620 N 1 2 3 4 5
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 41 NE2
REMARK 620 2 HEM V 201 NA 87.8
REMARK 620 3 HEM V 201 NB 91.1 90.3
REMARK 620 4 HEM V 201 NC 90.8 178.6 89.8
REMARK 620 5 HEM V 201 ND 84.4 89.3 175.4 90.5
REMARK 620 6 HIS V 92 NE2 178.7 93.0 87.9 88.5 96.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 601 CA1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP a 170 OD1
REMARK 620 2 OEX a 601 O1 137.4
REMARK 620 3 OEX a 601 O2 72.5 68.9
REMARK 620 4 OEX a 601 O5 102.1 81.0 69.8
REMARK 620 5 GLU a 189 OE1 150.2 69.8 137.2 93.0
REMARK 620 6 ALA a 344 O 81.4 69.7 71.2 137.5 104.5
REMARK 620 7 HOH a 738 O 93.0 103.7 138.0 151.9 63.9 67.8
REMARK 620 8 HOH a 779 O 87.1 133.7 135.1 76.3 71.6 145.9 80.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 601 MN4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP a 170 OD2
REMARK 620 2 OEX a 601 O5 100.2
REMARK 620 3 OEX a 601 O4 95.7 94.6
REMARK 620 4 GLU a 333 OE2 175.2 84.5 85.1
REMARK 620 5 HOH a 772 O 90.0 88.1 173.1 88.9
REMARK 620 6 HOH a 720 O 94.0 165.6 86.3 81.3 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 601 MN1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU a 189 OE2
REMARK 620 2 OEX a 601 O1 81.6
REMARK 620 3 OEX a 601 O5 100.9 92.3
REMARK 620 4 OEX a 601 O3 173.5 92.2 77.6
REMARK 620 5 HIS a 332 NE2 95.9 169.5 98.2 90.6
REMARK 620 6 ASP a 342 OD2 93.2 84.0 164.8 87.8 86.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 a 602 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS a 215 NE2
REMARK 620 2 HIS a 272 NE2 96.9
REMARK 620 3 HIS d 214 NE2 106.3 87.1
REMARK 620 4 HIS d 268 NE2 80.9 176.9 95.5
REMARK 620 5 BCT a 605 O1 151.1 93.9 100.8 87.0
REMARK 620 6 BCT a 605 O2 93.3 84.5 159.4 93.5 61.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 601 MN3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU a 333 OE1
REMARK 620 2 OEX a 601 O2 170.1
REMARK 620 3 OEX a 601 O3 79.2 97.2
REMARK 620 4 OEX a 601 O4 91.9 92.2 170.5
REMARK 620 5 OEX a 601 O5 95.9 93.0 87.0 90.7
REMARK 620 6 GLU c 354 OE2 82.5 87.9 80.7 101.6 167.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 601 MN2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP a 342 OD1
REMARK 620 2 OEX a 601 O1 82.3
REMARK 620 3 OEX a 601 O2 177.6 97.1
REMARK 620 4 OEX a 601 O3 92.6 87.4 89.6
REMARK 620 5 ALA a 344 OXT 89.7 92.1 88.0 177.5
REMARK 620 6 GLU c 354 OE1 81.5 163.8 99.2 92.6 88.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA c 511 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN c 39 OD1
REMARK 620 2 CLA c 511 NA 95.0
REMARK 620 3 CLA c 511 NB 98.7 91.6
REMARK 620 4 CLA c 511 NC 90.1 174.0 90.9
REMARK 620 5 CLA c 511 ND 86.7 90.7 174.0 86.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM e 101 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS e 23 NE2
REMARK 620 2 HEM e 101 NA 96.7
REMARK 620 3 HEM e 101 NB 101.5 89.3
REMARK 620 4 HEM e 101 NC 88.4 174.9 90.3
REMARK 620 5 HEM e 101 ND 73.2 89.9 174.5 90.9
REMARK 620 6 HIS f 24 NE2 168.5 78.5 88.9 96.4 96.2
REMARK 620 N 1 2 3 4 5
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 41 NE2
REMARK 620 2 HEM v 201 NA 89.9
REMARK 620 3 HEM v 201 NB 90.7 89.4
REMARK 620 4 HEM v 201 NC 85.9 175.7 89.8
REMARK 620 5 HEM v 201 ND 81.9 89.6 172.6 90.7
REMARK 620 6 HIS v 92 NE2 170.9 91.2 98.3 93.1 89.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA A 607 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 743 O
REMARK 620 2 CLA A 607 NA 84.4
REMARK 620 3 CLA A 607 NB 100.9 91.5
REMARK 620 4 CLA A 607 NC 98.1 175.6 91.6
REMARK 620 5 CLA A 607 ND 82.8 90.7 175.9 86.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA A 613 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 732 O
REMARK 620 2 CLA A 613 NA 79.1
REMARK 620 3 CLA A 613 NB 100.6 91.7
REMARK 620 4 CLA A 613 NC 104.6 174.8 91.0
REMARK 620 5 CLA A 613 ND 84.5 90.6 174.6 86.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 733 O
REMARK 620 2 CLA B 601 NA 81.8
REMARK 620 3 CLA B 601 NB 98.1 91.7
REMARK 620 4 CLA B 601 NC 101.4 175.3 91.3
REMARK 620 5 CLA B 601 ND 85.9 90.7 175.6 86.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B 607 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 772 O
REMARK 620 2 CLA B 607 NA 85.3
REMARK 620 3 CLA B 607 NB 97.3 91.7
REMARK 620 4 CLA B 607 NC 99.1 174.5 91.0
REMARK 620 5 CLA B 607 ND 87.6 90.4 174.8 86.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B 610 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 723 O
REMARK 620 2 CLA B 610 NA 88.6
REMARK 620 3 CLA B 610 NB 86.4 91.5
REMARK 620 4 CLA B 610 NC 96.0 174.6 91.5
REMARK 620 5 CLA B 610 ND 97.7 90.5 175.5 86.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C 505 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 661 O
REMARK 620 2 CLA C 505 NA 83.7
REMARK 620 3 CLA C 505 NB 98.3 91.6
REMARK 620 4 CLA C 505 NC 100.0 175.1 91.1
REMARK 620 5 CLA C 505 ND 86.3 90.4 175.2 86.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C 508 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 611 O
REMARK 620 2 CLA C 508 NA 84.3
REMARK 620 3 CLA C 508 NB 92.0 91.6
REMARK 620 4 CLA C 508 NC 100.8 174.2 91.0
REMARK 620 5 CLA C 508 ND 93.3 90.7 174.4 86.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA a 607 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH a 749 O
REMARK 620 2 CLA a 607 NA 84.3
REMARK 620 3 CLA a 607 NB 100.8 91.5
REMARK 620 4 CLA a 607 NC 98.9 175.3 91.3
REMARK 620 5 CLA a 607 ND 83.5 90.8 175.3 86.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA a 615 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH a 759 O
REMARK 620 2 CLA a 615 NA 84.3
REMARK 620 3 CLA a 615 NB 93.4 91.5
REMARK 620 4 CLA a 615 NC 99.3 175.3 91.3
REMARK 620 5 CLA a 615 ND 90.8 90.7 175.4 86.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA b 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH b 758 O
REMARK 620 2 CLA b 601 NA 82.2
REMARK 620 3 CLA b 601 NB 89.5 91.7
REMARK 620 4 CLA b 601 NC 101.1 175.6 91.3
REMARK 620 5 CLA b 601 ND 94.0 90.7 176.0 86.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA b 607 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH b 792 O
REMARK 620 2 CLA b 607 NA 87.2
REMARK 620 3 CLA b 607 NB 92.4 91.6
REMARK 620 4 CLA b 607 NC 97.8 174.2 91.1
REMARK 620 5 CLA b 607 ND 93.1 90.7 174.2 86.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA b 610 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH b 719 O
REMARK 620 2 CLA b 610 NA 93.6
REMARK 620 3 CLA b 610 NB 86.8 91.7
REMARK 620 4 CLA b 610 NC 90.7 174.9 91.2
REMARK 620 5 CLA b 610 ND 96.7 90.7 175.6 86.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA c 504 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH c 646 O
REMARK 620 2 CLA c 504 NA 83.5
REMARK 620 3 CLA c 504 NB 97.2 91.8
REMARK 620 4 CLA c 504 NC 99.6 175.5 91.0
REMARK 620 5 CLA c 504 ND 86.9 90.5 175.5 86.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA c 507 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH c 645 O
REMARK 620 2 CLA c 507 NA 82.5
REMARK 620 3 CLA c 507 NB 90.7 92.1
REMARK 620 4 CLA c 507 NC 102.1 174.5 90.8
REMARK 620 5 CLA c 507 ND 94.2 90.4 174.7 86.3
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OEX A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE2 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 A 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG A 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD A 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG A 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG B 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD B 624
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD B 625
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 626
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 D 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG D 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG D 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD D 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD D 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM E 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR H 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD H 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR K 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD L 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG L 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR T 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM V 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR Y 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OEX a 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE2 a 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT a 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO a 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO a 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR a 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 a 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD a 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG a 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG a 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG a 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG b 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD b 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 522
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR d 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 d 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG d 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG d 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG d 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG d 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM e 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD f 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR h 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD h 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG l 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG m 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR t 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide HEM v 201 and CYS v
REMARK 800 37
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide HEM v 201 and CYS v
REMARK 800 40
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide HEM v 201 and CYS v
REMARK 800 37
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5KAF RELATED DB: PDB
REMARK 900 CORRESPONDING DARK STATE RT STRUCTURE OF PHOTOSYSTEM II
REMARK 900 RELATED ID: 5KAI RELATED DB: PDB
REMARK 900 CORRESPONDING 2F STATE, NH3-BOUND RT STRUCTURE OF PHOTOSYSTEM II
DBREF 5TIS A 1 344 UNP P0A444 PSBA1_THEEB 1 344
DBREF 5TIS B 1 510 UNP Q8DIQ1 PSBB_THEEB 1 510
DBREF 5TIS C 13 473 UNP Q8DIF8 PSBC_THEEB 1 461
DBREF 5TIS D 1 352 UNP Q8CM25 PSBD_THEEB 1 352
DBREF 5TIS E 1 84 UNP Q8DIP0 PSBE_THEEB 1 84
DBREF 5TIS F 1 45 UNP Q8DIN9 PSBF_THEEB 1 45
DBREF 5TIS H 1 66 UNP Q8DJ43 PSBH_THEEB 1 66
DBREF 5TIS I 1 38 UNP Q8DJZ6 PSBI_THEEB 1 38
DBREF 5TIS J 1 40 UNP P59087 PSBJ_THEEB 1 40
DBREF 5TIS K 1 46 UNP Q9F1K9 PSBK_THEEB 1 46
DBREF 5TIS L 1 37 UNP Q8DIN8 PSBL_THEEB 1 37
DBREF 5TIS M 1 36 UNP Q8DHA7 PSBM_THEEB 1 36
DBREF 5TIS O -25 246 UNP P0A431 PSBO_THEEB 1 272
DBREF 5TIS T 1 32 UNP Q8DIQ0 PSBT_THEEB 1 32
DBREF 5TIS U -29 104 UNP Q9F1L5 PSBU_THEEB 1 134
DBREF 5TIS V -25 137 UNP P0A386 CY550_THEEB 1 163
DBREF 5TIS Y 1 46 UNP Q8DJI1 YCF12_THEEB 1 46
DBREF 5TIS X 1 41 UNP Q9F1R6 PSBX_THEEB 1 41
DBREF 5TIS Z 1 62 UNP Q8DHJ2 PSBZ_THEEB 1 62
DBREF 5TIS R 1 41 UNP Q8DKM3 PSBY_THEEB 1 41
DBREF 5TIS a 1 344 UNP P0A444 PSBA1_THEEB 1 344
DBREF 5TIS b 1 510 UNP Q8DIQ1 PSBB_THEEB 1 510
DBREF 5TIS c 13 473 UNP Q8DIF8 PSBC_THEEB 1 461
DBREF 5TIS d 1 352 UNP Q8CM25 PSBD_THEEB 1 352
DBREF 5TIS e 1 84 UNP Q8DIP0 PSBE_THEEB 1 84
DBREF 5TIS f 1 45 UNP Q8DIN9 PSBF_THEEB 1 45
DBREF 5TIS h 1 66 UNP Q8DJ43 PSBH_THEEB 1 66
DBREF 5TIS i 1 38 UNP Q8DJZ6 PSBI_THEEB 1 38
DBREF 5TIS j 1 40 UNP P59087 PSBJ_THEEB 1 40
DBREF 5TIS k 1 46 UNP Q9F1K9 PSBK_THEEB 1 46
DBREF 5TIS l 1 37 UNP Q8DIN8 PSBL_THEEB 1 37
DBREF 5TIS m 1 36 UNP Q8DHA7 PSBM_THEEB 1 36
DBREF 5TIS o -25 246 UNP P0A431 PSBO_THEEB 1 272
DBREF 5TIS t 1 32 UNP Q8DIQ0 PSBT_THEEB 1 32
DBREF 5TIS u -29 104 UNP Q9F1L5 PSBU_THEEB 1 134
DBREF 5TIS v -25 137 UNP P0A386 CY550_THEEB 1 163
DBREF 5TIS y 1 46 UNP Q8DJI1 YCF12_THEEB 1 46
DBREF 5TIS x 1 41 UNP Q9F1R6 PSBX_THEEB 1 41
DBREF 5TIS z 1 62 UNP Q8DHJ2 PSBZ_THEEB 1 62
DBREF 5TIS r 1 41 UNP Q8DKM3 PSBY_THEEB 1 41
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 FME 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 FME 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 FME 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 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 R 41 MET ASP TRP ARG VAL LEU VAL VAL LEU LEU PRO VAL LEU
SEQRES 2 R 41 LEU ALA ALA GLY TRP ALA VAL ARG ASN ILE LEU PRO TYR
SEQRES 3 R 41 ALA VAL LYS GLN VAL GLN LYS LEU LEU GLN LYS ALA LYS
SEQRES 4 R 41 ALA ALA
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 FME 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 FME 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 FME 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 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 r 41 MET ASP TRP ARG VAL LEU VAL VAL LEU LEU PRO VAL LEU
SEQRES 2 r 41 LEU ALA ALA GLY TRP ALA VAL ARG ASN ILE LEU PRO TYR
SEQRES 3 r 41 ALA VAL LYS GLN VAL GLN LYS LEU LEU GLN LYS ALA LYS
SEQRES 4 r 41 ALA ALA
MODRES 5TIS FME I 1 MET MODIFIED RESIDUE
MODRES 5TIS FME M 1 MET MODIFIED RESIDUE
MODRES 5TIS FME T 1 MET MODIFIED RESIDUE
MODRES 5TIS FME i 1 MET MODIFIED RESIDUE
MODRES 5TIS FME m 1 MET MODIFIED RESIDUE
MODRES 5TIS FME t 1 MET MODIFIED RESIDUE
HET FME I 1 10
HET FME M 1 10
HET FME T 1 10
HET FME i 1 10
HET FME m 1 10
HET FME t 1 10
HET OEX A 601 10
HET FE2 A 602 1
HET CL A 603 1
HET CL A 604 1
HET BCT A 605 4
HET CLA A 606 65
HET CLA A 607 65
HET PHO A 608 64
HET CLA A 609 54
HET BCR A 610 40
HET PL9 A 611 55
HET SQD A 612 52
HET CLA A 613 65
HET LHG A 614 47
HET UNL A 615 9
HET SQD A 616 54
HET UNL A 617 20
HET LHG A 618 49
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 CLA B 616 65
HET BCR B 617 40
HET BCR B 618 40
HET BCR B 619 40
HET LMG B 620 51
HET LMG B 621 51
HET UNL B 622 11
HET LHG B 623 49
HET SQD B 624 54
HET SQD B 625 54
HET LMG B 626 51
HET UNL B 627 15
HET LMG C 501 48
HET CLA C 502 65
HET CLA C 503 65
HET CLA C 504 65
HET CLA C 505 65
HET CLA C 506 65
HET CLA C 507 65
HET CLA C 508 65
HET CLA C 509 65
HET CLA C 510 65
HET CLA C 511 65
HET CLA C 512 65
HET CLA C 513 65
HET CLA C 514 65
HET BCR C 515 40
HET BCR C 516 40
HET DGD C 517 62
HET DGD C 518 62
HET DGD C 519 62
HET LMG C 520 48
HET LMG C 521 51
HET UNL C 522 17
HET UNL C 523 16
HET PHO D 401 64
HET CLA D 402 65
HET CLA D 403 65
HET BCR D 404 40
HET PL9 D 405 55
HET LHG D 406 49
HET LMG D 407 51
HET SQD D 408 43
HET SQD D 409 47
HET UNL D 410 18
HET UNL D 411 10
HET HEM E 101 43
HET UNL E 102 12
HET BCR H 101 40
HET DGD H 102 62
HET UNL H 103 7
HET UNL I 101 7
HET UNL I 102 20
HET UNL J 101 11
HET UNL J 102 12
HET BCR K 101 40
HET SQD L 101 49
HET LHG L 102 49
HET UNL M 101 15
HET UNL M 102 17
HET BCR T 101 40
HET UNL T 102 14
HET UNL T 103 12
HET HEM V 201 43
HET BCR Y 101 40
HET OEX a 601 10
HET FE2 a 602 1
HET CL a 603 1
HET CL a 604 1
HET BCT a 605 4
HET CLA a 606 65
HET CLA a 607 65
HET PHO a 608 64
HET PHO a 609 64
HET CLA a 610 65
HET BCR a 611 40
HET PL9 a 612 55
HET SQD a 613 54
HET LMG a 614 51
HET CLA a 615 65
HET LHG a 616 39
HET LHG a 617 42
HET UNL a 618 17
HET UNL a 619 12
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 606 129
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 47
HET BCR b 617 40
HET BCR b 618 40
HET BCR b 619 40
HET LMG b 620 51
HET SQD b 621 40
HET UNL b 622 17
HET UNL b 623 11
HET CLA c 501 65
HET CLA c 502 65
HET CLA c 503 65
HET CLA c 504 60
HET CLA c 505 65
HET CLA c 506 65
HET CLA c 507 65
HET CLA c 508 64
HET CLA c 509 65
HET CLA c 510 65
HET CLA c 511 65
HET CLA c 512 65
HET CLA c 513 65
HET BCR c 514 40
HET BCR c 515 40
HET DGD c 516 62
HET DGD c 517 62
HET DGD c 518 62
HET LMG c 519 37
HET LMG c 520 34
HET BCR c 521 40
HET BCR c 522 40
HET UNL c 523 8
HET UNL c 524 20
HET UNL c 525 12
HET CLA d 401 65
HET CLA d 402 65
HET BCR d 403 40
HET PL9 d 404 55
HET LHG d 405 49
HET LHG d 406 49
HET LMG d 407 51
HET LMG d 408 38
HET UNL d 409 17
HET HEM e 101 43
HET SQD f 101 41
HET BCR h 101 40
HET DGD h 102 62
HET UNL i 101 20
HET UNL j 801 15
HET UNL j 802 12
HET LHG l 101 49
HET UNL m 101 9
HET LMG m 102 51
HET UNL m 103 16
HET BCR t 101 40
HET UNL t 102 18
HET HEM v 201 43
HET UNL x 101 16
HETNAM FME N-FORMYLMETHIONINE
HETNAM OEX CA-MN4-O5 CLUSTER
HETNAM FE2 FE (II) ION
HETNAM CL CHLORIDE ION
HETNAM BCT BICARBONATE ION
HETNAM CLA CHLOROPHYLL A
HETNAM PHO PHEOPHYTIN A
HETNAM BCR BETA-CAROTENE
HETNAM PL9 2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,
HETNAM 2 PL9 6,10,14,18,22,26,30,34-HEXATRIACONTANONAENYL-2,5-
HETNAM 3 PL9 CYCLOHEXADIENE-1,4-DIONE-2,3-DIMETHYL-5-SOLANESYL-1,4-
HETNAM 4 PL9 BENZOQUINONE
HETNAM SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-
HETNAM 2 SQD GLUCOPYRANOSYL]-SN-GLYCEROL
HETNAM LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE
HETNAM UNL UNKNOWN LIGAND
HETNAM LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE
HETNAM DGD DIGALACTOSYL DIACYL GLYCEROL (DGDG)
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN PL9 PLASTOQUINONE 9
HETSYN SQD SULFOQUINOVOSYLDIACYLGLYCEROL
HETSYN HEM HEME
FORMUL 8 FME 6(C6 H11 N O3 S)
FORMUL 41 OEX 2(CA MN4 O5)
FORMUL 42 FE2 2(FE 2+)
FORMUL 43 CL 4(CL 1-)
FORMUL 45 BCT 2(C H O3 1-)
FORMUL 46 CLA 70(C55 H72 MG N4 O5 2+)
FORMUL 48 PHO 4(C55 H74 N4 O5)
FORMUL 50 BCR 22(C40 H56)
FORMUL 51 PL9 4(C53 H80 O2)
FORMUL 52 SQD 10(C41 H78 O12 S)
FORMUL 54 LHG 10(C38 H75 O10 P)
FORMUL 78 LMG 14(C45 H86 O10)
FORMUL 02 DGD 8(C51 H96 O15)
FORMUL 20 HEM 4(C34 H32 FE N4 O4)
FORMUL 30 HOH *1179(H2 O)
HELIX 1 AA1 ASN A 12 THR A 22 1 11
HELIX 2 AA2 VAL A 30 ALA A 55 1 26
HELIX 3 AA3 SER A 70 GLY A 74 5 5
HELIX 4 AA4 PRO A 95 ALA A 99 5 5
HELIX 5 AA5 SER A 101 ASN A 108 1 8
HELIX 6 AA6 GLY A 109 LEU A 137 1 29
HELIX 7 AA7 TRP A 142 LEU A 159 1 18
HELIX 8 AA8 LEU A 159 GLY A 166 1 8
HELIX 9 AA9 SER A 167 GLY A 171 5 5
HELIX 10 AB1 ILE A 176 ASN A 191 1 16
HELIX 11 AB2 ILE A 192 MET A 194 5 3
HELIX 12 AB3 HIS A 195 SER A 222 1 28
HELIX 13 AB4 SER A 232 TYR A 237 5 6
HELIX 14 AB5 ASN A 247 ILE A 259 1 13
HELIX 15 AB6 PHE A 260 SER A 264 5 5
HELIX 16 AB7 ASN A 267 ALA A 294 1 28
HELIX 17 AB8 THR A 316 HIS A 332 1 17
HELIX 18 AB9 PRO B 4 ILE B 13 5 10
HELIX 19 AC1 ASP B 15 PHE B 45 1 31
HELIX 20 AC2 PRO B 54 GLN B 58 5 5
HELIX 21 AC3 VAL B 62 LEU B 69 1 8
HELIX 22 AC4 SER B 92 TYR B 117 1 26
HELIX 23 AC5 LEU B 120 ARG B 124 5 5
HELIX 24 AC6 ASP B 134 PHE B 156 1 23
HELIX 25 AC7 GLY B 186 ASN B 191 5 6
HELIX 26 AC8 ASN B 194 VAL B 219 1 26
HELIX 27 AC9 PRO B 222 LEU B 229 1 8
HELIX 28 AD1 ASN B 233 GLY B 259 1 27
HELIX 29 AD2 PRO B 264 GLY B 269 1 6
HELIX 30 AD3 ARG B 272 SER B 277 1 6
HELIX 31 AD4 SER B 278 SER B 294 1 17
HELIX 32 AD5 THR B 297 ALA B 304 1 8
HELIX 33 AD6 PRO B 306 ASP B 313 1 8
HELIX 34 AD7 TYR B 314 ASN B 318 5 5
HELIX 35 AD8 PRO B 329 GLY B 333 5 5
HELIX 36 AD9 SER B 391 GLY B 396 1 6
HELIX 37 AE1 ASP B 413 ILE B 425 1 13
HELIX 38 AE2 SER B 446 PHE B 475 1 30
HELIX 39 AE3 ARG B 476 PHE B 479 5 4
HELIX 40 AE4 ASP C 27 GLY C 32 1 6
HELIX 41 AE5 ALA C 34 ILE C 43 5 10
HELIX 42 AE6 LEU C 45 HIS C 74 1 30
HELIX 43 AE7 PRO C 80 GLN C 84 5 5
HELIX 44 AE8 LEU C 88 LEU C 95 1 8
HELIX 45 AE9 GLY C 100 GLU C 104 5 5
HELIX 46 AF1 THR C 108 ARG C 135 1 28
HELIX 47 AF2 ASP C 153 PHE C 182 1 30
HELIX 48 AF3 ASP C 205 LYS C 215 1 11
HELIX 49 AF4 GLY C 222 VAL C 227 5 6
HELIX 50 AF5 ASN C 229 THR C 254 1 26
HELIX 51 AF6 PHE C 257 PHE C 264 1 8
HELIX 52 AF7 SER C 267 ASN C 293 1 27
HELIX 53 AF8 PRO C 298 GLY C 303 1 6
HELIX 54 AF9 THR C 305 LEU C 324 1 20
HELIX 55 AG1 GLY C 353 TRP C 359 5 7
HELIX 56 AG2 LEU C 366 PRO C 368 5 3
HELIX 57 AG3 ASP C 376 ASP C 383 1 8
HELIX 58 AG4 GLN C 385 THR C 397 1 13
HELIX 59 AG5 SER C 421 GLY C 454 1 34
HELIX 60 AG6 ASP C 460 MET C 469 5 10
HELIX 61 AG7 GLY D 13 LYS D 23 1 11
HELIX 62 AG8 SER D 33 VAL D 55 1 23
HELIX 63 AG9 SER D 66 GLY D 70 5 5
HELIX 64 AH1 ALA D 82 GLY D 86 5 5
HELIX 65 AH2 ASP D 100 LEU D 107 1 8
HELIX 66 AH3 GLY D 108 GLY D 137 1 30
HELIX 67 AH4 PRO D 140 PHE D 146 1 7
HELIX 68 AH5 PHE D 146 LEU D 158 1 13
HELIX 69 AH6 LEU D 158 GLN D 164 1 7
HELIX 70 AH7 SER D 166 ALA D 170 5 5
HELIX 71 AH8 VAL D 175 ASN D 190 1 16
HELIX 72 AH9 TRP D 191 LEU D 193 5 3
HELIX 73 AI1 ASN D 194 ASN D 220 1 27
HELIX 74 AI2 SER D 245 PHE D 257 1 13
HELIX 75 AI3 ASN D 263 LEU D 291 1 29
HELIX 76 AI4 PHE D 298 ASP D 308 1 11
HELIX 77 AI5 THR D 313 GLN D 334 1 22
HELIX 78 AI6 PRO D 335 ASN D 338 5 4
HELIX 79 AI7 PRO D 342 LEU D 346 5 5
HELIX 80 AI8 PRO E 9 THR E 15 1 7
HELIX 81 AI9 SER E 16 THR E 40 1 25
HELIX 82 AJ1 GLY E 41 GLY E 48 1 8
HELIX 83 AJ2 GLU E 71 LYS E 84 1 14
HELIX 84 AJ3 THR F 17 GLN F 41 1 25
HELIX 85 AJ4 THR H 5 LEU H 11 1 7
HELIX 86 AJ5 ARG H 12 SER H 16 5 5
HELIX 87 AJ6 THR H 27 ASN H 50 1 24
HELIX 88 AJ7 SER H 61 LEU H 65 5 5
HELIX 89 AJ8 GLU I 2 SER I 25 1 24
HELIX 90 AJ9 GLY I 26 ARG I 30 5 5
HELIX 91 AK1 PRO J 9 ALA J 32 1 24
HELIX 92 AK2 PRO K 12 ILE K 17 5 6
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 GLY K 44 1 18
HELIX 96 AK6 ASN L 13 ASN L 37 1 25
HELIX 97 AK7 LEU M 6 SER M 31 1 26
HELIX 98 AK8 THR O 6 VAL O 11 1 6
HELIX 99 AK9 GLY O 14 LYS O 18 5 5
HELIX 100 AL1 LEU O 182 VAL O 187 1 6
HELIX 101 AL2 GLU T 2 PHE T 23 1 22
HELIX 102 AL3 ASN U 11 LEU U 17 1 7
HELIX 103 AL4 GLY U 18 GLU U 23 5 6
HELIX 104 AL5 ASN U 31 TYR U 38 5 8
HELIX 105 AL6 PRO U 43 ASN U 52 1 10
HELIX 106 AL7 SER U 57 ILE U 64 5 8
HELIX 107 AL8 THR U 68 GLU U 77 1 10
HELIX 108 AL9 ASN U 78 GLU U 80 5 3
HELIX 109 AM1 GLU U 88 GLU U 93 1 6
HELIX 110 AM2 GLY U 94 ASP U 96 5 3
HELIX 111 AM3 THR V 22 CYS V 37 1 16
HELIX 112 AM4 CYS V 37 VAL V 42 1 6
HELIX 113 AM5 GLY V 43 ILE V 45 5 3
HELIX 114 AM6 ARG V 55 ALA V 62 1 8
HELIX 115 AM7 ASN V 68 ASN V 78 1 11
HELIX 116 AM8 PHE V 101 LEU V 107 5 7
HELIX 117 AM9 THR V 108 GLY V 127 1 20
HELIX 118 AN1 ASP V 128 TRP V 130 5 3
HELIX 119 AN2 GLY V 133 TYR V 137 5 5
HELIX 120 AN3 GLN Y 21 ARG Y 43 1 23
HELIX 121 AN4 THR X 4 ASP X 35 1 32
HELIX 122 AN5 THR Z 2 ALA Z 28 1 27
HELIX 123 AN6 TRP Z 33 PHE Z 59 1 27
HELIX 124 AN7 TRP R 3 LYS R 33 1 31
HELIX 125 AN8 ASN a 12 THR a 22 1 11
HELIX 126 AN9 VAL a 30 ALA a 55 1 26
HELIX 127 AO1 SER a 70 GLY a 74 5 5
HELIX 128 AO2 PRO a 95 ALA a 99 5 5
HELIX 129 AO3 SER a 101 ASN a 108 1 8
HELIX 130 AO4 GLY a 109 LEU a 137 1 29
HELIX 131 AO5 TRP a 142 LEU a 159 1 18
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 ALA a 294 1 28
HELIX 141 AP6 THR a 316 HIS a 332 1 17
HELIX 142 AP7 PRO b 4 ILE b 13 5 10
HELIX 143 AP8 ASP b 15 ALA b 43 1 29
HELIX 144 AP9 PRO b 54 GLN b 58 5 5
HELIX 145 AQ1 VAL b 62 LEU b 69 1 8
HELIX 146 AQ2 SER b 92 TYR b 117 1 26
HELIX 147 AQ3 LEU b 120 ARG b 124 5 5
HELIX 148 AQ4 ASP b 134 PHE b 156 1 23
HELIX 149 AQ5 GLY b 186 ASN b 191 5 6
HELIX 150 AQ6 ASN b 194 VAL b 219 1 26
HELIX 151 AQ7 PRO b 222 LEU b 229 1 8
HELIX 152 AQ8 ILE b 234 GLY b 259 1 26
HELIX 153 AQ9 PRO b 264 GLY b 269 1 6
HELIX 154 AR1 THR b 271 SER b 277 1 7
HELIX 155 AR2 SER b 278 SER b 294 1 17
HELIX 156 AR3 THR b 297 ALA b 304 1 8
HELIX 157 AR4 PRO b 306 ASP b 313 1 8
HELIX 158 AR5 TYR b 314 ASN b 318 5 5
HELIX 159 AR6 PRO b 329 GLY b 333 5 5
HELIX 160 AR7 SER b 391 GLY b 396 1 6
HELIX 161 AR8 ASP b 413 ILE b 425 1 13
HELIX 162 AR9 SER b 446 PHE b 475 1 30
HELIX 163 AS1 ARG b 476 PHE b 479 5 4
HELIX 164 AS2 SER b 487 GLU b 492 1 6
HELIX 165 AS3 ASP c 27 GLY c 32 1 6
HELIX 166 AS4 ALA c 34 ILE c 43 5 10
HELIX 167 AS5 LEU c 45 HIS c 74 1 30
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 182 1 30
HELIX 173 AT2 ASP c 205 PHE c 210 1 6
HELIX 174 AT3 PHE c 210 LYS c 215 1 6
HELIX 175 AT4 GLY c 222 VAL c 227 5 6
HELIX 176 AT5 ASN c 229 THR c 254 1 26
HELIX 177 AT6 PHE c 257 ARG c 262 1 6
HELIX 178 AT7 SER c 267 ASN c 293 1 27
HELIX 179 AT8 PRO c 298 GLY c 303 1 6
HELIX 180 AT9 THR c 305 LEU c 324 1 20
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 ASP c 460 GLU c 464 5 5
HELIX 187 AU7 PRO c 465 MET c 469 5 5
HELIX 188 AU8 GLY d 13 LYS d 23 1 11
HELIX 189 AU9 SER d 33 VAL d 55 1 23
HELIX 190 AV1 SER d 66 GLY d 70 5 5
HELIX 191 AV2 ALA d 82 GLY d 86 5 5
HELIX 192 AV3 ASP d 100 LEU d 107 1 8
HELIX 193 AV4 GLY d 108 GLY d 137 1 30
HELIX 194 AV5 PRO d 140 PHE d 146 1 7
HELIX 195 AV6 PHE d 146 LEU d 158 1 13
HELIX 196 AV7 LEU d 158 GLN d 164 1 7
HELIX 197 AV8 SER d 166 ALA d 170 5 5
HELIX 198 AV9 VAL d 175 ASN d 190 1 16
HELIX 199 AW1 TRP d 191 LEU d 193 5 3
HELIX 200 AW2 ASN d 194 ASN d 220 1 27
HELIX 201 AW3 SER d 230 ALA d 234 5 5
HELIX 202 AW4 SER d 245 GLY d 258 1 14
HELIX 203 AW5 ASN d 263 LEU d 291 1 29
HELIX 204 AW6 PHE d 298 ASP d 308 1 11
HELIX 205 AW7 THR d 313 GLN d 334 1 22
HELIX 206 AW8 PRO d 342 LEU d 346 5 5
HELIX 207 AW9 PRO e 9 ILE e 14 1 6
HELIX 208 AX1 SER e 16 THR e 40 1 25
HELIX 209 AX2 GLY e 41 GLY e 48 1 8
HELIX 210 AX3 GLU e 71 GLN e 82 1 12
HELIX 211 AX4 THR f 17 GLN f 41 1 25
HELIX 212 AX5 THR h 5 ARG h 12 1 8
HELIX 213 AX6 PRO h 13 SER h 16 5 4
HELIX 214 AX7 THR h 27 ASN h 50 1 24
HELIX 215 AX8 GLU i 2 LEU i 24 1 23
HELIX 216 AX9 GLY i 26 ARG i 30 5 5
HELIX 217 AY1 PRO j 9 ALA j 32 1 24
HELIX 218 AY2 PRO k 12 ILE k 17 5 6
HELIX 219 AY3 PHE k 18 ASP k 23 1 6
HELIX 220 AY4 VAL k 27 GLY k 44 1 18
HELIX 221 AY5 ASN l 13 ASN l 37 1 25
HELIX 222 AY6 LEU m 6 GLN m 32 1 27
HELIX 223 AY7 THR o 6 VAL o 11 1 6
HELIX 224 AY8 GLY o 14 LYS o 18 5 5
HELIX 225 AY9 GLU o 179 GLU o 181 5 3
HELIX 226 AZ1 LEU o 182 VAL o 187 1 6
HELIX 227 AZ2 GLU t 2 PHE t 23 1 22
HELIX 228 AZ3 ASN u 11 GLY u 18 1 8
HELIX 229 AZ4 THR u 19 GLU u 23 5 5
HELIX 230 AZ5 ASN u 31 TYR u 38 5 8
HELIX 231 AZ6 PRO u 43 ASN u 52 1 10
HELIX 232 AZ7 SER u 57 ILE u 64 5 8
HELIX 233 AZ8 THR u 68 GLU u 77 1 10
HELIX 234 AZ9 ASN u 78 GLU u 80 5 3
HELIX 235 BA1 GLU u 88 GLU u 93 1 6
HELIX 236 BA2 GLY u 94 ASP u 96 5 3
HELIX 237 BA3 THR v 22 CYS v 37 1 16
HELIX 238 BA4 CYS v 37 VAL v 42 1 6
HELIX 239 BA5 GLY v 43 ILE v 45 5 3
HELIX 240 BA6 ARG v 55 LEU v 61 1 7
HELIX 241 BA7 ASN v 68 ASN v 78 1 11
HELIX 242 BA8 PHE v 101 ARG v 105 5 5
HELIX 243 BA9 THR v 108 GLY v 127 1 20
HELIX 244 BB1 ASP v 128 TRP v 130 5 3
HELIX 245 BB2 GLY v 133 TYR v 137 5 5
HELIX 246 BB3 VAL y 18 ARG y 42 1 25
HELIX 247 BB4 THR x 4 ASP x 35 1 32
HELIX 248 BB5 ILE z 3 ALA z 28 1 26
HELIX 249 BB6 ASP z 32 PHE z 59 1 28
HELIX 250 BB7 TRP r 3 LYS r 33 1 31
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 2 ILE B 336 TRP B 340 0
SHEET 2 AA4 2 PHE B 430 ASP B 433 -1 O GLU B 431 N GLN B 338
SHEET 1 AA5 6 VAL B 377 ASP B 380 0
SHEET 2 AA5 6 ILE B 369 THR B 371 -1 N LEU B 370 O ALA B 379
SHEET 3 AA5 6 GLU B 353 VAL B 356 -1 N PHE B 355 O THR B 371
SHEET 4 AA5 6 HIS B 343 ARG B 347 -1 N PHE B 346 O LEU B 354
SHEET 5 AA5 6 THR B 398 TYR B 402 -1 O SER B 400 N VAL B 345
SHEET 6 AA5 6 THR B 410 PHE B 411 -1 O PHE B 411 N VAL B 399
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 30 PRO O 31 0
SHEET 2 AB1 2 SER O 135 ILE O 136 -1 O ILE O 136 N TYR O 30
SHEET 1 AB210 PHE O 65 PRO O 67 0
SHEET 2 AB210 TYR O 38 LYS O 53 -1 N VAL O 52 O VAL O 66
SHEET 3 AB210 GLU O 232 PRO O 245 -1 O LYS O 234 N LEU O 51
SHEET 4 AB210 GLU O 210 LEU O 220 -1 N GLN O 219 O VAL O 233
SHEET 5 AB210 LEU O 192 VAL O 204 -1 N ASN O 200 O THR O 214
SHEET 6 AB210 ASP O 141 PRO O 149 -1 N VAL O 148 O THR O 193
SHEET 7 AB210 LYS O 123 SER O 128 -1 N LYS O 123 O ASN O 147
SHEET 8 AB210 LEU O 93 ILE O 101 -1 N PHE O 95 O ALA O 127
SHEET 9 AB210 LEU O 78 VAL O 87 -1 N LYS O 86 O THR O 94
SHEET 10 AB210 TYR O 38 LYS O 53 -1 N LEU O 45 O LEU O 78
SHEET 1 AB3 3 LYS O 69 LEU O 70 0
SHEET 2 AB3 3 PHE O 103 GLN O 109 -1 O GLN O 109 N LYS O 69
SHEET 3 AB3 3 ARG O 115 THR O 121 -1 O ILE O 116 N VAL O 108
SHEET 1 AB4 2 ILE U 25 ASP U 26 0
SHEET 2 AB4 2 PHE U 82 THR U 83 1 O THR U 83 N ILE U 25
SHEET 1 AB5 2 THR V 9 PRO V 11 0
SHEET 2 AB5 2 THR V 18 THR V 20 -1 O ILE V 19 N VAL V 10
SHEET 1 AB6 2 ALA a 81 VAL a 82 0
SHEET 2 AB6 2 LEU a 174 GLY a 175 -1 O LEU a 174 N VAL a 82
SHEET 1 AB7 2 LEU a 297 ASN a 298 0
SHEET 2 AB7 2 GLY c 402 SER c 403 1 O GLY c 402 N ASN a 298
SHEET 1 AB8 2 MET b 166 VAL b 168 0
SHEET 2 AB8 2 SER b 177 GLN b 179 -1 O SER b 177 N VAL b 168
SHEET 1 AB9 2 ILE b 336 TRP b 340 0
SHEET 2 AB9 2 PHE b 430 ASP b 433 -1 O GLU b 431 N GLN b 338
SHEET 1 AC1 6 VAL b 377 ASP b 380 0
SHEET 2 AC1 6 ILE b 369 THR b 371 -1 N LEU b 370 O ALA b 379
SHEET 3 AC1 6 GLU b 353 VAL b 356 -1 N PHE b 355 O THR b 371
SHEET 4 AC1 6 HIS b 343 ARG b 347 -1 N PHE b 346 O LEU b 354
SHEET 5 AC1 6 THR b 398 TYR b 402 -1 O SER b 400 N VAL b 345
SHEET 6 AC1 6 THR b 410 PHE b 411 -1 O PHE b 411 N VAL b 399
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 30 PRO o 31 0
SHEET 2 AC6 2 SER o 135 ILE o 136 -1 O ILE o 136 N TYR o 30
SHEET 1 AC710 VAL o 66 PRO o 67 0
SHEET 2 AC710 TYR o 38 VAL o 52 -1 N VAL o 52 O VAL o 66
SHEET 3 AC710 GLU o 232 PRO o 245 -1 O LYS o 234 N LEU o 51
SHEET 4 AC710 GLU o 210 LEU o 220 -1 N SER o 217 O ILE o 235
SHEET 5 AC710 LEU o 192 ASP o 205 -1 N ASN o 200 O THR o 214
SHEET 6 AC710 ASP o 141 PRO o 149 -1 N VAL o 148 O THR o 193
SHEET 7 AC710 LYS o 123 SER o 128 -1 N LYS o 123 O ASN o 147
SHEET 8 AC710 LEU o 93 ILE o 101 -1 N GLU o 97 O LEU o 125
SHEET 9 AC710 LEU o 78 VAL o 87 -1 N GLN o 82 O ASP o 99
SHEET 10 AC710 TYR o 38 VAL o 52 -1 N ILE o 40 O GLY o 83
SHEET 1 AC8 3 LYS o 69 LEU o 70 0
SHEET 2 AC8 3 PHE o 103 GLN o 109 -1 O GLN o 109 N LYS o 69
SHEET 3 AC8 3 ARG o 115 THR o 121 -1 O ILE o 116 N VAL o 108
SHEET 1 AC9 2 ILE u 25 ASP u 26 0
SHEET 2 AC9 2 PHE u 82 THR u 83 1 O THR u 83 N ILE u 25
SHEET 1 AD1 2 THR v 9 PRO v 11 0
SHEET 2 AD1 2 THR v 18 THR v 20 -1 O ILE v 19 N VAL v 10
SSBOND 1 CYS O 19 CYS O 44 1555 1555 2.03
SSBOND 2 CYS o 19 CYS o 44 1555 1555 2.03
LINK OD1 ASP A 170 CA1 OEX A 601 1555 1555 2.69
LINK OD2 ASP A 170 MN4 OEX A 601 1555 1555 1.95
LINK OE1 GLU A 189 CA1 OEX A 601 1555 1555 3.19
LINK NE2 HIS A 215 FE FE2 A 602 1555 1555 2.16
LINK NE2 HIS A 272 FE FE2 A 602 1555 1555 2.20
LINK NE2 HIS A 332 MN1 OEX A 601 1555 1555 2.21
LINK OE1 GLU A 333 MN3 OEX A 601 1555 1555 2.16
LINK OE2 GLU A 333 MN4 OEX A 601 1555 1555 2.03
LINK OD1 ASP A 342 MN2 OEX A 601 1555 1555 2.12
LINK OD2 ASP A 342 MN1 OEX A 601 1555 1555 2.15
LINK O ALA A 344 CA1 OEX A 601 1555 1555 2.40
LINK OXT ALA A 344 MN2 OEX A 601 1555 1555 1.85
LINK OD1 ASN C 39 MG CLA C 512 1555 1555 2.18
LINK OE1 GLU C 354 MN2 OEX A 601 1555 1555 2.12
LINK OE2 GLU C 354 MN3 OEX A 601 1555 1555 2.00
LINK NE2 HIS D 214 FE FE2 A 602 1555 1555 2.17
LINK NE2 HIS D 268 FE FE2 A 602 1555 1555 2.21
LINK NE2 HIS E 23 FE HEM E 101 1555 1555 2.15
LINK NE2 HIS F 24 FE HEM E 101 1555 1555 2.16
LINK C FME I 1 N GLU I 2 1555 1555 1.33
LINK C FME M 1 N AGLU M 2 1555 1555 1.33
LINK C FME M 1 N BGLU M 2 1555 1555 1.33
LINK C FME T 1 N GLU T 2 1555 1555 1.33
LINK SG CYS V 37 CAB HEM V 201 1555 1555 1.70
LINK SG CYS V 37 CBB HEM V 201 1555 1555 1.72
LINK SG CYS V 40 CAC HEM V 201 1555 1555 1.87
LINK NE2 HIS V 41 FE HEM V 201 1555 1555 2.15
LINK NE2 HIS V 92 FE HEM V 201 1555 1555 2.15
LINK OD1 ASP a 170 CA1 OEX a 601 1555 1555 2.82
LINK OD2 ASP a 170 MN4 OEX a 601 1555 1555 2.00
LINK OE1 GLU a 189 CA1 OEX a 601 1555 1555 3.06
LINK OE2 GLU a 189 MN1 OEX a 601 1555 1555 1.77
LINK NE2 HIS a 215 FE FE2 a 602 1555 1555 2.15
LINK NE2 HIS a 272 FE FE2 a 602 1555 1555 2.20
LINK NE2 HIS a 332 MN1 OEX a 601 1555 1555 2.17
LINK OE1 GLU a 333 MN3 OEX a 601 1555 1555 2.09
LINK OE2 GLU a 333 MN4 OEX a 601 1555 1555 1.98
LINK OD1 ASP a 342 MN2 OEX a 601 1555 1555 2.18
LINK OD2 ASP a 342 MN1 OEX a 601 1555 1555 2.12
LINK O ALA a 344 CA1 OEX a 601 1555 1555 2.52
LINK OXT ALA a 344 MN2 OEX a 601 1555 1555 1.79
LINK OD1 ASN c 39 MG CLA c 511 1555 1555 2.20
LINK OE1 GLU c 354 MN2 OEX a 601 1555 1555 2.15
LINK OE2 GLU c 354 MN3 OEX a 601 1555 1555 2.09
LINK NE2 HIS d 214 FE FE2 a 602 1555 1555 2.18
LINK NE2 HIS d 268 FE FE2 a 602 1555 1555 2.20
LINK NE2 HIS e 23 FE HEM e 101 1555 1555 2.16
LINK NE2 HIS f 24 FE HEM e 101 1555 1555 2.16
LINK C FME i 1 N GLU i 2 1555 1555 1.33
LINK C FME m 1 N GLU m 2 1555 1555 1.33
LINK C FME t 1 N GLU t 2 1555 1555 1.33
LINK SG CYS v 37 CAB HEM v 201 1555 1555 1.70
LINK SG CYS v 37 CBB HEM v 201 1555 1555 1.66
LINK SG CYS v 40 CAC HEM v 201 1555 1555 1.86
LINK NE2 HIS v 41 FE HEM v 201 1555 1555 2.13
LINK NE2 HIS v 92 FE HEM v 201 1555 1555 2.15
LINK CA1 OEX A 601 O HOH A 772 1555 1555 2.58
LINK CA1 OEX A 601 O HOH A 714 1555 1555 2.46
LINK MN4 OEX A 601 O HOH A 738 1555 1555 2.12
LINK MN4 OEX A 601 O HOH A 723 1555 1555 2.17
LINK FE FE2 A 602 O2 BCT A 605 1555 1555 2.18
LINK FE FE2 A 602 O1 BCT A 605 1555 1555 2.17
LINK MG CLA A 607 O HOH A 743 1555 1555 2.14
LINK MG CLA A 613 O HOH A 732 1555 1555 2.16
LINK MG CLA B 601 O HOH B 733 1555 1555 2.15
LINK MG CLA B 607 O HOH B 772 1555 1555 2.16
LINK MG CLA B 610 O HOH B 723 1555 1555 2.15
LINK MG CLA C 505 O HOH C 661 1555 1555 2.15
LINK MG CLA C 508 O HOH C 611 1555 1555 2.15
LINK CA1 OEX a 601 O HOH a 738 1555 1555 2.45
LINK CA1 OEX a 601 O HOH a 779 1555 1555 2.62
LINK MN4 OEX a 601 O HOH a 772 1555 1555 2.24
LINK MN4 OEX a 601 O HOH a 720 1555 1555 2.27
LINK FE FE2 a 602 O1 BCT a 605 1555 1555 2.17
LINK FE FE2 a 602 O2 BCT a 605 1555 1555 2.18
LINK MG CLA a 607 O HOH a 749 1555 1555 2.15
LINK MG CLA a 615 O HOH a 759 1555 1555 2.16
LINK MG CLA b 601 O HOH b 758 1555 1555 2.15
LINK MG CLA b 607 O HOH b 792 1555 1555 2.17
LINK MG CLA b 610 O HOH b 719 1555 1555 2.15
LINK MG CLA c 504 O HOH c 646 1555 1555 2.15
LINK MG CLA c 507 O HOH c 645 1555 1555 2.16
CISPEP 1 TYR U 42 PRO U 43 0 -1.96
CISPEP 2 ALA U 53 PRO U 54 0 -0.29
CISPEP 3 THR V 63 PRO V 64 0 -3.04
CISPEP 4 GLN o 3 THR o 4 0 0.48
CISPEP 5 GLU o 54 GLU o 55 0 1.49
CISPEP 6 PRO o 56 LYS o 57 0 5.48
CISPEP 7 TYR u 42 PRO u 43 0 -0.91
CISPEP 8 ALA u 53 PRO u 54 0 3.79
CISPEP 9 THR v 63 PRO v 64 0 -1.70
SITE 1 AC1 14 ASP A 170 GLU A 189 HIS A 332 GLU A 333
SITE 2 AC1 14 HIS A 337 ASP A 342 ALA A 344 HOH A 710
SITE 3 AC1 14 HOH A 714 HOH A 723 HOH A 738 HOH A 772
SITE 4 AC1 14 GLU C 354 ARG C 357
SITE 1 AC2 5 HIS A 215 HIS A 272 BCT A 605 HIS D 214
SITE 2 AC2 5 HIS D 268
SITE 1 AC3 4 ASN A 181 GLU A 333 HOH A 734 LYS D 317
SITE 1 AC4 4 ASN A 338 PHE A 339 HOH A 773 GLU C 354
SITE 1 AC5 8 HIS A 215 GLU A 244 TYR A 246 HIS A 272
SITE 2 AC5 8 FE2 A 602 HIS D 214 TYR D 244 HIS D 268
SITE 1 AC6 16 PRO A 150 SER A 153 VAL A 157 MET A 183
SITE 2 AC6 16 PHE A 186 ILE A 192 LEU A 193 HIS A 198
SITE 3 AC6 16 GLY A 201 THR A 286 ALA A 287 ILE A 290
SITE 4 AC6 16 CLA A 607 CLA A 613 PHO D 401 CLA D 402
SITE 1 AC7 14 GLN A 199 VAL A 202 ALA A 203 CLA A 606
SITE 2 AC7 14 PHO A 608 PL9 A 611 HOH A 743 PHE D 157
SITE 3 AC7 14 VAL D 175 ILE D 178 PHE D 179 LEU D 182
SITE 4 AC7 14 CLA D 402 LMG D 407
SITE 1 AC8 16 PHE A 206 LEU A 210 MET A 214 LEU A 258
SITE 2 AC8 16 CLA A 607 TRP D 48 ILE D 114 GLY D 121
SITE 3 AC8 16 PHE D 125 GLN D 129 ASN D 142 PHE D 146
SITE 4 AC8 16 PHE D 153 GLY D 174 LEU D 279 CLA D 402
SITE 1 AC9 12 ILE A 36 THR A 40 PHE A 93 PRO A 95
SITE 2 AC9 12 ILE A 96 TRP A 97 LEU A 114 HIS A 118
SITE 3 AC9 12 LEU A 121 LMG C 501 VAL I 12 PHE I 15
SITE 1 AD1 1 ALA A 43
SITE 1 AD2 10 MET A 214 HIS A 215 LEU A 218 HIS A 252
SITE 2 AD2 10 PHE A 255 SER A 264 PHE A 265 LEU A 271
SITE 3 AD2 10 CLA A 607 TYR D 42
SITE 1 AD3 16 ASN A 267 SER A 270 PHE A 273 PHE A 274
SITE 2 AD3 16 LHG A 618 HOH A 713 GLN C 28 ALA C 34
SITE 3 AD3 16 TRP C 36 CLA C 509 DGD C 519 SER D 230
SITE 4 AD3 16 PHE D 232 ARG D 233 PHE K 37 BCR Y 101
SITE 1 AD4 15 PHE A 158 MET A 172 ILE A 176 THR A 179
SITE 2 AD4 15 PHE A 180 MET A 183 CLA A 606 HOH A 732
SITE 3 AD4 15 HOH A 741 HOH A 767 MET D 198 VAL D 201
SITE 4 AD4 15 ALA D 202 PHO D 401 PL9 D 405
SITE 1 AD5 14 ARG A 140 TRP A 142 PHE A 273 HOH A 750
SITE 2 AD5 14 TRP C 36 TRP C 443 ARG C 447 CLA C 505
SITE 3 AD5 14 CLA C 509 GLU D 219 ASN D 220 ALA D 229
SITE 4 AD5 14 THR D 231 PHE D 232
SITE 1 AD6 9 ASP A 25 ARG A 27 LEU A 28 ILE A 38
SITE 2 AD6 9 THR A 45 PHE T 22 TRP b 113 TYR b 117
SITE 3 AD6 9 BCR b 619
SITE 1 AD7 5 TYR A 262 SQD A 612 HOH A 769 PHE E 10
SITE 2 AD7 5 SER E 11
SITE 1 AD8 9 TRP B 185 GLY B 186 PHE B 190 CLA B 602
SITE 2 AD8 9 LMG B 621 HOH B 733 PHE C 181 PHE H 41
SITE 3 AD8 9 BCR H 101
SITE 1 AD9 15 GLY B 189 PHE B 190 GLY B 197 HIS B 201
SITE 2 AD9 15 VAL B 208 PHE B 247 CLA B 601 CLA B 603
SITE 3 AD9 15 HOH B 788 ILE D 159 LEU D 162 PHE H 38
SITE 4 AD9 15 ILE H 45 TYR H 49 DGD H 102
SITE 1 AE1 17 ARG B 68 LEU B 69 ALA B 146 CYS B 150
SITE 2 AE1 17 PHE B 153 HIS B 201 HIS B 202 VAL B 252
SITE 3 AE1 17 THR B 262 CLA B 602 CLA B 604 CLA B 605
SITE 4 AE1 17 CLA B 606 CLA B 609 CLA B 610 HOH B 724
SITE 5 AE1 17 MET H 35
SITE 1 AE2 18 TRP B 33 PHE B 61 PHE B 65 ARG B 68
SITE 2 AE2 18 LEU B 149 VAL B 245 ALA B 248 ALA B 249
SITE 3 AE2 18 VAL B 252 PHE B 451 HIS B 455 PHE B 458
SITE 4 AE2 18 CLA B 603 CLA B 605 CLA B 607 CLA B 612
SITE 5 AE2 18 CLA B 613 CLA B 615
SITE 1 AE3 16 THR B 27 VAL B 30 ALA B 34 VAL B 62
SITE 2 AE3 16 MET B 66 ARG B 68 HIS B 100 LEU B 103
SITE 3 AE3 16 ALA B 205 CLA B 603 CLA B 604 CLA B 606
SITE 4 AE3 16 CLA B 609 CLA B 610 CLA B 615 HOH B 718
SITE 1 AE4 16 LEU B 69 VAL B 71 PHE B 90 TRP B 91
SITE 2 AE4 16 VAL B 96 HIS B 100 LEU B 106 GLY B 152
SITE 3 AE4 16 PHE B 153 PHE B 156 HIS B 157 PHE B 162
SITE 4 AE4 16 PRO B 164 CLA B 603 CLA B 605 BCR B 619
SITE 1 AE5 12 TRP B 33 TYR B 40 GLN B 58 GLY B 59
SITE 2 AE5 12 PHE B 61 THR B 327 GLY B 328 PRO B 329
SITE 3 AE5 12 TRP B 450 CLA B 604 LMG B 620 HOH B 772
SITE 1 AE6 14 THR B 236 SER B 239 SER B 240 ALA B 243
SITE 2 AE6 14 PHE B 247 PHE B 463 HIS B 466 CLA B 609
SITE 3 AE6 14 CLA B 610 HOH B 767 PHE D 120 ILE D 123
SITE 4 AE6 14 MET D 126 SQD D 409
SITE 1 AE7 16 PHE B 139 VAL B 208 ALA B 212 PHE B 215
SITE 2 AE7 16 HIS B 216 VAL B 219 PRO B 221 PRO B 222
SITE 3 AE7 16 CLA B 603 CLA B 605 CLA B 608 CLA B 610
SITE 4 AE7 16 THR H 27 MET H 31 LEU H 39 BCR H 101
SITE 1 AE8 13 PHE B 139 HIS B 142 MET B 231 VAL B 237
SITE 2 AE8 13 SER B 240 SER B 241 CLA B 603 CLA B 605
SITE 3 AE8 13 CLA B 608 CLA B 609 CLA B 612 CLA B 615
SITE 4 AE8 13 HOH B 723
SITE 1 AE9 17 TRP B 5 TYR B 6 ARG B 7 VAL B 8
SITE 2 AE9 17 HIS B 9 LEU B 238 LEU B 461 PHE B 462
SITE 3 AE9 17 GLY B 465 TRP B 468 HIS B 469 ARG B 472
SITE 4 AE9 17 CLA B 612 CLA B 613 CLA B 614 LHG B 623
SITE 5 AE9 17 HOH B 739
SITE 1 AF1 16 HIS B 9 LEU B 12 LEU B 19 HIS B 23
SITE 2 AF1 16 HIS B 26 THR B 27 VAL B 237 LEU B 238
SITE 3 AF1 16 SER B 241 CLA B 604 CLA B 610 CLA B 611
SITE 4 AF1 16 CLA B 613 CLA B 614 CLA B 615 HOH B 730
SITE 1 AF2 11 HIS B 9 HIS B 26 VAL B 30 PHE B 462
SITE 2 AF2 11 CLA B 604 CLA B 611 CLA B 612 CLA B 614
SITE 3 AF2 11 BCR B 617 LMG B 620 LHG B 623
SITE 1 AF3 11 VAL B 8 HIS B 9 CLA B 611 CLA B 612
SITE 2 AF3 11 CLA B 613 BCR B 617 LMG B 620 SQD B 624
SITE 3 AF3 11 GLN L 8 VAL L 10 PHE M 21
SITE 1 AF4 12 HIS B 23 MET B 138 HIS B 142 LEU B 145
SITE 2 AF4 12 CLA B 604 CLA B 605 CLA B 610 CLA B 612
SITE 3 AF4 12 CLA B 616 BCR B 619 LEU H 11 LEU H 14
SITE 1 AF5 9 ILE B 20 LEU B 24 ALA B 110 TRP B 113
SITE 2 AF5 9 HIS B 114 CLA B 615 BCR B 619 THR H 5
SITE 3 AF5 9 LEU H 7
SITE 1 AF6 7 MET B 25 CLA B 613 CLA B 614 BCR B 618
SITE 2 AF6 7 SQD B 624 PHE t 19 BCR t 101
SITE 1 AF7 8 LEU B 29 GLY B 32 SER B 36 VAL B 102
SITE 2 AF7 8 GLY B 105 BCR B 617 LMG B 626 BCR t 101
SITE 1 AF8 6 LEU B 109 TRP B 113 CLA B 606 CLA B 615
SITE 2 AF8 6 CLA B 616 SQD B 625
SITE 1 AF9 9 THR B 327 PRO B 329 PHE B 453 CLA B 607
SITE 2 AF9 9 CLA B 613 CLA B 614 LHG L 102 ASN M 4
SITE 3 AF9 9 ALA M 10
SITE 1 AG1 6 PRO B 183 GLU B 184 TRP B 185 CLA B 601
SITE 2 AG1 6 HOH B 705 LEU C 204
SITE 1 AG2 14 ASN A 234 TYR B 6 ARG B 7 PHE B 464
SITE 2 AG2 14 TRP B 468 CLA B 611 CLA B 613 HOH B 739
SITE 3 AG2 14 TYR D 141 TRP D 266 PHE D 269 LHG L 102
SITE 4 AG2 14 PHE M 14 PRO M 18
SITE 1 AG3 12 ARG B 18 SER B 104 PHE B 108 TRP B 115
SITE 2 AG3 12 CLA B 614 BCR B 617 HOH B 708 ARG L 7
SITE 3 AG3 12 ARG l 14 TYR l 18 TYR m 26 PHE t 23
SITE 1 AG4 9 TRP B 113 TYR B 117 BCR B 619 TRP a 20
SITE 2 AG4 9 ASN a 26 LEU a 28 LEU a 42 THR a 45
SITE 3 AG4 9 PHE t 22
SITE 1 AG5 9 SER B 76 TRP B 78 BCR B 618 ALA a 54
SITE 2 AG5 9 ASP a 103 GLY o 112 GLY o 113 PHE t 10
SITE 3 AG5 9 ALA t 11
SITE 1 AG6 13 TRP A 97 GLU A 98 CLA A 609 LEU C 214
SITE 2 AG6 13 SER C 216 PHE C 218 GLU C 221 TRP C 223
SITE 3 AG6 13 CLA C 506 DGD C 517 HOH C 601 LYS I 5
SITE 4 AG6 13 TYR I 9
SITE 1 AG7 17 THR C 94 LEU C 95 LEU C 168 GLY C 171
SITE 2 AG7 17 ALA C 172 LEU C 175 VAL C 233 HIS C 237
SITE 3 AG7 17 ILE C 240 MET C 282 PHE C 289 TYR C 297
SITE 4 AG7 17 CLA C 503 CLA C 504 CLA C 507 CLA C 508
SITE 5 AG7 17 BCR C 516
SITE 1 AG8 14 TRP C 63 HIS C 91 LEU C 279 MET C 282
SITE 2 AG8 14 ALA C 286 TYR C 297 HIS C 430 LEU C 433
SITE 3 AG8 14 PHE C 437 CLA C 502 CLA C 504 CLA C 511
SITE 4 AG8 14 CLA C 513 HOH C 663
SITE 1 AG9 12 ILE C 60 VAL C 61 THR C 68 LEU C 88
SITE 2 AG9 12 HIS C 91 VAL C 114 HIS C 118 CLA C 502
SITE 3 AG9 12 CLA C 503 CLA C 508 CLA C 511 CLA C 513
SITE 1 AH1 16 PHE A 285 LHG A 614 TRP C 63 PHE C 70
SITE 2 AH1 16 GLN C 84 GLY C 85 TRP C 425 SER C 429
SITE 3 AH1 16 CLA C 509 DGD C 518 DGD C 519 LMG C 520
SITE 4 AH1 16 HOH C 608 HOH C 661 PRO K 26 VAL K 30
SITE 1 AH2 11 PHE A 33 TRP A 131 PHE C 264 TYR C 274
SITE 2 AH2 11 HIS C 441 LEU C 442 ALA C 445 ARG C 449
SITE 3 AH2 11 LMG C 501 CLA C 508 HOH C 615
SITE 1 AH3 12 LEU C 165 ILE C 243 GLY C 247 TRP C 250
SITE 2 AH3 12 HIS C 251 THR C 255 PRO C 256 PHE C 257
SITE 3 AH3 12 TRP C 259 ALA C 260 CLA C 502 CLA C 508
SITE 1 AH4 14 MET C 157 LEU C 161 HIS C 164 TRP C 266
SITE 2 AH4 14 TYR C 271 TYR C 274 SER C 275 MET C 282
SITE 3 AH4 14 CLA C 502 CLA C 504 CLA C 506 CLA C 507
SITE 4 AH4 14 CLA C 510 HOH C 611
SITE 1 AH5 18 SQD A 612 LHG A 614 PHE C 33 TRP C 36
SITE 2 AH5 18 ALA C 37 GLY C 38 ASN C 39 LEU C 272
SITE 3 AH5 18 PHE C 436 PHE C 437 GLY C 440 TRP C 443
SITE 4 AH5 18 HIS C 444 CLA C 505 CLA C 510 CLA C 511
SITE 5 AH5 18 CLA C 512 DGD C 518
SITE 1 AH6 16 ASN C 39 LEU C 49 ALA C 52 HIS C 53
SITE 2 AH6 16 HIS C 56 TYR C 149 GLY C 268 TYR C 271
SITE 3 AH6 16 LEU C 272 SER C 275 LEU C 279 CLA C 508
SITE 4 AH6 16 CLA C 509 CLA C 511 CLA C 512 CLA C 513
SITE 1 AH7 12 ASN C 39 HIS C 56 LEU C 59 PHE C 436
SITE 2 AH7 12 PHE C 437 CLA C 503 CLA C 504 CLA C 509
SITE 3 AH7 12 CLA C 510 CLA C 512 PRO K 29 LEU K 33
SITE 1 AH8 19 THR C 24 ARG C 26 TRP C 35 GLY C 38
SITE 2 AH8 19 ASN C 39 ARG C 41 LEU C 42 LYS C 48
SITE 3 AH8 19 GLY C 126 PHE C 127 ILE C 134 CLA C 509
SITE 4 AH8 19 CLA C 510 CLA C 511 TRP K 39 GLN K 40
SITE 5 AH8 19 BCR K 101 ASN Y 45 VAL Z 20
SITE 1 AH9 11 HIS C 53 PHE C 146 PHE C 147 PHE C 163
SITE 2 AH9 11 HIS C 164 VAL C 167 ILE C 170 CLA C 503
SITE 3 AH9 11 CLA C 504 CLA C 510 CLA C 514
SITE 1 AI1 8 LEU C 50 VAL C 124 GLY C 128 TYR C 131
SITE 2 AI1 8 HIS C 132 TYR C 143 CLA C 513 BCR C 515
SITE 1 AI2 5 SER C 121 CLA C 514 TYR K 15 GLY Z 55
SITE 2 AI2 5 ASN Z 58
SITE 1 AI3 5 ILE C 209 LEU C 213 ASP C 232 PHE C 264
SITE 2 AI3 5 CLA C 502
SITE 1 AI4 21 LEU A 91 PRO C 217 GLY C 219 GLY C 220
SITE 2 AI4 21 GLU C 221 GLY C 222 TRP C 223 SER C 226
SITE 3 AI4 21 VAL C 227 CYS C 288 PHE C 292 ASN C 293
SITE 4 AI4 21 ASN C 294 THR C 295 ASP C 360 PHE C 361
SITE 5 AI4 21 ARG C 362 LEU C 438 LMG C 501 HOH C 644
SITE 6 AI4 21 HOH C 651
SITE 1 AI5 16 PHE A 197 GLU C 83 GLN C 84 GLY C 85
SITE 2 AI5 16 SER C 406 ASN C 418 PHE C 419 VAL C 420
SITE 3 AI5 16 TRP C 425 CLA C 505 CLA C 509 DGD C 519
SITE 4 AI5 16 LMG C 520 HOH C 620 TYR J 33 HOH J 203
SITE 1 AI6 17 PHE A 300 ASN A 301 SER A 305 SQD A 612
SITE 2 AI6 17 ASN C 405 SER C 406 VAL C 407 ASN C 415
SITE 3 AI6 17 SER C 416 ASN C 418 CLA C 505 DGD C 518
SITE 4 AI6 17 ALA J 32 TYR J 33 GLY J 37 SER J 38
SITE 5 AI6 17 SER J 39
SITE 1 AI7 4 HIS C 74 CLA C 505 DGD C 518 HOH C 647
SITE 1 AI8 11 PHE B 151 ALA B 155 PHE B 156 THR B 159
SITE 2 AI8 11 LEU B 161 PRO B 183 LEU C 204 ASP C 205
SITE 3 AI8 11 PRO C 206 TRP C 239 HOH C 609
SITE 1 AI9 13 LEU A 41 THR A 45 TYR A 126 GLN A 130
SITE 2 AI9 13 TYR A 147 PRO A 279 VAL A 283 CLA A 606
SITE 3 AI9 13 CLA A 613 ALA D 208 LEU D 209 ILE D 213
SITE 4 AI9 13 TRP D 253
SITE 1 AJ1 17 CLA A 606 CLA A 607 PHO A 608 PRO D 149
SITE 2 AJ1 17 VAL D 152 VAL D 156 LEU D 182 PHE D 185
SITE 3 AJ1 17 GLN D 186 TRP D 191 THR D 192 HIS D 197
SITE 4 AJ1 17 GLY D 200 VAL D 201 SER D 282 ALA D 283
SITE 5 AJ1 17 VAL D 286
SITE 1 AJ2 18 ILE D 35 PRO D 39 LEU D 43 LEU D 89
SITE 2 AJ2 18 LEU D 90 LEU D 91 LEU D 92 TRP D 93
SITE 3 AJ2 18 THR D 112 PHE D 113 LEU D 116 HIS D 117
SITE 4 AJ2 18 VAL H 40 HOH H 203 GLY X 13 LEU X 14
SITE 5 AJ2 18 LEU X 15 GLY X 17
SITE 1 AJ3 10 TYR D 42 GLY D 46 GLY D 47 LEU D 49
SITE 2 AJ3 10 THR D 50 LMG D 407 PRO F 29 THR F 30
SITE 3 AJ3 10 PHE F 33 VAL J 25
SITE 1 AJ4 13 PHE A 52 CLA A 613 MET D 198 MET D 199
SITE 2 AJ4 13 HIS D 214 THR D 217 TRP D 253 ALA D 260
SITE 3 AJ4 13 PHE D 261 LEU D 267 LHG D 406 LEU L 29
SITE 4 AJ4 13 LHG L 102
SITE 1 AJ5 15 ILE D 256 PHE D 257 ALA D 260 PHE D 261
SITE 2 AJ5 15 SER D 262 ASN D 263 TRP D 266 PL9 D 405
SITE 3 AJ5 15 HOH D 501 HOH D 554 ASN L 13 THR L 15
SITE 4 AJ5 15 TYR L 18 LEU L 19 PHE T 17
SITE 1 AJ6 17 CLA A 607 TYR D 67 GLY D 70 CYS D 71
SITE 2 AJ6 17 ASN D 72 PHE D 73 BCR D 404 HOH D 521
SITE 3 AJ6 17 THR F 30 ILE F 37 MET F 40 GLN F 41
SITE 4 AJ6 17 PHE J 28 GLY J 31 ALA J 32 LEU J 36
SITE 5 AJ6 17 HOH J 201
SITE 1 AJ7 9 ARG D 24 ARG D 26 HOH E 202 PHE F 16
SITE 2 AJ7 9 THR F 17 VAL F 18 GLN R 30 LEU R 34
SITE 3 AJ7 9 ASP X 35
SITE 1 AJ8 9 ARG B 230 CLA B 608 ASP D 16 ASP D 19
SITE 2 AJ8 9 LYS D 23 TRP D 32 LEU D 127 ARG D 134
SITE 3 AJ8 9 HOH D 504
SITE 1 AJ9 16 ILE E 13 ARG E 18 TYR E 19 HIS E 23
SITE 2 AJ9 16 LEU E 30 HOH E 204 HOH E 208 ARG F 19
SITE 3 AJ9 16 TRP F 20 VAL F 23 HIS F 24 ALA F 27
SITE 4 AJ9 16 ILE F 31 HOH F 101 ALA R 19 ILE R 23
SITE 1 AK1 7 CLA B 601 CLA B 609 PHE H 34 MET H 35
SITE 2 AK1 7 LEU H 37 PHE H 38 PHE H 41
SITE 1 AK2 17 TYR B 193 TRP B 257 TYR B 258 TYR B 273
SITE 2 AK2 17 GLN B 274 SER B 277 CLA B 602 HOH B 719
SITE 3 AK2 17 HIS D 87 LEU D 162 HOH D 527 TYR H 49
SITE 4 AK2 17 ASN H 50 VAL H 60 SER H 61 TRP H 62
SITE 5 AK2 17 HOH H 207
SITE 1 AK3 8 ALA C 55 GLY C 58 LEU C 59 SER C 122
SITE 2 AK3 8 GLY C 126 CLA C 512 PHE K 32 SER Z 16
SITE 1 AK4 11 ARG L 14 TYR L 18 HOH L 201 TYR M 26
SITE 2 AK4 11 PHE T 23 ARG b 18 PHE b 108 TRP b 115
SITE 3 AK4 11 CLA b 614 BCR b 617 BCR b 618
SITE 1 AK5 16 SER A 232 ASN A 234 PRO B 4 TRP B 5
SITE 2 AK5 16 TYR B 6 LMG B 620 LHG B 623 TRP D 266
SITE 3 AK5 16 PHE D 273 PL9 D 405 HOH D 501 GLU L 11
SITE 4 AK5 16 LEU L 12 ASN L 13 SER L 16 PHE M 21
SITE 1 AK6 3 PHE T 18 TRP b 33 BCR b 618
SITE 1 AK7 18 ALA V 36 CYS V 37 CYS V 40 HIS V 41
SITE 2 AK7 18 THR V 46 THR V 48 LEU V 52 ASP V 53
SITE 3 AK7 18 LEU V 54 THR V 58 LEU V 59 TYR V 75
SITE 4 AK7 18 TYR V 82 HIS V 92 HOH V 304 HOH V 306
SITE 5 AK7 18 HOH V 313 HOH V 321
SITE 1 AK8 11 SQD A 612 PHE C 62 THR J 15 LEU K 31
SITE 2 AK8 11 ALA K 34 VAL K 38 ILE Y 28 GLY Y 29
SITE 3 AK8 11 GLY Y 32 PRO Y 33 SER Z 16
SITE 1 AK9 16 ASP a 61 ASP a 170 GLU a 189 HIS a 332
SITE 2 AK9 16 GLU a 333 HIS a 337 ASP a 342 ALA a 344
SITE 3 AK9 16 HOH a 720 HOH a 734 HOH a 738 HOH a 739
SITE 4 AK9 16 HOH a 772 HOH a 779 GLU c 354 ARG c 357
SITE 1 AL1 5 HIS a 215 HIS a 272 BCT a 605 HIS d 214
SITE 2 AL1 5 HIS d 268
SITE 1 AL2 5 ASN a 181 HIS a 332 GLU a 333 HOH a 746
SITE 2 AL2 5 LYS d 317
SITE 1 AL3 4 ASN a 338 PHE a 339 GLU c 354 HOH c 667
SITE 1 AL4 9 HIS a 215 GLU a 244 TYR a 246 HIS a 272
SITE 2 AL4 9 FE2 a 602 HOH a 713 HIS d 214 TYR d 244
SITE 3 AL4 9 HIS d 268
SITE 1 AL5 16 PRO a 150 SER a 153 VAL a 157 MET a 183
SITE 2 AL5 16 PHE a 186 ILE a 192 LEU a 193 HIS a 198
SITE 3 AL5 16 GLY a 201 THR a 286 ALA a 287 ILE a 290
SITE 4 AL5 16 CLA a 607 PHO a 608 CLA a 615 CLA d 401
SITE 1 AL6 17 GLN a 199 VAL a 202 ALA a 203 LEU a 210
SITE 2 AL6 17 CLA a 606 PHO a 609 PL9 a 612 LHG a 617
SITE 3 AL6 17 HOH a 749 HOH a 751 PHE d 157 VAL d 175
SITE 4 AL6 17 ILE d 178 PHE d 179 LEU d 182 CLA d 401
SITE 5 AL6 17 LMG d 407
SITE 1 AL7 15 LEU a 41 ALA a 44 THR a 45 TYR a 126
SITE 2 AL7 15 GLN a 130 TYR a 147 PRO a 279 VAL a 283
SITE 3 AL7 15 CLA a 606 CLA a 615 ALA d 208 LEU d 209
SITE 4 AL7 15 ILE d 213 TRP d 253 PHE d 257
SITE 1 AL8 14 LEU a 210 MET a 214 CLA a 607 ALA d 41
SITE 2 AL8 14 TRP d 48 GLY d 121 LEU d 122 PHE d 125
SITE 3 AL8 14 GLN d 129 ASN d 142 PHE d 146 PHE d 153
SITE 4 AL8 14 LEU d 279 CLA d 401
SITE 1 AL9 13 ILE a 36 THR a 40 PHE a 93 PRO a 95
SITE 2 AL9 13 ILE a 96 TRP a 97 LEU a 114 HIS a 118
SITE 3 AL9 13 LMG a 614 TYR i 9 VAL i 12 THR i 13
SITE 4 AL9 13 PHE i 15
SITE 1 AM1 2 LEU a 42 ALA a 43
SITE 1 AM2 13 MET a 214 HIS a 215 LEU a 218 HIS a 252
SITE 2 AM2 13 PHE a 255 ALA a 263 SER a 264 PHE a 265
SITE 3 AM2 13 LEU a 271 CLA a 607 LHG a 617 PRO d 39
SITE 4 AM2 13 LEU d 45
SITE 1 AM3 12 ASN a 267 SER a 270 TRP a 278 VAL a 281
SITE 2 AM3 12 HOH a 701 HOH a 741 GLN c 28 TRP c 36
SITE 3 AM3 12 SER d 230 PHE d 232 ARG d 233 PHE k 37
SITE 1 AM4 12 TRP a 97 GLU a 98 CLA a 610 LYS c 215
SITE 2 AM4 12 SER c 216 PHE c 218 GLU c 221 TRP c 223
SITE 3 AM4 12 CLA c 505 DGD c 516 LYS i 5 TYR i 9
SITE 1 AM5 15 PHE a 158 MET a 172 ILE a 176 THR a 179
SITE 2 AM5 15 MET a 183 CLA a 606 PHO a 608 HOH a 759
SITE 3 AM5 15 MET d 198 VAL d 201 ALA d 202 CLA d 401
SITE 4 AM5 15 PL9 d 404 LHG d 406 PHE t 10
SITE 1 AM6 13 ARG a 140 TRP a 142 PHE a 273 PHE c 33
SITE 2 AM6 13 TRP c 36 TRP c 443 ARG c 447 CLA c 508
SITE 3 AM6 13 GLU d 219 ASN d 220 ALA d 229 THR d 231
SITE 4 AM6 13 PHE d 232
SITE 1 AM7 7 TYR a 262 CLA a 607 PL9 a 612 LEU d 37
SITE 2 AM7 7 PRO e 9 PHE e 10 SER e 11
SITE 1 AM8 9 GLY b 186 PRO b 187 PHE b 190 CLA b 602
SITE 2 AM8 9 LMG b 620 HOH b 758 PHE h 41 LEU h 55
SITE 3 AM8 9 BCR h 101
SITE 1 AM9 16 GLY b 189 PHE b 190 PRO b 192 GLY b 197
SITE 2 AM9 16 HIS b 201 ALA b 205 PHE b 247 CLA b 601
SITE 3 AM9 16 CLA b 603 HOH b 795 ILE d 159 PHE h 38
SITE 4 AM9 16 PHE h 41 ILE h 45 TYR h 49 DGD h 102
SITE 1 AN1 14 ARG b 68 LEU b 69 ALA b 146 CYS b 150
SITE 2 AN1 14 PHE b 153 HIS b 201 HIS b 202 VAL b 252
SITE 3 AN1 14 THR b 262 CLA b 602 CLA b 604 CLA b 605
SITE 4 AN1 14 CLA b 606 HOH b 766
SITE 1 AN2 20 TRP b 33 PHE b 61 PHE b 65 ARG b 68
SITE 2 AN2 20 LEU b 149 VAL b 245 ALA b 248 ALA b 249
SITE 3 AN2 20 VAL b 252 PHE b 451 HIS b 455 PHE b 458
SITE 4 AN2 20 CLA b 603 CLA b 605 CLA b 607 CLA b 610
SITE 5 AN2 20 CLA b 611 CLA b 612 CLA b 613 CLA b 615
SITE 1 AN3 17 THR b 27 VAL b 30 ALA b 31 ALA b 34
SITE 2 AN3 17 VAL b 62 MET b 66 ARG b 68 VAL b 96
SITE 3 AN3 17 HIS b 100 LEU b 103 ALA b 205 GLY b 209
SITE 4 AN3 17 CLA b 603 CLA b 604 CLA b 606 CLA b 612
SITE 5 AN3 17 HOH b 755
SITE 1 AN4 17 LEU b 69 GLY b 70 VAL b 71 TRP b 91
SITE 2 AN4 17 VAL b 96 ALA b 99 HIS b 100 VAL b 102
SITE 3 AN4 17 GLY b 152 PHE b 153 PHE b 156 HIS b 157
SITE 4 AN4 17 PHE b 162 PRO b 164 CLA b 603 CLA b 605
SITE 5 AN4 17 BCR b 619
SITE 1 AN5 15 TRP b 33 TYR b 40 GLN b 58 GLY b 59
SITE 2 AN5 15 PHE b 61 THR b 327 GLY b 328 TRP b 450
SITE 3 AN5 15 PHE b 451 CLA b 604 HOH b 792 PHE d 196
SITE 4 AN5 15 MET d 199 LHG d 405 LMG m 102
SITE 1 AN6 10 THR b 236 SER b 239 ALA b 243 PHE b 463
SITE 2 AN6 10 HIS b 466 CLA b 609 CLA b 610 PHE d 120
SITE 3 AN6 10 CLA d 402 LMG d 408
SITE 1 AN7 14 PHE b 139 VAL b 208 ALA b 212 PHE b 215
SITE 2 AN7 14 HIS b 216 PRO b 221 PRO b 222 LEU b 229
SITE 3 AN7 14 CLA b 608 CLA b 610 THR h 27 MET h 31
SITE 4 AN7 14 LEU h 39 BCR h 101
SITE 1 AN8 14 HIS b 23 PHE b 139 HIS b 142 LEU b 143
SITE 2 AN8 14 MET b 231 THR b 236 VAL b 237 SER b 241
SITE 3 AN8 14 CLA b 604 CLA b 608 CLA b 609 CLA b 612
SITE 4 AN8 14 CLA b 615 HOH b 719
SITE 1 AN9 18 TRP b 5 TYR b 6 ARG b 7 VAL b 8
SITE 2 AN9 18 HIS b 9 LEU b 461 PHE b 462 PHE b 464
SITE 3 AN9 18 GLY b 465 TRP b 468 HIS b 469 ARG b 472
SITE 4 AN9 18 CLA b 604 CLA b 612 CLA b 613 CLA b 614
SITE 5 AN9 18 HOH b 746 LHG d 405
SITE 1 AO1 16 HIS b 9 LEU b 19 HIS b 23 HIS b 26
SITE 2 AO1 16 THR b 27 VAL b 237 LEU b 238 SER b 241
SITE 3 AO1 16 CLA b 604 CLA b 605 CLA b 610 CLA b 611
SITE 4 AO1 16 CLA b 613 CLA b 614 CLA b 615 HOH b 768
SITE 1 AO2 10 HIS b 26 VAL b 30 PHE b 462 CLA b 604
SITE 2 AO2 10 CLA b 611 CLA b 612 CLA b 614 BCR b 617
SITE 3 AO2 10 BCR b 618 LHG d 405
SITE 1 AO3 11 SQD L 101 VAL b 8 HIS b 9 TRP b 115
SITE 2 AO3 11 CLA b 611 CLA b 612 CLA b 613 BCR b 617
SITE 3 AO3 11 HOH b 800 GLN l 8 PHE m 21
SITE 1 AO4 10 HIS b 23 LEU b 24 MET b 138 HIS b 142
SITE 2 AO4 10 LEU b 145 CLA b 604 CLA b 610 CLA b 612
SITE 3 AO4 10 CLA b 616 LEU h 11
SITE 1 AO5 8 ILE b 20 LEU b 24 TRP b 113 HIS b 114
SITE 2 AO5 8 CLA b 615 BCR b 619 HOH b 787 THR h 5
SITE 1 AO6 7 SQD L 101 MET b 25 TRP b 115 CLA b 613
SITE 2 AO6 7 CLA b 614 BCR b 618 LEU m 13
SITE 1 AO7 11 SQD L 101 BCR T 101 LEU b 29 GLY b 32
SITE 2 AO7 11 TRP b 33 SER b 36 ILE b 101 VAL b 102
SITE 3 AO7 11 GLY b 105 CLA b 613 BCR b 617
SITE 1 AO8 5 SQD A 616 LEU b 109 TRP b 113 CLA b 606
SITE 2 AO8 5 CLA b 616
SITE 1 AO9 6 GLU b 184 TRP b 185 CLA b 601 MET c 180
SITE 2 AO9 6 LEU c 204 LMG c 520
SITE 1 AP1 7 ILE A 50 LEU A 102 ASP A 103 LEU A 106
SITE 2 AP1 7 HOH A 701 TRP b 75 LEU b 98
SITE 1 AP2 13 LEU c 95 LEU c 168 GLY c 171 ALA c 172
SITE 2 AP2 13 LEU c 175 HIS c 237 PHE c 289 TYR c 297
SITE 3 AP2 13 CLA c 502 CLA c 503 CLA c 507 BCR c 515
SITE 4 AP2 13 HOH c 666
SITE 1 AP3 14 TRP c 63 HIS c 91 LEU c 95 LEU c 279
SITE 2 AP3 14 MET c 282 ALA c 286 TYR c 297 HIS c 430
SITE 3 AP3 14 LEU c 433 PHE c 437 CLA c 501 CLA c 503
SITE 4 AP3 14 CLA c 510 CLA c 512
SITE 1 AP4 11 ILE c 60 VAL c 61 ALA c 64 THR c 68
SITE 2 AP4 11 LEU c 88 HIS c 91 VAL c 114 HIS c 118
SITE 3 AP4 11 LEU c 279 CLA c 501 CLA c 502
SITE 1 AP5 15 TRP c 63 MET c 67 PHE c 70 GLN c 84
SITE 2 AP5 15 GLY c 85 ILE c 87 TRP c 425 SER c 429
SITE 3 AP5 15 CLA c 508 DGD c 517 LMG c 519 HOH c 634
SITE 4 AP5 15 HOH c 646 PRO k 26 VAL k 30
SITE 1 AP6 11 TRP a 131 LMG a 614 PHE c 264 TYR c 274
SITE 2 AP6 11 HIS c 441 LEU c 442 ALA c 445 ARG c 449
SITE 3 AP6 11 CLA c 507 BCR c 515 HOH c 632
SITE 1 AP7 13 LEU c 165 ILE c 243 GLY c 247 TRP c 250
SITE 2 AP7 13 HIS c 251 THR c 255 PRO c 256 PHE c 257
SITE 3 AP7 13 TRP c 259 PHE c 264 CLA c 507 LEU i 24
SITE 4 AP7 13 SER i 25
SITE 1 AP8 17 MET c 157 THR c 158 LEU c 161 HIS c 164
SITE 2 AP8 17 LEU c 168 PHE c 264 TRP c 266 TYR c 271
SITE 3 AP8 17 TYR c 274 SER c 275 LEU c 279 CLA c 501
SITE 4 AP8 17 CLA c 505 CLA c 506 CLA c 509 HOH c 602
SITE 5 AP8 17 HOH c 645
SITE 1 AP9 18 LHG a 616 PHE c 33 TRP c 36 ALA c 37
SITE 2 AP9 18 GLY c 38 ASN c 39 ALA c 40 LEU c 272
SITE 3 AP9 18 LEU c 276 PHE c 436 GLY c 440 TRP c 443
SITE 4 AP9 18 HIS c 444 ARG c 447 CLA c 504 CLA c 509
SITE 5 AP9 18 CLA c 510 CLA c 511
SITE 1 AQ1 15 ASN c 39 LEU c 49 ALA c 52 HIS c 53
SITE 2 AQ1 15 HIS c 56 GLY c 268 TYR c 271 LEU c 272
SITE 3 AQ1 15 SER c 275 LEU c 279 CLA c 507 CLA c 508
SITE 4 AQ1 15 CLA c 510 CLA c 511 CLA c 512
SITE 1 AQ2 11 ASN c 39 HIS c 56 LEU c 59 PHE c 437
SITE 2 AQ2 11 CLA c 502 CLA c 508 CLA c 509 CLA c 511
SITE 3 AQ2 11 LMG c 519 PRO k 29 LEU k 33
SITE 1 AQ3 18 ARG c 26 TRP c 35 GLY c 38 ASN c 39
SITE 2 AQ3 18 ARG c 41 LEU c 42 LYS c 48 PHE c 127
SITE 3 AQ3 18 CLA c 508 CLA c 509 CLA c 510 BCR c 522
SITE 4 AQ3 18 TRP k 39 GLN k 40 ASN y 45 LEU y 46
SITE 5 AQ3 18 MET z 19 VAL z 20
SITE 1 AQ4 11 HIS c 53 PHE c 146 PHE c 147 ILE c 160
SITE 2 AQ4 11 PHE c 163 HIS c 164 ILE c 170 CLA c 502
SITE 3 AQ4 11 CLA c 509 CLA c 513 BCR c 514
SITE 1 AQ5 10 LEU c 50 VAL c 54 VAL c 124 GLY c 128
SITE 2 AQ5 10 TYR c 131 HIS c 132 LEU c 140 TYR c 143
SITE 3 AQ5 10 CLA c 512 BCR c 514
SITE 1 AQ6 6 SER c 121 VAL c 124 CLA c 512 CLA c 513
SITE 2 AQ6 6 TYR k 15 VAL z 51
SITE 1 AQ7 7 ILE c 209 LEU c 213 GLY c 236 ILE c 240
SITE 2 AQ7 7 PHE c 264 CLA c 501 CLA c 505
SITE 1 AQ8 21 LEU a 91 PHE a 155 LMG a 614 PRO c 217
SITE 2 AQ8 21 GLY c 219 GLY c 220 GLU c 221 GLY c 222
SITE 3 AQ8 21 TRP c 223 SER c 226 PHE c 284 PHE c 292
SITE 4 AQ8 21 ASN c 293 ASN c 294 THR c 295 ASP c 360
SITE 5 AQ8 21 PHE c 361 ARG c 362 HOH c 604 HOH c 651
SITE 6 AQ8 21 HOH c 659
SITE 1 AQ9 15 PHE a 197 GLU c 83 GLN c 84 GLY c 85
SITE 2 AQ9 15 SER c 406 ASN c 418 PHE c 419 VAL c 420
SITE 3 AQ9 15 TRP c 425 CLA c 504 DGD c 518 LMG c 519
SITE 4 AQ9 15 HOH c 624 LMG d 407 TYR j 33
SITE 1 AR1 17 GLN a 199 PHE a 300 ASN a 301 SER a 305
SITE 2 AR1 17 ASN c 405 SER c 406 ASN c 415 SER c 416
SITE 3 AR1 17 VAL c 417 ASN c 418 DGD c 517 LMG d 407
SITE 4 AR1 17 ALA j 32 TYR j 33 GLY j 37 SER j 38
SITE 5 AR1 17 SER j 39
SITE 1 AR2 7 HIS c 74 CLA c 504 CLA c 510 DGD c 517
SITE 2 AR2 7 HOH c 660 ASP k 23 GLN y 21
SITE 1 AR3 9 ALA b 155 THR b 159 LEU b 161 PRO b 183
SITE 2 AR3 9 TRP b 185 LMG b 620 LEU c 204 ASP c 205
SITE 3 AR3 9 HOH c 606
SITE 1 AR4 12 PHE c 62 BCR c 522 THR j 15 ILE k 28
SITE 2 AR4 12 LEU k 31 ALA k 34 VAL k 38 ILE y 28
SITE 3 AR4 12 GLY y 29 GLY y 32 SER z 16 PHE z 17
SITE 1 AR5 8 ALA c 55 GLY c 58 LEU c 59 SER c 122
SITE 2 AR5 8 ALA c 123 CLA c 511 BCR c 521 PHE k 32
SITE 1 AR6 19 PHE a 206 CLA a 606 CLA a 607 PHO a 609
SITE 2 AR6 19 CLA a 615 PRO d 149 VAL d 152 VAL d 156
SITE 3 AR6 19 LEU d 182 PHE d 185 GLN d 186 TRP d 191
SITE 4 AR6 19 THR d 192 HIS d 197 GLY d 200 VAL d 201
SITE 5 AR6 19 SER d 282 ALA d 283 VAL d 286
SITE 1 AR7 15 CLA b 608 CYS d 40 LEU d 43 LEU d 89
SITE 2 AR7 15 LEU d 90 LEU d 91 LEU d 92 TRP d 93
SITE 3 AR7 15 THR d 112 PHE d 113 LEU d 116 HIS d 117
SITE 4 AR7 15 GLY x 13 LEU x 14 LEU x 15
SITE 1 AR8 12 TYR d 42 LEU d 43 GLY d 46 GLY d 47
SITE 2 AR8 12 LEU d 49 THR d 50 LMG d 407 PRO f 29
SITE 3 AR8 12 THR f 30 PHE f 33 VAL j 21 VAL j 25
SITE 1 AR9 14 PHE a 52 CLA a 615 MET d 198 MET d 199
SITE 2 AR9 14 HIS d 214 THR d 217 TRP d 253 ALA d 260
SITE 3 AR9 14 PHE d 261 LEU d 267 VAL d 274 VAL l 26
SITE 4 AR9 14 LHG l 101 PHE t 10
SITE 1 AS1 14 ASN a 234 TYR b 6 ARG b 7 PHE b 464
SITE 2 AS1 14 TRP b 468 CLA b 607 CLA b 611 CLA b 613
SITE 3 AS1 14 HOH b 746 TYR d 141 ILE d 144 PHE d 269
SITE 4 AS1 14 HOH d 520 LHG l 101
SITE 1 AS2 15 CLA a 615 ILE d 256 PHE d 257 ALA d 260
SITE 2 AS2 15 PHE d 261 SER d 262 ASN d 263 TRP d 266
SITE 3 AS2 15 HOH d 527 ASN l 13 LEU l 19 LHG l 101
SITE 4 AS2 15 HOH l 203 PHE t 17 ALA t 20
SITE 1 AS3 18 CLA a 607 DGD c 517 DGD c 518 TYR d 67
SITE 2 AS3 18 GLY d 70 CYS d 71 ASN d 72 PHE d 73
SITE 3 AS3 18 BCR d 403 THR f 30 ILE f 37 MET f 40
SITE 4 AS3 18 GLN f 41 PHE j 28 GLY j 31 ALA j 32
SITE 5 AS3 18 LEU j 36 HOH j 901
SITE 1 AS4 6 ALA b 228 ARG b 230 CLA b 608 ASP d 19
SITE 2 AS4 6 LYS d 23 TRP d 32
SITE 1 AS5 13 ILE e 13 ARG e 18 TYR e 19 HIS e 23
SITE 2 AS5 13 THR e 26 LEU e 30 HOH e 201 ARG f 19
SITE 3 AS5 13 TRP f 20 VAL f 23 HIS f 24 VAL f 28
SITE 4 AS5 13 ALA r 19
SITE 1 AS6 8 ARG d 24 ARG d 26 HOH e 203 PHE f 16
SITE 2 AS6 8 THR f 17 VAL f 18 LEU r 34 ASP x 35
SITE 1 AS7 4 CLA b 601 CLA b 609 LEU h 37 PHE h 38
SITE 1 AS8 15 TYR b 193 PHE b 250 TYR b 258 TYR b 273
SITE 2 AS8 15 SER b 277 CLA b 602 HIS d 87 LEU d 162
SITE 3 AS8 15 TYR h 49 ASN h 50 VAL h 60 SER h 61
SITE 4 AS8 15 TRP h 62 HOH h 202 HOH h 203
SITE 1 AS9 14 SER a 232 ASN a 234 PRO b 4 TRP b 5
SITE 2 AS9 14 TYR b 6 TRP d 266 PHE d 273 PL9 d 404
SITE 3 AS9 14 LHG d 405 LHG d 406 GLU l 11 LEU l 12
SITE 4 AS9 14 ASN l 13 SER l 16
SITE 1 AT1 10 THR b 327 LYS b 332 VAL b 457 CLA b 607
SITE 2 AT1 10 PHE l 35 ASN m 4 LEU m 6 ALA m 10
SITE 3 AT1 10 HOH m 202 HOH m 204
SITE 1 AT2 6 TRP B 33 MET B 37 BCR B 617 BCR B 618
SITE 2 AT2 6 PHE t 18 PHE t 22
SITE 1 AT3 21 PHE v 33 ALA v 36 ALA v 38 SER v 39
SITE 2 AT3 21 CYS v 40 HIS v 41 THR v 46 THR v 48
SITE 3 AT3 21 LEU v 52 ASP v 53 LEU v 54 THR v 58
SITE 4 AT3 21 TYR v 75 TYR v 82 HIS v 92 PRO v 93
SITE 5 AT3 21 HOH v 306 HOH v 307 HOH v 309 HOH v 319
SITE 6 AT3 21 HOH v 322
SITE 1 AT4 23 ALA v 36 CYS v 37 ALA v 38 SER v 39
SITE 2 AT4 23 HIS v 41 VAL v 42 ILE v 45 THR v 46
SITE 3 AT4 23 LYS v 47 THR v 48 LEU v 52 ASP v 53
SITE 4 AT4 23 LEU v 54 THR v 58 TYR v 75 TYR v 82
SITE 5 AT4 23 HIS v 92 PRO v 93 HOH v 306 HOH v 307
SITE 6 AT4 23 HOH v 309 HOH v 319 HOH v 322
SITE 1 AT5 21 PHE v 33 ALA v 36 ALA v 38 SER v 39
SITE 2 AT5 21 CYS v 40 HIS v 41 THR v 46 THR v 48
SITE 3 AT5 21 LEU v 52 ASP v 53 LEU v 54 THR v 58
SITE 4 AT5 21 TYR v 75 TYR v 82 HIS v 92 PRO v 93
SITE 5 AT5 21 HOH v 306 HOH v 307 HOH v 309 HOH v 319
SITE 6 AT5 21 HOH v 322
CRYST1 117.870 223.140 310.710 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 0.008484 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004481 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003218 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
