HEADER PHOTOSYNTHESIS 23-MAY-12 4FBY
TITLE FS X-RAY DIFFRACTION OF PHOTOSYSTEM II
CAVEAT 4FBY CHIRALITY ERRORS ON THE CHIRAL CENTERS OF SOME OF THE DGD
CAVEAT 2 4FBY AND LMG LIGANDS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOTOSYSTEM Q(B) PROTEIN 1;
COMPND 3 CHAIN: A, G;
COMPND 4 SYNONYM: 32 KDA THYLAKOID MEMBRANE PROTEIN 1, PHOTOSYSTEM II PROTEIN
COMPND 5 D1 1;
COMPND 6 EC: 1.10.3.9;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PHOTOSYSTEM II CORE LIGHT HARVESTING PROTEIN;
COMPND 9 CHAIN: B, N;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: PHOTOSYSTEM II CP43 PROTEIN;
COMPND 12 CHAIN: C, P;
COMPND 13 MOL_ID: 4;
COMPND 14 MOLECULE: PHOTOSYSTEM II D2 PROTEIN;
COMPND 15 CHAIN: D, Q;
COMPND 16 SYNONYM: PSII D2 PROTEIN, PHOTOSYSTEM Q(A) PROTEIN;
COMPND 17 EC: 1.10.3.9;
COMPND 18 MOL_ID: 5;
COMPND 19 MOLECULE: CYTOCHROME B559 SUBUNIT ALPHA;
COMPND 20 CHAIN: E, R;
COMPND 21 SYNONYM: PSII REACTION CENTER SUBUNIT V;
COMPND 22 MOL_ID: 6;
COMPND 23 MOLECULE: CYTOCHROME B559 SUBUNIT BETA;
COMPND 24 CHAIN: F, S;
COMPND 25 SYNONYM: PSII REACTION CENTER SUBUNIT VI;
COMPND 26 MOL_ID: 7;
COMPND 27 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN H;
COMPND 28 CHAIN: H, W;
COMPND 29 SYNONYM: PSII-H;
COMPND 30 MOL_ID: 8;
COMPND 31 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN I;
COMPND 32 CHAIN: I, a;
COMPND 33 SYNONYM: PSII-I, PSII 4.4 KDA PROTEIN;
COMPND 34 MOL_ID: 9;
COMPND 35 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN J;
COMPND 36 CHAIN: J, b;
COMPND 37 SYNONYM: PSII-J;
COMPND 38 MOL_ID: 10;
COMPND 39 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN K;
COMPND 40 CHAIN: K, c;
COMPND 41 SYNONYM: PSII-K;
COMPND 42 MOL_ID: 11;
COMPND 43 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN L;
COMPND 44 CHAIN: L, d;
COMPND 45 SYNONYM: PSII-L, PSII 5 KDA PROTEIN;
COMPND 46 MOL_ID: 12;
COMPND 47 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN M;
COMPND 48 CHAIN: M, e;
COMPND 49 SYNONYM: PSII-M;
COMPND 50 MOL_ID: 13;
COMPND 51 MOLECULE: PHOTOSYSTEM II MANGANESE-STABILIZING POLYPEPTIDE;
COMPND 52 CHAIN: O, f;
COMPND 53 SYNONYM: MSP;
COMPND 54 MOL_ID: 14;
COMPND 55 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN T;
COMPND 56 CHAIN: T, g;
COMPND 57 SYNONYM: PSII-T, PSII-TC;
COMPND 58 MOL_ID: 15;
COMPND 59 MOLECULE: PHOTOSYSTEM II 12 KDA EXTRINSIC PROTEIN;
COMPND 60 CHAIN: U, h;
COMPND 61 SYNONYM: PS II COMPLEX 12 KDA EXTRINSIC PROTEIN, PSII-U;
COMPND 62 MOL_ID: 16;
COMPND 63 MOLECULE: CYTOCHROME C-550;
COMPND 64 CHAIN: V, i;
COMPND 65 SYNONYM: CYTOCHROME C-549, CYTOCHROME C550, LOW-POTENTIAL CYTOCHROME
COMPND 66 C;
COMPND 67 MOL_ID: 17;
COMPND 68 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN YCF12;
COMPND 69 CHAIN: y, m;
COMPND 70 MOL_ID: 18;
COMPND 71 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN X;
COMPND 72 CHAIN: X, j;
COMPND 73 MOL_ID: 19;
COMPND 74 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN Y;
COMPND 75 CHAIN: Y, k;
COMPND 76 MOL_ID: 20;
COMPND 77 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN Z;
COMPND 78 CHAIN: Z, l;
COMPND 79 SYNONYM: PSII-Z
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 3 ORGANISM_TAXID: 197221;
SOURCE 4 STRAIN: BP-1;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 7 ORGANISM_TAXID: 197221;
SOURCE 8 STRAIN: BP-1;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 11 ORGANISM_TAXID: 197221;
SOURCE 12 STRAIN: BP-1;
SOURCE 13 MOL_ID: 4;
SOURCE 14 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 15 ORGANISM_TAXID: 197221;
SOURCE 16 STRAIN: BP-1;
SOURCE 17 MOL_ID: 5;
SOURCE 18 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 19 ORGANISM_TAXID: 197221;
SOURCE 20 STRAIN: BP-1;
SOURCE 21 MOL_ID: 6;
SOURCE 22 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 23 ORGANISM_TAXID: 197221;
SOURCE 24 STRAIN: BP-1;
SOURCE 25 MOL_ID: 7;
SOURCE 26 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 27 ORGANISM_TAXID: 197221;
SOURCE 28 STRAIN: BP-1;
SOURCE 29 MOL_ID: 8;
SOURCE 30 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 31 ORGANISM_TAXID: 197221;
SOURCE 32 STRAIN: BP-1;
SOURCE 33 MOL_ID: 9;
SOURCE 34 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 35 ORGANISM_TAXID: 197221;
SOURCE 36 STRAIN: BP-1;
SOURCE 37 MOL_ID: 10;
SOURCE 38 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 39 ORGANISM_TAXID: 197221;
SOURCE 40 STRAIN: BP-1;
SOURCE 41 MOL_ID: 11;
SOURCE 42 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 43 ORGANISM_TAXID: 197221;
SOURCE 44 STRAIN: BP-1;
SOURCE 45 MOL_ID: 12;
SOURCE 46 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 47 ORGANISM_TAXID: 197221;
SOURCE 48 STRAIN: BP-1;
SOURCE 49 MOL_ID: 13;
SOURCE 50 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 51 ORGANISM_TAXID: 197221;
SOURCE 52 STRAIN: BP-1;
SOURCE 53 MOL_ID: 14;
SOURCE 54 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 55 ORGANISM_TAXID: 197221;
SOURCE 56 STRAIN: BP-1;
SOURCE 57 MOL_ID: 15;
SOURCE 58 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 59 ORGANISM_TAXID: 197221;
SOURCE 60 STRAIN: BP-1;
SOURCE 61 MOL_ID: 16;
SOURCE 62 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 63 ORGANISM_TAXID: 197221;
SOURCE 64 STRAIN: BP-1;
SOURCE 65 MOL_ID: 17;
SOURCE 66 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 67 ORGANISM_TAXID: 197221;
SOURCE 68 STRAIN: BP-1;
SOURCE 69 MOL_ID: 18;
SOURCE 70 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 71 ORGANISM_TAXID: 197221;
SOURCE 72 STRAIN: BP-1;
SOURCE 73 MOL_ID: 19;
SOURCE 74 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 75 ORGANISM_TAXID: 197221;
SOURCE 76 STRAIN: BP-1;
SOURCE 77 MOL_ID: 20;
SOURCE 78 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 79 ORGANISM_TAXID: 197221;
SOURCE 80 STRAIN: BP-1
KEYWDS PHOTOSYSTEM, PS II, PS2, MEMBRANE COMPLEX, TRANSMEMBRANE ALPHA-HELIX,
KEYWDS 2 PHOTOSYNTHESIS, X-RAY FREE ELECTRON LASER, PHOTOSYSTEM II, REACTION
KEYWDS 3 CENTER, IRON, MANGANESE, LIGHT HARVESTING, ELECTRON TRANSPORT, WATER
KEYWDS 4 OXIDATION, THYLAKOID MEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.KERN,R.ALONSO-MORI,J.HELLMICH,R.TRAN,J.HATTNE,H.LAKSMONO,
AUTHOR 2 C.GLOECKNER,N.ECHOLS,R.G.SIERRA,J.SELLBERG,B.LASSALLE-KAISER,
AUTHOR 3 R.J.GILDEA,P.GLATZEL,R.W.GROSSE-KUNSTLEVE,M.J.LATIMER,T.A.MCQUEEN,
AUTHOR 4 D.DIFIORE,A.R.FRY,M.M.MESSERSCHMIDT,A.MIAHNAHRI,D.W.SCHAFER,
AUTHOR 5 M.M.SEIBERT,D.SOKARAS,T.-C.WENG,P.H.ZWART,W.E.WHITE,P.D.ADAMS,
AUTHOR 6 M.J.BOGAN,S.BOUTET,G.J.WILLIAMS,J.MESSINGER,N.K.SAUTER,A.ZOUNI,
AUTHOR 7 U.BERGMANN,J.YANO,V.K.YACHANDRA
REVDAT 7 14-FEB-18 4FBY 1 REMARK
REVDAT 6 29-NOV-17 4FBY 1 REMARK
REVDAT 5 15-NOV-17 4FBY 1 REMARK
REVDAT 4 21-DEC-16 4FBY 1 REMARK
REVDAT 3 09-JAN-13 4FBY 1 JRNL
REVDAT 2 25-JUL-12 4FBY 1 HET
REVDAT 1 20-JUN-12 4FBY 0
JRNL AUTH J.KERN,R.ALONSO-MORI,J.HELLMICH,R.TRAN,J.HATTNE,H.LAKSMONO,
JRNL AUTH 2 C.GLOCKNER,N.ECHOLS,R.G.SIERRA,J.SELLBERG,B.LASSALLE-KAISER,
JRNL AUTH 3 R.J.GILDEA,P.GLATZEL,R.W.GROSSE-KUNSTLEVE,M.J.LATIMER,
JRNL AUTH 4 T.A.MCQUEEN,D.DIFIORE,A.R.FRY,M.MESSERSCHMIDT,A.MIAHNAHRI,
JRNL AUTH 5 D.W.SCHAFER,M.M.SEIBERT,D.SOKARAS,T.C.WENG,P.H.ZWART,
JRNL AUTH 6 W.E.WHITE,P.D.ADAMS,M.J.BOGAN,S.BOUTET,G.J.WILLIAMS,
JRNL AUTH 7 J.MESSINGER,N.K.SAUTER,A.ZOUNI,U.BERGMANN,J.YANO,
JRNL AUTH 8 V.K.YACHANDRA
JRNL TITL ROOM TEMPERATURE FEMTOSECOND X-RAY DIFFRACTION OF
JRNL TITL 2 PHOTOSYSTEM II MICROCRYSTALS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 109 9721 2012
JRNL REFN ISSN 0027-8424
JRNL PMID 22665786
JRNL DOI 10.1073/PNAS.1204598109
REMARK 2
REMARK 2 RESOLUTION. 6.56 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.3
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 6.56
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 85.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.480
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 17914
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.367
REMARK 3 R VALUE (WORKING SET) : 0.366
REMARK 3 FREE R VALUE : 0.385
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 895
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 85.8920 - 11.9035 1.00 3031 160 0.3942 0.3855
REMARK 3 2 11.9035 - 9.4520 1.00 2923 152 0.3181 0.3419
REMARK 3 3 9.4520 - 8.2583 1.00 2884 153 0.3270 0.3471
REMARK 3 4 8.2583 - 7.5037 1.00 2866 149 0.3526 0.3996
REMARK 3 5 7.5037 - 6.9662 1.00 2835 150 0.3913 0.4193
REMARK 3 6 6.9662 - 6.5556 0.88 2480 131 0.4272 0.4568
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.73
REMARK 3 K_SOL : 0.29
REMARK 3 B_SOL : 73.83
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 1.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 40.290
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.83
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 150.1
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.95850
REMARK 3 B22 (A**2) : 43.00520
REMARK 3 B33 (A**2) : -39.04670
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 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 : 0.007 52048
REMARK 3 ANGLE : 1.483 71500
REMARK 3 CHIRALITY : 0.095 7242
REMARK 3 PLANARITY : 0.008 7548
REMARK 3 DIHEDRAL : 16.095 19968
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: NULL
REMARK 4
REMARK 4 4FBY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-12.
REMARK 100 THE DEPOSITION ID IS D_1000072709.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-SEP-11
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 2984
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : FREE ELECTRON LASER
REMARK 200 BEAMLINE : CXI
REMARK 200 X-RAY GENERATOR MODEL : SLAC LCLS BEAMLINE CXI
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.323
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : KB MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : CS-PAD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CCTBX.XFEL
REMARK 200 DATA SCALING SOFTWARE : CCTBX.XFEL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17962
REMARK 200 RESOLUTION RANGE HIGH (A) : 6.556
REMARK 200 RESOLUTION RANGE LOW (A) : 85.890
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 6.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 6.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.84
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.740
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3BZ1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 4% PEG 2000, 5 MM CACL2, 100 MM PIPES,
REMARK 280 PH 7.0, BATCH, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 65.39150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 154.31500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 113.88200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 154.31500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 65.39150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 113.88200
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYMMETRIC UNIT
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 40-MERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, H, I, J, K,
REMARK 350 AND CHAINS: L, M, O, T, U, V, y, X, Y,
REMARK 350 AND CHAINS: Z, G, N, P, Q, R, S, W, a, b,
REMARK 350 AND CHAINS: c, d, e, f, g, h, i, m, j,
REMARK 350 AND CHAINS: k, l
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 THR A 3
REMARK 465 THR A 4
REMARK 465 LEU A 5
REMARK 465 GLN A 6
REMARK 465 ARG A 7
REMARK 465 ARG A 8
REMARK 465 GLU A 9
REMARK 465 MET B 1
REMARK 465 GLU B 492
REMARK 465 TRP B 493
REMARK 465 GLY B 494
REMARK 465 PHE B 495
REMARK 465 TYR B 496
REMARK 465 GLN B 497
REMARK 465 LYS B 498
REMARK 465 VAL B 499
REMARK 465 GLY B 500
REMARK 465 ASP B 501
REMARK 465 VAL B 502
REMARK 465 THR B 503
REMARK 465 THR B 504
REMARK 465 ARG B 505
REMARK 465 ARG B 506
REMARK 465 LYS B 507
REMARK 465 GLU B 508
REMARK 465 ALA B 509
REMARK 465 VAL B 510
REMARK 465 MET C 13
REMARK 465 VAL C 14
REMARK 465 THR C 15
REMARK 465 LEU C 16
REMARK 465 SER C 17
REMARK 465 SER C 18
REMARK 465 ASN C 19
REMARK 465 SER C 20
REMARK 465 ILE C 21
REMARK 465 PHE C 22
REMARK 465 ALA C 23
REMARK 465 THR C 24
REMARK 465 ASN C 25
REMARK 465 ARG C 26
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 ILE D 3
REMARK 465 ALA D 4
REMARK 465 ILE D 5
REMARK 465 GLY D 6
REMARK 465 ARG D 7
REMARK 465 ALA D 8
REMARK 465 PRO D 9
REMARK 465 ALA D 10
REMARK 465 GLU D 11
REMARK 465 ARG D 12
REMARK 465 ALA E 2
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 ASP I 36
REMARK 465 LEU I 37
REMARK 465 GLU I 38
REMARK 465 MET J 2
REMARK 465 SER J 3
REMARK 465 GLU J 4
REMARK 465 GLY J 5
REMARK 465 GLY J 6
REMARK 465 SER M 35
REMARK 465 SER M 36
REMARK 465 ALA O 27
REMARK 465 LYS O 28
REMARK 465 GLN O 29
REMARK 465 ALA U 31
REMARK 465 THR U 32
REMARK 465 ALA U 33
REMARK 465 SER U 34
REMARK 465 THR U 35
REMARK 465 GLU U 36
REMARK 465 GLU U 37
REMARK 465 MET 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 ARG X 48
REMARK 465 SER X 49
REMARK 465 LEU X 50
REMARK 465 MET G 1
REMARK 465 THR G 2
REMARK 465 THR G 3
REMARK 465 THR G 4
REMARK 465 LEU G 5
REMARK 465 GLN G 6
REMARK 465 ARG G 7
REMARK 465 ARG G 8
REMARK 465 GLU G 9
REMARK 465 MET N 1
REMARK 465 GLU N 492
REMARK 465 TRP N 493
REMARK 465 GLY N 494
REMARK 465 PHE N 495
REMARK 465 TYR N 496
REMARK 465 GLN N 497
REMARK 465 LYS N 498
REMARK 465 VAL N 499
REMARK 465 GLY N 500
REMARK 465 ASP N 501
REMARK 465 VAL N 502
REMARK 465 THR N 503
REMARK 465 THR N 504
REMARK 465 ARG N 505
REMARK 465 ARG N 506
REMARK 465 LYS N 507
REMARK 465 GLU N 508
REMARK 465 ALA N 509
REMARK 465 VAL N 510
REMARK 465 MET P 13
REMARK 465 VAL P 14
REMARK 465 THR P 15
REMARK 465 LEU P 16
REMARK 465 SER P 17
REMARK 465 SER P 18
REMARK 465 ASN P 19
REMARK 465 SER P 20
REMARK 465 ILE P 21
REMARK 465 PHE P 22
REMARK 465 ALA P 23
REMARK 465 THR P 24
REMARK 465 ASN P 25
REMARK 465 ARG P 26
REMARK 465 MET Q 1
REMARK 465 THR Q 2
REMARK 465 ILE Q 3
REMARK 465 ALA Q 4
REMARK 465 ILE Q 5
REMARK 465 GLY Q 6
REMARK 465 ARG Q 7
REMARK 465 ALA Q 8
REMARK 465 PRO Q 9
REMARK 465 ALA Q 10
REMARK 465 GLU Q 11
REMARK 465 ARG Q 12
REMARK 465 ALA R 2
REMARK 465 THR S 2
REMARK 465 SER S 3
REMARK 465 ASN S 4
REMARK 465 THR S 5
REMARK 465 PRO S 6
REMARK 465 ASN S 7
REMARK 465 GLN S 8
REMARK 465 GLU S 9
REMARK 465 PRO S 10
REMARK 465 ASP a 36
REMARK 465 LEU a 37
REMARK 465 GLU a 38
REMARK 465 MET b 2
REMARK 465 SER b 3
REMARK 465 GLU b 4
REMARK 465 GLY b 5
REMARK 465 GLY b 6
REMARK 465 SER e 35
REMARK 465 SER e 36
REMARK 465 ALA f 27
REMARK 465 LYS f 28
REMARK 465 GLN f 29
REMARK 465 ALA h 31
REMARK 465 THR h 32
REMARK 465 ALA h 33
REMARK 465 SER h 34
REMARK 465 THR h 35
REMARK 465 GLU h 36
REMARK 465 GLU h 37
REMARK 465 MET m 1
REMARK 465 GLY m 2
REMARK 465 ILE m 3
REMARK 465 PHE m 4
REMARK 465 ASN m 5
REMARK 465 GLY m 6
REMARK 465 ILE m 7
REMARK 465 ILE m 8
REMARK 465 GLU m 9
REMARK 465 PHE m 10
REMARK 465 LEU m 11
REMARK 465 SER m 12
REMARK 465 ASN m 13
REMARK 465 ILE m 14
REMARK 465 ASN m 15
REMARK 465 PHE m 16
REMARK 465 GLU m 17
REMARK 465 VAL m 18
REMARK 465 ARG j 48
REMARK 465 SER j 49
REMARK 465 LEU j 50
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 TYR C 143 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU C 462 CG CD OE1 OE2
REMARK 470 LYS H 20 CG CD CE NZ
REMARK 470 ARG O 53 CG CD NE CZ NH1 NH2
REMARK 470 GLU O 80 CG CD OE1 OE2
REMARK 470 LYS O 85 CG CD CE NZ
REMARK 470 ARG O 233 CG CD NE CZ NH1 NH2
REMARK 470 GLU V 41 CG CD OE1 OE2
REMARK 470 ARG y 43 CG CD NE CZ NH1 NH2
REMARK 470 TYR P 143 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU P 462 CG CD OE1 OE2
REMARK 470 LYS W 20 CG CD CE NZ
REMARK 470 ARG f 53 CG CD NE CZ NH1 NH2
REMARK 470 GLU f 80 CG CD OE1 OE2
REMARK 470 LYS f 85 CG CD CE NZ
REMARK 470 ARG f 233 CG CD NE CZ NH1 NH2
REMARK 470 GLU i 41 CG CD OE1 OE2
REMARK 470 ARG m 43 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O PHE Z 60 OG SER f 115 3755 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO B 484 C - N - CA ANGL. DEV. = 11.3 DEGREES
REMARK 500 LEU B 486 CA - CB - CG ANGL. DEV. = 16.2 DEGREES
REMARK 500 PRO N 484 C - N - CA ANGL. DEV. = 11.5 DEGREES
REMARK 500 LEU N 486 CA - CB - CG ANGL. DEV. = 15.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 12 106.61 128.67
REMARK 500 GLN A 130 -7.13 -56.20
REMARK 500 PRO A 141 -119.24 -71.51
REMARK 500 TRP A 142 -17.50 47.07
REMARK 500 LEU A 159 -46.53 -137.26
REMARK 500 ILE A 176 -71.85 -56.70
REMARK 500 GLU A 226 9.02 -151.35
REMARK 500 GLU A 242 -60.62 -90.58
REMARK 500 ILE A 259 -80.60 -101.73
REMARK 500 PHE A 260 137.21 -178.21
REMARK 500 GLN A 261 -65.00 -27.16
REMARK 500 PHE A 302 34.02 -96.36
REMARK 500 ARG A 334 -69.30 -26.23
REMARK 500 LEU A 343 58.74 -108.20
REMARK 500 VAL B 11 1.83 -61.99
REMARK 500 ILE B 13 -27.06 -38.87
REMARK 500 ASN B 14 62.99 -151.66
REMARK 500 PRO B 16 -35.47 -34.16
REMARK 500 ASP B 119 52.38 -93.70
REMARK 500 ARG B 127 -78.05 -58.11
REMARK 500 SER B 177 -179.56 178.41
REMARK 500 PRO B 183 -179.82 -51.48
REMARK 500 GLU B 184 101.34 -167.29
REMARK 500 ASP B 188 -1.24 -59.73
REMARK 500 LEU B 218 -69.07 -103.94
REMARK 500 LEU B 229 38.92 -81.19
REMARK 500 ARG B 230 48.71 17.96
REMARK 500 MET B 231 178.45 -57.36
REMARK 500 GLU B 235 15.91 -68.87
REMARK 500 SER B 294 29.55 -75.91
REMARK 500 ASP B 313 40.21 -93.35
REMARK 500 LYS B 349 -48.09 -22.44
REMARK 500 PRO B 414 -62.91 -19.16
REMARK 500 GLU B 435 -75.77 -59.21
REMARK 500 THR B 436 -73.88 -22.40
REMARK 500 SER B 480 -18.09 73.93
REMARK 500 ILE B 482 -162.54 -117.97
REMARK 500 PRO B 484 -177.23 17.56
REMARK 500 GLU B 485 172.31 67.66
REMARK 500 LEU B 486 67.99 -160.19
REMARK 500 PRO B 488 -103.47 22.80
REMARK 500 GLN B 490 101.92 -166.02
REMARK 500 GLU C 29 -155.52 -148.94
REMARK 500 TRP C 36 3.15 -67.69
REMARK 500 LEU C 45 54.76 -141.83
REMARK 500 SER C 46 -54.81 -19.19
REMARK 500 LYS C 79 134.99 -170.24
REMARK 500 ILE C 87 -3.29 -142.96
REMARK 500 ARG C 135 -67.02 -124.86
REMARK 500 GLU C 141 -42.73 -28.72
REMARK 500
REMARK 500 THIS ENTRY HAS 386 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 HIS B 23 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PL9 A 406
REMARK 610 DGD A 407
REMARK 610 LHG A 408
REMARK 610 SQD A 409
REMARK 610 LMG A 410
REMARK 610 LHG A 411
REMARK 610 DGD B 621
REMARK 610 LMG B 622
REMARK 610 LMG B 623
REMARK 610 SQD B 624
REMARK 610 SQD B 627
REMARK 610 DGD B 628
REMARK 610 DGD C 516
REMARK 610 DGD C 517
REMARK 610 LMG C 519
REMARK 610 LMG C 520
REMARK 610 LMG D 406
REMARK 610 LMG D 407
REMARK 610 DGD D 408
REMARK 610 LMT D 409
REMARK 610 LMG D 412
REMARK 610 LMG E 102
REMARK 610 SQD F 101
REMARK 610 LMG I 102
REMARK 610 PL9 J 101
REMARK 610 LMG M 101
REMARK 610 PL9 G 407
REMARK 610 DGD G 408
REMARK 610 SQD G 410
REMARK 610 LHG G 409
REMARK 610 LMG G 411
REMARK 610 LHG G 412
REMARK 610 SQD N 601
REMARK 610 DGD N 602
REMARK 610 LMG N 623
REMARK 610 LMG N 622
REMARK 610 DGD P 517
REMARK 610 DGD P 518
REMARK 610 LMG P 520
REMARK 610 LMG P 521
REMARK 610 LMG Q 401
REMARK 610 LMG Q 407
REMARK 610 SQD Q 408
REMARK 610 DGD Q 409
REMARK 610 LMG Q 406
REMARK 610 LMT Q 410
REMARK 610 LMG R 102
REMARK 610 SQD S 102
REMARK 610 DGD W 102
REMARK 610 LMG a 102
REMARK 610 PL9 b 101
REMARK 610 LMG e 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 FE2 A 413 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 215 NE2
REMARK 620 2 HIS D 214 NE2 129.1
REMARK 620 3 HIS A 272 NE2 103.5 103.6
REMARK 620 4 BCT D 410 O3 136.4 85.4 90.2
REMARK 620 5 BCT D 410 O2 85.2 141.3 80.9 56.0
REMARK 620 6 HIS D 268 NE2 78.3 91.4 157.8 74.7 77.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 G 414 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS Q 214 NE2
REMARK 620 2 HIS G 215 NE2 128.6
REMARK 620 3 HIS G 272 NE2 101.5 103.9
REMARK 620 4 BCT Q 411 O3 89.5 133.7 90.4
REMARK 620 5 BCT Q 411 O2 145.0 80.7 86.3 56.1
REMARK 620 6 HIS Q 268 NE2 92.9 79.3 157.8 72.7 72.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM R 101 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS R 23 NE2
REMARK 620 2 HEM R 101 NA 81.0
REMARK 620 3 HEM R 101 NB 100.8 89.2
REMARK 620 4 HEM R 101 NC 99.0 178.8 89.6
REMARK 620 5 HEM R 101 ND 78.9 90.0 179.1 91.2
REMARK 620 6 HIS S 24 NE2 155.9 74.9 79.0 105.1 101.0
REMARK 620 N 1 2 3 4 5
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 79.1
REMARK 620 3 HEM E 101 NB 100.7 89.5
REMARK 620 4 HEM E 101 NC 100.8 179.1 89.6
REMARK 620 5 HEM E 101 ND 78.8 89.4 178.8 91.5
REMARK 620 6 HIS F 24 NE2 153.2 74.1 80.7 106.0 99.2
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 67 NE2
REMARK 620 2 HEM V 201 NA 90.1
REMARK 620 3 HEM V 201 NB 92.6 87.0
REMARK 620 4 HEM V 201 NC 89.9 179.0 92.1
REMARK 620 5 HEM V 201 ND 87.3 91.2 178.2 89.8
REMARK 620 6 HIS V 118 NE2 168.5 78.9 90.0 101.1 89.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEC A 412 MN2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 342 OD1
REMARK 620 2 ALA A 344 OXT 80.6
REMARK 620 3 ASP A 342 OD2 48.9 128.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM i 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS i 118 NE2
REMARK 620 2 HEM i 201 NA 80.0
REMARK 620 3 HEM i 201 NB 89.4 86.3
REMARK 620 4 HEM i 201 NC 99.9 178.2 91.8
REMARK 620 5 HEM i 201 ND 90.4 92.1 178.4 89.7
REMARK 620 6 HIS i 67 NE2 168.9 88.8 89.7 91.2 90.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEC A 412 MN3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 354 OE2
REMARK 620 2 GLU A 333 OE1 65.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEC G 413 MN2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA G 344 OXT
REMARK 620 2 ASP G 342 OD1 75.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEC A 412 MN4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 333 OE2
REMARK 620 2 ASP A 170 OD2 164.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEC G 413 MN4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU G 333 OE2
REMARK 620 2 ASP G 170 OD2 141.2
REMARK 620 N 1
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 95.7
REMARK 620 3 CLA C 511 NB 76.5 93.7
REMARK 620 4 CLA C 511 NC 84.1 176.8 89.3
REMARK 620 5 CLA C 511 ND 102.3 90.9 175.3 86.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA P 511 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN P 39 OD1
REMARK 620 2 CLA P 511 NA 95.3
REMARK 620 3 CLA P 511 NB 78.1 93.6
REMARK 620 4 CLA P 511 NC 84.6 176.8 89.6
REMARK 620 5 CLA P 511 ND 100.9 90.9 175.5 85.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEC G 413 CA1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU G 189 OE1
REMARK 620 2 ASP G 170 OD1 139.9
REMARK 620 3 ASP G 170 OD2 157.5 41.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEC A 412 CA1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 189 OE1
REMARK 620 2 ASP A 170 OD1 136.8
REMARK 620 3 ASP A 170 OD2 154.6 41.6
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OEC A 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD A 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD B 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG B 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG B 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD B 624
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT B 625
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT B 626
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD B 627
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD B 628
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT B 629
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT B 630
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR C 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR C 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD C 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD C 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD C 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG C 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG C 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR D 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG D 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG D 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD D 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT D 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT D 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG D 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM E 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG E 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD F 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR H 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR I 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG I 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT I 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 J 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR J 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR K 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG M 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT M 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA O 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR T 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR T 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR T 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM V 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR Z 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD G 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA G 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA G 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA G 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO G 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA G 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 G 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD G 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG G 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD G 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG G 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG G 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OEC G 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 G 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD N 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD N 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT N 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT N 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR N 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG N 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG N 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT N 624
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT N 625
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA P 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA P 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA P 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA P 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA P 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA P 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA P 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA P 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA P 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA P 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA P 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA P 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA P 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR P 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR P 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR P 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD P 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD P 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD P 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: RC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG P 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: RC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG P 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: RC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG Q 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: RC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA Q 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: RC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO Q 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: RC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA Q 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: RC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 Q 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: RC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG Q 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: RC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG Q 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: SC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD Q 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: SC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD Q 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: SC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT Q 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: SC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT Q 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: SC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM R 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: SC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG R 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: SC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR S 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: SC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD S 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: SC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR W 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: TC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD W 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: TC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR a 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: TC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG a 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: TC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT a 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: TC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 b 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: TC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR b 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: TC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR c 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: TC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT e 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: TC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG e 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: UC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA f 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: UC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM i 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3BZ1 RELATED DB: PDB
REMARK 900 SYNCHROTRON STRUCTURE USING IDENTICAL CRYSTALLIZATION PROTOCOL
REMARK 900 RELATED ID: 3BZ2 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CHAIN "Y" AND "K":THE DEPOSITORS KNOW THE SEQUENCE
REMARK 999 (UNIPROT ID Q8DKM3) BUT DUE TO POOR DENSITY CAN'T
REMARK 999 ASIGN IT WITH CERTAINTY TO THE DENSITY. INSTEAD CHAIN
REMARK 999 Y WAS MODELED AS POLY-ALA.
REMARK 999 MET ASP TRP ARG VAL LEU VAL VAL LEU LEU PRO VAL LEU LEU ALA
REMARK 999 ALA GLY TRP ALA VAL ARG ASN ILE LEU PRO TYR ALA VAL LYS GLN
REMARK 999 VAL GLN LYS LEU LEU GLN LYS ALA LYS ALA ALA
REMARK 999 THE SEQUENCE MATCHES TO UNIPROT REFERENCE Q8DKM3
DBREF 4FBY A 1 344 UNP P0A444 PSBA1_THEEB 1 344
DBREF 4FBY B 1 510 UNP Q8DIQ1 Q8DIQ1_THEEB 1 510
DBREF 4FBY C 13 473 UNP Q8DIF8 Q8DIF8_THEEB 1 461
DBREF 4FBY D 1 352 UNP Q8CM25 PSBD_THEEB 1 352
DBREF 4FBY E 2 84 UNP Q8DIP0 PSBE_THEEB 2 84
DBREF 4FBY F 2 45 UNP Q8DIN9 PSBF_THEEB 2 45
DBREF 4FBY H 2 66 UNP Q8DJ43 PSBH_THEEB 2 66
DBREF 4FBY I 1 38 UNP Q8DJZ6 PSBI_THEEB 1 38
DBREF 4FBY J 2 40 UNP P59087 PSBJ_THEEB 2 40
DBREF 4FBY K 10 46 UNP Q9F1K9 PSBK_THEEB 10 46
DBREF 4FBY L 1 37 UNP Q8DIN8 PSBL_THEEB 1 37
DBREF 4FBY M 1 36 UNP Q8DHA7 PSBM_THEEB 1 36
DBREF 4FBY O 27 272 UNP P0A431 PSBO_THEEB 27 272
DBREF 4FBY T 1 32 UNP Q8DIQ0 PSBT_THEEB 1 32
DBREF 4FBY U 31 134 UNP Q9F1L5 PSBU_THEEB 31 134
DBREF 4FBY V 27 163 UNP P0A386 CY550_THEEB 27 163
DBREF 4FBY y 1 46 UNP Q8DJI1 YCF12_THEEB 1 46
DBREF 4FBY X 11 50 UNP Q9F1R6 PSBX_THEEB 2 41
DBREF 4FBY Y 1 28 PDB 4FBY 4FBY 1 28
DBREF 4FBY Z 1 62 UNP Q8DHJ2 PSBZ_THEEB 1 62
DBREF 4FBY G 1 344 UNP P0A444 PSBA1_THEEB 1 344
DBREF 4FBY N 1 510 UNP Q8DIQ1 Q8DIQ1_THEEB 1 510
DBREF 4FBY P 13 473 UNP Q8DIF8 Q8DIF8_THEEB 1 461
DBREF 4FBY Q 1 352 UNP Q8CM25 PSBD_THEEB 1 352
DBREF 4FBY R 2 84 UNP Q8DIP0 PSBE_THEEB 2 84
DBREF 4FBY S 2 45 UNP Q8DIN9 PSBF_THEEB 2 45
DBREF 4FBY W 2 66 UNP Q8DJ43 PSBH_THEEB 2 66
DBREF 4FBY a 1 38 UNP Q8DJZ6 PSBI_THEEB 1 38
DBREF 4FBY b 2 40 UNP P59087 PSBJ_THEEB 2 40
DBREF 4FBY c 10 46 UNP Q9F1K9 PSBK_THEEB 10 46
DBREF 4FBY d 1 37 UNP Q8DIN8 PSBL_THEEB 1 37
DBREF 4FBY e 1 36 UNP Q8DHA7 PSBM_THEEB 1 36
DBREF 4FBY f 27 272 UNP P0A431 PSBO_THEEB 27 272
DBREF 4FBY g 1 32 UNP Q8DIQ0 PSBT_THEEB 1 32
DBREF 4FBY h 31 134 UNP Q9F1L5 PSBU_THEEB 31 134
DBREF 4FBY i 27 163 UNP P0A386 CY550_THEEB 27 163
DBREF 4FBY m 1 46 UNP Q8DJI1 YCF12_THEEB 1 46
DBREF 4FBY j 11 50 UNP Q9F1R6 PSBX_THEEB 2 41
DBREF 4FBY k 1 28 PDB 4FBY 4FBY 1 28
DBREF 4FBY l 1 62 UNP Q8DHJ2 PSBZ_THEEB 1 62
SEQRES 1 A 344 MET THR THR THR LEU GLN ARG ARG GLU SER ALA ASN LEU
SEQRES 2 A 344 TRP GLU ARG PHE CYS ASN TRP VAL THR SER THR ASP ASN
SEQRES 3 A 344 ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE MET ILE PRO
SEQRES 4 A 344 THR LEU LEU ALA ALA THR ILE CYS PHE VAL ILE ALA PHE
SEQRES 5 A 344 ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY ILE ARG GLU
SEQRES 6 A 344 PRO VAL SER GLY SER LEU LEU TYR GLY ASN ASN ILE ILE
SEQRES 7 A 344 THR GLY ALA VAL VAL PRO SER SER ASN ALA ILE GLY LEU
SEQRES 8 A 344 HIS PHE TYR PRO ILE TRP GLU ALA ALA SER LEU ASP GLU
SEQRES 9 A 344 TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU ILE ILE PHE
SEQRES 10 A 344 HIS PHE LEU LEU GLY ALA SER CYS TYR MET GLY ARG GLN
SEQRES 11 A 344 TRP GLU LEU SER TYR ARG LEU GLY MET ARG PRO TRP ILE
SEQRES 12 A 344 CYS VAL ALA TYR SER ALA PRO LEU ALA SER ALA PHE ALA
SEQRES 13 A 344 VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY SER PHE SER
SEQRES 14 A 344 ASP GLY MET PRO LEU GLY ILE SER GLY THR PHE ASN PHE
SEQRES 15 A 344 MET ILE VAL PHE GLN ALA GLU HIS ASN ILE LEU MET HIS
SEQRES 16 A 344 PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL PHE GLY GLY
SEQRES 17 A 344 ALA LEU PHE CYS ALA MET HIS GLY SER LEU VAL THR SER
SEQRES 18 A 344 SER LEU ILE ARG GLU THR THR GLU THR GLU SER ALA ASN
SEQRES 19 A 344 TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU THR TYR ASN
SEQRES 20 A 344 ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG LEU ILE PHE
SEQRES 21 A 344 GLN TYR ALA SER PHE ASN ASN SER ARG SER LEU HIS PHE
SEQRES 22 A 344 PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL TRP PHE THR
SEQRES 23 A 344 ALA LEU GLY ILE SER THR MET ALA PHE ASN LEU ASN GLY
SEQRES 24 A 344 PHE ASN PHE ASN HIS SER VAL ILE ASP ALA LYS GLY ASN
SEQRES 25 A 344 VAL ILE ASN THR TRP ALA ASP ILE ILE ASN ARG ALA ASN
SEQRES 26 A 344 LEU GLY MET GLU VAL MET HIS GLU ARG ASN ALA HIS ASN
SEQRES 27 A 344 PHE PRO LEU ASP LEU ALA
SEQRES 1 B 510 MET GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE
SEQRES 2 B 510 ASN ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS
SEQRES 3 B 510 THR ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU
SEQRES 4 B 510 TYR GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU
SEQRES 5 B 510 ASN PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE
SEQRES 6 B 510 MET ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP
SEQRES 7 B 510 SER ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP
SEQRES 8 B 510 SER PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER
SEQRES 9 B 510 GLY LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR
SEQRES 10 B 510 TRP ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU
SEQRES 11 B 510 PRO ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU
SEQRES 12 B 510 PHE LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE
SEQRES 13 B 510 HIS LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER
SEQRES 14 B 510 ASP PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA
SEQRES 15 B 510 PRO GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO
SEQRES 16 B 510 GLY GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL
SEQRES 17 B 510 GLY ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO
SEQRES 18 B 510 PRO GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE
SEQRES 19 B 510 GLU THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE
SEQRES 20 B 510 ALA ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER
SEQRES 21 B 510 ALA THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR
SEQRES 22 B 510 GLN TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG
SEQRES 23 B 510 ARG VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU
SEQRES 24 B 510 GLU ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR
SEQRES 25 B 510 ASP TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE
SEQRES 26 B 510 ARG THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN
SEQRES 27 B 510 ALA TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY
SEQRES 28 B 510 GLU GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU
SEQRES 29 B 510 SER PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL
SEQRES 30 B 510 LYS ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR
SEQRES 31 B 510 SER PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY
SEQRES 32 B 510 GLY GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR
SEQRES 33 B 510 VAL LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE
SEQRES 34 B 510 PHE GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE
SEQRES 35 B 510 PHE ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS
SEQRES 36 B 510 ALA VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP
SEQRES 37 B 510 HIS GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY
SEQRES 38 B 510 ILE ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY
SEQRES 39 B 510 PHE TYR GLN LYS VAL GLY ASP VAL THR THR ARG ARG LYS
SEQRES 40 B 510 GLU ALA VAL
SEQRES 1 C 461 MET VAL THR LEU SER SER ASN SER ILE PHE ALA THR ASN
SEQRES 2 C 461 ARG ASP GLN GLU SER SER GLY PHE ALA TRP TRP ALA GLY
SEQRES 3 C 461 ASN ALA ARG LEU ILE ASN LEU SER GLY LYS LEU LEU GLY
SEQRES 4 C 461 ALA HIS VAL ALA HIS ALA GLY LEU ILE VAL PHE TRP ALA
SEQRES 5 C 461 GLY ALA MET THR LEU PHE GLU LEU ALA HIS PHE ILE PRO
SEQRES 6 C 461 GLU LYS PRO MET TYR GLU GLN GLY LEU ILE LEU ILE PRO
SEQRES 7 C 461 HIS ILE ALA THR LEU GLY TRP GLY VAL GLY PRO GLY GLY
SEQRES 8 C 461 GLU VAL VAL ASP THR PHE PRO PHE PHE VAL VAL GLY VAL
SEQRES 9 C 461 VAL HIS LEU ILE SER SER ALA VAL LEU GLY PHE GLY GLY
SEQRES 10 C 461 VAL TYR HIS ALA ILE ARG GLY PRO GLU THR LEU GLU GLU
SEQRES 11 C 461 TYR SER SER PHE PHE GLY TYR ASP TRP LYS ASP LYS ASN
SEQRES 12 C 461 LYS MET THR THR ILE LEU GLY PHE HIS LEU ILE VAL LEU
SEQRES 13 C 461 GLY ILE GLY ALA LEU LEU LEU VAL ALA LYS ALA MET PHE
SEQRES 14 C 461 PHE GLY GLY LEU TYR ASP THR TRP ALA PRO GLY GLY GLY
SEQRES 15 C 461 ASP VAL ARG VAL ILE THR ASN PRO THR LEU ASP PRO ARG
SEQRES 16 C 461 VAL ILE PHE GLY TYR LEU LEU LYS SER PRO PHE GLY GLY
SEQRES 17 C 461 GLU GLY TRP ILE VAL SER VAL ASN ASN LEU GLU ASP VAL
SEQRES 18 C 461 VAL GLY GLY HIS ILE TRP ILE GLY LEU ILE CYS ILE ALA
SEQRES 19 C 461 GLY GLY ILE TRP HIS ILE LEU THR THR PRO PHE GLY TRP
SEQRES 20 C 461 ALA ARG ARG ALA PHE ILE TRP SER GLY GLU ALA TYR LEU
SEQRES 21 C 461 SER TYR SER LEU GLY ALA LEU SER MET MET GLY PHE ILE
SEQRES 22 C 461 ALA THR CYS PHE VAL TRP PHE ASN ASN THR VAL TYR PRO
SEQRES 23 C 461 SER GLU PHE TYR GLY PRO THR GLY PRO GLU ALA SER GLN
SEQRES 24 C 461 ALA GLN ALA MET THR PHE LEU ILE ARG ASP GLN LYS LEU
SEQRES 25 C 461 GLY ALA ASN VAL GLY SER ALA GLN GLY PRO THR GLY LEU
SEQRES 26 C 461 GLY LYS TYR LEU MET ARG SER PRO THR GLY GLU ILE ILE
SEQRES 27 C 461 PHE GLY GLY GLU THR MET ARG PHE TRP ASP PHE ARG GLY
SEQRES 28 C 461 PRO TRP LEU GLU PRO LEU ARG GLY PRO ASN GLY LEU ASP
SEQRES 29 C 461 LEU ASN LYS ILE LYS ASN ASP ILE GLN PRO TRP GLN GLU
SEQRES 30 C 461 ARG ARG ALA ALA GLU TYR MET THR HIS ALA PRO LEU GLY
SEQRES 31 C 461 SER LEU ASN SER VAL GLY GLY VAL ALA THR GLU ILE ASN
SEQRES 32 C 461 SER VAL ASN PHE VAL SER PRO ARG SER TRP LEU ALA THR
SEQRES 33 C 461 SER HIS PHE VAL LEU ALA PHE PHE PHE LEU VAL GLY HIS
SEQRES 34 C 461 LEU TRP HIS ALA GLY ARG ALA ARG ALA ALA ALA ALA GLY
SEQRES 35 C 461 PHE GLU LYS GLY ILE ASP ARG GLU SER GLU PRO VAL LEU
SEQRES 36 C 461 SER MET PRO SER LEU ASP
SEQRES 1 D 352 MET THR ILE ALA ILE GLY ARG ALA PRO ALA GLU ARG GLY
SEQRES 2 D 352 TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS ARG ASP ARG
SEQRES 3 D 352 PHE VAL PHE VAL GLY TRP SER GLY ILE LEU LEU PHE PRO
SEQRES 4 D 352 CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU THR GLY THR
SEQRES 5 D 352 THR PHE VAL THR SER TRP TYR THR HIS GLY LEU ALA SER
SEQRES 6 D 352 SER TYR LEU GLU GLY CYS ASN PHE LEU THR VAL ALA VAL
SEQRES 7 D 352 SER THR PRO ALA ASN SER MET GLY HIS SER LEU LEU LEU
SEQRES 8 D 352 LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE THR ARG TRP
SEQRES 9 D 352 CYS GLN LEU GLY GLY LEU TRP THR PHE ILE ALA LEU HIS
SEQRES 10 D 352 GLY ALA PHE GLY LEU ILE GLY PHE MET LEU ARG GLN PHE
SEQRES 11 D 352 GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO TYR ASN ALA
SEQRES 12 D 352 ILE ALA PHE SER ALA PRO ILE ALA VAL PHE VAL SER VAL
SEQRES 13 D 352 PHE LEU ILE TYR PRO LEU GLY GLN SER SER TRP PHE PHE
SEQRES 14 D 352 ALA PRO SER PHE GLY VAL ALA ALA ILE PHE ARG PHE LEU
SEQRES 15 D 352 LEU PHE PHE GLN GLY PHE HIS ASN TRP THR LEU ASN PRO
SEQRES 16 D 352 PHE HIS MET MET GLY VAL ALA GLY VAL LEU GLY GLY ALA
SEQRES 17 D 352 LEU LEU CYS ALA ILE HIS GLY ALA THR VAL GLU ASN THR
SEQRES 18 D 352 LEU PHE GLN ASP GLY GLU GLY ALA SER THR PHE ARG ALA
SEQRES 19 D 352 PHE ASN PRO THR GLN ALA GLU GLU THR TYR SER MET VAL
SEQRES 20 D 352 THR ALA ASN ARG PHE TRP SER GLN ILE PHE GLY ILE ALA
SEQRES 21 D 352 PHE SER ASN LYS ARG TRP LEU HIS PHE PHE MET LEU PHE
SEQRES 22 D 352 VAL PRO VAL THR GLY LEU TRP MET SER ALA ILE GLY VAL
SEQRES 23 D 352 VAL GLY LEU ALA LEU ASN LEU ARG SER TYR ASP PHE ILE
SEQRES 24 D 352 SER GLN GLU ILE ARG ALA ALA GLU ASP PRO GLU PHE GLU
SEQRES 25 D 352 THR PHE TYR THR LYS ASN LEU LEU LEU ASN GLU GLY ILE
SEQRES 26 D 352 ARG ALA TRP MET ALA PRO GLN ASP GLN PRO HIS GLU ASN
SEQRES 27 D 352 PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG GLY ASN ALA
SEQRES 28 D 352 LEU
SEQRES 1 E 83 ALA GLY THR THR GLY GLU ARG PRO PHE SER ASP ILE ILE
SEQRES 2 E 83 THR SER VAL ARG TYR TRP VAL ILE HIS SER ILE THR ILE
SEQRES 3 E 83 PRO ALA LEU PHE ILE ALA GLY TRP LEU PHE VAL SER THR
SEQRES 4 E 83 GLY LEU ALA TYR ASP VAL PHE GLY THR PRO ARG PRO ASP
SEQRES 5 E 83 SER TYR TYR ALA GLN GLU GLN ARG SER ILE PRO LEU VAL
SEQRES 6 E 83 THR ASP ARG PHE GLU ALA LYS GLN GLN VAL GLU THR PHE
SEQRES 7 E 83 LEU GLU GLN LEU LYS
SEQRES 1 F 44 THR SER ASN THR PRO ASN GLN GLU PRO VAL SER TYR PRO
SEQRES 2 F 44 ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR LEU ALA
SEQRES 3 F 44 VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA ALA MET
SEQRES 4 F 44 GLN PHE ILE GLN ARG
SEQRES 1 H 65 ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO LEU
SEQRES 2 H 65 ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY THR
SEQRES 3 H 65 THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU VAL
SEQRES 4 H 65 PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR LEU
SEQRES 5 H 65 ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU GLY
SEQRES 1 I 38 MET GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR
SEQRES 2 I 38 PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY
SEQRES 3 I 38 ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP LEU GLU
SEQRES 1 J 39 MET SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL ALA
SEQRES 2 J 39 THR VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY LEU
SEQRES 3 J 39 PHE PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER LEU
SEQRES 1 K 37 LYS LEU PRO GLU ALA TYR ALA ILE PHE ASP PRO LEU VAL
SEQRES 2 K 37 ASP VAL LEU PRO VAL ILE PRO VAL LEU PHE LEU ALA LEU
SEQRES 3 K 37 ALA PHE VAL TRP GLN ALA ALA VAL GLY PHE ARG
SEQRES 1 L 37 MET GLU PRO ASN PRO ASN ARG GLN PRO VAL GLU LEU ASN
SEQRES 2 L 37 ARG THR SER LEU TYR LEU GLY LEU LEU LEU ILE LEU VAL
SEQRES 3 L 37 LEU ALA LEU LEU PHE SER SER TYR PHE PHE ASN
SEQRES 1 M 36 MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU
SEQRES 2 M 36 PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR
SEQRES 3 M 36 VAL GLN THR GLU SER GLN GLN LYS SER SER
SEQRES 1 O 246 ALA LYS GLN THR LEU THR TYR ASP ASP ILE VAL GLY THR
SEQRES 2 O 246 GLY LEU ALA ASN LYS CYS PRO THR LEU ASP ASP THR ALA
SEQRES 3 O 246 ARG GLY ALA TYR PRO ILE ASP SER SER GLN THR TYR ARG
SEQRES 4 O 246 ILE ALA ARG LEU CYS LEU GLN PRO THR THR PHE LEU VAL
SEQRES 5 O 246 LYS GLU GLU PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE
SEQRES 6 O 246 VAL PRO THR LYS LEU VAL THR ARG GLU THR THR SER LEU
SEQRES 7 O 246 ASP GLN ILE GLN GLY GLU LEU LYS VAL ASN SER ASP GLY
SEQRES 8 O 246 SER LEU THR PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN
SEQRES 9 O 246 PRO VAL THR VAL GLN MET ALA GLY GLY GLU ARG ILE PRO
SEQRES 10 O 246 LEU LEU PHE THR VAL LYS ASN LEU VAL ALA SER THR GLN
SEQRES 11 O 246 PRO ASN VAL THR SER ILE THR THR SER THR ASP PHE LYS
SEQRES 12 O 246 GLY GLU PHE ASN VAL PRO SER TYR ARG THR ALA ASN PHE
SEQRES 13 O 246 LEU ASP PRO LYS GLY ARG GLY LEU ALA SER GLY TYR ASP
SEQRES 14 O 246 SER ALA ILE ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU
SEQRES 15 O 246 ALA ARG ALA ASN VAL LYS ARG PHE SER LEU THR LYS GLY
SEQRES 16 O 246 GLN ILE SER LEU ASN VAL ALA LYS VAL ASP GLY ARG THR
SEQRES 17 O 246 GLY GLU ILE ALA GLY THR PHE GLU SER GLU GLN LEU SER
SEQRES 18 O 246 ASP ASP ASP MET GLY ALA HIS GLU PRO HIS GLU VAL LYS
SEQRES 19 O 246 ILE GLN GLY VAL PHE TYR ALA SER ILE GLU PRO ALA
SEQRES 1 T 32 MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE
SEQRES 2 T 32 ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO
SEQRES 3 T 32 PRO ARG ILE THR LYS LYS
SEQRES 1 U 104 ALA THR ALA SER THR GLU GLU GLU LEU VAL ASN VAL VAL
SEQRES 2 U 104 ASP GLU LYS LEU GLY THR ALA TYR GLY GLU LYS ILE ASP
SEQRES 3 U 104 LEU ASN ASN THR ASN ILE ALA ALA PHE ILE GLN TYR ARG
SEQRES 4 U 104 GLY LEU TYR PRO THR LEU ALA LYS LEU ILE VAL LYS ASN
SEQRES 5 U 104 ALA PRO TYR GLU SER VAL GLU ASP VAL LEU ASN ILE PRO
SEQRES 6 U 104 GLY LEU THR GLU ARG GLN LYS GLN ILE LEU ARG GLU ASN
SEQRES 7 U 104 LEU GLU HIS PHE THR VAL THR GLU VAL GLU THR ALA LEU
SEQRES 8 U 104 VAL GLU GLY GLY ASP ARG TYR ASN ASN GLY LEU TYR LYS
SEQRES 1 V 137 ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN
SEQRES 2 V 137 SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR
SEQRES 3 V 137 LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER
SEQRES 4 V 137 CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU
SEQRES 5 V 137 ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO
SEQRES 6 V 137 ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN
SEQRES 7 V 137 PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL
SEQRES 8 V 137 HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET
SEQRES 9 V 137 ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY
SEQRES 10 V 137 HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP
SEQRES 11 V 137 GLY GLY GLY LYS VAL TYR TYR
SEQRES 1 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 40 THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY LEU
SEQRES 2 X 40 LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA VAL
SEQRES 3 X 40 LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG SER
SEQRES 4 X 40 LEU
SEQRES 1 Y 28 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 2 Y 28 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 3 Y 28 UNK UNK
SEQRES 1 Z 62 MET THR ILE LEU PHE GLN LEU ALA LEU ALA ALA LEU VAL
SEQRES 2 Z 62 ILE LEU SER PHE VAL MET VAL ILE GLY VAL PRO VAL ALA
SEQRES 3 Z 62 TYR ALA SER PRO GLN ASP TRP ASP ARG SER LYS GLN LEU
SEQRES 4 Z 62 ILE PHE LEU GLY SER GLY LEU TRP ILE ALA LEU VAL LEU
SEQRES 5 Z 62 VAL VAL GLY VAL LEU ASN PHE PHE VAL VAL
SEQRES 1 G 344 MET THR THR THR LEU GLN ARG ARG GLU SER ALA ASN LEU
SEQRES 2 G 344 TRP GLU ARG PHE CYS ASN TRP VAL THR SER THR ASP ASN
SEQRES 3 G 344 ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE MET ILE PRO
SEQRES 4 G 344 THR LEU LEU ALA ALA THR ILE CYS PHE VAL ILE ALA PHE
SEQRES 5 G 344 ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY ILE ARG GLU
SEQRES 6 G 344 PRO VAL SER GLY SER LEU LEU TYR GLY ASN ASN ILE ILE
SEQRES 7 G 344 THR GLY ALA VAL VAL PRO SER SER ASN ALA ILE GLY LEU
SEQRES 8 G 344 HIS PHE TYR PRO ILE TRP GLU ALA ALA SER LEU ASP GLU
SEQRES 9 G 344 TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU ILE ILE PHE
SEQRES 10 G 344 HIS PHE LEU LEU GLY ALA SER CYS TYR MET GLY ARG GLN
SEQRES 11 G 344 TRP GLU LEU SER TYR ARG LEU GLY MET ARG PRO TRP ILE
SEQRES 12 G 344 CYS VAL ALA TYR SER ALA PRO LEU ALA SER ALA PHE ALA
SEQRES 13 G 344 VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY SER PHE SER
SEQRES 14 G 344 ASP GLY MET PRO LEU GLY ILE SER GLY THR PHE ASN PHE
SEQRES 15 G 344 MET ILE VAL PHE GLN ALA GLU HIS ASN ILE LEU MET HIS
SEQRES 16 G 344 PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL PHE GLY GLY
SEQRES 17 G 344 ALA LEU PHE CYS ALA MET HIS GLY SER LEU VAL THR SER
SEQRES 18 G 344 SER LEU ILE ARG GLU THR THR GLU THR GLU SER ALA ASN
SEQRES 19 G 344 TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU THR TYR ASN
SEQRES 20 G 344 ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG LEU ILE PHE
SEQRES 21 G 344 GLN TYR ALA SER PHE ASN ASN SER ARG SER LEU HIS PHE
SEQRES 22 G 344 PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL TRP PHE THR
SEQRES 23 G 344 ALA LEU GLY ILE SER THR MET ALA PHE ASN LEU ASN GLY
SEQRES 24 G 344 PHE ASN PHE ASN HIS SER VAL ILE ASP ALA LYS GLY ASN
SEQRES 25 G 344 VAL ILE ASN THR TRP ALA ASP ILE ILE ASN ARG ALA ASN
SEQRES 26 G 344 LEU GLY MET GLU VAL MET HIS GLU ARG ASN ALA HIS ASN
SEQRES 27 G 344 PHE PRO LEU ASP LEU ALA
SEQRES 1 N 510 MET GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE
SEQRES 2 N 510 ASN ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS
SEQRES 3 N 510 THR ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU
SEQRES 4 N 510 TYR GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU
SEQRES 5 N 510 ASN PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE
SEQRES 6 N 510 MET ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP
SEQRES 7 N 510 SER ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP
SEQRES 8 N 510 SER PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER
SEQRES 9 N 510 GLY LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR
SEQRES 10 N 510 TRP ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU
SEQRES 11 N 510 PRO ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU
SEQRES 12 N 510 PHE LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE
SEQRES 13 N 510 HIS LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER
SEQRES 14 N 510 ASP PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA
SEQRES 15 N 510 PRO GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO
SEQRES 16 N 510 GLY GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL
SEQRES 17 N 510 GLY ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO
SEQRES 18 N 510 PRO GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE
SEQRES 19 N 510 GLU THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE
SEQRES 20 N 510 ALA ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER
SEQRES 21 N 510 ALA THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR
SEQRES 22 N 510 GLN TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG
SEQRES 23 N 510 ARG VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU
SEQRES 24 N 510 GLU ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR
SEQRES 25 N 510 ASP TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE
SEQRES 26 N 510 ARG THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN
SEQRES 27 N 510 ALA TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY
SEQRES 28 N 510 GLU GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU
SEQRES 29 N 510 SER PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL
SEQRES 30 N 510 LYS ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR
SEQRES 31 N 510 SER PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY
SEQRES 32 N 510 GLY GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR
SEQRES 33 N 510 VAL LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE
SEQRES 34 N 510 PHE GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE
SEQRES 35 N 510 PHE ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS
SEQRES 36 N 510 ALA VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP
SEQRES 37 N 510 HIS GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY
SEQRES 38 N 510 ILE ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY
SEQRES 39 N 510 PHE TYR GLN LYS VAL GLY ASP VAL THR THR ARG ARG LYS
SEQRES 40 N 510 GLU ALA VAL
SEQRES 1 P 461 MET VAL THR LEU SER SER ASN SER ILE PHE ALA THR ASN
SEQRES 2 P 461 ARG ASP GLN GLU SER SER GLY PHE ALA TRP TRP ALA GLY
SEQRES 3 P 461 ASN ALA ARG LEU ILE ASN LEU SER GLY LYS LEU LEU GLY
SEQRES 4 P 461 ALA HIS VAL ALA HIS ALA GLY LEU ILE VAL PHE TRP ALA
SEQRES 5 P 461 GLY ALA MET THR LEU PHE GLU LEU ALA HIS PHE ILE PRO
SEQRES 6 P 461 GLU LYS PRO MET TYR GLU GLN GLY LEU ILE LEU ILE PRO
SEQRES 7 P 461 HIS ILE ALA THR LEU GLY TRP GLY VAL GLY PRO GLY GLY
SEQRES 8 P 461 GLU VAL VAL ASP THR PHE PRO PHE PHE VAL VAL GLY VAL
SEQRES 9 P 461 VAL HIS LEU ILE SER SER ALA VAL LEU GLY PHE GLY GLY
SEQRES 10 P 461 VAL TYR HIS ALA ILE ARG GLY PRO GLU THR LEU GLU GLU
SEQRES 11 P 461 TYR SER SER PHE PHE GLY TYR ASP TRP LYS ASP LYS ASN
SEQRES 12 P 461 LYS MET THR THR ILE LEU GLY PHE HIS LEU ILE VAL LEU
SEQRES 13 P 461 GLY ILE GLY ALA LEU LEU LEU VAL ALA LYS ALA MET PHE
SEQRES 14 P 461 PHE GLY GLY LEU TYR ASP THR TRP ALA PRO GLY GLY GLY
SEQRES 15 P 461 ASP VAL ARG VAL ILE THR ASN PRO THR LEU ASP PRO ARG
SEQRES 16 P 461 VAL ILE PHE GLY TYR LEU LEU LYS SER PRO PHE GLY GLY
SEQRES 17 P 461 GLU GLY TRP ILE VAL SER VAL ASN ASN LEU GLU ASP VAL
SEQRES 18 P 461 VAL GLY GLY HIS ILE TRP ILE GLY LEU ILE CYS ILE ALA
SEQRES 19 P 461 GLY GLY ILE TRP HIS ILE LEU THR THR PRO PHE GLY TRP
SEQRES 20 P 461 ALA ARG ARG ALA PHE ILE TRP SER GLY GLU ALA TYR LEU
SEQRES 21 P 461 SER TYR SER LEU GLY ALA LEU SER MET MET GLY PHE ILE
SEQRES 22 P 461 ALA THR CYS PHE VAL TRP PHE ASN ASN THR VAL TYR PRO
SEQRES 23 P 461 SER GLU PHE TYR GLY PRO THR GLY PRO GLU ALA SER GLN
SEQRES 24 P 461 ALA GLN ALA MET THR PHE LEU ILE ARG ASP GLN LYS LEU
SEQRES 25 P 461 GLY ALA ASN VAL GLY SER ALA GLN GLY PRO THR GLY LEU
SEQRES 26 P 461 GLY LYS TYR LEU MET ARG SER PRO THR GLY GLU ILE ILE
SEQRES 27 P 461 PHE GLY GLY GLU THR MET ARG PHE TRP ASP PHE ARG GLY
SEQRES 28 P 461 PRO TRP LEU GLU PRO LEU ARG GLY PRO ASN GLY LEU ASP
SEQRES 29 P 461 LEU ASN LYS ILE LYS ASN ASP ILE GLN PRO TRP GLN GLU
SEQRES 30 P 461 ARG ARG ALA ALA GLU TYR MET THR HIS ALA PRO LEU GLY
SEQRES 31 P 461 SER LEU ASN SER VAL GLY GLY VAL ALA THR GLU ILE ASN
SEQRES 32 P 461 SER VAL ASN PHE VAL SER PRO ARG SER TRP LEU ALA THR
SEQRES 33 P 461 SER HIS PHE VAL LEU ALA PHE PHE PHE LEU VAL GLY HIS
SEQRES 34 P 461 LEU TRP HIS ALA GLY ARG ALA ARG ALA ALA ALA ALA GLY
SEQRES 35 P 461 PHE GLU LYS GLY ILE ASP ARG GLU SER GLU PRO VAL LEU
SEQRES 36 P 461 SER MET PRO SER LEU ASP
SEQRES 1 Q 352 MET THR ILE ALA ILE GLY ARG ALA PRO ALA GLU ARG GLY
SEQRES 2 Q 352 TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS ARG ASP ARG
SEQRES 3 Q 352 PHE VAL PHE VAL GLY TRP SER GLY ILE LEU LEU PHE PRO
SEQRES 4 Q 352 CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU THR GLY THR
SEQRES 5 Q 352 THR PHE VAL THR SER TRP TYR THR HIS GLY LEU ALA SER
SEQRES 6 Q 352 SER TYR LEU GLU GLY CYS ASN PHE LEU THR VAL ALA VAL
SEQRES 7 Q 352 SER THR PRO ALA ASN SER MET GLY HIS SER LEU LEU LEU
SEQRES 8 Q 352 LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE THR ARG TRP
SEQRES 9 Q 352 CYS GLN LEU GLY GLY LEU TRP THR PHE ILE ALA LEU HIS
SEQRES 10 Q 352 GLY ALA PHE GLY LEU ILE GLY PHE MET LEU ARG GLN PHE
SEQRES 11 Q 352 GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO TYR ASN ALA
SEQRES 12 Q 352 ILE ALA PHE SER ALA PRO ILE ALA VAL PHE VAL SER VAL
SEQRES 13 Q 352 PHE LEU ILE TYR PRO LEU GLY GLN SER SER TRP PHE PHE
SEQRES 14 Q 352 ALA PRO SER PHE GLY VAL ALA ALA ILE PHE ARG PHE LEU
SEQRES 15 Q 352 LEU PHE PHE GLN GLY PHE HIS ASN TRP THR LEU ASN PRO
SEQRES 16 Q 352 PHE HIS MET MET GLY VAL ALA GLY VAL LEU GLY GLY ALA
SEQRES 17 Q 352 LEU LEU CYS ALA ILE HIS GLY ALA THR VAL GLU ASN THR
SEQRES 18 Q 352 LEU PHE GLN ASP GLY GLU GLY ALA SER THR PHE ARG ALA
SEQRES 19 Q 352 PHE ASN PRO THR GLN ALA GLU GLU THR TYR SER MET VAL
SEQRES 20 Q 352 THR ALA ASN ARG PHE TRP SER GLN ILE PHE GLY ILE ALA
SEQRES 21 Q 352 PHE SER ASN LYS ARG TRP LEU HIS PHE PHE MET LEU PHE
SEQRES 22 Q 352 VAL PRO VAL THR GLY LEU TRP MET SER ALA ILE GLY VAL
SEQRES 23 Q 352 VAL GLY LEU ALA LEU ASN LEU ARG SER TYR ASP PHE ILE
SEQRES 24 Q 352 SER GLN GLU ILE ARG ALA ALA GLU ASP PRO GLU PHE GLU
SEQRES 25 Q 352 THR PHE TYR THR LYS ASN LEU LEU LEU ASN GLU GLY ILE
SEQRES 26 Q 352 ARG ALA TRP MET ALA PRO GLN ASP GLN PRO HIS GLU ASN
SEQRES 27 Q 352 PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG GLY ASN ALA
SEQRES 28 Q 352 LEU
SEQRES 1 R 83 ALA GLY THR THR GLY GLU ARG PRO PHE SER ASP ILE ILE
SEQRES 2 R 83 THR SER VAL ARG TYR TRP VAL ILE HIS SER ILE THR ILE
SEQRES 3 R 83 PRO ALA LEU PHE ILE ALA GLY TRP LEU PHE VAL SER THR
SEQRES 4 R 83 GLY LEU ALA TYR ASP VAL PHE GLY THR PRO ARG PRO ASP
SEQRES 5 R 83 SER TYR TYR ALA GLN GLU GLN ARG SER ILE PRO LEU VAL
SEQRES 6 R 83 THR ASP ARG PHE GLU ALA LYS GLN GLN VAL GLU THR PHE
SEQRES 7 R 83 LEU GLU GLN LEU LYS
SEQRES 1 S 44 THR SER ASN THR PRO ASN GLN GLU PRO VAL SER TYR PRO
SEQRES 2 S 44 ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR LEU ALA
SEQRES 3 S 44 VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA ALA MET
SEQRES 4 S 44 GLN PHE ILE GLN ARG
SEQRES 1 W 65 ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO LEU
SEQRES 2 W 65 ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY THR
SEQRES 3 W 65 THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU VAL
SEQRES 4 W 65 PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR LEU
SEQRES 5 W 65 ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU GLY
SEQRES 1 a 38 MET GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR
SEQRES 2 a 38 PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY
SEQRES 3 a 38 ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP LEU GLU
SEQRES 1 b 39 MET SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL ALA
SEQRES 2 b 39 THR VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY LEU
SEQRES 3 b 39 PHE PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER LEU
SEQRES 1 c 37 LYS LEU PRO GLU ALA TYR ALA ILE PHE ASP PRO LEU VAL
SEQRES 2 c 37 ASP VAL LEU PRO VAL ILE PRO VAL LEU PHE LEU ALA LEU
SEQRES 3 c 37 ALA PHE VAL TRP GLN ALA ALA VAL GLY PHE ARG
SEQRES 1 d 37 MET GLU PRO ASN PRO ASN ARG GLN PRO VAL GLU LEU ASN
SEQRES 2 d 37 ARG THR SER LEU TYR LEU GLY LEU LEU LEU ILE LEU VAL
SEQRES 3 d 37 LEU ALA LEU LEU PHE SER SER TYR PHE PHE ASN
SEQRES 1 e 36 MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU
SEQRES 2 e 36 PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR
SEQRES 3 e 36 VAL GLN THR GLU SER GLN GLN LYS SER SER
SEQRES 1 f 246 ALA LYS GLN THR LEU THR TYR ASP ASP ILE VAL GLY THR
SEQRES 2 f 246 GLY LEU ALA ASN LYS CYS PRO THR LEU ASP ASP THR ALA
SEQRES 3 f 246 ARG GLY ALA TYR PRO ILE ASP SER SER GLN THR TYR ARG
SEQRES 4 f 246 ILE ALA ARG LEU CYS LEU GLN PRO THR THR PHE LEU VAL
SEQRES 5 f 246 LYS GLU GLU PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE
SEQRES 6 f 246 VAL PRO THR LYS LEU VAL THR ARG GLU THR THR SER LEU
SEQRES 7 f 246 ASP GLN ILE GLN GLY GLU LEU LYS VAL ASN SER ASP GLY
SEQRES 8 f 246 SER LEU THR PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN
SEQRES 9 f 246 PRO VAL THR VAL GLN MET ALA GLY GLY GLU ARG ILE PRO
SEQRES 10 f 246 LEU LEU PHE THR VAL LYS ASN LEU VAL ALA SER THR GLN
SEQRES 11 f 246 PRO ASN VAL THR SER ILE THR THR SER THR ASP PHE LYS
SEQRES 12 f 246 GLY GLU PHE ASN VAL PRO SER TYR ARG THR ALA ASN PHE
SEQRES 13 f 246 LEU ASP PRO LYS GLY ARG GLY LEU ALA SER GLY TYR ASP
SEQRES 14 f 246 SER ALA ILE ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU
SEQRES 15 f 246 ALA ARG ALA ASN VAL LYS ARG PHE SER LEU THR LYS GLY
SEQRES 16 f 246 GLN ILE SER LEU ASN VAL ALA LYS VAL ASP GLY ARG THR
SEQRES 17 f 246 GLY GLU ILE ALA GLY THR PHE GLU SER GLU GLN LEU SER
SEQRES 18 f 246 ASP ASP ASP MET GLY ALA HIS GLU PRO HIS GLU VAL LYS
SEQRES 19 f 246 ILE GLN GLY VAL PHE TYR ALA SER ILE GLU PRO ALA
SEQRES 1 g 32 MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE
SEQRES 2 g 32 ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO
SEQRES 3 g 32 PRO ARG ILE THR LYS LYS
SEQRES 1 h 104 ALA THR ALA SER THR GLU GLU GLU LEU VAL ASN VAL VAL
SEQRES 2 h 104 ASP GLU LYS LEU GLY THR ALA TYR GLY GLU LYS ILE ASP
SEQRES 3 h 104 LEU ASN ASN THR ASN ILE ALA ALA PHE ILE GLN TYR ARG
SEQRES 4 h 104 GLY LEU TYR PRO THR LEU ALA LYS LEU ILE VAL LYS ASN
SEQRES 5 h 104 ALA PRO TYR GLU SER VAL GLU ASP VAL LEU ASN ILE PRO
SEQRES 6 h 104 GLY LEU THR GLU ARG GLN LYS GLN ILE LEU ARG GLU ASN
SEQRES 7 h 104 LEU GLU HIS PHE THR VAL THR GLU VAL GLU THR ALA LEU
SEQRES 8 h 104 VAL GLU GLY GLY ASP ARG TYR ASN ASN GLY LEU TYR LYS
SEQRES 1 i 137 ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN
SEQRES 2 i 137 SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR
SEQRES 3 i 137 LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER
SEQRES 4 i 137 CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU
SEQRES 5 i 137 ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO
SEQRES 6 i 137 ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN
SEQRES 7 i 137 PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL
SEQRES 8 i 137 HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET
SEQRES 9 i 137 ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY
SEQRES 10 i 137 HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP
SEQRES 11 i 137 GLY GLY GLY LYS VAL TYR TYR
SEQRES 1 m 46 MET GLY ILE PHE ASN GLY ILE ILE GLU PHE LEU SER ASN
SEQRES 2 m 46 ILE ASN PHE GLU VAL ILE ALA GLN LEU THR MET ILE ALA
SEQRES 3 m 46 MET ILE GLY ILE ALA GLY PRO MET ILE ILE PHE LEU LEU
SEQRES 4 m 46 ALA VAL ARG ARG GLY ASN LEU
SEQRES 1 j 40 THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY LEU
SEQRES 2 j 40 LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA VAL
SEQRES 3 j 40 LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG SER
SEQRES 4 j 40 LEU
SEQRES 1 k 28 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 2 k 28 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 3 k 28 UNK UNK
SEQRES 1 l 62 MET THR ILE LEU PHE GLN LEU ALA LEU ALA ALA LEU VAL
SEQRES 2 l 62 ILE LEU SER PHE VAL MET VAL ILE GLY VAL PRO VAL ALA
SEQRES 3 l 62 TYR ALA SER PRO GLN ASP TRP ASP ARG SER LYS GLN LEU
SEQRES 4 l 62 ILE PHE LEU GLY SER GLY LEU TRP ILE ALA LEU VAL LEU
SEQRES 5 l 62 VAL VAL GLY VAL LEU ASN PHE PHE VAL VAL
HET CLA A 401 65
HET CLA A 402 65
HET CLA A 403 65
HET PHO A 404 64
HET CLA A 405 65
HET PL9 A 406 45
HET DGD A 407 56
HET LHG A 408 39
HET SQD A 409 51
HET LMG A 410 51
HET LHG A 411 37
HET OEC A 412 5
HET FE2 A 413 1
HET SQD A 414 54
HET CLA B 601 65
HET CLA B 602 65
HET CLA B 603 65
HET CLA B 604 65
HET CLA B 605 65
HET CLA B 606 65
HET CLA B 607 65
HET CLA B 608 65
HET CLA B 609 65
HET CLA B 610 65
HET CLA B 611 65
HET CLA B 612 65
HET CLA B 613 65
HET CLA B 614 65
HET CLA B 615 65
HET CLA B 616 65
HET BCR B 617 40
HET BCR B 618 40
HET BCR B 619 40
HET BCR B 620 40
HET DGD B 621 58
HET LMG B 622 49
HET LMG B 623 49
HET SQD B 624 43
HET LMT B 625 35
HET LMT B 626 35
HET SQD B 627 47
HET DGD B 628 52
HET LMT B 629 35
HET LMT B 630 35
HET CLA C 501 65
HET CLA C 502 65
HET CLA C 503 65
HET CLA C 504 65
HET CLA C 505 65
HET CLA C 506 65
HET CLA C 507 65
HET CLA C 508 65
HET CLA C 509 65
HET BCR C 514 40
HET CLA C 510 65
HET BCR C 515 40
HET CLA C 511 65
HET DGD C 516 53
HET CLA C 512 65
HET DGD C 517 62
HET CLA C 513 65
HET DGD C 518 66
HET LMG C 519 48
HET LMG C 520 45
HET PHO D 402 64
HET PL9 D 404 55
HET CLA D 401 65
HET LMG D 406 46
HET LMG D 407 48
HET CLA D 403 65
HET BCR D 405 40
HET BCT D 410 4
HET CL D 411 1
HET DGD D 408 63
HET LMT D 409 31
HET LMG D 412 42
HET HEM E 101 43
HET LMG E 102 44
HET SQD F 101 45
HET BCR H 101 40
HET BCR I 101 40
HET LMG I 102 43
HET LMT I 103 35
HET PL9 J 101 35
HET BCR J 102 40
HET BCR K 101 40
HET LMG M 101 42
HET LMT M 102 35
HET CA O 301 1
HET BCR T 101 40
HET BCR T 102 40
HET BCR T 103 40
HET HEM V 201 43
HET BCR Z 101 40
HET SQD G 401 54
HET CLA G 402 65
HET CLA G 403 65
HET PHO G 405 64
HET CLA G 404 65
HET PL9 G 407 45
HET CLA G 406 65
HET DGD G 408 56
HET SQD G 410 51
HET LHG G 409 39
HET LMG G 411 51
HET LHG G 412 37
HET OEC G 413 5
HET FE2 G 414 1
HET CL G 415 1
HET SQD N 601 47
HET DGD N 602 52
HET LMT N 603 35
HET LMT N 604 35
HET CLA N 605 65
HET CLA N 606 65
HET CLA N 607 65
HET CLA N 608 65
HET CLA N 609 65
HET CLA N 610 65
HET CLA N 611 65
HET CLA N 612 65
HET CLA N 613 65
HET CLA N 614 65
HET CLA N 615 65
HET CLA N 616 65
HET CLA N 617 65
HET BCR N 621 40
HET CLA N 618 65
HET CLA N 619 65
HET LMG N 623 49
HET CLA N 620 65
HET LMT N 625 35
HET LMG N 622 49
HET LMT N 624 35
HET CLA P 501 65
HET CLA P 502 65
HET CLA P 503 65
HET CLA P 504 65
HET CLA P 505 65
HET CLA P 506 65
HET CLA P 507 65
HET CLA P 508 65
HET CLA P 509 65
HET CLA P 510 65
HET CLA P 511 65
HET BCR P 514 40
HET CLA P 512 65
HET BCR P 515 40
HET CLA P 513 65
HET DGD P 517 53
HET DGD P 518 62
HET BCR P 516 40
HET LMG P 520 48
HET DGD P 519 66
HET LMG P 521 45
HET PHO Q 403 64
HET LMG Q 401 42
HET PL9 Q 405 55
HET CLA Q 402 65
HET LMG Q 407 48
HET CLA Q 404 65
HET SQD Q 408 43
HET DGD Q 409 63
HET LMG Q 406 46
HET LMT Q 410 31
HET BCT Q 411 4
HET HEM R 101 43
HET LMG R 102 44
HET BCR S 101 40
HET SQD S 102 45
HET BCR W 101 40
HET DGD W 102 58
HET BCR a 101 40
HET LMG a 102 43
HET LMT a 103 35
HET PL9 b 101 35
HET BCR b 102 40
HET BCR c 101 40
HET LMT e 101 35
HET LMG e 102 42
HET CA f 301 1
HET HEM i 201 43
HETNAM CLA CHLOROPHYLL A
HETNAM PHO PHEOPHYTIN A
HETNAM PL9 2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,
HETNAM 2 PL9 6,10,14,18,22,26,30,34-HEXATRIACONTANONAENYL-2,5-
HETNAM 3 PL9 CYCLOHEXADIENE-1,4-DIONE-2,3-DIMETHYL-5-SOLANESYL-1,4-
HETNAM 4 PL9 BENZOQUINONE
HETNAM DGD DIGALACTOSYL DIACYL GLYCEROL (DGDG)
HETNAM LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE
HETNAM SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-
HETNAM 2 SQD GLUCOPYRANOSYL]-SN-GLYCEROL
HETNAM LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE
HETNAM OEC OXYGEN EVOLVING SYSTEM
HETNAM FE2 FE (II) ION
HETNAM BCR BETA-CAROTENE
HETNAM LMT DODECYL-BETA-D-MALTOSIDE
HETNAM BCT BICARBONATE ION
HETNAM CL CHLORIDE ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM CA CALCIUM ION
HETSYN PL9 PLASTOQUINONE 9
HETSYN SQD SULFOQUINOVOSYLDIACYLGLYCEROL
HETSYN HEM HEME
FORMUL 41 CLA 70(C55 H72 MG N4 O5 2+)
FORMUL 44 PHO 4(C55 H74 N4 O5)
FORMUL 46 PL9 6(C53 H80 O2)
FORMUL 47 DGD 14(C51 H96 O15)
FORMUL 48 LHG 4(C38 H75 O10 P)
FORMUL 49 SQD 10(C41 H78 O12 S)
FORMUL 50 LMG 22(C45 H86 O10)
FORMUL 52 OEC 2(CA MN4 O4)
FORMUL 53 FE2 2(FE 2+)
FORMUL 71 BCR 24(C40 H56)
FORMUL 79 LMT 14(C24 H46 O11)
FORMUL 12 BCT 2(C H O3 1-)
FORMUL 13 CL 2(CL 1-)
FORMUL 17 HEM 4(C34 H32 FE N4 O4)
FORMUL 29 CA 2(CA 2+)
HELIX 1 1 ASN A 12 THR A 22 1 11
HELIX 2 2 PHE A 33 ALA A 55 1 23
HELIX 3 3 SER A 70 GLY A 74 5 5
HELIX 4 4 PRO A 95 ALA A 99 5 5
HELIX 5 5 SER A 101 ASN A 108 1 8
HELIX 6 6 GLY A 109 LEU A 137 1 29
HELIX 7 7 TRP A 142 TYR A 147 1 6
HELIX 8 8 TYR A 147 LEU A 159 1 13
HELIX 9 9 LEU A 159 GLY A 166 1 8
HELIX 10 10 SER A 167 GLY A 171 5 5
HELIX 11 11 ILE A 176 ASN A 191 1 16
HELIX 12 12 ILE A 192 MET A 194 5 3
HELIX 13 13 HIS A 195 SER A 222 1 28
HELIX 14 14 ASN A 247 ILE A 259 1 13
HELIX 15 15 PHE A 260 SER A 264 5 5
HELIX 16 16 ASN A 267 MET A 293 1 27
HELIX 17 17 THR A 316 HIS A 332 1 17
HELIX 18 18 GLU A 333 HIS A 337 5 5
HELIX 19 19 PRO B 4 ILE B 13 5 10
HELIX 20 20 ASP B 15 ALA B 43 1 29
HELIX 21 21 PRO B 54 GLN B 58 5 5
HELIX 22 22 VAL B 62 ARG B 68 1 7
HELIX 23 23 SER B 92 TYR B 117 1 26
HELIX 24 24 LEU B 120 ARG B 124 5 5
HELIX 25 25 ASP B 134 HIS B 157 1 24
HELIX 26 26 GLY B 186 ASN B 191 5 6
HELIX 27 27 ASN B 194 VAL B 219 1 26
HELIX 28 28 PRO B 222 LEU B 229 1 8
HELIX 29 29 ASN B 233 GLU B 235 5 3
HELIX 30 30 THR B 236 GLY B 259 1 24
HELIX 31 31 PRO B 264 GLY B 269 1 6
HELIX 32 32 THR B 271 SER B 277 1 7
HELIX 33 33 SER B 278 SER B 294 1 17
HELIX 34 34 THR B 297 ILE B 305 1 9
HELIX 35 35 PRO B 306 TYR B 312 1 7
HELIX 36 36 ASP B 313 ASN B 318 5 6
HELIX 37 37 PRO B 329 GLY B 333 5 5
HELIX 38 38 ARG B 384 SER B 388 5 5
HELIX 39 39 SER B 391 GLY B 396 1 6
HELIX 40 40 ASP B 413 ILE B 425 1 13
HELIX 41 41 SER B 446 PHE B 475 1 30
HELIX 42 42 ALA C 34 ILE C 43 5 10
HELIX 43 43 GLY C 47 PHE C 75 1 29
HELIX 44 44 LEU C 88 LEU C 95 1 8
HELIX 45 45 GLY C 100 GLU C 104 5 5
HELIX 46 46 THR C 108 ARG C 135 1 28
HELIX 47 47 ASP C 153 PHE C 181 1 29
HELIX 48 48 ASP C 205 PHE C 210 1 6
HELIX 49 49 GLY C 211 LYS C 215 5 5
HELIX 50 50 GLY C 222 VAL C 227 5 6
HELIX 51 51 ASN C 229 LEU C 253 1 25
HELIX 52 52 GLY C 258 PHE C 264 1 7
HELIX 53 53 SER C 267 ASN C 293 1 27
HELIX 54 54 THR C 305 LEU C 324 1 20
HELIX 55 55 ASN C 327 ALA C 331 5 5
HELIX 56 56 GLY C 353 TRP C 359 5 7
HELIX 57 57 LEU C 366 ARG C 370 5 5
HELIX 58 58 ASP C 376 ASP C 383 1 8
HELIX 59 59 GLN C 385 THR C 397 1 13
HELIX 60 60 SER C 421 ALA C 453 1 33
HELIX 61 61 GLU C 464 MET C 469 5 6
HELIX 62 62 TRP D 14 LYS D 23 1 10
HELIX 63 63 VAL D 30 PHE D 54 1 25
HELIX 64 64 SER D 57 GLY D 62 1 6
HELIX 65 65 SER D 66 GLY D 70 5 5
HELIX 66 66 ASP D 100 LEU D 107 1 8
HELIX 67 67 GLY D 108 GLY D 137 1 30
HELIX 68 68 PRO D 140 PHE D 146 1 7
HELIX 69 69 PHE D 146 LEU D 158 1 13
HELIX 70 70 LEU D 158 GLN D 164 1 7
HELIX 71 71 SER D 166 ALA D 170 5 5
HELIX 72 72 VAL D 175 ASN D 190 1 16
HELIX 73 73 TRP D 191 LEU D 193 5 3
HELIX 74 74 ASN D 194 ASN D 220 1 27
HELIX 75 75 SER D 245 PHE D 257 1 13
HELIX 76 76 ASN D 263 LEU D 291 1 29
HELIX 77 77 PHE D 298 ASP D 308 1 11
HELIX 78 78 THR D 313 GLN D 334 1 22
HELIX 79 79 PRO D 335 ASN D 338 5 4
HELIX 80 80 PRO E 9 SER E 16 1 8
HELIX 81 81 SER E 16 THR E 40 1 25
HELIX 82 82 GLY E 41 PHE E 47 1 7
HELIX 83 83 GLU E 71 GLN E 82 1 12
HELIX 84 84 THR F 17 GLN F 41 1 25
HELIX 85 85 THR H 5 ARG H 12 1 8
HELIX 86 86 THR H 27 ASN H 50 1 24
HELIX 87 87 GLU I 2 SER I 25 1 24
HELIX 88 88 PRO J 9 ALA J 32 1 24
HELIX 89 89 PRO K 12 ILE K 17 5 6
HELIX 90 90 PHE K 18 ASP K 23 1 6
HELIX 91 91 VAL K 24 PRO K 26 5 3
HELIX 92 92 VAL K 27 VAL K 43 1 17
HELIX 93 93 ASN L 13 ASN L 37 1 25
HELIX 94 94 LEU M 6 SER M 31 1 26
HELIX 95 95 THR O 32 ILE O 36 5 5
HELIX 96 96 GLY O 40 LYS O 44 5 5
HELIX 97 97 LEU O 208 VAL O 213 1 6
HELIX 98 98 GLU T 2 PHE T 23 1 22
HELIX 99 99 ASN U 41 LEU U 47 1 7
HELIX 100 100 ASN U 61 TYR U 68 5 8
HELIX 101 101 TYR U 72 ASN U 82 1 11
HELIX 102 102 SER U 87 ILE U 94 5 8
HELIX 103 103 THR U 98 LEU U 109 1 12
HELIX 104 104 GLU U 118 GLU U 123 1 6
HELIX 105 105 GLY U 124 ASP U 126 5 3
HELIX 106 106 THR V 48 CYS V 63 1 16
HELIX 107 107 CYS V 63 VAL V 68 1 6
HELIX 108 108 GLY V 69 ILE V 71 5 3
HELIX 109 109 ARG V 81 LEU V 87 1 7
HELIX 110 110 ASN V 94 MET V 102 1 9
HELIX 111 111 SER V 120 ALA V 124 5 5
HELIX 112 112 PRO V 128 LEU V 133 1 6
HELIX 113 113 THR V 134 GLY V 153 1 20
HELIX 114 114 GLY V 153 GLY V 158 1 6
HELIX 115 115 GLN y 21 ARG y 42 1 22
HELIX 116 116 THR X 13 GLN X 42 1 30
HELIX 117 117 UNK Y 2 UNK Y 13 1 12
HELIX 118 118 UNK Y 14 UNK Y 25 1 12
HELIX 119 119 THR Z 2 SER Z 29 1 28
HELIX 120 120 ARG Z 35 VAL Z 62 1 28
HELIX 121 121 ASN G 12 THR G 22 1 11
HELIX 122 122 PHE G 33 ALA G 55 1 23
HELIX 123 123 SER G 70 GLY G 74 5 5
HELIX 124 124 PRO G 95 ALA G 99 5 5
HELIX 125 125 SER G 101 ASN G 108 1 8
HELIX 126 126 GLY G 109 LEU G 137 1 29
HELIX 127 127 TRP G 142 TYR G 147 1 6
HELIX 128 128 TYR G 147 LEU G 159 1 13
HELIX 129 129 LEU G 159 GLY G 166 1 8
HELIX 130 130 SER G 167 GLY G 171 5 5
HELIX 131 131 ILE G 176 ASN G 191 1 16
HELIX 132 132 ILE G 192 MET G 194 5 3
HELIX 133 133 HIS G 195 SER G 222 1 28
HELIX 134 134 ASN G 247 ILE G 259 1 13
HELIX 135 135 PHE G 260 SER G 264 5 5
HELIX 136 136 ASN G 267 MET G 293 1 27
HELIX 137 137 THR G 316 HIS G 332 1 17
HELIX 138 138 GLU G 333 HIS G 337 5 5
HELIX 139 139 PRO N 4 ILE N 13 5 10
HELIX 140 140 ASP N 15 ALA N 43 1 29
HELIX 141 141 PRO N 54 GLN N 58 5 5
HELIX 142 142 VAL N 62 ARG N 68 1 7
HELIX 143 143 SER N 92 TYR N 117 1 26
HELIX 144 144 LEU N 120 ARG N 124 5 5
HELIX 145 145 ASP N 134 HIS N 157 1 24
HELIX 146 146 GLY N 186 ASN N 191 5 6
HELIX 147 147 ASN N 194 VAL N 219 1 26
HELIX 148 148 PRO N 222 LEU N 229 1 8
HELIX 149 149 ASN N 233 GLU N 235 5 3
HELIX 150 150 THR N 236 GLY N 259 1 24
HELIX 151 151 PRO N 264 GLY N 269 1 6
HELIX 152 152 THR N 271 SER N 277 1 7
HELIX 153 153 SER N 278 SER N 294 1 17
HELIX 154 154 THR N 297 ILE N 305 1 9
HELIX 155 155 PRO N 306 TYR N 312 1 7
HELIX 156 156 ASP N 313 ASN N 318 5 6
HELIX 157 157 PRO N 329 GLY N 333 5 5
HELIX 158 158 ARG N 384 SER N 388 5 5
HELIX 159 159 SER N 391 GLY N 396 1 6
HELIX 160 160 ASP N 413 ILE N 425 1 13
HELIX 161 161 SER N 446 PHE N 475 1 30
HELIX 162 162 ALA P 34 ILE P 43 5 10
HELIX 163 163 GLY P 47 PHE P 75 1 29
HELIX 164 164 LEU P 88 LEU P 95 1 8
HELIX 165 165 GLY P 100 GLU P 104 5 5
HELIX 166 166 THR P 108 ARG P 135 1 28
HELIX 167 167 ASP P 153 PHE P 181 1 29
HELIX 168 168 ASP P 205 PHE P 210 1 6
HELIX 169 169 GLY P 211 LYS P 215 5 5
HELIX 170 170 GLY P 222 VAL P 227 5 6
HELIX 171 171 ASN P 229 LEU P 253 1 25
HELIX 172 172 GLY P 258 PHE P 264 1 7
HELIX 173 173 SER P 267 ASN P 293 1 27
HELIX 174 174 THR P 305 LEU P 324 1 20
HELIX 175 175 ASN P 327 ALA P 331 5 5
HELIX 176 176 GLY P 353 TRP P 359 5 7
HELIX 177 177 LEU P 366 ARG P 370 5 5
HELIX 178 178 ASP P 376 ASP P 383 1 8
HELIX 179 179 GLN P 385 THR P 397 1 13
HELIX 180 180 SER P 421 GLY P 454 1 34
HELIX 181 181 GLU P 464 MET P 469 5 6
HELIX 182 182 TRP Q 14 LYS Q 23 1 10
HELIX 183 183 VAL Q 30 PHE Q 54 1 25
HELIX 184 184 SER Q 57 GLY Q 62 1 6
HELIX 185 185 SER Q 66 GLY Q 70 5 5
HELIX 186 186 ASP Q 100 LEU Q 107 1 8
HELIX 187 187 GLY Q 108 GLY Q 137 1 30
HELIX 188 188 PRO Q 140 PHE Q 146 1 7
HELIX 189 189 PHE Q 146 LEU Q 158 1 13
HELIX 190 190 LEU Q 158 GLN Q 164 1 7
HELIX 191 191 SER Q 166 ALA Q 170 5 5
HELIX 192 192 VAL Q 175 ASN Q 190 1 16
HELIX 193 193 TRP Q 191 LEU Q 193 5 3
HELIX 194 194 ASN Q 194 ASN Q 220 1 27
HELIX 195 195 SER Q 245 PHE Q 257 1 13
HELIX 196 196 ASN Q 263 LEU Q 291 1 29
HELIX 197 197 PHE Q 298 ASP Q 308 1 11
HELIX 198 198 THR Q 313 GLN Q 334 1 22
HELIX 199 199 PRO Q 335 ASN Q 338 5 4
HELIX 200 200 PRO Q 342 LEU Q 346 5 5
HELIX 201 201 PRO R 9 SER R 16 1 8
HELIX 202 202 SER R 16 THR R 40 1 25
HELIX 203 203 GLY R 41 PHE R 47 1 7
HELIX 204 204 GLU R 71 GLN R 82 1 12
HELIX 205 205 THR S 17 GLN S 41 1 25
HELIX 206 206 THR W 5 ARG W 12 1 8
HELIX 207 207 THR W 27 ASN W 50 1 24
HELIX 208 208 GLU a 2 SER a 25 1 24
HELIX 209 209 PRO b 9 ALA b 32 1 24
HELIX 210 210 PRO c 12 ILE c 17 5 6
HELIX 211 211 PHE c 18 ASP c 23 1 6
HELIX 212 212 VAL c 24 PRO c 26 5 3
HELIX 213 213 VAL c 27 VAL c 43 1 17
HELIX 214 214 ASN d 13 ASN d 37 1 25
HELIX 215 215 LEU e 6 SER e 31 1 26
HELIX 216 216 THR f 32 ILE f 36 5 5
HELIX 217 217 GLY f 40 LYS f 44 5 5
HELIX 218 218 LEU f 208 VAL f 213 1 6
HELIX 219 219 GLU g 2 PHE g 23 1 22
HELIX 220 220 ASN h 41 LEU h 47 1 7
HELIX 221 221 ASN h 61 TYR h 68 5 8
HELIX 222 222 TYR h 72 ASN h 82 1 11
HELIX 223 223 SER h 87 ILE h 94 5 8
HELIX 224 224 THR h 98 LEU h 109 1 12
HELIX 225 225 GLU h 118 GLU h 123 1 6
HELIX 226 226 GLY h 124 ASP h 126 5 3
HELIX 227 227 THR i 48 CYS i 63 1 16
HELIX 228 228 CYS i 63 VAL i 68 1 6
HELIX 229 229 GLY i 69 ILE i 71 5 3
HELIX 230 230 ARG i 81 LEU i 87 1 7
HELIX 231 231 ASN i 94 MET i 102 1 9
HELIX 232 232 SER i 120 ALA i 124 5 5
HELIX 233 233 PHE i 127 ARG i 131 5 5
HELIX 234 234 THR i 134 GLY i 153 1 20
HELIX 235 235 GLY i 153 GLY i 158 1 6
HELIX 236 236 GLN m 21 ARG m 42 1 22
HELIX 237 237 THR j 13 GLN j 42 1 30
HELIX 238 238 UNK k 2 UNK k 13 1 12
HELIX 239 239 UNK k 14 UNK k 25 1 12
HELIX 240 240 THR l 2 SER l 29 1 28
HELIX 241 241 ARG l 35 VAL l 62 1 28
SHEET 1 A 2 ALA A 81 VAL A 82 0
SHEET 2 A 2 LEU A 174 GLY A 175 -1 O LEU A 174 N VAL A 82
SHEET 1 B 2 LEU A 297 ASN A 298 0
SHEET 2 B 2 GLY C 402 SER C 403 1 O GLY C 402 N ASN A 298
SHEET 1 C 2 MET B 166 VAL B 168 0
SHEET 2 C 2 SER B 177 GLN B 179 -1 O SER B 177 N VAL B 168
SHEET 1 D 6 VAL B 377 ASP B 380 0
SHEET 2 D 6 ILE B 369 THR B 371 -1 N LEU B 370 O ALA B 379
SHEET 3 D 6 GLU B 353 VAL B 356 -1 N PHE B 355 O THR B 371
SHEET 4 D 6 ILE B 336 ARG B 347 -1 N PHE B 346 O LEU B 354
SHEET 5 D 6 THR B 398 TYR B 402 -1 O SER B 400 N VAL B 345
SHEET 6 D 6 THR B 410 PHE B 411 -1 O PHE B 411 N VAL B 399
SHEET 1 E 5 VAL B 377 ASP B 380 0
SHEET 2 E 5 ILE B 369 THR B 371 -1 N LEU B 370 O ALA B 379
SHEET 3 E 5 GLU B 353 VAL B 356 -1 N PHE B 355 O THR B 371
SHEET 4 E 5 ILE B 336 ARG B 347 -1 N PHE B 346 O LEU B 354
SHEET 5 E 5 ILE B 429 ASP B 433 -1 O GLU B 431 N GLN B 338
SHEET 1 F 2 LEU C 185 ASP C 187 0
SHEET 2 F 2 ASP C 195 ARG C 197 -1 O ARG C 197 N LEU C 185
SHEET 1 G 2 LEU C 341 ARG C 343 0
SHEET 2 G 2 ILE C 349 PHE C 351 -1 O ILE C 350 N MET C 342
SHEET 1 H 2 ALA D 77 VAL D 78 0
SHEET 2 H 2 PHE D 173 GLY D 174 -1 O PHE D 173 N VAL D 78
SHEET 1 I 2 TYR O 56 PRO O 57 0
SHEET 2 I 2 SER O 161 ILE O 162 -1 O ILE O 162 N TYR O 56
SHEET 1 J10 PHE O 91 PRO O 93 0
SHEET 2 J10 ARG O 65 LYS O 79 -1 N VAL O 78 O VAL O 92
SHEET 3 J10 GLU O 258 GLU O 270 -1 O LYS O 260 N LEU O 77
SHEET 4 J10 GLU O 236 LEU O 246 -1 N SER O 243 O ILE O 261
SHEET 5 J10 LEU O 218 LYS O 229 -1 N LYS O 229 O ALA O 238
SHEET 6 J10 PHE O 168 PRO O 175 -1 N VAL O 174 O THR O 219
SHEET 7 J10 LYS O 149 SER O 154 -1 N LYS O 149 O ASN O 173
SHEET 8 J10 LEU O 119 ILE O 127 -1 N PHE O 121 O ALA O 153
SHEET 9 J10 LEU O 104 VAL O 113 -1 N GLN O 108 O GLU O 124
SHEET 10 J10 ARG O 65 LYS O 79 -1 N LEU O 71 O LEU O 104
SHEET 1 K 3 LYS O 95 LEU O 96 0
SHEET 2 K 3 PHE O 129 GLN O 135 -1 O GLN O 135 N LYS O 95
SHEET 3 K 3 ARG O 141 THR O 147 -1 O ILE O 142 N VAL O 134
SHEET 1 L 2 ILE U 55 ASP U 56 0
SHEET 2 L 2 PHE U 112 THR U 113 1 O THR U 113 N ILE U 55
SHEET 1 M 2 THR V 35 PRO V 37 0
SHEET 2 M 2 THR V 44 THR V 46 -1 O ILE V 45 N VAL V 36
SHEET 1 N 2 ALA G 81 VAL G 82 0
SHEET 2 N 2 LEU G 174 GLY G 175 -1 O LEU G 174 N VAL G 82
SHEET 1 O 2 LEU G 297 ASN G 298 0
SHEET 2 O 2 GLY P 402 SER P 403 1 O GLY P 402 N ASN G 298
SHEET 1 P 2 MET N 166 VAL N 168 0
SHEET 2 P 2 SER N 177 GLN N 179 -1 O SER N 177 N VAL N 168
SHEET 1 Q 6 VAL N 377 ASP N 380 0
SHEET 2 Q 6 ILE N 369 THR N 371 -1 N LEU N 370 O ALA N 379
SHEET 3 Q 6 GLU N 353 VAL N 356 -1 N PHE N 355 O THR N 371
SHEET 4 Q 6 ILE N 336 ARG N 347 -1 N PHE N 346 O LEU N 354
SHEET 5 Q 6 THR N 398 TYR N 402 -1 O SER N 400 N VAL N 345
SHEET 6 Q 6 THR N 410 PHE N 411 -1 O PHE N 411 N VAL N 399
SHEET 1 R 5 VAL N 377 ASP N 380 0
SHEET 2 R 5 ILE N 369 THR N 371 -1 N LEU N 370 O ALA N 379
SHEET 3 R 5 GLU N 353 VAL N 356 -1 N PHE N 355 O THR N 371
SHEET 4 R 5 ILE N 336 ARG N 347 -1 N PHE N 346 O LEU N 354
SHEET 5 R 5 ILE N 429 ASP N 433 -1 O GLU N 431 N GLN N 338
SHEET 1 S 2 LEU P 185 ASP P 187 0
SHEET 2 S 2 ASP P 195 ARG P 197 -1 O ARG P 197 N LEU P 185
SHEET 1 T 2 LEU P 341 ARG P 343 0
SHEET 2 T 2 ILE P 349 PHE P 351 -1 O ILE P 350 N MET P 342
SHEET 1 U 2 ALA Q 77 VAL Q 78 0
SHEET 2 U 2 PHE Q 173 GLY Q 174 -1 O PHE Q 173 N VAL Q 78
SHEET 1 V 2 TYR f 56 PRO f 57 0
SHEET 2 V 2 SER f 161 ILE f 162 -1 O ILE f 162 N TYR f 56
SHEET 1 W10 PHE f 91 PRO f 93 0
SHEET 2 W10 ARG f 65 LYS f 79 -1 N VAL f 78 O VAL f 92
SHEET 3 W10 GLU f 258 GLU f 270 -1 O VAL f 264 N GLN f 72
SHEET 4 W10 GLU f 236 LEU f 246 -1 N SER f 243 O ILE f 261
SHEET 5 W10 LEU f 218 LYS f 229 -1 N LYS f 229 O ALA f 238
SHEET 6 W10 PHE f 168 PRO f 175 -1 N VAL f 174 O THR f 219
SHEET 7 W10 LYS f 149 SER f 154 -1 N LYS f 149 O ASN f 173
SHEET 8 W10 LEU f 119 ILE f 127 -1 N PHE f 121 O ALA f 153
SHEET 9 W10 LEU f 104 VAL f 113 -1 N GLN f 108 O GLU f 124
SHEET 10 W10 ARG f 65 LYS f 79 -1 N LEU f 71 O LEU f 104
SHEET 1 X 3 LYS f 95 LEU f 96 0
SHEET 2 X 3 PHE f 129 GLN f 135 -1 O GLN f 135 N LYS f 95
SHEET 3 X 3 ARG f 141 THR f 147 -1 O ILE f 142 N VAL f 134
SHEET 1 Y 2 ILE h 55 ASP h 56 0
SHEET 2 Y 2 PHE h 112 THR h 113 1 O THR h 113 N ILE h 55
SHEET 1 Z 2 THR i 35 PRO i 37 0
SHEET 2 Z 2 THR i 44 THR i 46 -1 O ILE i 45 N VAL i 36
SSBOND 1 CYS O 45 CYS O 70 1555 1555 2.03
SSBOND 2 CYS f 45 CYS f 70 1555 1555 2.03
LINK NE2 HIS A 215 FE FE2 A 413 1555 1555 2.43
LINK NE2 HIS Q 214 FE FE2 G 414 1555 1555 2.43
LINK NE2 HIS G 215 FE FE2 G 414 1555 1555 2.44
LINK NE2 HIS R 23 FE HEM R 101 1555 1555 2.46
LINK NE2 HIS E 23 FE HEM E 101 1555 1555 2.46
LINK NE2 HIS V 67 FE HEM V 201 1555 1555 2.46
LINK NE2 HIS D 214 FE FE2 A 413 1555 1555 2.46
LINK OD1 ASP A 342 MN2 OEC A 412 1555 1555 2.48
LINK NE2 HIS i 118 FE HEM i 201 1555 1555 2.48
LINK NE2 HIS V 118 FE HEM V 201 1555 1555 2.49
LINK NE2 HIS A 272 FE FE2 A 413 1555 1555 2.50
LINK NE2 HIS i 67 FE HEM i 201 1555 1555 2.50
LINK NE2 HIS G 272 FE FE2 G 414 1555 1555 2.51
LINK FE FE2 G 414 O3 BCT Q 411 1555 1555 2.52
LINK NE2 HIS S 24 FE HEM R 101 1555 1555 2.53
LINK NE2 HIS F 24 FE HEM E 101 1555 1555 2.54
LINK FE FE2 A 413 O3 BCT D 410 1555 1555 2.54
LINK OXT ALA A 344 MN2 OEC A 412 1555 1555 2.55
LINK OE2 GLU C 354 MN3 OEC A 412 1555 1555 2.56
LINK FE FE2 A 413 O2 BCT D 410 1555 1555 2.56
LINK FE FE2 G 414 O2 BCT Q 411 1555 1555 2.57
LINK OE1 GLU G 333 MN3 OEC G 413 1555 1555 2.58
LINK OXT ALA G 344 MN2 OEC G 413 1555 1555 2.59
LINK OE1 GLU A 333 MN3 OEC A 412 1555 1555 2.60
LINK NE2 HIS Q 268 FE FE2 G 414 1555 1555 2.62
LINK NE2 HIS D 268 FE FE2 A 413 1555 1555 2.62
LINK OE2 GLU A 333 MN4 OEC A 412 1555 1555 2.63
LINK NE2 HIS A 332 MN1 OEC A 412 1555 1555 2.64
LINK OD1 ASP G 342 MN2 OEC G 413 1555 1555 2.64
LINK OD2 ASP A 170 MN4 OEC A 412 1555 1555 2.67
LINK OE2 GLU G 333 MN4 OEC G 413 1555 1555 2.69
LINK OD2 ASP G 170 MN4 OEC G 413 1555 1555 2.73
LINK NE2 HIS G 332 MN1 OEC G 413 1555 1555 2.77
LINK OD2 ASP A 342 MN2 OEC A 412 1555 1555 2.78
LINK OD1 ASN C 39 MG CLA C 511 1555 1555 2.86
LINK OD1 ASN P 39 MG CLA P 511 1555 1555 2.87
LINK OE1 GLU G 189 CA1 OEC G 413 1555 1555 2.91
LINK OE1 GLU A 189 CA1 OEC A 412 1555 1555 2.94
LINK OD1 ASP G 170 CA1 OEC G 413 1555 1555 3.01
LINK OD1 ASP A 170 CA1 OEC A 412 1555 1555 3.06
LINK OD2 ASP A 170 CA1 OEC A 412 1555 1555 3.13
LINK OD2 ASP G 170 CA1 OEC G 413 1555 1555 3.14
LINK OE1 GLU f 140 CA CA f 301 1555 1555 3.17
CISPEP 1 THR V 89 PRO V 90 0 -0.66
CISPEP 2 THR i 89 PRO i 90 0 -0.52
SITE 1 AC1 21 PHE A 119 TYR A 147 PRO A 150 SER A 153
SITE 2 AC1 21 VAL A 157 MET A 183 PHE A 186 GLN A 187
SITE 3 AC1 21 LEU A 193 HIS A 198 GLY A 201 VAL A 205
SITE 4 AC1 21 THR A 286 ILE A 290 CLA A 402 CLA A 403
SITE 5 AC1 21 PHO A 404 LEU D 182 LEU D 205 CLA D 401
SITE 6 AC1 21 PHE T 17
SITE 1 AC2 15 THR A 45 VAL A 157 PHE A 158 MET A 172
SITE 2 AC2 15 ILE A 176 THR A 179 PHE A 180 MET A 183
SITE 3 AC2 15 CLA A 401 PHO A 404 MET D 198 VAL D 201
SITE 4 AC2 15 GLY D 206 CLA D 401 PL9 D 404
SITE 1 AC3 15 GLN A 199 VAL A 202 ALA A 203 LEU A 210
SITE 2 AC3 15 TRP A 278 CLA A 401 DGD C 518 PHE D 157
SITE 3 AC3 15 VAL D 175 ILE D 178 PHE D 179 PHE D 181
SITE 4 AC3 15 LEU D 182 CLA D 401 PHO D 402
SITE 1 AC4 18 LEU A 41 ALA A 44 THR A 45 TYR A 126
SITE 2 AC4 18 GLN A 130 ALA A 146 TYR A 147 LEU A 174
SITE 3 AC4 18 VAL A 283 CLA A 401 CLA A 402 SQD A 414
SITE 4 AC4 18 LEU D 205 ALA D 208 LEU D 209 ILE D 213
SITE 5 AC4 18 TRP D 253 PHE D 257
SITE 1 AC5 16 ILE A 36 PRO A 39 THR A 40 PHE A 93
SITE 2 AC5 16 PRO A 95 ILE A 96 TRP A 97 LEU A 114
SITE 3 AC5 16 HIS A 118 LEU A 121 DGD A 407 SQD A 414
SITE 4 AC5 16 TYR I 9 VAL I 12 BCR I 101 LMG I 102
SITE 1 AC6 16 PHE A 211 HIS A 215 LEU A 218 HIS A 252
SITE 2 AC6 16 PHE A 255 SER A 264 PHE A 265 LEU A 271
SITE 3 AC6 16 PHE A 274 PHE D 38 ALA D 41 TYR D 42
SITE 4 AC6 16 LEU D 45 ALA F 22 THR F 25 PL9 J 101
SITE 1 AC7 14 PHE A 93 PRO A 95 TRP A 97 GLU A 98
SITE 2 AC7 14 CLA A 405 LEU C 214 LYS C 215 SER C 216
SITE 3 AC7 14 PRO C 217 TRP C 223 PHE C 284 LYS I 5
SITE 4 AC7 14 TYR I 9 GLY O 38
SITE 1 AC8 15 ARG A 140 TRP A 142 VAL A 145 PHE A 273
SITE 2 AC8 15 SQD A 409 TRP C 36 TRP C 443 ARG C 447
SITE 3 AC8 15 CLA C 504 CLA C 508 ASN D 220 ALA D 229
SITE 4 AC8 15 SER D 230 THR D 231 PHE D 232
SITE 1 AC9 14 ASN A 267 SER A 270 PHE A 273 PHE A 274
SITE 2 AC9 14 LHG A 408 LHG A 411 TRP C 36 CLA C 508
SITE 3 AC9 14 DGD C 517 DGD C 518 PHE D 232 ARG D 233
SITE 4 AC9 14 PL9 J 101 PHE K 37
SITE 1 BC1 17 SER A 232 ASN A 234 TRP B 5 TYR B 6
SITE 2 BC1 17 CLA B 611 LMG B 622 TRP D 266 PHE D 273
SITE 3 BC1 17 GLU L 11 LEU L 12 ASN L 13 SER L 16
SITE 4 BC1 17 LEU L 19 GLY L 20 LEU L 22 ILE L 24
SITE 5 BC1 17 VAL L 26
SITE 1 BC2 8 TYR A 262 ASN A 266 SQD A 409 TRP C 35
SITE 2 BC2 8 DGD C 517 LMG E 102 BCR J 102 PHE K 45
SITE 1 BC3 8 ASP A 170 GLU A 189 HIS A 332 GLU A 333
SITE 2 BC3 8 HIS A 337 ASP A 342 ALA A 344 GLU C 354
SITE 1 BC4 5 HIS A 215 HIS A 272 HIS D 214 HIS D 268
SITE 2 BC4 5 BCT D 410
SITE 1 BC5 17 TRP A 20 ASN A 26 ARG A 27 LEU A 28
SITE 2 BC5 17 VAL A 30 ILE A 38 LEU A 41 LEU A 42
SITE 3 BC5 17 THR A 45 PHO A 404 CLA A 405 BCR I 101
SITE 4 BC5 17 TRP N 113 TYR N 117 CLA N 610 CLA N 620
SITE 5 BC5 17 BCR T 103
SITE 1 BC6 9 TRP B 185 PRO B 187 PHE B 190 ILE B 207
SITE 2 BC6 9 VAL B 208 CLA B 602 PHE H 41 ILE H 44
SITE 3 BC6 9 BCR H 101
SITE 1 BC7 18 GLU B 184 GLY B 189 GLY B 197 ALA B 200
SITE 2 BC7 18 HIS B 201 ALA B 204 ALA B 205 VAL B 208
SITE 3 BC7 18 PHE B 246 PHE B 247 CLA B 601 CLA B 603
SITE 4 BC7 18 DGD B 621 VAL D 154 PHE H 38 PHE H 41
SITE 5 BC7 18 ILE H 45 TYR H 49
SITE 1 BC8 19 ARG B 68 LEU B 69 ALA B 146 LEU B 149
SITE 2 BC8 19 CYS B 150 PHE B 153 VAL B 198 HIS B 201
SITE 3 BC8 19 HIS B 202 PHE B 247 VAL B 252 THR B 262
SITE 4 BC8 19 CLA B 602 CLA B 604 CLA B 605 CLA B 606
SITE 5 BC8 19 CLA B 609 PHE H 38 LEU H 42
SITE 1 BC9 18 TRP B 33 PHE B 61 PHE B 65 ARG B 68
SITE 2 BC9 18 VAL B 245 ALA B 248 ALA B 249 VAL B 252
SITE 3 BC9 18 PHE B 451 HIS B 455 PHE B 458 PHE B 462
SITE 4 BC9 18 CLA B 603 CLA B 605 CLA B 607 CLA B 612
SITE 5 BC9 18 CLA B 613 CLA B 615
SITE 1 CC1 20 THR B 27 VAL B 30 ALA B 31 TRP B 33
SITE 2 CC1 20 ALA B 34 VAL B 62 PHE B 65 MET B 66
SITE 3 CC1 20 ARG B 68 LEU B 69 HIS B 100 LEU B 103
SITE 4 CC1 20 GLY B 147 ALA B 205 CLA B 603 CLA B 604
SITE 5 CC1 20 CLA B 606 CLA B 610 CLA B 612 CLA B 615
SITE 1 CC2 17 LEU B 69 TRP B 91 ALA B 99 LEU B 103
SITE 2 CC2 17 LEU B 106 GLY B 152 PHE B 153 PHE B 156
SITE 3 CC2 17 HIS B 157 PHE B 162 PRO B 164 CLA B 603
SITE 4 CC2 17 CLA B 605 CLA B 616 BCR B 620 LMT B 625
SITE 5 CC2 17 SQD G 401
SITE 1 CC3 18 TRP B 33 MET B 37 TYR B 40 GLN B 58
SITE 2 CC3 18 GLY B 59 PHE B 61 GLY B 328 PRO B 329
SITE 3 CC3 18 TRP B 450 ALA B 454 CLA B 604 BCR B 617
SITE 4 CC3 18 BCR B 618 BCR B 619 LMG B 623 MET D 281
SITE 5 CC3 18 LEU L 27 PHE M 14
SITE 1 CC4 17 THR B 236 SER B 239 ALA B 243 PHE B 246
SITE 2 CC4 17 PHE B 463 HIS B 466 LEU B 474 CLA B 609
SITE 3 CC4 17 CLA B 610 SQD B 624 PHE D 120 ILE D 123
SITE 4 CC4 17 MET D 126 LEU D 127 PHE D 130 CLA D 403
SITE 5 CC4 17 LEU H 43
SITE 1 CC5 17 PHE B 139 LEU B 143 VAL B 208 ALA B 212
SITE 2 CC5 17 PHE B 215 HIS B 216 PRO B 221 PRO B 222
SITE 3 CC5 17 LEU B 229 CLA B 603 CLA B 608 CLA B 610
SITE 4 CC5 17 THR H 27 MET H 31 PHE H 34 LEU H 46
SITE 5 CC5 17 BCR H 101
SITE 1 CC6 12 HIS B 23 PHE B 139 HIS B 142 LEU B 143
SITE 2 CC6 12 VAL B 237 SER B 240 CLA B 605 CLA B 608
SITE 3 CC6 12 CLA B 609 CLA B 612 CLA B 615 BCR H 101
SITE 1 CC7 18 LMG A 410 TRP B 5 TYR B 6 ARG B 7
SITE 2 CC7 18 VAL B 8 HIS B 9 LEU B 238 ILE B 242
SITE 3 CC7 18 PHE B 462 PHE B 464 GLY B 465 TRP B 468
SITE 4 CC7 18 HIS B 469 ARG B 472 CLA B 612 CLA B 613
SITE 5 CC7 18 CLA B 614 LMG B 622
SITE 1 CC8 19 HIS B 9 LEU B 12 LEU B 19 ALA B 22
SITE 2 CC8 19 HIS B 23 HIS B 26 THR B 27 ILE B 234
SITE 3 CC8 19 VAL B 237 LEU B 238 SER B 241 VAL B 245
SITE 4 CC8 19 CLA B 604 CLA B 605 CLA B 610 CLA B 611
SITE 5 CC8 19 CLA B 613 CLA B 614 CLA B 615
SITE 1 CC9 8 HIS B 9 HIS B 26 VAL B 30 PHE B 462
SITE 2 CC9 8 CLA B 604 CLA B 611 CLA B 612 CLA B 614
SITE 1 DC1 11 VAL B 8 HIS B 9 TRP B 115 CLA B 611
SITE 2 DC1 11 CLA B 612 CLA B 613 BCR B 617 SQD B 627
SITE 3 DC1 11 VAL L 10 LMG e 102 PHE g 8
SITE 1 DC2 12 HIS B 23 MET B 138 ILE B 141 HIS B 142
SITE 2 DC2 12 LEU B 145 CLA B 604 CLA B 605 CLA B 610
SITE 3 DC2 12 CLA B 612 CLA B 616 LEU H 14 ASN H 15
SITE 1 DC3 10 ILE B 20 LEU B 24 TRP B 113 HIS B 114
SITE 2 DC3 10 LEU B 120 CLA B 606 CLA B 615 BCR B 620
SITE 3 DC3 10 SQD G 401 THR H 5
SITE 1 DC4 15 ALA B 21 MET B 25 LEU B 29 TRP B 115
SITE 2 DC4 15 CLA B 607 CLA B 614 BCR B 618 BCR B 619
SITE 3 DC4 15 LMG B 623 SQD B 627 ILE M 9 ALA M 10
SITE 4 DC4 15 LEU M 13 LMT M 102 PHE g 19
SITE 1 DC5 14 TRP B 33 SER B 36 MET B 37 TYR B 40
SITE 2 DC5 14 CLA B 607 BCR B 617 BCR B 619 LMT B 629
SITE 3 DC5 14 LMG Q 407 ILE g 4 PHE g 8 ALA g 11
SITE 4 DC5 14 PHE g 17 PHE g 22
SITE 1 DC6 9 LEU B 29 GLY B 32 TRP B 33 ILE B 101
SITE 2 DC6 9 GLY B 105 CLA B 607 BCR B 617 BCR B 618
SITE 3 DC6 9 DGD B 628
SITE 1 DC7 9 LEU B 109 CYS B 112 TRP B 113 TYR B 117
SITE 2 DC7 9 CLA B 606 CLA B 616 LMT B 625 SQD G 401
SITE 3 DC7 9 PHE g 22
SITE 1 DC8 14 TYR B 193 PHE B 250 TYR B 258 TYR B 273
SITE 2 DC8 14 SER B 277 PHE B 463 CLA B 602 HIS D 87
SITE 3 DC8 14 SER D 165 TYR H 49 ASN H 50 VAL H 60
SITE 4 DC8 14 SER H 61 TRP H 62
SITE 1 DC9 9 LMG A 410 TRP B 5 TYR B 6 ARG B 7
SITE 2 DC9 9 PHE B 464 TRP B 468 CLA B 611 TYR D 141
SITE 3 DC9 9 PHE D 269
SITE 1 EC1 11 THR B 327 GLY B 328 PRO B 329 LYS B 332
SITE 2 EC1 11 PHE B 453 CLA B 607 BCR B 617 ILE D 284
SITE 3 EC1 11 PHE L 35 LEU M 6 LMT M 102
SITE 1 EC2 10 LYS B 227 ALA B 228 ARG B 230 LEU B 474
SITE 2 EC2 10 CLA B 608 LMT B 626 LYS D 23 TRP D 32
SITE 3 EC2 10 ARG D 134 LEU D 135
SITE 1 EC3 5 TRP B 91 PHE B 162 CLA B 606 BCR B 620
SITE 2 EC3 5 DGD B 628
SITE 1 EC4 8 ARG B 224 LEU B 225 LYS B 227 SQD B 624
SITE 2 EC4 8 ASP D 16 ASP D 19 ALA H 32 MET H 35
SITE 1 EC5 13 ARG B 18 LEU B 29 SER B 104 TRP B 115
SITE 2 EC5 13 CLA B 614 BCR B 617 ASN L 4 ARG d 14
SITE 3 EC5 13 TYR d 18 TYR e 26 LMG e 102 PHE g 19
SITE 4 EC5 13 PHE g 23
SITE 1 EC6 10 TRP B 75 ASP B 87 GLY B 89 PHE B 90
SITE 2 EC6 10 TRP B 91 VAL B 102 BCR B 619 LMT B 625
SITE 3 EC6 10 LMT B 630 LMG a 102
SITE 1 EC7 6 SER B 36 ALA B 43 THR B 44 BCR B 618
SITE 2 EC7 6 LEU G 72 VAL g 7
SITE 1 EC8 7 GLY B 85 ASP B 87 DGD B 628 ALA G 100
SITE 2 EC8 7 BCR a 101 LMG a 102 LYS f 95
SITE 1 EC9 16 LEU C 95 LEU C 168 GLY C 171 ALA C 172
SITE 2 EC9 16 ILE C 224 VAL C 233 HIS C 237 ILE C 240
SITE 3 EC9 16 ALA C 278 MET C 282 VAL C 296 TYR C 297
SITE 4 EC9 16 CLA C 502 CLA C 503 CLA C 507 BCR C 515
SITE 1 FC1 16 TRP C 63 HIS C 91 TRP C 97 LEU C 174
SITE 2 FC1 16 LYS C 178 PHE C 182 LEU C 279 MET C 282
SITE 3 FC1 16 ALA C 286 TYR C 297 HIS C 430 LEU C 433
SITE 4 FC1 16 PHE C 437 CLA C 501 CLA C 503 CLA C 510
SITE 1 FC2 15 ILE C 60 VAL C 61 ALA C 64 THR C 68
SITE 2 FC2 15 LEU C 88 HIS C 91 VAL C 114 HIS C 118
SITE 3 FC2 15 MET C 282 CLA C 501 CLA C 502 CLA C 509
SITE 4 FC2 15 CLA C 510 CLA C 512 LMG C 520
SITE 1 FC3 17 PHE A 285 LHG A 408 TRP C 63 MET C 67
SITE 2 FC3 17 PHE C 70 GLN C 84 GLY C 85 ILE C 87
SITE 3 FC3 17 LEU C 404 TRP C 425 SER C 429 CLA C 508
SITE 4 FC3 17 CLA C 510 DGD C 517 DGD C 518 LMG C 519
SITE 5 FC3 17 PRO K 26
SITE 1 FC4 15 PHE A 33 MET A 127 TRP A 131 ILE C 265
SITE 2 FC4 15 TYR C 274 GLY C 277 ALA C 278 LEU C 438
SITE 3 FC4 15 HIS C 441 LEU C 442 ALA C 445 ARG C 449
SITE 4 FC4 15 CLA C 507 BCR C 515 PHE I 23
SITE 1 FC5 15 LEU C 161 LEU C 165 LEU C 213 ILE C 243
SITE 2 FC5 15 GLY C 247 TRP C 250 HIS C 251 THR C 255
SITE 3 FC5 15 PRO C 256 PHE C 257 TRP C 259 ALA C 260
SITE 4 FC5 15 PHE C 264 CLA C 507 BCR C 515
SITE 1 FC6 14 MET C 157 LEU C 161 HIS C 164 ILE C 240
SITE 2 FC6 14 PHE C 264 TRP C 266 TYR C 271 TYR C 274
SITE 3 FC6 14 SER C 275 CLA C 501 CLA C 505 CLA C 506
SITE 4 FC6 14 CLA C 509 BCR C 515
SITE 1 FC7 18 LHG A 408 SQD A 409 TRP C 36 ALA C 37
SITE 2 FC7 18 ASN C 39 ALA C 40 GLU C 269 LEU C 276
SITE 3 FC7 18 PHE C 436 PHE C 437 GLY C 440 TRP C 443
SITE 4 FC7 18 HIS C 444 ARG C 447 CLA C 504 CLA C 509
SITE 5 FC7 18 CLA C 510 VAL K 30
SITE 1 FC8 20 ASN C 39 LEU C 42 ILE C 43 LEU C 49
SITE 2 FC8 20 ALA C 52 HIS C 53 HIS C 56 TYR C 149
SITE 3 FC8 20 TRP C 151 GLY C 268 TYR C 271 LEU C 272
SITE 4 FC8 20 SER C 275 LEU C 279 CLA C 503 CLA C 507
SITE 5 FC8 20 CLA C 508 CLA C 510 CLA C 511 CLA C 512
SITE 1 FC9 13 ASN C 39 HIS C 56 LEU C 59 PHE C 436
SITE 2 FC9 13 PHE C 437 CLA C 502 CLA C 503 CLA C 504
SITE 3 FC9 13 CLA C 508 CLA C 509 PRO K 29 VAL K 30
SITE 4 FC9 13 LEU K 33
SITE 1 GC1 21 GLN C 28 TRP C 35 GLY C 38 ASN C 39
SITE 2 GC1 21 ARG C 41 LEU C 42 LYS C 48 ALA C 52
SITE 3 GC1 21 PHE C 127 ILE C 134 CLA C 509 BCR C 514
SITE 4 GC1 21 PHE K 32 LEU K 33 TRP K 39 GLN K 40
SITE 5 GC1 21 MET Z 19 VAL Z 20 PRO Z 24 ILE y 35
SITE 6 GC1 21 LEU y 46
SITE 1 GC2 14 LEU C 50 HIS C 53 ALA C 57 PHE C 147
SITE 2 GC2 14 PHE C 163 HIS C 164 VAL C 167 ILE C 170
SITE 3 GC2 14 GLY C 171 LEU C 174 CLA C 503 CLA C 509
SITE 4 GC2 14 CLA C 513 BCR Z 101
SITE 1 GC3 9 VAL C 54 GLY C 128 TYR C 131 HIS C 132
SITE 2 GC3 9 PRO C 137 LEU C 140 PHE C 147 CLA C 512
SITE 3 GC3 9 BCR Z 101
SITE 1 GC4 14 ALA C 55 LEU C 59 VAL C 116 LEU C 119
SITE 2 GC4 14 ILE C 120 SER C 122 ALA C 123 CLA C 511
SITE 3 GC4 14 PHE K 18 PHE K 32 BCR K 101 LEU Z 9
SITE 4 GC4 14 VAL Z 13 BCR Z 101
SITE 1 GC5 15 ILE C 209 PHE C 210 TYR C 212 LEU C 213
SITE 2 GC5 15 VAL C 227 ASP C 232 VAL C 233 ILE C 240
SITE 3 GC5 15 PHE C 264 CLA C 501 CLA C 505 CLA C 506
SITE 4 GC5 15 CLA C 507 VAL I 20 LEU I 24
SITE 1 GC6 14 PHE A 155 ILE A 163 PRO C 217 PHE C 218
SITE 2 GC6 14 GLY C 219 GLY C 220 GLY C 222 VAL C 225
SITE 3 GC6 14 CYS C 288 PHE C 292 ASN C 294 PRO C 307
SITE 4 GC6 14 PHE C 361 ARG C 362
SITE 1 GC7 20 PHE A 197 THR A 292 SQD A 409 LHG A 411
SITE 2 GC7 20 TYR C 82 GLU C 83 GLN C 84 GLY C 85
SITE 3 GC7 20 LEU C 404 SER C 406 ASN C 418 VAL C 420
SITE 4 GC7 20 TRP C 425 THR C 428 SER C 429 CLA C 504
SITE 5 GC7 20 DGD C 518 LMG C 519 TYR J 33 BCR J 102
SITE 1 GC8 23 LEU A 200 TRP A 278 PHE A 300 ASN A 301
SITE 2 GC8 23 PHE A 302 SER A 305 CLA A 403 SQD A 409
SITE 3 GC8 23 ASN C 405 ASN C 415 SER C 416 ASN C 418
SITE 4 GC8 23 CLA C 504 DGD C 517 LMG D 406 PHE J 29
SITE 5 GC8 23 ALA J 32 TYR J 33 GLY J 37 SER J 38
SITE 6 GC8 23 SER J 39 BCR J 102 GLN V 60
SITE 1 GC9 7 HIS C 74 CLA C 504 DGD C 517 ASP K 23
SITE 2 GC9 7 VAL K 27 VAL K 30 ILE y 25
SITE 1 HC1 7 ASP C 107 PHE C 109 VAL C 114 VAL C 117
SITE 2 HC1 7 HIS C 118 CLA C 503 PHE Z 59
SITE 1 HC2 22 PHE A 206 CLA A 401 CLA A 402 CLA A 403
SITE 2 HC2 22 TRP D 48 LEU D 122 PRO D 149 VAL D 152
SITE 3 HC2 22 VAL D 156 LEU D 182 PHE D 185 GLN D 186
SITE 4 HC2 22 TRP D 191 THR D 192 HIS D 197 GLY D 200
SITE 5 HC2 22 VAL D 201 VAL D 204 LEU D 279 SER D 282
SITE 6 HC2 22 ALA D 283 PHO D 402
SITE 1 HC3 20 PHE A 206 ALA A 209 LEU A 210 MET A 214
SITE 2 HC3 20 CLA A 403 ALA D 41 TRP D 48 ILE D 114
SITE 3 HC3 20 GLY D 118 LEU D 122 PHE D 125 ASN D 142
SITE 4 HC3 20 ALA D 145 PHE D 146 ALA D 148 PRO D 149
SITE 5 HC3 20 PHE D 153 PRO D 275 LEU D 279 CLA D 401
SITE 1 HC4 15 CLA B 608 PRO D 39 LEU D 43 LEU D 89
SITE 2 HC4 15 LEU D 90 LEU D 91 LEU D 92 TRP D 93
SITE 3 HC4 15 THR D 112 PHE D 113 HIS D 117 LMT D 409
SITE 4 HC4 15 GLY X 22 LEU X 23 GLY X 26
SITE 1 HC5 19 PHE A 52 ILE A 53 CLA A 402 MET D 199
SITE 2 HC5 19 ILE D 213 HIS D 214 THR D 217 TRP D 253
SITE 3 HC5 19 ALA D 260 PHE D 261 LEU D 267 PHE D 273
SITE 4 HC5 19 VAL D 274 THR D 277 LMG D 407 LEU L 23
SITE 5 HC5 19 VAL L 26 LEU L 29 PHE T 10
SITE 1 HC6 11 TYR D 42 GLY D 46 GLY D 47 LEU D 49
SITE 2 HC6 11 THR D 50 PHE D 101 LMG D 406 PRO F 29
SITE 3 HC6 11 PHE F 33 VAL J 21 VAL J 25
SITE 1 HC7 12 DGD C 518 TYR D 67 GLY D 70 CYS D 71
SITE 2 HC7 12 PHE D 73 BCR D 405 ILE F 37 GLN F 41
SITE 3 HC7 12 PHE J 28 GLY J 31 ALA J 32 GLY J 37
SITE 1 HC8 12 PHE D 257 ALA D 260 PHE D 261 SER D 262
SITE 2 HC8 12 ASN D 263 TRP D 266 PL9 D 404 THR L 15
SITE 3 HC8 12 TYR L 18 LEU L 19 ALA T 20 BCR T 102
SITE 1 HC9 6 ASP D 100 PHE D 101 LMT D 409 LEU E 42
SITE 2 HC9 6 ASP E 45 VAL E 46
SITE 1 IC1 8 LEU D 92 TRP D 93 GLY D 99 CLA D 403
SITE 2 IC1 8 DGD D 408 ILE X 21 SER X 25 GLY X 26
SITE 1 IC2 9 HIS A 215 GLU A 244 TYR A 246 HIS A 272
SITE 2 IC2 9 FE2 A 413 HIS D 214 TYR D 244 LYS D 264
SITE 3 IC2 9 HIS D 268
SITE 1 IC3 2 GLU A 333 LYS D 317
SITE 1 IC4 9 LEU A 72 LEU A 102 ASP A 103 ARG D 304
SITE 2 IC4 9 ALA N 43 TRP N 75 SER N 76 LEU N 98
SITE 3 IC4 9 GLY O 138
SITE 1 IC5 14 ARG E 8 PHE E 10 ILE E 13 ARG E 18
SITE 2 IC5 14 TYR E 19 HIS E 23 THR E 26 LEU E 30
SITE 3 IC5 14 ILE F 15 ARG F 19 TRP F 20 HIS F 24
SITE 4 IC5 14 ALA F 27 ILE F 31
SITE 1 IC6 7 TYR A 262 LHG A 411 PHE D 27 PRO E 9
SITE 2 IC6 7 PHE E 10 SER E 11 PL9 J 101
SITE 1 IC7 7 TRP D 21 ARG D 26 GLU E 7 PHE F 16
SITE 2 IC7 7 THR F 17 VAL F 18 THR X 33
SITE 1 IC8 9 CLA B 601 CLA B 609 CLA B 610 MET H 35
SITE 2 IC8 9 LEU H 37 PHE H 38 PHE H 41 THR X 11
SITE 3 IC8 9 LEU X 16
SITE 1 IC9 9 VAL A 35 ILE A 38 LEU A 42 ALA A 43
SITE 2 IC9 9 TRP A 105 CLA A 405 SQD A 414 PHE I 15
SITE 3 IC9 9 LMT N 604
SITE 1 JC1 7 CLA A 405 MET I 1 THR I 3 LEU I 4
SITE 2 JC1 7 LMT I 103 DGD N 602 LMT N 604
SITE 1 JC2 6 THR I 3 ILE I 6 ILE I 10 VAL I 11
SITE 2 JC2 6 PHE I 14 LMG I 102
SITE 1 JC3 4 PL9 A 406 SQD A 409 LMG E 102 VAL J 16
SITE 1 JC4 5 LHG A 411 DGD C 517 DGD C 518 PHE J 29
SITE 2 JC4 5 TYR J 33
SITE 1 JC5 15 BCR C 514 ALA J 14 THR J 15 GLY J 18
SITE 2 JC5 15 MET J 19 LEU K 21 LEU K 31 PHE K 37
SITE 3 JC5 15 VAL K 38 ALA K 41 SER Z 16 PHE Z 17
SITE 4 JC5 15 ILE y 28 GLY y 29 GLY y 32
SITE 1 JC6 7 GLU M 30 SER M 31 CLA N 618 PRO d 9
SITE 2 JC6 7 VAL d 10 LEU e 25 GLN e 32
SITE 1 JC7 6 TYR B 40 BCR B 617 LMG B 623 GLN M 5
SITE 2 JC7 6 MET e 1 MET g 1
SITE 1 JC8 3 GLU O 81 GLU O 140 HIS O 257
SITE 1 JC9 14 ALA N 21 MET N 25 LEU N 29 TRP N 115
SITE 2 JC9 14 SQD N 601 CLA N 618 BCR N 621 LMG N 623
SITE 3 JC9 14 PHE T 19 BCR T 102 ILE e 9 ALA e 10
SITE 4 JC9 14 LEU e 13 LMT e 101
SITE 1 KC1 15 LMG D 407 TRP N 33 SER N 36 MET N 37
SITE 2 KC1 15 LMT N 603 CLA N 611 BCR N 621 ILE T 4
SITE 3 KC1 15 PHE T 8 ALA T 11 PHE T 17 PHE T 18
SITE 4 KC1 15 ILE T 21 PHE T 22 BCR T 101
SITE 1 KC2 8 SQD A 414 LEU N 106 LEU N 109 CYS N 112
SITE 2 KC2 8 TYR N 117 CLA N 610 CLA N 620 PHE T 22
SITE 1 KC3 14 ALA V 62 CYS V 63 HIS V 67 THR V 74
SITE 2 KC3 14 LEU V 78 ASP V 79 THR V 84 LEU V 85
SITE 3 KC3 14 LEU V 98 TYR V 101 MET V 102 TYR V 108
SITE 4 KC3 14 HIS V 118 PRO V 119
SITE 1 KC4 11 PHE C 112 VAL C 116 SER C 121 VAL C 124
SITE 2 KC4 11 CLA C 512 CLA C 513 BCR C 514 TYR K 15
SITE 3 KC4 11 VAL Z 54 GLY Z 55 ASN Z 58
SITE 1 KC5 17 TRP B 113 TYR B 117 CLA B 606 CLA B 616
SITE 2 KC5 17 BCR B 620 TRP G 20 ASN G 26 ARG G 27
SITE 3 KC5 17 LEU G 28 VAL G 30 ILE G 38 LEU G 41
SITE 4 KC5 17 LEU G 42 THR G 45 PHO G 405 CLA G 406
SITE 5 KC5 17 BCR a 101
SITE 1 KC6 20 PHE G 119 TYR G 147 PRO G 150 SER G 153
SITE 2 KC6 20 VAL G 157 MET G 183 PHE G 186 GLN G 187
SITE 3 KC6 20 LEU G 193 HIS G 198 VAL G 205 THR G 286
SITE 4 KC6 20 ILE G 290 CLA G 403 CLA G 404 PHO G 405
SITE 5 KC6 20 LEU Q 182 LEU Q 205 CLA Q 402 PHE g 17
SITE 1 KC7 14 THR G 45 VAL G 157 PHE G 158 MET G 172
SITE 2 KC7 14 ILE G 176 THR G 179 MET G 183 CLA G 402
SITE 3 KC7 14 PHO G 405 MET Q 198 VAL Q 201 GLY Q 206
SITE 4 KC7 14 CLA Q 402 PL9 Q 405
SITE 1 KC8 16 GLN G 199 VAL G 202 ALA G 203 LEU G 210
SITE 2 KC8 16 TRP G 278 CLA G 402 DGD P 519 PHE Q 157
SITE 3 KC8 16 VAL Q 175 ILE Q 178 PHE Q 179 PHE Q 181
SITE 4 KC8 16 LEU Q 182 CLA Q 402 PHO Q 403 PL9 b 101
SITE 1 KC9 19 ALA G 44 THR G 45 ILE G 115 TYR G 126
SITE 2 KC9 19 GLN G 130 ALA G 146 TYR G 147 PRO G 150
SITE 3 KC9 19 LEU G 174 VAL G 283 SQD G 401 CLA G 402
SITE 4 KC9 19 CLA G 403 LEU Q 205 ALA Q 208 LEU Q 209
SITE 5 KC9 19 ILE Q 213 TRP Q 253 PHE Q 257
SITE 1 LC1 15 ILE G 36 PRO G 39 THR G 40 PHE G 93
SITE 2 LC1 15 PRO G 95 ILE G 96 TRP G 97 LEU G 114
SITE 3 LC1 15 HIS G 118 LEU G 121 SQD G 401 DGD G 408
SITE 4 LC1 15 TYR a 9 VAL a 12 LMG a 102
SITE 1 LC2 16 PHE G 211 HIS G 215 LEU G 218 HIS G 252
SITE 2 LC2 16 PHE G 255 SER G 264 PHE G 265 LEU G 271
SITE 3 LC2 16 PHE G 274 PHE Q 38 ALA Q 41 TYR Q 42
SITE 4 LC2 16 LEU Q 45 ALA S 22 THR S 25 PL9 b 101
SITE 1 LC3 14 PHE G 93 PRO G 95 TRP G 97 GLU G 98
SITE 2 LC3 14 CLA G 406 LEU P 214 LYS P 215 SER P 216
SITE 3 LC3 14 PRO P 217 TRP P 223 PHE P 284 LYS a 5
SITE 4 LC3 14 TYR a 9 GLY f 38
SITE 1 LC4 14 ARG G 140 TRP G 142 PHE G 273 SQD G 410
SITE 2 LC4 14 TRP P 36 ARG P 447 CLA P 504 CLA P 508
SITE 3 LC4 14 CLA P 510 ASN Q 220 ALA Q 229 SER Q 230
SITE 4 LC4 14 THR Q 231 PHE Q 232
SITE 1 LC5 13 ASN G 267 SER G 270 PHE G 273 PHE G 274
SITE 2 LC5 13 LHG G 409 LHG G 412 TRP P 36 CLA P 508
SITE 3 LC5 13 DGD P 518 DGD P 519 ARG Q 233 PL9 b 101
SITE 4 LC5 13 PHE c 37
SITE 1 LC6 17 SER G 232 ASN G 234 TRP N 5 TYR N 6
SITE 2 LC6 17 CLA N 615 LMG N 622 TRP Q 266 PHE Q 270
SITE 3 LC6 17 PHE Q 273 PL9 Q 405 GLU d 11 LEU d 12
SITE 4 LC6 17 ASN d 13 SER d 16 GLY d 20 ILE d 24
SITE 5 LC6 17 VAL d 26
SITE 1 LC7 8 TYR G 262 ASN G 266 SQD G 410 TRP P 35
SITE 2 LC7 8 DGD P 518 LMG R 102 BCR b 102 PHE c 45
SITE 1 LC8 7 ASP G 170 GLU G 189 HIS G 332 GLU G 333
SITE 2 LC8 7 ASP G 342 ALA G 344 GLU P 354
SITE 1 LC9 5 HIS G 215 HIS G 272 HIS Q 214 HIS Q 268
SITE 2 LC9 5 BCT Q 411
SITE 1 MC1 2 GLU G 333 LYS Q 317
SITE 1 MC2 12 ARG L 14 TYR L 18 TYR M 26 ARG N 18
SITE 2 MC2 12 LEU N 29 SER N 104 TRP N 115 CLA N 618
SITE 3 MC2 12 PHE T 19 PHE T 23 BCR T 101 ASN d 4
SITE 1 MC3 10 LMG I 102 TRP N 75 ASP N 87 GLY N 89
SITE 2 MC3 10 PHE N 90 TRP N 91 LEU N 98 VAL N 102
SITE 3 MC3 10 LMT N 604 LMT N 624
SITE 1 MC4 7 LEU A 72 SER N 36 ALA N 43 LEU N 437
SITE 2 MC4 7 ILE T 4 VAL T 7 BCR T 102
SITE 1 MC5 7 ALA A 100 BCR I 101 LMG I 102 GLY N 85
SITE 2 MC5 7 ASP N 87 DGD N 602 LYS O 95
SITE 1 MC6 8 TRP N 185 PHE N 190 ILE N 207 VAL N 208
SITE 2 MC6 8 CLA N 606 PHE W 41 ILE W 44 BCR W 101
SITE 1 MC7 18 GLU N 184 GLY N 189 GLY N 197 ALA N 200
SITE 2 MC7 18 HIS N 201 ALA N 204 ALA N 205 VAL N 208
SITE 3 MC7 18 PHE N 246 PHE N 247 CLA N 605 CLA N 607
SITE 4 MC7 18 VAL Q 154 PHE W 38 PHE W 41 ILE W 45
SITE 5 MC7 18 TYR W 49 DGD W 102
SITE 1 MC8 20 ARG N 68 LEU N 69 ALA N 146 LEU N 149
SITE 2 MC8 20 CYS N 150 PHE N 153 VAL N 198 HIS N 201
SITE 3 MC8 20 HIS N 202 PHE N 247 ALA N 248 VAL N 252
SITE 4 MC8 20 THR N 262 CLA N 606 CLA N 608 CLA N 609
SITE 5 MC8 20 CLA N 610 CLA N 613 PHE W 38 LEU W 42
SITE 1 MC9 19 TRP N 33 PHE N 61 PHE N 65 ARG N 68
SITE 2 MC9 19 VAL N 245 ALA N 248 ALA N 249 VAL N 252
SITE 3 MC9 19 PHE N 451 HIS N 455 PHE N 458 PHE N 462
SITE 4 MC9 19 CLA N 607 CLA N 609 CLA N 611 CLA N 615
SITE 5 MC9 19 CLA N 616 CLA N 617 CLA N 619
SITE 1 NC1 20 THR N 27 VAL N 30 ALA N 31 TRP N 33
SITE 2 NC1 20 ALA N 34 VAL N 62 PHE N 65 MET N 66
SITE 3 NC1 20 ARG N 68 LEU N 69 HIS N 100 LEU N 103
SITE 4 NC1 20 GLY N 147 ALA N 205 CLA N 607 CLA N 608
SITE 5 NC1 20 CLA N 610 CLA N 614 CLA N 616 CLA N 619
SITE 1 NC2 17 SQD A 414 LEU N 69 TRP N 91 ALA N 99
SITE 2 NC2 17 LEU N 103 LEU N 106 GLY N 152 PHE N 153
SITE 3 NC2 17 PHE N 156 HIS N 157 PHE N 162 PRO N 164
SITE 4 NC2 17 CLA N 607 CLA N 609 CLA N 620 LMT N 624
SITE 5 NC2 17 BCR T 103
SITE 1 NC3 16 TRP N 33 MET N 37 TYR N 40 GLN N 58
SITE 2 NC3 16 GLY N 59 PHE N 61 GLY N 328 PRO N 329
SITE 3 NC3 16 TRP N 450 ALA N 454 CLA N 608 BCR N 621
SITE 4 NC3 16 LMG N 623 MET Q 281 BCR T 102 PHE e 14
SITE 1 NC4 15 THR N 236 SER N 239 SER N 240 ALA N 243
SITE 2 NC4 15 PHE N 246 PHE N 463 HIS N 466 LEU N 474
SITE 3 NC4 15 CLA N 613 CLA N 614 PHE Q 120 ILE Q 123
SITE 4 NC4 15 MET Q 126 LEU Q 127 PHE Q 130
SITE 1 NC5 16 PHE N 139 LEU N 143 ALA N 212 PHE N 215
SITE 2 NC5 16 HIS N 216 ARG N 220 PRO N 221 PRO N 222
SITE 3 NC5 16 LEU N 229 CLA N 607 CLA N 612 CLA N 614
SITE 4 NC5 16 THR W 27 MET W 31 PHE W 34 BCR W 101
SITE 1 NC6 11 PHE N 139 HIS N 142 LEU N 143 THR N 236
SITE 2 NC6 11 VAL N 237 SER N 240 CLA N 609 CLA N 612
SITE 3 NC6 11 CLA N 613 CLA N 616 CLA N 619
SITE 1 NC7 20 LMG G 411 TRP N 5 TYR N 6 ARG N 7
SITE 2 NC7 20 VAL N 8 HIS N 9 LEU N 238 ILE N 242
SITE 3 NC7 20 LEU N 461 PHE N 462 PHE N 464 GLY N 465
SITE 4 NC7 20 TRP N 468 HIS N 469 ARG N 472 CLA N 608
SITE 5 NC7 20 CLA N 616 CLA N 617 CLA N 618 LMG N 622
SITE 1 NC8 19 HIS N 9 LEU N 12 LEU N 19 ALA N 22
SITE 2 NC8 19 HIS N 23 HIS N 26 THR N 27 ILE N 234
SITE 3 NC8 19 VAL N 237 LEU N 238 SER N 241 VAL N 245
SITE 4 NC8 19 CLA N 608 CLA N 609 CLA N 614 CLA N 615
SITE 5 NC8 19 CLA N 617 CLA N 618 CLA N 619
SITE 1 NC9 9 HIS N 9 HIS N 26 VAL N 30 LEU N 461
SITE 2 NC9 9 PHE N 462 CLA N 608 CLA N 615 CLA N 616
SITE 3 NC9 9 CLA N 618
SITE 1 OC1 12 LMG M 101 VAL N 8 HIS N 9 ALA N 22
SITE 2 OC1 12 TRP N 115 SQD N 601 CLA N 615 CLA N 616
SITE 3 OC1 12 CLA N 617 PHE T 8 BCR T 101 VAL d 10
SITE 1 OC2 10 MET N 138 ILE N 141 HIS N 142 LEU N 145
SITE 2 OC2 10 CLA N 608 CLA N 609 CLA N 614 CLA N 616
SITE 3 OC2 10 CLA N 620 LEU W 14
SITE 1 OC3 11 SQD A 414 ILE N 20 LEU N 24 ALA N 110
SITE 2 OC3 11 TRP N 113 HIS N 114 LEU N 120 CLA N 610
SITE 3 OC3 11 CLA N 619 BCR T 103 THR W 5
SITE 1 OC4 8 LEU N 29 GLY N 32 TRP N 33 SER N 36
SITE 2 OC4 8 ILE N 101 CLA N 611 BCR T 101 BCR T 102
SITE 1 OC5 9 LMG G 411 TRP N 5 TYR N 6 ARG N 7
SITE 2 OC5 9 PHE N 464 TRP N 468 CLA N 615 TYR Q 141
SITE 3 OC5 9 PHE Q 269
SITE 1 OC6 11 THR N 327 GLY N 328 PRO N 329 LYS N 332
SITE 2 OC6 11 PHE N 453 CLA N 611 ILE Q 284 BCR T 101
SITE 3 OC6 11 PHE d 35 LEU e 6 LMT e 101
SITE 1 OC7 4 TRP N 91 PHE N 162 DGD N 602 CLA N 610
SITE 1 OC8 8 ARG N 224 LEU N 225 LYS N 227 ASP Q 16
SITE 2 OC8 8 ASP Q 19 SQD Q 408 ALA W 32 MET W 35
SITE 1 OC9 15 LEU P 95 LEU P 168 GLY P 171 ALA P 172
SITE 2 OC9 15 ILE P 224 VAL P 233 HIS P 237 ILE P 240
SITE 3 OC9 15 MET P 282 VAL P 296 TYR P 297 CLA P 502
SITE 4 OC9 15 CLA P 503 CLA P 507 BCR P 516
SITE 1 PC1 14 TRP P 63 HIS P 91 TRP P 97 LEU P 174
SITE 2 PC1 14 LYS P 178 LEU P 279 MET P 282 ALA P 286
SITE 3 PC1 14 TYR P 297 HIS P 430 LEU P 433 PHE P 437
SITE 4 PC1 14 CLA P 501 CLA P 503
SITE 1 PC2 13 ILE P 60 VAL P 61 ALA P 64 THR P 68
SITE 2 PC2 13 LEU P 88 HIS P 91 VAL P 114 HIS P 118
SITE 3 PC2 13 CLA P 501 CLA P 502 CLA P 510 CLA P 512
SITE 4 PC2 13 LMG P 521
SITE 1 PC3 18 PHE G 285 LHG G 409 TRP P 63 MET P 67
SITE 2 PC3 18 PHE P 70 GLN P 84 GLY P 85 ILE P 87
SITE 3 PC3 18 LEU P 404 TRP P 425 SER P 429 CLA P 508
SITE 4 PC3 18 CLA P 510 DGD P 518 DGD P 519 LMG P 520
SITE 5 PC3 18 PRO c 26 VAL c 30
SITE 1 PC4 16 PHE G 33 MET G 127 TRP G 131 PHE P 264
SITE 2 PC4 16 ILE P 265 TYR P 274 GLY P 277 ALA P 278
SITE 3 PC4 16 MET P 281 HIS P 441 LEU P 442 ALA P 445
SITE 4 PC4 16 ARG P 449 CLA P 507 BCR P 516 PHE a 23
SITE 1 PC5 14 LEU P 161 LEU P 165 LEU P 213 ILE P 243
SITE 2 PC5 14 GLY P 247 TRP P 250 HIS P 251 THR P 255
SITE 3 PC5 14 PRO P 256 PHE P 257 TRP P 259 ALA P 260
SITE 4 PC5 14 PHE P 264 CLA P 507
SITE 1 PC6 13 MET P 157 LEU P 161 HIS P 164 PHE P 264
SITE 2 PC6 13 TRP P 266 TYR P 271 TYR P 274 SER P 275
SITE 3 PC6 13 CLA P 501 CLA P 505 CLA P 506 CLA P 509
SITE 4 PC6 13 BCR P 516
SITE 1 PC7 19 LHG G 409 SQD G 410 TRP P 36 ALA P 37
SITE 2 PC7 19 ASN P 39 ALA P 40 GLU P 269 LEU P 272
SITE 3 PC7 19 LEU P 276 PHE P 436 PHE P 437 GLY P 440
SITE 4 PC7 19 TRP P 443 HIS P 444 ARG P 447 CLA P 504
SITE 5 PC7 19 CLA P 509 CLA P 510 VAL c 30
SITE 1 PC8 19 ASN P 39 LEU P 42 ILE P 43 LEU P 49
SITE 2 PC8 19 ALA P 52 HIS P 53 HIS P 56 TYR P 149
SITE 3 PC8 19 TRP P 151 GLY P 268 TYR P 271 LEU P 272
SITE 4 PC8 19 SER P 275 LEU P 279 CLA P 507 CLA P 508
SITE 5 PC8 19 CLA P 510 CLA P 511 CLA P 512
SITE 1 PC9 14 LHG G 409 ASN P 39 HIS P 56 LEU P 59
SITE 2 PC9 14 LEU P 279 PHE P 436 PHE P 437 CLA P 503
SITE 3 PC9 14 CLA P 504 CLA P 508 CLA P 509 CLA P 511
SITE 4 PC9 14 PRO c 29 LEU c 33
SITE 1 QC1 23 GLN P 28 TRP P 35 GLY P 38 ASN P 39
SITE 2 QC1 23 ARG P 41 LEU P 42 LYS P 48 ALA P 52
SITE 3 QC1 23 PHE P 127 ILE P 134 CLA P 509 CLA P 510
SITE 4 QC1 23 BCR P 514 PHE c 32 LEU c 33 TRP c 39
SITE 5 QC1 23 GLN c 40 MET l 19 VAL l 20 PRO l 24
SITE 6 QC1 23 ILE m 35 ASN m 45 LEU m 46
SITE 1 QC2 14 LEU P 50 HIS P 53 ALA P 57 PHE P 147
SITE 2 QC2 14 PHE P 163 HIS P 164 VAL P 167 ILE P 170
SITE 3 QC2 14 LEU P 174 CLA P 503 CLA P 509 CLA P 513
SITE 4 QC2 14 BCR P 515 LMG P 521
SITE 1 QC3 12 LEU P 50 VAL P 54 GLY P 128 TYR P 131
SITE 2 QC3 12 HIS P 132 PRO P 137 LEU P 140 TYR P 143
SITE 3 QC3 12 PHE P 147 ILE P 170 CLA P 512 BCR P 515
SITE 1 QC4 13 ALA P 55 LEU P 59 VAL P 116 LEU P 119
SITE 2 QC4 13 ILE P 120 SER P 122 ALA P 123 CLA P 511
SITE 3 QC4 13 BCR P 515 PHE c 32 BCR c 101 LEU l 9
SITE 4 QC4 13 VAL l 13
SITE 1 QC5 10 VAL P 116 SER P 121 VAL P 124 CLA P 512
SITE 2 QC5 10 CLA P 513 BCR P 514 TYR c 15 VAL l 54
SITE 3 QC5 10 GLY l 55 ASN l 58
SITE 1 QC6 12 ILE P 209 TYR P 212 LEU P 213 VAL P 227
SITE 2 QC6 12 ASP P 232 VAL P 233 ILE P 240 PHE P 264
SITE 3 QC6 12 CLA P 501 CLA P 505 CLA P 507 VAL a 20
SITE 1 QC7 16 LEU G 151 PHE G 155 ILE G 163 PRO P 217
SITE 2 QC7 16 PHE P 218 GLY P 219 GLY P 220 GLY P 222
SITE 3 QC7 16 VAL P 225 PHE P 284 CYS P 288 PHE P 292
SITE 4 QC7 16 ASN P 294 PRO P 307 PHE P 361 ARG P 362
SITE 1 QC8 20 PHE G 197 THR G 292 SQD G 410 LHG G 412
SITE 2 QC8 20 TYR P 82 GLU P 83 GLN P 84 GLY P 85
SITE 3 QC8 20 LEU P 404 SER P 406 ASN P 418 VAL P 420
SITE 4 QC8 20 TRP P 425 THR P 428 SER P 429 CLA P 504
SITE 5 QC8 20 DGD P 519 LMG P 520 TYR b 33 BCR b 102
SITE 1 QC9 23 LEU G 200 TRP G 278 PHE G 300 ASN G 301
SITE 2 QC9 23 PHE G 302 SER G 305 CLA G 404 SQD G 410
SITE 3 QC9 23 ASN P 405 ASN P 415 SER P 416 ASN P 418
SITE 4 QC9 23 CLA P 504 DGD P 518 LMG Q 406 PHE b 29
SITE 5 QC9 23 ALA b 32 TYR b 33 GLY b 37 SER b 38
SITE 6 QC9 23 SER b 39 BCR b 102 GLN i 60
SITE 1 RC1 8 HIS P 74 CLA P 504 DGD P 518 BCR b 102
SITE 2 RC1 8 ASP c 23 VAL c 27 VAL c 30 ILE m 25
SITE 1 RC2 8 ASP P 107 PHE P 109 VAL P 114 VAL P 117
SITE 2 RC2 8 HIS P 118 CLA P 503 CLA P 512 PHE l 59
SITE 1 RC3 9 ALA B 43 TRP B 75 SER B 76 TRP B 78
SITE 2 RC3 9 LEU B 98 LEU G 102 ASP G 103 ARG Q 304
SITE 3 RC3 9 GLY f 138
SITE 1 RC4 22 PHE G 206 CLA G 402 CLA G 403 CLA G 404
SITE 2 RC4 22 TRP Q 48 PRO Q 149 VAL Q 152 PHE Q 153
SITE 3 RC4 22 VAL Q 156 LEU Q 182 PHE Q 185 GLN Q 186
SITE 4 RC4 22 TRP Q 191 THR Q 192 HIS Q 197 GLY Q 200
SITE 5 RC4 22 VAL Q 201 VAL Q 204 LEU Q 279 SER Q 282
SITE 6 RC4 22 ALA Q 283 PHO Q 403
SITE 1 RC5 18 PHE G 206 ALA G 209 LEU G 210 MET G 214
SITE 2 RC5 18 CLA G 404 ALA Q 41 TRP Q 48 GLY Q 118
SITE 3 RC5 18 LEU Q 122 PHE Q 125 ASN Q 142 ALA Q 145
SITE 4 RC5 18 PHE Q 146 ALA Q 148 PHE Q 153 PRO Q 275
SITE 5 RC5 18 LEU Q 279 CLA Q 402
SITE 1 RC6 14 LEU Q 43 LEU Q 89 LEU Q 90 LEU Q 91
SITE 2 RC6 14 LEU Q 92 TRP Q 93 TRP Q 104 THR Q 112
SITE 3 RC6 14 PHE Q 113 HIS Q 117 LMT Q 410 GLY j 22
SITE 4 RC6 14 LEU j 23 GLY j 26
SITE 1 RC7 20 ILE G 53 ILE G 77 CLA G 403 LMG G 411
SITE 2 RC7 20 MET Q 199 HIS Q 214 THR Q 217 TRP Q 253
SITE 3 RC7 20 ALA Q 260 PHE Q 261 LEU Q 267 PHE Q 273
SITE 4 RC7 20 VAL Q 274 THR Q 277 LMG Q 407 LEU d 23
SITE 5 RC7 20 VAL d 26 LEU d 27 LEU d 29 PHE g 10
SITE 1 RC8 11 DGD P 519 TYR Q 67 GLY Q 70 PHE Q 73
SITE 2 RC8 11 ILE S 37 GLN S 41 BCR S 101 PHE b 28
SITE 3 RC8 11 GLY b 31 ALA b 32 GLY b 37
SITE 1 RC9 14 BCR B 618 PHE Q 257 ALA Q 260 PHE Q 261
SITE 2 RC9 14 SER Q 262 ASN Q 263 TRP Q 266 PL9 Q 405
SITE 3 RC9 14 THR d 15 TYR d 18 LEU d 19 PHE g 10
SITE 4 RC9 14 PHE g 17 ALA g 20
SITE 1 SC1 8 ALA N 228 ARG N 230 LEU N 474 LMT N 625
SITE 2 SC1 8 LYS Q 23 TRP Q 32 ARG Q 134 LEU Q 135
SITE 1 SC2 6 ASP Q 100 PHE Q 101 LMT Q 410 LEU R 42
SITE 2 SC2 6 ASP R 45 VAL R 46
SITE 1 SC3 8 LEU Q 92 TRP Q 93 GLY Q 99 CLA Q 404
SITE 2 SC3 8 DGD Q 409 ILE j 21 SER j 25 GLY j 26
SITE 1 SC4 9 HIS G 215 GLU G 244 TYR G 246 HIS G 272
SITE 2 SC4 9 FE2 G 414 HIS Q 214 TYR Q 244 LYS Q 264
SITE 3 SC4 9 HIS Q 268
SITE 1 SC5 14 ARG R 8 PHE R 10 ILE R 13 ARG R 18
SITE 2 SC5 14 TYR R 19 HIS R 23 THR R 26 LEU R 30
SITE 3 SC5 14 ILE S 15 ARG S 19 TRP S 20 HIS S 24
SITE 4 SC5 14 ALA S 27 ILE S 31
SITE 1 SC6 7 TYR G 262 LHG G 412 PHE Q 27 PRO R 9
SITE 2 SC6 7 PHE R 10 SER R 11 PL9 b 101
SITE 1 SC7 11 TYR Q 42 GLY Q 46 GLY Q 47 LEU Q 49
SITE 2 SC7 11 THR Q 50 PHE Q 101 LMG Q 406 PRO S 29
SITE 3 SC7 11 PHE S 33 VAL b 21 VAL b 25
SITE 1 SC8 8 ARG Q 24 ARG Q 26 GLU R 7 PHE S 16
SITE 2 SC8 8 THR S 17 VAL S 18 LEU j 32 THR j 33
SITE 1 SC9 9 CLA N 605 CLA N 613 MET W 35 LEU W 37
SITE 2 SC9 9 PHE W 38 PHE W 41 THR j 11 ILE j 12
SITE 3 SC9 9 LEU j 16
SITE 1 TC1 14 TYR N 193 PHE N 250 TYR N 258 TYR N 273
SITE 2 TC1 14 SER N 277 PHE N 463 CLA N 606 HIS Q 87
SITE 3 TC1 14 SER Q 165 TYR W 49 ASN W 50 VAL W 60
SITE 4 TC1 14 SER W 61 TRP W 62
SITE 1 TC2 7 LMT B 630 ILE G 38 LEU G 42 ALA G 43
SITE 2 TC2 7 TRP G 105 SQD G 401 PHE a 15
SITE 1 TC3 7 DGD B 628 LMT B 630 CLA G 406 MET a 1
SITE 2 TC3 7 THR a 3 LEU a 4 LMT a 103
SITE 1 TC4 4 THR a 3 ILE a 6 ILE a 10 LMG a 102
SITE 1 TC5 6 CLA G 404 PL9 G 407 SQD G 410 LMG R 102
SITE 2 TC5 6 VAL b 16 GLY b 20
SITE 1 TC6 6 LHG G 412 DGD P 518 DGD P 519 LMG P 520
SITE 2 TC6 6 PHE b 29 TYR b 33
SITE 1 TC7 16 BCR P 514 ALA b 14 THR b 15 GLY b 18
SITE 2 TC7 16 MET b 19 LEU c 21 LEU c 31 PHE c 32
SITE 3 TC7 16 PHE c 37 VAL c 38 ALA c 41 SER l 16
SITE 4 TC7 16 PHE l 17 ILE m 28 GLY m 29 GLY m 32
SITE 1 TC8 5 MET M 1 TYR N 40 LMG N 623 BCR T 101
SITE 2 TC8 5 GLN e 5
SITE 1 TC9 7 CLA B 614 SQD B 627 PRO L 9 VAL L 10
SITE 2 TC9 7 GLN M 32 GLU e 30 SER e 31
SITE 1 UC1 3 GLU f 81 GLU f 140 HIS f 257
SITE 1 UC2 13 ALA i 62 CYS i 63 HIS i 67 THR i 74
SITE 2 UC2 13 LEU i 78 ASP i 79 THR i 84 LEU i 85
SITE 3 UC2 13 TYR i 101 MET i 102 TYR i 108 HIS i 118
SITE 4 UC2 13 PRO i 119
CRYST1 130.783 227.764 308.630 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 0.007646 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004391 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003240 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
