HEADER PHOTOSYNTHESIS 12-OCT-15 5E7C
TITLE MACROMOLECULAR DIFFRACTIVE IMAGING USING IMPERFECT CRYSTALS - BRAGG
TITLE 2 DATA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOTOSYSTEM II PROTEIN D1 1;
COMPND 3 CHAIN: A, a;
COMPND 4 SYNONYM: PSII D1 PROTEIN 1,PHOTOSYSTEM II Q(B) PROTEIN 1;
COMPND 5 EC: 1.10.3.9;
COMPND 6 OTHER_DETAILS: PHOTOSYSTEM Q(B) PROTEIN 1;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PHOTOSYSTEM II CP47 REACTION CENTER PROTEIN;
COMPND 9 CHAIN: B, b;
COMPND 10 SYNONYM: PSII 47 KDA PROTEIN,PROTEIN CP-47;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: PHOTOSYSTEM II CP43 REACTION CENTER PROTEIN;
COMPND 13 CHAIN: C, c;
COMPND 14 SYNONYM: PSII 43 KDA PROTEIN,PROTEIN CP-43;
COMPND 15 MOL_ID: 4;
COMPND 16 MOLECULE: PHOTOSYSTEM II D2 PROTEIN;
COMPND 17 CHAIN: D, d;
COMPND 18 SYNONYM: PSII D2 PROTEIN,PHOTOSYSTEM II Q(A) PROTEIN;
COMPND 19 EC: 1.10.3.9;
COMPND 20 MOL_ID: 5;
COMPND 21 MOLECULE: CYTOCHROME B559 SUBUNIT ALPHA;
COMPND 22 CHAIN: E, e;
COMPND 23 SYNONYM: PSII REACTION CENTER SUBUNIT V;
COMPND 24 MOL_ID: 6;
COMPND 25 MOLECULE: CYTOCHROME B559 SUBUNIT BETA;
COMPND 26 CHAIN: F, f;
COMPND 27 SYNONYM: PSII REACTION CENTER SUBUNIT VI;
COMPND 28 MOL_ID: 7;
COMPND 29 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN H;
COMPND 30 CHAIN: H, h;
COMPND 31 SYNONYM: PSII-H;
COMPND 32 MOL_ID: 8;
COMPND 33 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN I;
COMPND 34 CHAIN: I, i;
COMPND 35 SYNONYM: PSII-I,PSII 4.4 KDA PROTEIN;
COMPND 36 MOL_ID: 9;
COMPND 37 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN J;
COMPND 38 CHAIN: J, j;
COMPND 39 SYNONYM: PSII-J;
COMPND 40 MOL_ID: 10;
COMPND 41 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN K;
COMPND 42 CHAIN: K, k;
COMPND 43 SYNONYM: PSII-K;
COMPND 44 MOL_ID: 11;
COMPND 45 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN L;
COMPND 46 CHAIN: L, l;
COMPND 47 SYNONYM: PSII-L;
COMPND 48 MOL_ID: 12;
COMPND 49 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN M;
COMPND 50 CHAIN: M, m;
COMPND 51 SYNONYM: PSII-M;
COMPND 52 MOL_ID: 13;
COMPND 53 MOLECULE: PHOTOSYSTEM II MANGANESE-STABILIZING POLYPEPTIDE;
COMPND 54 CHAIN: O, o;
COMPND 55 SYNONYM: MSP;
COMPND 56 MOL_ID: 14;
COMPND 57 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN T;
COMPND 58 CHAIN: T, t;
COMPND 59 SYNONYM: PSII-TC;
COMPND 60 MOL_ID: 15;
COMPND 61 MOLECULE: PHOTOSYSTEM II 12 KDA EXTRINSIC PROTEIN;
COMPND 62 CHAIN: U, u;
COMPND 63 SYNONYM: PS II COMPLEX 12 KDA EXTRINSIC PROTEIN,PSII-U;
COMPND 64 MOL_ID: 16;
COMPND 65 MOLECULE: CYTOCHROME C-550;
COMPND 66 CHAIN: V, v;
COMPND 67 SYNONYM: CYTOCHROME C-549,CYTOCHROME C550,LOW-POTENTIAL CYTOCHROME C;
COMPND 68 MOL_ID: 17;
COMPND 69 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN YCF12;
COMPND 70 CHAIN: Y, y;
COMPND 71 MOL_ID: 18;
COMPND 72 MOLECULE: PHOTOSYSTEM II REACTION CENTER X PROTEIN;
COMPND 73 CHAIN: X, x;
COMPND 74 MOL_ID: 19;
COMPND 75 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN Z;
COMPND 76 CHAIN: Z, z;
COMPND 77 SYNONYM: PSII-Z
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 3 ORGANISM_TAXID: 197221;
SOURCE 4 STRAIN: BP-1;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 7 ORGANISM_TAXID: 197221;
SOURCE 8 STRAIN: BP-1;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 11 ORGANISM_TAXID: 197221;
SOURCE 12 STRAIN: BP-1;
SOURCE 13 MOL_ID: 4;
SOURCE 14 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 15 ORGANISM_TAXID: 197221;
SOURCE 16 STRAIN: BP-1;
SOURCE 17 MOL_ID: 5;
SOURCE 18 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 19 ORGANISM_TAXID: 197221;
SOURCE 20 STRAIN: BP-1;
SOURCE 21 MOL_ID: 6;
SOURCE 22 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 23 ORGANISM_TAXID: 197221;
SOURCE 24 STRAIN: BP-1;
SOURCE 25 MOL_ID: 7;
SOURCE 26 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 27 ORGANISM_TAXID: 197221;
SOURCE 28 STRAIN: BP-1;
SOURCE 29 MOL_ID: 8;
SOURCE 30 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 31 ORGANISM_TAXID: 197221;
SOURCE 32 STRAIN: BP-1;
SOURCE 33 MOL_ID: 9;
SOURCE 34 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 35 ORGANISM_TAXID: 197221;
SOURCE 36 STRAIN: BP-1;
SOURCE 37 MOL_ID: 10;
SOURCE 38 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 39 ORGANISM_TAXID: 197221;
SOURCE 40 STRAIN: BP-1;
SOURCE 41 MOL_ID: 11;
SOURCE 42 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 43 ORGANISM_TAXID: 197221;
SOURCE 44 STRAIN: BP-1;
SOURCE 45 MOL_ID: 12;
SOURCE 46 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 47 ORGANISM_TAXID: 197221;
SOURCE 48 STRAIN: BP-1;
SOURCE 49 MOL_ID: 13;
SOURCE 50 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 51 ORGANISM_TAXID: 197221;
SOURCE 52 STRAIN: BP-1;
SOURCE 53 MOL_ID: 14;
SOURCE 54 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 55 ORGANISM_TAXID: 197221;
SOURCE 56 STRAIN: BP-1;
SOURCE 57 MOL_ID: 15;
SOURCE 58 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 59 ORGANISM_TAXID: 197221;
SOURCE 60 STRAIN: BP-1;
SOURCE 61 MOL_ID: 16;
SOURCE 62 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 63 ORGANISM_TAXID: 197221;
SOURCE 64 STRAIN: BP-1;
SOURCE 65 MOL_ID: 17;
SOURCE 66 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 67 ORGANISM_TAXID: 197221;
SOURCE 68 STRAIN: BP-1;
SOURCE 69 MOL_ID: 18;
SOURCE 70 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 71 ORGANISM_TAXID: 197221;
SOURCE 72 STRAIN: BP-1;
SOURCE 73 MOL_ID: 19;
SOURCE 74 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 75 ORGANISM_TAXID: 197221;
SOURCE 76 STRAIN: BP-1
KEYWDS PHOTOSYSTEM II, XFEL, SFX, PHOTOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR K.AYYER,O.YEFANOV,D.OBERTHUER,S.ROY-CHOWDHURY,L.GALLI,V.MARIANI,
AUTHOR 2 S.BASU,J.COE,C.E.CONRAD,R.FROMME,A.SCHAFFNER,K.DOERNER,D.JAMES,
AUTHOR 3 C.KUPITZ,M.METZ,G.NELSON,P.L.XAVIER,K.R.BEYERLEIN,M.SCHMIDT,
AUTHOR 4 I.SARROU,J.C.H.SPENCE,U.WEIERSTALL,T.A.WHITE,J.-H.YANG,Y.ZHAO,
AUTHOR 5 M.LIANG,A.AQUILA,M.S.HUNTER,J.S.ROBINSON,J.E.KOGLIN,S.BOUTET,
AUTHOR 6 P.FROMME,A.BARTY,H.N.CHAPMAN
REVDAT 9 13-NOV-24 5E7C 1 REMARK
REVDAT 8 10-JAN-24 5E7C 1 REMARK
REVDAT 7 13-DEC-23 5E7C 1 REMARK
REVDAT 6 30-MAR-22 5E7C 1 REMARK FORMUL LINK
REVDAT 5 14-NOV-18 5E7C 1 REMARK
REVDAT 4 24-JAN-18 5E7C 1 REMARK
REVDAT 3 02-MAR-16 5E7C 1 JRNL
REVDAT 2 17-FEB-16 5E7C 1 JRNL
REVDAT 1 10-FEB-16 5E7C 0
JRNL AUTH K.AYYER,O.M.YEFANOV,D.OBERTHUR,S.ROY-CHOWDHURY,L.GALLI,
JRNL AUTH 2 V.MARIANI,S.BASU,J.COE,C.E.CONRAD,R.FROMME,A.SCHAFFER,
JRNL AUTH 3 K.DORNER,D.JAMES,C.KUPITZ,M.METZ,G.NELSON,P.L.XAVIER,
JRNL AUTH 4 K.R.BEYERLEIN,M.SCHMIDT,I.SARROU,J.C.SPENCE,U.WEIERSTALL,
JRNL AUTH 5 T.A.WHITE,J.H.YANG,Y.ZHAO,M.LIANG,A.AQUILA,M.S.HUNTER,
JRNL AUTH 6 J.S.ROBINSON,J.E.KOGLIN,S.BOUTET,P.FROMME,A.BARTY,
JRNL AUTH 7 H.N.CHAPMAN
JRNL TITL MACROMOLECULAR DIFFRACTIVE IMAGING USING IMPERFECT CRYSTALS.
JRNL REF NATURE V. 530 202 2016
JRNL REFN ESSN 1476-4687
JRNL PMID 26863980
JRNL DOI 10.1038/NATURE16949
REMARK 2
REMARK 2 RESOLUTION. 4.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 4.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.93
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 55609
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.248
REMARK 3 R VALUE (WORKING SET) : 0.247
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.890
REMARK 3 FREE R VALUE TEST SET COUNT : 2718
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 29.9252 - 11.7725 1.00 2950 158 0.2845 0.3180
REMARK 3 2 11.7725 - 9.4406 1.00 2847 140 0.1927 0.2368
REMARK 3 3 9.4406 - 8.2761 1.00 2807 165 0.1801 0.1935
REMARK 3 4 8.2761 - 7.5326 1.00 2819 148 0.1955 0.2146
REMARK 3 5 7.5326 - 7.0001 1.00 2776 158 0.2230 0.2546
REMARK 3 6 7.0001 - 6.5921 1.00 2766 168 0.2305 0.2611
REMARK 3 7 6.5921 - 6.2651 1.00 2775 151 0.2374 0.2999
REMARK 3 8 6.2651 - 5.9946 1.00 2785 141 0.2615 0.3106
REMARK 3 9 5.9946 - 5.7656 1.00 2782 136 0.2576 0.2859
REMARK 3 10 5.7656 - 5.5679 1.00 2730 143 0.2644 0.2881
REMARK 3 11 5.5679 - 5.3948 1.00 2787 137 0.2740 0.3227
REMARK 3 12 5.3948 - 5.2415 1.00 2758 152 0.2822 0.2971
REMARK 3 13 5.2415 - 5.1042 1.00 2744 143 0.2862 0.3518
REMARK 3 14 5.1042 - 4.9802 1.00 2774 129 0.2967 0.3517
REMARK 3 15 4.9802 - 4.8675 1.00 2747 128 0.3045 0.3128
REMARK 3 16 4.8675 - 4.7643 1.00 2754 130 0.3092 0.2868
REMARK 3 17 4.7643 - 4.6694 1.00 2773 132 0.3242 0.3209
REMARK 3 18 4.6694 - 4.5816 1.00 2748 118 0.3281 0.3472
REMARK 3 19 4.5816 - 4.5000 1.00 2769 141 0.3483 0.3644
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.570
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.620
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.011 51858
REMARK 3 ANGLE : 1.482 71398
REMARK 3 CHIRALITY : 0.650 7190
REMARK 3 PLANARITY : 0.009 7760
REMARK 3 DIHEDRAL : 22.881 21404
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 5E7C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000214435.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-NOV-14
REMARK 200 TEMPERATURE (KELVIN) : 293.15
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : FREE ELECTRON LASER
REMARK 200 BEAMLINE : CXI
REMARK 200 X-RAY GENERATOR MODEL : SLAC LCLS BEAMLINE CXI
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.308
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : CS-PAD CXI-2
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL
REMARK 200 DATA SCALING SOFTWARE : CRYSTFEL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55609
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.500
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 1.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.0100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.62
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.490
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: MODIFIED VERSION OF 3ARC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM PIPES PH 7.0, 5 MM CACL2, 10 MM
REMARK 280 TOCOPHEROL, AND 10-17% PEG 2000, LIQUID DIFFUSION, TEMPERATURE
REMARK 280 283K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 66.62500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 153.54500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 113.13000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 153.54500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 66.62500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 113.13000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 38-MERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 38-MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, H, I, J, K,
REMARK 350 AND CHAINS: L, M, O, T, U, V, Y, X, Z,
REMARK 350 AND CHAINS: a, b, c, d, e, f, h, i, j, k,
REMARK 350 AND CHAINS: l, m, o, t, u, v, y, x, z
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 SER b 36 CA CB OG
REMARK 480 SER b 239 CA CB OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG1 THR c 24 OE1 GLU c 138 2.03
REMARK 500 OE2 GLU C 464 OG SER D 245 2.11
REMARK 500 OH TYR A 235 OE1 GLU L 11 2.13
REMARK 500 O PHE b 432 NZ LYS o 178 2.15
REMARK 500 OH TYR d 141 O4 LHG b 624 2.15
REMARK 500 O TYR e 56 N ALA v 1 2.15
REMARK 500 NE2 GLN C 28 O7 SQD A 611 2.16
REMARK 500 OE2 GLU c 464 OG SER d 245 2.16
REMARK 500 OH TYR D 141 O4 LHG B 622 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG z 35 CB - CG - CD ANGL. DEV. = 16.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 VAL A 30 -82.73 -93.46
REMARK 500 LEU A 159 -54.32 -124.70
REMARK 500 ILE A 259 -93.67 -101.34
REMARK 500 TYR B 117 56.60 -92.67
REMARK 500 PHE B 162 83.35 -150.16
REMARK 500 ASP B 313 46.00 -92.93
REMARK 500 PHE B 383 -78.20 -86.31
REMARK 500 ASP C 107 113.87 -160.89
REMARK 500 GLU C 221 -65.67 -124.82
REMARK 500 TRP C 223 -138.09 47.19
REMARK 500 SER C 416 -46.01 174.64
REMARK 500 SER C 416 -48.38 175.61
REMARK 500 ARG D 12 42.97 -156.37
REMARK 500 VAL D 30 -70.25 -107.18
REMARK 500 SER D 65 14.61 -147.67
REMARK 500 PRO D 140 44.37 -91.56
REMARK 500 ALA D 234 32.55 -77.74
REMARK 500 PRO D 309 1.98 -66.51
REMARK 500 ALA D 351 -52.17 71.61
REMARK 500 LYS H 63 32.45 -83.67
REMARK 500 LYS H 63 31.80 -83.15
REMARK 500 LEU H 65 -87.75 -149.97
REMARK 500 LYS I 33 -119.68 -110.38
REMARK 500 SER J 39 -4.01 72.98
REMARK 500 ASN O 58 -3.42 149.83
REMARK 500 ARG O 73 -163.03 69.62
REMARK 500 ASN U 29 -37.45 -139.10
REMARK 500 TYR U 103 -144.19 -113.67
REMARK 500 ASN V 49 81.74 -159.19
REMARK 500 ASP V 67 36.37 -88.99
REMARK 500 PHE V 101 79.83 -116.81
REMARK 500 ASP X 35 69.28 -115.99
REMARK 500 VAL a 30 -82.07 -93.24
REMARK 500 LEU a 159 -51.84 -128.51
REMARK 500 ILE a 259 -93.94 -100.97
REMARK 500 TYR b 117 54.38 -96.83
REMARK 500 PHE b 162 81.97 -154.65
REMARK 500 ASP b 313 48.06 -92.52
REMARK 500 PHE b 383 -79.08 -85.38
REMARK 500 GLU b 485 48.54 -103.22
REMARK 500 ASN c 25 6.27 56.00
REMARK 500 ASP c 107 114.75 -164.66
REMARK 500 GLU c 221 -69.18 -123.40
REMARK 500 TRP c 223 -140.86 50.72
REMARK 500 SER c 416 -48.20 170.48
REMARK 500 SER c 416 -53.16 172.59
REMARK 500 SER c 463 54.26 -142.35
REMARK 500 ARG d 12 40.75 -157.53
REMARK 500 VAL d 30 -67.22 -105.37
REMARK 500 SER d 65 11.71 -141.71
REMARK 500
REMARK 500 THIS ENTRY HAS 69 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 LMG A 612
REMARK 610 LMG B 621
REMARK 610 DGD C 516
REMARK 610 DGD C 517
REMARK 610 DGD C 518
REMARK 610 LMG C 519
REMARK 610 LMG C 520
REMARK 610 DGD D 406
REMARK 610 LHG E 101
REMARK 610 DGD H 102
REMARK 610 LMG J 101
REMARK 610 SQD X 101
REMARK 610 LMG Z 101
REMARK 610 LMG a 611
REMARK 610 LMG b 623
REMARK 610 DGD c 517
REMARK 610 DGD c 518
REMARK 610 DGD c 519
REMARK 610 LMG c 520
REMARK 610 LMG c 521
REMARK 610 DGD d 405
REMARK 610 LHG e 101
REMARK 610 DGD h 102
REMARK 610 LMG j 101
REMARK 610 SQD x 101
REMARK 610 LMG z 101
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX A 601 CA1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 170 OD1
REMARK 620 2 OEX A 601 O1 155.0
REMARK 620 3 OEX A 601 O2 90.8 75.2
REMARK 620 4 OEX A 601 O5 120.6 76.8 76.7
REMARK 620 5 ASP A 170 OD2 42.0 153.1 87.6 79.2
REMARK 620 6 ALA A 344 O 80.2 77.5 82.7 150.4 121.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX A 601 MN4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 170 OD2
REMARK 620 2 OEX A 601 O5 95.0
REMARK 620 3 OEX A 601 O4 87.7 92.5
REMARK 620 4 GLU A 333 OE2 166.0 77.3 104.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX A 601 MN1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 189 OE2
REMARK 620 2 OEX A 601 O1 92.6
REMARK 620 3 OEX A 601 O5 81.8 82.4
REMARK 620 4 OEX A 601 O3 162.1 92.0 81.6
REMARK 620 5 HIS A 332 NE2 92.3 173.3 102.7 84.7
REMARK 620 6 ASP A 342 OD2 106.7 87.8 167.4 90.8 86.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 A 613 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 215 NE2
REMARK 620 2 HIS A 272 NE2 95.1
REMARK 620 3 BCT A 604 O1 168.5 80.1
REMARK 620 4 BCT A 604 O2 115.2 92.8 55.1
REMARK 620 5 HIS D 214 NE2 96.0 83.4 93.8 148.8
REMARK 620 6 HIS D 268 NE2 87.4 168.5 99.4 96.3 85.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX A 601 MN3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 333 OE1
REMARK 620 2 OEX A 601 O2 172.6
REMARK 620 3 OEX A 601 O3 80.7 93.2
REMARK 620 4 OEX A 601 O4 102.8 83.2 175.9
REMARK 620 5 OEX A 601 O5 82.7 92.4 81.5 96.6
REMARK 620 6 GLU C 354 OE2 83.9 99.3 81.8 100.8 160.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX A 601 MN2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 342 OD1
REMARK 620 2 OEX A 601 O1 88.3
REMARK 620 3 OEX A 601 O2 173.4 89.0
REMARK 620 4 OEX A 601 O3 98.6 78.9 86.8
REMARK 620 5 ALA A 344 OXT 80.7 89.8 93.2 168.7
REMARK 620 6 GLU C 354 OE1 89.5 157.8 95.2 79.6 111.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C 511 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C 39 OD1
REMARK 620 2 CLA C 511 NA 107.9
REMARK 620 3 CLA C 511 NB 87.5 93.2
REMARK 620 4 CLA C 511 NC 79.6 172.2 89.3
REMARK 620 5 CLA C 511 ND 85.5 90.9 172.7 87.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM E 102 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 23 NE2
REMARK 620 2 HEM E 102 NA 101.5
REMARK 620 3 HEM E 102 NB 114.1 90.2
REMARK 620 4 HEM E 102 NC 82.7 174.0 92.0
REMARK 620 5 HEM E 102 ND 61.8 90.4 175.8 87.9
REMARK 620 6 HIS F 24 NE2 140.6 82.0 105.1 92.1 79.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG J 102 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY J 31 O
REMARK 620 2 ALA J 34 O 68.1
REMARK 620 3 LEU J 36 O 93.2 110.8
REMARK 620 4 LMG J 101 O4 60.5 127.2 84.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA O 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR O 138 O
REMARK 620 2 ASN O 200 OD1 113.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM V 202 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS V 41 NE2
REMARK 620 2 HEM V 202 NA 100.3
REMARK 620 3 HEM V 202 NB 88.2 93.0
REMARK 620 4 HEM V 202 NC 72.8 173.1 87.6
REMARK 620 5 HEM V 202 ND 79.9 89.5 168.1 88.5
REMARK 620 6 HIS V 92 NE2 156.6 102.1 97.3 84.7 93.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 601 CA1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP a 170 OD1
REMARK 620 2 OEX a 601 O1 154.0
REMARK 620 3 OEX a 601 O2 91.7 75.2
REMARK 620 4 OEX a 601 O5 122.6 76.8 76.7
REMARK 620 5 ASP a 170 OD2 42.5 153.6 86.7 80.4
REMARK 620 6 ALA a 344 O 78.2 78.7 86.8 153.3 120.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 601 MN4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP a 170 OD2
REMARK 620 2 OEX a 601 O5 93.7
REMARK 620 3 OEX a 601 O4 85.6 92.5
REMARK 620 4 GLU a 333 OE2 163.3 78.7 109.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 601 MN1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU a 189 OE2
REMARK 620 2 OEX a 601 O1 98.1
REMARK 620 3 OEX a 601 O5 89.6 82.4
REMARK 620 4 OEX a 601 O3 165.7 92.0 81.6
REMARK 620 5 HIS a 332 NE2 78.5 173.5 103.0 92.3
REMARK 620 6 ASP a 342 OD2 96.8 91.1 171.4 93.1 83.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 a 615 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS a 215 NE2
REMARK 620 2 HIS a 272 NE2 86.6
REMARK 620 3 BCT a 603 O1 161.8 94.0
REMARK 620 4 BCT a 603 O2 107.4 95.3 54.4
REMARK 620 5 HIS d 214 NE2 105.3 87.3 92.8 147.2
REMARK 620 6 HIS d 268 NE2 95.0 176.5 83.5 81.2 95.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 601 MN3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU a 333 OE1
REMARK 620 2 OEX a 601 O2 171.9
REMARK 620 3 OEX a 601 O3 85.6 93.2
REMARK 620 4 OEX a 601 O4 97.7 83.2 175.9
REMARK 620 5 OEX a 601 O5 79.6 92.4 81.5 96.6
REMARK 620 6 GLU c 354 OE2 85.5 101.9 76.4 106.2 154.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 601 MN2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP a 342 OD1
REMARK 620 2 OEX a 601 O1 85.9
REMARK 620 3 OEX a 601 O2 174.1 89.0
REMARK 620 4 OEX a 601 O3 95.1 78.9 86.8
REMARK 620 5 ALA a 344 OXT 85.4 85.0 91.3 163.8
REMARK 620 6 GLU c 354 OE1 85.5 152.3 100.4 75.7 120.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA c 512 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN c 39 OD1
REMARK 620 2 CLA c 512 NA 103.2
REMARK 620 3 CLA c 512 NB 89.0 92.7
REMARK 620 4 CLA c 512 NC 84.7 171.8 89.6
REMARK 620 5 CLA c 512 ND 83.9 91.4 172.4 87.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM e 102 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS e 23 NE2
REMARK 620 2 HEM e 102 NA 109.6
REMARK 620 3 HEM e 102 NB 112.3 88.0
REMARK 620 4 HEM e 102 NC 79.8 170.1 91.0
REMARK 620 5 HEM e 102 ND 67.3 91.9 179.5 89.2
REMARK 620 6 HIS f 24 NE2 159.6 73.4 87.8 96.7 92.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA f 102 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG f 45 O
REMARK 620 2 ARG f 45 OXT 42.7
REMARK 620 3 GLU v 23 OE1 150.4 146.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG j 102 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY j 31 O
REMARK 620 2 ALA j 34 O 85.8
REMARK 620 3 LEU j 36 O 102.9 110.7
REMARK 620 4 LMG j 101 O4 69.4 154.6 81.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA o 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR o 138 O
REMARK 620 2 ASN o 200 OD1 159.6
REMARK 620 3 VAL o 201 O 84.4 75.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM v 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS v 41 NE2
REMARK 620 2 HEM v 201 NA 93.2
REMARK 620 3 HEM v 201 NB 79.8 90.4
REMARK 620 4 HEM v 201 NC 81.1 174.4 88.8
REMARK 620 5 HEM v 201 ND 90.3 92.1 169.9 87.7
REMARK 620 6 HIS v 92 NE2 163.3 103.1 96.4 82.5 92.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OEX A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD A 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE2 A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG B 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD B 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 D 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD D 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG D 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG D 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG E 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM E 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR F 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR H 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD H 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG J 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG J 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR K 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG L 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA O 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR T 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM V 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD X 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG Z 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OEX a 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT a 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO a 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR a 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 a 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD a 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG a 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD a 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG a 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE2 a 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD b 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD b 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA b 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG b 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG b 624
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL c 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 522
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO d 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 d 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD d 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG d 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG e 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM e 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR f 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA f 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR h 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD h 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG j 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG j 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR k 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG l 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA o 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR t 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM v 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD x 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG z 101
DBREF 5E7C A 11 344 UNP P0A444 PSBA1_THEEB 11 344
DBREF 5E7C B 2 505 UNP Q8DIQ1 PSBB_THEEB 2 505
DBREF 5E7C C 23 473 UNP Q8DIF8 PSBC_THEEB 11 461
DBREF 5E7C D 11 352 UNP Q8CM25 PSBD_THEEB 11 352
DBREF 5E7C E 4 84 UNP Q8DIP0 PSBE_THEEB 4 84
DBREF 5E7C F 12 45 UNP Q8DIN9 PSBF_THEEB 12 45
DBREF 5E7C H 2 66 UNP Q8DJ43 PSBH_THEEB 2 66
DBREF 5E7C I 1 38 UNP Q8DJZ6 PSBI_THEEB 1 38
DBREF 5E7C J 3 40 UNP P59087 PSBJ_THEEB 3 40
DBREF 5E7C K 10 46 UNP Q9F1K9 PSBK_THEEB 10 46
DBREF 5E7C L 1 37 UNP Q8DIN8 PSBL_THEEB 1 37
DBREF 5E7C M 1 34 UNP Q8DHA7 PSBM_THEEB 1 34
DBREF 5E7C O 4 246 UNP P0A431 PSBO_THEEB 30 272
DBREF 5E7C T 1 30 UNP Q8DIQ0 PSBT_THEEB 1 30
DBREF 5E7C U 8 104 UNP Q9F1L5 PSBU_THEEB 38 134
DBREF 5E7C V 1 137 UNP P0A386 CY550_THEEB 27 163
DBREF 5E7C Y 18 46 UNP Q8DJI1 YCF12_THEEB 18 46
DBREF 5E7C X 2 40 UNP Q9F1R6 PSBX_THEEB 2 40
DBREF 5E7C Z 1 62 UNP Q8DHJ2 PSBZ_THEEB 1 62
DBREF 5E7C a 11 344 UNP P0A444 PSBA1_THEEB 11 344
DBREF 5E7C b 2 505 UNP Q8DIQ1 PSBB_THEEB 2 505
DBREF 5E7C c 23 473 UNP Q8DIF8 PSBC_THEEB 11 461
DBREF 5E7C d 11 352 UNP Q8CM25 PSBD_THEEB 11 352
DBREF 5E7C e 4 84 UNP Q8DIP0 PSBE_THEEB 4 84
DBREF 5E7C f 12 45 UNP Q8DIN9 PSBF_THEEB 12 45
DBREF 5E7C h 2 66 UNP Q8DJ43 PSBH_THEEB 2 66
DBREF 5E7C i 1 38 UNP Q8DJZ6 PSBI_THEEB 1 38
DBREF 5E7C j 3 40 UNP P59087 PSBJ_THEEB 3 40
DBREF 5E7C k 10 46 UNP Q9F1K9 PSBK_THEEB 10 46
DBREF 5E7C l 1 37 UNP Q8DIN8 PSBL_THEEB 1 37
DBREF 5E7C m 1 34 UNP Q8DHA7 PSBM_THEEB 1 34
DBREF 5E7C o 4 246 UNP P0A431 PSBO_THEEB 30 272
DBREF 5E7C t 1 30 UNP Q8DIQ0 PSBT_THEEB 1 30
DBREF 5E7C u 8 104 UNP Q9F1L5 PSBU_THEEB 38 134
DBREF 5E7C v 1 137 UNP P0A386 CY550_THEEB 27 163
DBREF 5E7C y 18 46 UNP Q8DJI1 YCF12_THEEB 18 46
DBREF 5E7C x 2 40 UNP Q9F1R6 PSBX_THEEB 2 40
DBREF 5E7C z 1 62 UNP Q8DHJ2 PSBZ_THEEB 1 62
SEQADV 5E7C ALA A 286 UNP P0A444 THR 286 CONFLICT
SEQADV 5E7C ALA a 286 UNP P0A444 THR 286 CONFLICT
SEQRES 1 A 334 ALA ASN LEU TRP GLU ARG PHE CYS ASN TRP VAL THR SER
SEQRES 2 A 334 THR ASP ASN ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE
SEQRES 3 A 334 MET ILE PRO THR LEU LEU ALA ALA THR ILE CYS PHE VAL
SEQRES 4 A 334 ILE ALA PHE ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY
SEQRES 5 A 334 ILE ARG GLU PRO VAL SER GLY SER LEU LEU TYR GLY ASN
SEQRES 6 A 334 ASN ILE ILE THR GLY ALA VAL VAL PRO SER SER ASN ALA
SEQRES 7 A 334 ILE GLY LEU HIS PHE TYR PRO ILE TRP GLU ALA ALA SER
SEQRES 8 A 334 LEU ASP GLU TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU
SEQRES 9 A 334 ILE ILE PHE HIS PHE LEU LEU GLY ALA SER CYS TYR MET
SEQRES 10 A 334 GLY ARG GLN TRP GLU LEU SER TYR ARG LEU GLY MET ARG
SEQRES 11 A 334 PRO TRP ILE CYS VAL ALA TYR SER ALA PRO LEU ALA SER
SEQRES 12 A 334 ALA PHE ALA VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY
SEQRES 13 A 334 SER PHE SER ASP GLY MET PRO LEU GLY ILE SER GLY THR
SEQRES 14 A 334 PHE ASN PHE MET ILE VAL PHE GLN ALA GLU HIS ASN ILE
SEQRES 15 A 334 LEU MET HIS PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL
SEQRES 16 A 334 PHE GLY GLY ALA LEU PHE CYS ALA MET HIS GLY SER LEU
SEQRES 17 A 334 VAL THR SER SER LEU ILE ARG GLU THR THR GLU THR GLU
SEQRES 18 A 334 SER ALA ASN TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU
SEQRES 19 A 334 THR TYR ASN ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG
SEQRES 20 A 334 LEU ILE PHE GLN TYR ALA SER PHE ASN ASN SER ARG SER
SEQRES 21 A 334 LEU HIS PHE PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL
SEQRES 22 A 334 TRP PHE ALA ALA LEU GLY ILE SER THR MET ALA PHE ASN
SEQRES 23 A 334 LEU ASN GLY PHE ASN PHE ASN HIS SER VAL ILE ASP ALA
SEQRES 24 A 334 LYS GLY ASN VAL ILE ASN THR TRP ALA ASP ILE ILE ASN
SEQRES 25 A 334 ARG ALA ASN LEU GLY MET GLU VAL MET HIS GLU ARG ASN
SEQRES 26 A 334 ALA HIS ASN PHE PRO LEU ASP LEU ALA
SEQRES 1 B 504 GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE ASN
SEQRES 2 B 504 ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS THR
SEQRES 3 B 504 ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU TYR
SEQRES 4 B 504 GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU ASN
SEQRES 5 B 504 PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE MET
SEQRES 6 B 504 ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP SER
SEQRES 7 B 504 ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP SER
SEQRES 8 B 504 PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER GLY
SEQRES 9 B 504 LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR TRP
SEQRES 10 B 504 ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU PRO
SEQRES 11 B 504 ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU PHE
SEQRES 12 B 504 LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE HIS
SEQRES 13 B 504 LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER ASP
SEQRES 14 B 504 PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA PRO
SEQRES 15 B 504 GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO GLY
SEQRES 16 B 504 GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL GLY
SEQRES 17 B 504 ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO PRO
SEQRES 18 B 504 GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE GLU
SEQRES 19 B 504 THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE ALA
SEQRES 20 B 504 ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER ALA
SEQRES 21 B 504 THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR GLN
SEQRES 22 B 504 TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG ARG
SEQRES 23 B 504 VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU GLU
SEQRES 24 B 504 ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR ASP
SEQRES 25 B 504 TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE ARG
SEQRES 26 B 504 THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN ALA
SEQRES 27 B 504 TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY GLU
SEQRES 28 B 504 GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU SER
SEQRES 29 B 504 PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL LYS
SEQRES 30 B 504 ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR SER
SEQRES 31 B 504 PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY GLY
SEQRES 32 B 504 GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR VAL
SEQRES 33 B 504 LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE PHE
SEQRES 34 B 504 GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE PHE
SEQRES 35 B 504 ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS ALA
SEQRES 36 B 504 VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP HIS
SEQRES 37 B 504 GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY ILE
SEQRES 38 B 504 ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY PHE
SEQRES 39 B 504 TYR GLN LYS VAL GLY ASP VAL THR THR ARG
SEQRES 1 C 451 ALA THR ASN ARG ASP GLN GLU SER SER GLY PHE ALA TRP
SEQRES 2 C 451 TRP ALA GLY ASN ALA ARG LEU ILE ASN LEU SER GLY LYS
SEQRES 3 C 451 LEU LEU GLY ALA HIS VAL ALA HIS ALA GLY LEU ILE VAL
SEQRES 4 C 451 PHE TRP ALA GLY ALA MET THR LEU PHE GLU LEU ALA HIS
SEQRES 5 C 451 PHE ILE PRO GLU LYS PRO MET TYR GLU GLN GLY LEU ILE
SEQRES 6 C 451 LEU ILE PRO HIS ILE ALA THR LEU GLY TRP GLY VAL GLY
SEQRES 7 C 451 PRO GLY GLY GLU VAL VAL ASP THR PHE PRO PHE PHE VAL
SEQRES 8 C 451 VAL GLY VAL VAL HIS LEU ILE SER SER ALA VAL LEU GLY
SEQRES 9 C 451 PHE GLY GLY VAL TYR HIS ALA ILE ARG GLY PRO GLU THR
SEQRES 10 C 451 LEU GLU GLU TYR SER SER PHE PHE GLY TYR ASP TRP LYS
SEQRES 11 C 451 ASP LYS ASN LYS MET THR THR ILE LEU GLY PHE HIS LEU
SEQRES 12 C 451 ILE VAL LEU GLY ILE GLY ALA LEU LEU LEU VAL ALA LYS
SEQRES 13 C 451 ALA MET PHE PHE GLY GLY LEU TYR ASP THR TRP ALA PRO
SEQRES 14 C 451 GLY GLY GLY ASP VAL ARG VAL ILE THR ASN PRO THR LEU
SEQRES 15 C 451 ASP PRO ARG VAL ILE PHE GLY TYR LEU LEU LYS SER PRO
SEQRES 16 C 451 PHE GLY GLY GLU GLY TRP ILE VAL SER VAL ASN ASN LEU
SEQRES 17 C 451 GLU ASP VAL VAL GLY GLY HIS ILE TRP ILE GLY LEU ILE
SEQRES 18 C 451 CYS ILE ALA GLY GLY ILE TRP HIS ILE LEU THR THR PRO
SEQRES 19 C 451 PHE GLY TRP ALA ARG ARG ALA PHE ILE TRP SER GLY GLU
SEQRES 20 C 451 ALA TYR LEU SER TYR SER LEU GLY ALA LEU SER MET MET
SEQRES 21 C 451 GLY PHE ILE ALA THR CYS PHE VAL TRP PHE ASN ASN THR
SEQRES 22 C 451 VAL TYR PRO SER GLU PHE TYR GLY PRO THR GLY PRO GLU
SEQRES 23 C 451 ALA SER GLN ALA GLN ALA MET THR PHE LEU ILE ARG ASP
SEQRES 24 C 451 GLN LYS LEU GLY ALA ASN VAL GLY SER ALA GLN GLY PRO
SEQRES 25 C 451 THR GLY LEU GLY LYS TYR LEU MET ARG SER PRO THR GLY
SEQRES 26 C 451 GLU ILE ILE PHE GLY GLY GLU THR MET ARG PHE TRP ASP
SEQRES 27 C 451 PHE ARG GLY PRO TRP LEU GLU PRO LEU ARG GLY PRO ASN
SEQRES 28 C 451 GLY LEU ASP LEU ASN LYS ILE LYS ASN ASP ILE GLN PRO
SEQRES 29 C 451 TRP GLN GLU ARG ARG ALA ALA GLU TYR MET THR HIS ALA
SEQRES 30 C 451 PRO LEU GLY SER LEU ASN SER VAL GLY GLY VAL ALA THR
SEQRES 31 C 451 GLU ILE ASN SER VAL ASN PHE VAL SER PRO ARG SER TRP
SEQRES 32 C 451 LEU ALA THR SER HIS PHE VAL LEU ALA PHE PHE PHE LEU
SEQRES 33 C 451 VAL GLY HIS LEU TRP HIS ALA GLY ARG ALA ARG ALA ALA
SEQRES 34 C 451 ALA ALA GLY PHE GLU LYS GLY ILE ASP ARG GLU SER GLU
SEQRES 35 C 451 PRO VAL LEU SER MET PRO SER LEU ASP
SEQRES 1 D 342 GLU ARG GLY TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS
SEQRES 2 D 342 ARG ASP ARG PHE VAL PHE VAL GLY TRP SER GLY ILE LEU
SEQRES 3 D 342 LEU PHE PRO CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU
SEQRES 4 D 342 THR GLY THR THR PHE VAL THR SER TRP TYR THR HIS GLY
SEQRES 5 D 342 LEU ALA SER SER TYR LEU GLU GLY CYS ASN PHE LEU THR
SEQRES 6 D 342 VAL ALA VAL SER THR PRO ALA ASN SER MET GLY HIS SER
SEQRES 7 D 342 LEU LEU LEU LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE
SEQRES 8 D 342 THR ARG TRP CYS GLN LEU GLY GLY LEU TRP THR PHE ILE
SEQRES 9 D 342 ALA LEU HIS GLY ALA PHE GLY LEU ILE GLY PHE MET LEU
SEQRES 10 D 342 ARG GLN PHE GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO
SEQRES 11 D 342 TYR ASN ALA ILE ALA PHE SER ALA PRO ILE ALA VAL PHE
SEQRES 12 D 342 VAL SER VAL PHE LEU ILE TYR PRO LEU GLY GLN SER SER
SEQRES 13 D 342 TRP PHE PHE ALA PRO SER PHE GLY VAL ALA ALA ILE PHE
SEQRES 14 D 342 ARG PHE LEU LEU PHE PHE GLN GLY PHE HIS ASN TRP THR
SEQRES 15 D 342 LEU ASN PRO PHE HIS MET MET GLY VAL ALA GLY VAL LEU
SEQRES 16 D 342 GLY GLY ALA LEU LEU CYS ALA ILE HIS GLY ALA THR VAL
SEQRES 17 D 342 GLU ASN THR LEU PHE GLN ASP GLY GLU GLY ALA SER THR
SEQRES 18 D 342 PHE ARG ALA PHE ASN PRO THR GLN ALA GLU GLU THR TYR
SEQRES 19 D 342 SER MET VAL THR ALA ASN ARG PHE TRP SER GLN ILE PHE
SEQRES 20 D 342 GLY ILE ALA PHE SER ASN LYS ARG TRP LEU HIS PHE PHE
SEQRES 21 D 342 MET LEU PHE VAL PRO VAL THR GLY LEU TRP MET SER ALA
SEQRES 22 D 342 ILE GLY VAL VAL GLY LEU ALA LEU ASN LEU ARG SER TYR
SEQRES 23 D 342 ASP PHE ILE SER GLN GLU ILE ARG ALA ALA GLU ASP PRO
SEQRES 24 D 342 GLU PHE GLU THR PHE TYR THR LYS ASN LEU LEU LEU ASN
SEQRES 25 D 342 GLU GLY ILE ARG ALA TRP MET ALA PRO GLN ASP GLN PRO
SEQRES 26 D 342 HIS GLU ASN PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG
SEQRES 27 D 342 GLY ASN ALA LEU
SEQRES 1 E 81 THR THR GLY GLU ARG PRO PHE SER ASP ILE ILE THR SER
SEQRES 2 E 81 VAL ARG TYR TRP VAL ILE HIS SER ILE THR ILE PRO ALA
SEQRES 3 E 81 LEU PHE ILE ALA GLY TRP LEU PHE VAL SER THR GLY LEU
SEQRES 4 E 81 ALA TYR ASP VAL PHE GLY THR PRO ARG PRO ASP SER TYR
SEQRES 5 E 81 TYR ALA GLN GLU GLN ARG SER ILE PRO LEU VAL THR ASP
SEQRES 6 E 81 ARG PHE GLU ALA LYS GLN GLN VAL GLU THR PHE LEU GLU
SEQRES 7 E 81 GLN LEU LYS
SEQRES 1 F 34 SER TYR PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS
SEQRES 2 F 34 THR LEU ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE
SEQRES 3 F 34 ALA ALA MET GLN PHE ILE GLN ARG
SEQRES 1 H 65 ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO LEU
SEQRES 2 H 65 ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY THR
SEQRES 3 H 65 THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU VAL
SEQRES 4 H 65 PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR LEU
SEQRES 5 H 65 ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU GLY
SEQRES 1 I 38 MET GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR
SEQRES 2 I 38 PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY
SEQRES 3 I 38 ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP LEU GLU
SEQRES 1 J 38 SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL ALA THR
SEQRES 2 J 38 VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY LEU PHE
SEQRES 3 J 38 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 34 MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU
SEQRES 2 M 34 PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR
SEQRES 3 M 34 VAL GLN THR GLU SER GLN GLN LYS
SEQRES 1 O 243 THR LEU THR TYR ASP ASP ILE VAL GLY THR GLY LEU ALA
SEQRES 2 O 243 ASN LYS CYS PRO THR LEU ASP ASP THR ALA ARG GLY ALA
SEQRES 3 O 243 TYR PRO ILE ASP SER SER GLN THR TYR ARG ILE ALA ARG
SEQRES 4 O 243 LEU CYS LEU GLN PRO THR THR PHE LEU VAL LYS GLU GLU
SEQRES 5 O 243 PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE VAL PRO THR
SEQRES 6 O 243 LYS LEU VAL THR ARG GLU THR THR SER LEU ASP GLN ILE
SEQRES 7 O 243 GLN GLY GLU LEU LYS VAL ASN SER ASP GLY SER LEU THR
SEQRES 8 O 243 PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN PRO VAL THR
SEQRES 9 O 243 VAL GLN MET ALA GLY GLY GLU ARG ILE PRO LEU LEU PHE
SEQRES 10 O 243 THR VAL LYS ASN LEU VAL ALA SER THR GLN PRO ASN VAL
SEQRES 11 O 243 THR SER ILE THR THR SER THR ASP PHE LYS GLY GLU PHE
SEQRES 12 O 243 ASN VAL PRO SER TYR ARG THR ALA ASN PHE LEU ASP PRO
SEQRES 13 O 243 LYS GLY ARG GLY LEU ALA SER GLY TYR ASP SER ALA ILE
SEQRES 14 O 243 ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU ALA ARG ALA
SEQRES 15 O 243 ASN VAL LYS ARG PHE SER LEU THR LYS GLY GLN ILE SER
SEQRES 16 O 243 LEU ASN VAL ALA LYS VAL ASP GLY ARG THR GLY GLU ILE
SEQRES 17 O 243 ALA GLY THR PHE GLU SER GLU GLN LEU SER ASP ASP ASP
SEQRES 18 O 243 MET GLY ALA HIS GLU PRO HIS GLU VAL LYS ILE GLN GLY
SEQRES 19 O 243 VAL PHE TYR ALA SER ILE GLU PRO ALA
SEQRES 1 T 30 MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE
SEQRES 2 T 30 ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO
SEQRES 3 T 30 PRO ARG ILE THR
SEQRES 1 U 97 GLU LEU VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA
SEQRES 2 U 97 TYR GLY GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA
SEQRES 3 U 97 ALA PHE ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA
SEQRES 4 U 97 LYS LEU ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU
SEQRES 5 U 97 ASP VAL LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS
SEQRES 6 U 97 GLN ILE LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR
SEQRES 7 U 97 GLU VAL GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR
SEQRES 8 U 97 ASN ASN GLY LEU TYR LYS
SEQRES 1 V 137 ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN
SEQRES 2 V 137 SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR
SEQRES 3 V 137 LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER
SEQRES 4 V 137 CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU
SEQRES 5 V 137 ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO
SEQRES 6 V 137 ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN
SEQRES 7 V 137 PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL
SEQRES 8 V 137 HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET
SEQRES 9 V 137 ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY
SEQRES 10 V 137 HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP
SEQRES 11 V 137 GLY GLY GLY LYS VAL TYR TYR
SEQRES 1 Y 29 VAL ILE ALA GLN LEU THR MET ILE ALA MET ILE GLY ILE
SEQRES 2 Y 29 ALA GLY PRO MET ILE ILE PHE LEU LEU ALA VAL ARG ARG
SEQRES 3 Y 29 GLY ASN LEU
SEQRES 1 X 39 THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY LEU
SEQRES 2 X 39 LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA VAL
SEQRES 3 X 39 LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG SER
SEQRES 1 Z 62 MET THR ILE LEU PHE GLN LEU ALA LEU ALA ALA LEU VAL
SEQRES 2 Z 62 ILE LEU SER PHE VAL MET VAL ILE GLY VAL PRO VAL ALA
SEQRES 3 Z 62 TYR ALA SER PRO GLN ASP TRP ASP ARG SER LYS GLN LEU
SEQRES 4 Z 62 ILE PHE LEU GLY SER GLY LEU TRP ILE ALA LEU VAL LEU
SEQRES 5 Z 62 VAL VAL GLY VAL LEU ASN PHE PHE VAL VAL
SEQRES 1 a 334 ALA ASN LEU TRP GLU ARG PHE CYS ASN TRP VAL THR SER
SEQRES 2 a 334 THR ASP ASN ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE
SEQRES 3 a 334 MET ILE PRO THR LEU LEU ALA ALA THR ILE CYS PHE VAL
SEQRES 4 a 334 ILE ALA PHE ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY
SEQRES 5 a 334 ILE ARG GLU PRO VAL SER GLY SER LEU LEU TYR GLY ASN
SEQRES 6 a 334 ASN ILE ILE THR GLY ALA VAL VAL PRO SER SER ASN ALA
SEQRES 7 a 334 ILE GLY LEU HIS PHE TYR PRO ILE TRP GLU ALA ALA SER
SEQRES 8 a 334 LEU ASP GLU TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU
SEQRES 9 a 334 ILE ILE PHE HIS PHE LEU LEU GLY ALA SER CYS TYR MET
SEQRES 10 a 334 GLY ARG GLN TRP GLU LEU SER TYR ARG LEU GLY MET ARG
SEQRES 11 a 334 PRO TRP ILE CYS VAL ALA TYR SER ALA PRO LEU ALA SER
SEQRES 12 a 334 ALA PHE ALA VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY
SEQRES 13 a 334 SER PHE SER ASP GLY MET PRO LEU GLY ILE SER GLY THR
SEQRES 14 a 334 PHE ASN PHE MET ILE VAL PHE GLN ALA GLU HIS ASN ILE
SEQRES 15 a 334 LEU MET HIS PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL
SEQRES 16 a 334 PHE GLY GLY ALA LEU PHE CYS ALA MET HIS GLY SER LEU
SEQRES 17 a 334 VAL THR SER SER LEU ILE ARG GLU THR THR GLU THR GLU
SEQRES 18 a 334 SER ALA ASN TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU
SEQRES 19 a 334 THR TYR ASN ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG
SEQRES 20 a 334 LEU ILE PHE GLN TYR ALA SER PHE ASN ASN SER ARG SER
SEQRES 21 a 334 LEU HIS PHE PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL
SEQRES 22 a 334 TRP PHE ALA ALA LEU GLY ILE SER THR MET ALA PHE ASN
SEQRES 23 a 334 LEU ASN GLY PHE ASN PHE ASN HIS SER VAL ILE ASP ALA
SEQRES 24 a 334 LYS GLY ASN VAL ILE ASN THR TRP ALA ASP ILE ILE ASN
SEQRES 25 a 334 ARG ALA ASN LEU GLY MET GLU VAL MET HIS GLU ARG ASN
SEQRES 26 a 334 ALA HIS ASN PHE PRO LEU ASP LEU ALA
SEQRES 1 b 504 GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE ASN
SEQRES 2 b 504 ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS THR
SEQRES 3 b 504 ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU TYR
SEQRES 4 b 504 GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU ASN
SEQRES 5 b 504 PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE MET
SEQRES 6 b 504 ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP SER
SEQRES 7 b 504 ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP SER
SEQRES 8 b 504 PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER GLY
SEQRES 9 b 504 LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR TRP
SEQRES 10 b 504 ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU PRO
SEQRES 11 b 504 ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU PHE
SEQRES 12 b 504 LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE HIS
SEQRES 13 b 504 LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER ASP
SEQRES 14 b 504 PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA PRO
SEQRES 15 b 504 GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO GLY
SEQRES 16 b 504 GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL GLY
SEQRES 17 b 504 ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO PRO
SEQRES 18 b 504 GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE GLU
SEQRES 19 b 504 THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE ALA
SEQRES 20 b 504 ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER ALA
SEQRES 21 b 504 THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR GLN
SEQRES 22 b 504 TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG ARG
SEQRES 23 b 504 VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU GLU
SEQRES 24 b 504 ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR ASP
SEQRES 25 b 504 TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE ARG
SEQRES 26 b 504 THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN ALA
SEQRES 27 b 504 TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY GLU
SEQRES 28 b 504 GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU SER
SEQRES 29 b 504 PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL LYS
SEQRES 30 b 504 ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR SER
SEQRES 31 b 504 PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY GLY
SEQRES 32 b 504 GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR VAL
SEQRES 33 b 504 LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE PHE
SEQRES 34 b 504 GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE PHE
SEQRES 35 b 504 ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS ALA
SEQRES 36 b 504 VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP HIS
SEQRES 37 b 504 GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY ILE
SEQRES 38 b 504 ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY PHE
SEQRES 39 b 504 TYR GLN LYS VAL GLY ASP VAL THR THR ARG
SEQRES 1 c 451 ALA THR ASN ARG ASP GLN GLU SER SER GLY PHE ALA TRP
SEQRES 2 c 451 TRP ALA GLY ASN ALA ARG LEU ILE ASN LEU SER GLY LYS
SEQRES 3 c 451 LEU LEU GLY ALA HIS VAL ALA HIS ALA GLY LEU ILE VAL
SEQRES 4 c 451 PHE TRP ALA GLY ALA MET THR LEU PHE GLU LEU ALA HIS
SEQRES 5 c 451 PHE ILE PRO GLU LYS PRO MET TYR GLU GLN GLY LEU ILE
SEQRES 6 c 451 LEU ILE PRO HIS ILE ALA THR LEU GLY TRP GLY VAL GLY
SEQRES 7 c 451 PRO GLY GLY GLU VAL VAL ASP THR PHE PRO PHE PHE VAL
SEQRES 8 c 451 VAL GLY VAL VAL HIS LEU ILE SER SER ALA VAL LEU GLY
SEQRES 9 c 451 PHE GLY GLY VAL TYR HIS ALA ILE ARG GLY PRO GLU THR
SEQRES 10 c 451 LEU GLU GLU TYR SER SER PHE PHE GLY TYR ASP TRP LYS
SEQRES 11 c 451 ASP LYS ASN LYS MET THR THR ILE LEU GLY PHE HIS LEU
SEQRES 12 c 451 ILE VAL LEU GLY ILE GLY ALA LEU LEU LEU VAL ALA LYS
SEQRES 13 c 451 ALA MET PHE PHE GLY GLY LEU TYR ASP THR TRP ALA PRO
SEQRES 14 c 451 GLY GLY GLY ASP VAL ARG VAL ILE THR ASN PRO THR LEU
SEQRES 15 c 451 ASP PRO ARG VAL ILE PHE GLY TYR LEU LEU LYS SER PRO
SEQRES 16 c 451 PHE GLY GLY GLU GLY TRP ILE VAL SER VAL ASN ASN LEU
SEQRES 17 c 451 GLU ASP VAL VAL GLY GLY HIS ILE TRP ILE GLY LEU ILE
SEQRES 18 c 451 CYS ILE ALA GLY GLY ILE TRP HIS ILE LEU THR THR PRO
SEQRES 19 c 451 PHE GLY TRP ALA ARG ARG ALA PHE ILE TRP SER GLY GLU
SEQRES 20 c 451 ALA TYR LEU SER TYR SER LEU GLY ALA LEU SER MET MET
SEQRES 21 c 451 GLY PHE ILE ALA THR CYS PHE VAL TRP PHE ASN ASN THR
SEQRES 22 c 451 VAL TYR PRO SER GLU PHE TYR GLY PRO THR GLY PRO GLU
SEQRES 23 c 451 ALA SER GLN ALA GLN ALA MET THR PHE LEU ILE ARG ASP
SEQRES 24 c 451 GLN LYS LEU GLY ALA ASN VAL GLY SER ALA GLN GLY PRO
SEQRES 25 c 451 THR GLY LEU GLY LYS TYR LEU MET ARG SER PRO THR GLY
SEQRES 26 c 451 GLU ILE ILE PHE GLY GLY GLU THR MET ARG PHE TRP ASP
SEQRES 27 c 451 PHE ARG GLY PRO TRP LEU GLU PRO LEU ARG GLY PRO ASN
SEQRES 28 c 451 GLY LEU ASP LEU ASN LYS ILE LYS ASN ASP ILE GLN PRO
SEQRES 29 c 451 TRP GLN GLU ARG ARG ALA ALA GLU TYR MET THR HIS ALA
SEQRES 30 c 451 PRO LEU GLY SER LEU ASN SER VAL GLY GLY VAL ALA THR
SEQRES 31 c 451 GLU ILE ASN SER VAL ASN PHE VAL SER PRO ARG SER TRP
SEQRES 32 c 451 LEU ALA THR SER HIS PHE VAL LEU ALA PHE PHE PHE LEU
SEQRES 33 c 451 VAL GLY HIS LEU TRP HIS ALA GLY ARG ALA ARG ALA ALA
SEQRES 34 c 451 ALA ALA GLY PHE GLU LYS GLY ILE ASP ARG GLU SER GLU
SEQRES 35 c 451 PRO VAL LEU SER MET PRO SER LEU ASP
SEQRES 1 d 342 GLU ARG GLY TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS
SEQRES 2 d 342 ARG ASP ARG PHE VAL PHE VAL GLY TRP SER GLY ILE LEU
SEQRES 3 d 342 LEU PHE PRO CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU
SEQRES 4 d 342 THR GLY THR THR PHE VAL THR SER TRP TYR THR HIS GLY
SEQRES 5 d 342 LEU ALA SER SER TYR LEU GLU GLY CYS ASN PHE LEU THR
SEQRES 6 d 342 VAL ALA VAL SER THR PRO ALA ASN SER MET GLY HIS SER
SEQRES 7 d 342 LEU LEU LEU LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE
SEQRES 8 d 342 THR ARG TRP CYS GLN LEU GLY GLY LEU TRP THR PHE ILE
SEQRES 9 d 342 ALA LEU HIS GLY ALA PHE GLY LEU ILE GLY PHE MET LEU
SEQRES 10 d 342 ARG GLN PHE GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO
SEQRES 11 d 342 TYR ASN ALA ILE ALA PHE SER ALA PRO ILE ALA VAL PHE
SEQRES 12 d 342 VAL SER VAL PHE LEU ILE TYR PRO LEU GLY GLN SER SER
SEQRES 13 d 342 TRP PHE PHE ALA PRO SER PHE GLY VAL ALA ALA ILE PHE
SEQRES 14 d 342 ARG PHE LEU LEU PHE PHE GLN GLY PHE HIS ASN TRP THR
SEQRES 15 d 342 LEU ASN PRO PHE HIS MET MET GLY VAL ALA GLY VAL LEU
SEQRES 16 d 342 GLY GLY ALA LEU LEU CYS ALA ILE HIS GLY ALA THR VAL
SEQRES 17 d 342 GLU ASN THR LEU PHE GLN ASP GLY GLU GLY ALA SER THR
SEQRES 18 d 342 PHE ARG ALA PHE ASN PRO THR GLN ALA GLU GLU THR TYR
SEQRES 19 d 342 SER MET VAL THR ALA ASN ARG PHE TRP SER GLN ILE PHE
SEQRES 20 d 342 GLY ILE ALA PHE SER ASN LYS ARG TRP LEU HIS PHE PHE
SEQRES 21 d 342 MET LEU PHE VAL PRO VAL THR GLY LEU TRP MET SER ALA
SEQRES 22 d 342 ILE GLY VAL VAL GLY LEU ALA LEU ASN LEU ARG SER TYR
SEQRES 23 d 342 ASP PHE ILE SER GLN GLU ILE ARG ALA ALA GLU ASP PRO
SEQRES 24 d 342 GLU PHE GLU THR PHE TYR THR LYS ASN LEU LEU LEU ASN
SEQRES 25 d 342 GLU GLY ILE ARG ALA TRP MET ALA PRO GLN ASP GLN PRO
SEQRES 26 d 342 HIS GLU ASN PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG
SEQRES 27 d 342 GLY ASN ALA LEU
SEQRES 1 e 81 THR THR GLY GLU ARG PRO PHE SER ASP ILE ILE THR SER
SEQRES 2 e 81 VAL ARG TYR TRP VAL ILE HIS SER ILE THR ILE PRO ALA
SEQRES 3 e 81 LEU PHE ILE ALA GLY TRP LEU PHE VAL SER THR GLY LEU
SEQRES 4 e 81 ALA TYR ASP VAL PHE GLY THR PRO ARG PRO ASP SER TYR
SEQRES 5 e 81 TYR ALA GLN GLU GLN ARG SER ILE PRO LEU VAL THR ASP
SEQRES 6 e 81 ARG PHE GLU ALA LYS GLN GLN VAL GLU THR PHE LEU GLU
SEQRES 7 e 81 GLN LEU LYS
SEQRES 1 f 34 SER TYR PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS
SEQRES 2 f 34 THR LEU ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE
SEQRES 3 f 34 ALA ALA MET GLN PHE ILE GLN ARG
SEQRES 1 h 65 ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO LEU
SEQRES 2 h 65 ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY THR
SEQRES 3 h 65 THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU VAL
SEQRES 4 h 65 PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR LEU
SEQRES 5 h 65 ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU GLY
SEQRES 1 i 38 MET GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR
SEQRES 2 i 38 PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY
SEQRES 3 i 38 ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP LEU GLU
SEQRES 1 j 38 SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL ALA THR
SEQRES 2 j 38 VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY LEU PHE
SEQRES 3 j 38 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 34 MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU
SEQRES 2 m 34 PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR
SEQRES 3 m 34 VAL GLN THR GLU SER GLN GLN LYS
SEQRES 1 o 243 THR LEU THR TYR ASP ASP ILE VAL GLY THR GLY LEU ALA
SEQRES 2 o 243 ASN LYS CYS PRO THR LEU ASP ASP THR ALA ARG GLY ALA
SEQRES 3 o 243 TYR PRO ILE ASP SER SER GLN THR TYR ARG ILE ALA ARG
SEQRES 4 o 243 LEU CYS LEU GLN PRO THR THR PHE LEU VAL LYS GLU GLU
SEQRES 5 o 243 PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE VAL PRO THR
SEQRES 6 o 243 LYS LEU VAL THR ARG GLU THR THR SER LEU ASP GLN ILE
SEQRES 7 o 243 GLN GLY GLU LEU LYS VAL ASN SER ASP GLY SER LEU THR
SEQRES 8 o 243 PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN PRO VAL THR
SEQRES 9 o 243 VAL GLN MET ALA GLY GLY GLU ARG ILE PRO LEU LEU PHE
SEQRES 10 o 243 THR VAL LYS ASN LEU VAL ALA SER THR GLN PRO ASN VAL
SEQRES 11 o 243 THR SER ILE THR THR SER THR ASP PHE LYS GLY GLU PHE
SEQRES 12 o 243 ASN VAL PRO SER TYR ARG THR ALA ASN PHE LEU ASP PRO
SEQRES 13 o 243 LYS GLY ARG GLY LEU ALA SER GLY TYR ASP SER ALA ILE
SEQRES 14 o 243 ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU ALA ARG ALA
SEQRES 15 o 243 ASN VAL LYS ARG PHE SER LEU THR LYS GLY GLN ILE SER
SEQRES 16 o 243 LEU ASN VAL ALA LYS VAL ASP GLY ARG THR GLY GLU ILE
SEQRES 17 o 243 ALA GLY THR PHE GLU SER GLU GLN LEU SER ASP ASP ASP
SEQRES 18 o 243 MET GLY ALA HIS GLU PRO HIS GLU VAL LYS ILE GLN GLY
SEQRES 19 o 243 VAL PHE TYR ALA SER ILE GLU PRO ALA
SEQRES 1 t 30 MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE
SEQRES 2 t 30 ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO
SEQRES 3 t 30 PRO ARG ILE THR
SEQRES 1 u 97 GLU LEU VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA
SEQRES 2 u 97 TYR GLY GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA
SEQRES 3 u 97 ALA PHE ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA
SEQRES 4 u 97 LYS LEU ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU
SEQRES 5 u 97 ASP VAL LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS
SEQRES 6 u 97 GLN ILE LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR
SEQRES 7 u 97 GLU VAL GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR
SEQRES 8 u 97 ASN ASN GLY LEU TYR LYS
SEQRES 1 v 137 ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN
SEQRES 2 v 137 SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR
SEQRES 3 v 137 LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER
SEQRES 4 v 137 CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU
SEQRES 5 v 137 ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO
SEQRES 6 v 137 ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN
SEQRES 7 v 137 PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL
SEQRES 8 v 137 HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET
SEQRES 9 v 137 ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY
SEQRES 10 v 137 HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP
SEQRES 11 v 137 GLY GLY GLY LYS VAL TYR TYR
SEQRES 1 y 29 VAL ILE ALA GLN LEU THR MET ILE ALA MET ILE GLY ILE
SEQRES 2 y 29 ALA GLY PRO MET ILE ILE PHE LEU LEU ALA VAL ARG ARG
SEQRES 3 y 29 GLY ASN LEU
SEQRES 1 x 39 THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY LEU
SEQRES 2 x 39 LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA VAL
SEQRES 3 x 39 LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG SER
SEQRES 1 z 62 MET THR ILE LEU PHE GLN LEU ALA LEU ALA ALA LEU VAL
SEQRES 2 z 62 ILE LEU SER PHE VAL MET VAL ILE GLY VAL PRO VAL ALA
SEQRES 3 z 62 TYR ALA SER PRO GLN ASP TRP ASP ARG SER LYS GLN LEU
SEQRES 4 z 62 ILE PHE LEU GLY SER GLY LEU TRP ILE ALA LEU VAL LEU
SEQRES 5 z 62 VAL VAL GLY VAL LEU ASN PHE PHE VAL VAL
HET OEX A 601 10
HET CL A 602 1
HET CL A 603 1
HET BCT A 604 4
HET CLA A 605 65
HET CLA A 606 65
HET PHO A 607 64
HET CLA A 608 65
HET BCR A 609 40
HET PL9 A 610 55
HET SQD A 611 54
HET LMG A 612 51
HET FE2 A 613 1
HET CA B 601 1
HET CLA B 602 65
HET CLA B 603 65
HET CLA B 604 65
HET CLA B 605 65
HET CLA B 606 65
HET CLA B 607 130
HET CLA B 608 65
HET CLA B 609 65
HET CLA B 610 65
HET CLA B 611 65
HET CLA B 612 65
HET CLA B 613 65
HET CLA B 614 65
HET CLA B 615 65
HET CLA B 616 65
HET CLA B 617 65
HET BCR B 618 40
HET BCR B 619 40
HET BCR B 620 40
HET LMG B 621 51
HET LHG B 622 49
HET SQD B 623 54
HET CLA C 501 65
HET CLA C 502 65
HET CLA C 503 65
HET CLA C 504 65
HET CLA C 505 65
HET CLA C 506 65
HET CLA C 507 65
HET CLA C 508 65
HET CLA C 509 65
HET CLA C 510 65
HET CLA C 511 65
HET CLA C 512 65
HET CLA C 513 65
HET BCR C 514 40
HET BCR C 515 40
HET DGD C 516 62
HET DGD C 517 62
HET DGD C 518 62
HET LMG C 519 51
HET LMG C 520 51
HET BCR C 521 40
HET PHO D 401 64
HET CLA D 402 65
HET CLA D 403 65
HET CLA D 404 65
HET PL9 D 405 55
HET DGD D 406 62
HET LHG D 407 49
HET LHG D 408 49
HET LHG E 101 42
HET HEM E 102 43
HET BCR F 101 40
HET CA F 102 1
HET BCR H 101 40
HET DGD H 102 62
HET LMG J 101 51
HET MG J 102 1
HET BCR K 101 40
HET LHG L 101 49
HET CA O 301 1
HET BCR T 101 40
HET CL V 201 1
HET HEM V 202 43
HET SQD X 101 43
HET LMG Z 101 37
HET OEX a 601 10
HET CL a 602 1
HET BCT a 603 4
HET CLA a 604 65
HET CLA a 605 65
HET PHO a 606 64
HET CLA a 607 65
HET BCR a 608 40
HET PL9 a 609 55
HET SQD a 610 54
HET LMG a 611 51
HET SQD a 612 54
HET CLA a 613 65
HET LHG a 614 49
HET FE2 a 615 1
HET SQD b 601 54
HET SQD b 602 54
HET CA b 603 1
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 609 130
HET CLA b 610 65
HET CLA b 611 65
HET CLA b 612 65
HET CLA b 613 65
HET CLA b 614 65
HET CLA b 615 65
HET CLA b 616 65
HET CLA b 617 65
HET CLA b 618 65
HET CLA b 619 65
HET BCR b 620 40
HET BCR b 621 40
HET BCR b 622 40
HET LMG b 623 51
HET LHG b 624 49
HET CL c 501 1
HET CLA c 502 65
HET CLA c 503 65
HET CLA c 504 65
HET CLA c 505 65
HET CLA c 506 65
HET CLA c 507 65
HET CLA c 508 65
HET CLA c 509 65
HET CLA c 510 65
HET CLA c 511 65
HET CLA c 512 65
HET CLA c 513 65
HET CLA c 514 65
HET BCR c 515 40
HET BCR c 516 40
HET DGD c 517 62
HET DGD c 518 62
HET DGD c 519 62
HET LMG c 520 51
HET LMG c 521 51
HET BCR c 522 40
HET PHO d 401 64
HET CLA d 402 65
HET CLA d 403 65
HET PL9 d 404 55
HET DGD d 405 62
HET LHG d 406 49
HET LHG e 101 42
HET HEM e 102 43
HET BCR f 101 40
HET CA f 102 1
HET BCR h 101 40
HET DGD h 102 62
HET LMG j 101 51
HET MG j 102 1
HET BCR k 101 40
HET LHG l 101 49
HET CA o 301 1
HET BCR t 101 40
HET CL u 201 1
HET HEM v 201 43
HET SQD x 101 43
HET LMG z 101 37
HETNAM OEX CA-MN4-O5 CLUSTER
HETNAM CL CHLORIDE ION
HETNAM BCT BICARBONATE ION
HETNAM CLA CHLOROPHYLL A
HETNAM PHO PHEOPHYTIN A
HETNAM BCR BETA-CAROTENE
HETNAM PL9 2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,
HETNAM 2 PL9 6,10,14,18,22,26,30,34-HEXATRIACONTANONAENYL-2,5-
HETNAM 3 PL9 CYCLOHEXADIENE-1,4-DIONE-2,3-DIMETHYL-5-SOLANESYL-1,4-
HETNAM 4 PL9 BENZOQUINONE
HETNAM SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-
HETNAM 2 SQD GLUCOPYRANOSYL]-SN-GLYCEROL
HETNAM LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE
HETNAM FE2 FE (II) ION
HETNAM CA CALCIUM ION
HETNAM LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE
HETNAM DGD DIGALACTOSYL DIACYL GLYCEROL (DGDG)
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM MG MAGNESIUM ION
HETSYN PL9 PLASTOQUINONE 9
HETSYN SQD SULFOQUINOVOSYLDIACYLGLYCEROL
HETSYN HEM HEME
FORMUL 39 OEX 2(CA MN4 O5)
FORMUL 40 CL 6(CL 1-)
FORMUL 42 BCT 2(C H O3 1-)
FORMUL 43 CLA 70(C55 H72 MG N4 O5)
FORMUL 45 PHO 4(C55 H74 N4 O5)
FORMUL 47 BCR 22(C40 H56)
FORMUL 48 PL9 4(C53 H80 O2)
FORMUL 49 SQD 8(C41 H78 O12 S)
FORMUL 50 LMG 12(C45 H86 O10)
FORMUL 51 FE2 2(FE 2+)
FORMUL 52 CA 6(CA 2+)
FORMUL 73 LHG 10(C38 H75 O10 P)
FORMUL 90 DGD 10(C51 H96 O15)
FORMUL 05 HEM 4(C34 H32 FE N4 O4)
FORMUL 11 MG 2(MG 2+)
HELIX 1 AA1 ASN A 12 THR A 22 1 11
HELIX 2 AA2 VAL A 30 ALA A 55 1 26
HELIX 3 AA3 SER A 70 GLY A 74 5 5
HELIX 4 AA4 PRO A 95 ALA A 99 5 5
HELIX 5 AA5 SER A 101 ASN A 108 1 8
HELIX 6 AA6 GLY A 109 LEU A 137 1 29
HELIX 7 AA7 TRP A 142 LEU A 159 1 18
HELIX 8 AA8 LEU A 159 GLY A 166 1 8
HELIX 9 AA9 SER A 167 GLY A 171 5 5
HELIX 10 AB1 ILE A 176 ASN A 191 1 16
HELIX 11 AB2 ILE A 192 MET A 194 5 3
HELIX 12 AB3 HIS A 195 SER A 222 1 28
HELIX 13 AB4 SER A 232 TYR A 237 5 6
HELIX 14 AB5 ASN A 247 ILE A 259 1 13
HELIX 15 AB6 PHE A 260 SER A 264 5 5
HELIX 16 AB7 ASN A 267 ALA A 294 1 28
HELIX 17 AB8 THR A 316 HIS A 332 1 17
HELIX 18 AB9 TYR B 6 ILE B 13 5 8
HELIX 19 AC1 ASP B 15 PHE B 45 1 31
HELIX 20 AC2 PRO B 54 GLN B 58 5 5
HELIX 21 AC3 VAL B 62 LEU B 69 1 8
HELIX 22 AC4 SER B 92 TYR B 117 1 26
HELIX 23 AC5 LEU B 120 ARG B 124 5 5
HELIX 24 AC6 ASP B 134 PHE B 156 1 23
HELIX 25 AC7 GLY B 186 ASN B 191 5 6
HELIX 26 AC8 ASN B 194 VAL B 219 1 26
HELIX 27 AC9 PRO B 222 LEU B 229 1 8
HELIX 28 AD1 ASN B 233 GLY B 259 1 27
HELIX 29 AD2 PRO B 264 GLY B 269 1 6
HELIX 30 AD3 THR B 271 SER B 277 1 7
HELIX 31 AD4 SER B 278 SER B 294 1 17
HELIX 32 AD5 THR B 297 ALA B 304 1 8
HELIX 33 AD6 PRO B 306 ASP B 313 1 8
HELIX 34 AD7 TYR B 314 GLY B 322 5 9
HELIX 35 AD8 PRO B 329 GLY B 333 5 5
HELIX 36 AD9 SER B 391 GLY B 396 1 6
HELIX 37 AE1 ASP B 413 ILE B 425 1 13
HELIX 38 AE2 SER B 446 PHE B 475 1 30
HELIX 39 AE3 ARG B 476 PHE B 479 5 4
HELIX 40 AE4 SER B 487 VAL B 491 5 5
HELIX 41 AE5 ASP B 501 ARG B 505 5 5
HELIX 42 AE6 ASP C 27 GLY C 32 1 6
HELIX 43 AE7 ALA C 34 ILE C 43 5 10
HELIX 44 AE8 LEU C 45 PHE C 75 1 31
HELIX 45 AE9 PRO C 80 GLN C 84 5 5
HELIX 46 AF1 ILE C 87 LEU C 95 1 9
HELIX 47 AF2 GLY C 100 GLU C 104 5 5
HELIX 48 AF3 THR C 108 ARG C 135 1 28
HELIX 49 AF4 ASP C 153 PHE C 182 1 30
HELIX 50 AF5 ASP C 205 LEU C 214 1 10
HELIX 51 AF6 GLY C 222 VAL C 227 5 6
HELIX 52 AF7 ASN C 229 THR C 254 1 26
HELIX 53 AF8 PHE C 257 PHE C 264 1 8
HELIX 54 AF9 SER C 267 ASN C 293 1 27
HELIX 55 AG1 PRO C 298 GLY C 303 1 6
HELIX 56 AG2 THR C 305 LEU C 324 1 20
HELIX 57 AG3 GLY C 353 TRP C 359 5 7
HELIX 58 AG4 LEU C 366 PRO C 368 5 3
HELIX 59 AG5 ASP C 376 ASP C 383 1 8
HELIX 60 AG6 GLN C 385 THR C 397 1 13
HELIX 61 AG7 SER C 421 GLY C 454 1 34
HELIX 62 AG8 ASP C 460 MET C 469 5 10
HELIX 63 AG9 GLY D 13 LYS D 23 1 11
HELIX 64 AH1 VAL D 30 VAL D 55 1 26
HELIX 65 AH2 SER D 66 GLY D 70 5 5
HELIX 66 AH3 ALA D 82 GLY D 86 5 5
HELIX 67 AH4 ASP D 100 LEU D 107 1 8
HELIX 68 AH5 GLY D 108 GLY D 137 1 30
HELIX 69 AH6 PRO D 140 LEU D 158 1 19
HELIX 70 AH7 LEU D 158 GLN D 164 1 7
HELIX 71 AH8 SER D 166 ALA D 170 5 5
HELIX 72 AH9 VAL D 175 ASN D 190 1 16
HELIX 73 AI1 TRP D 191 LEU D 193 5 3
HELIX 74 AI2 ASN D 194 ASN D 220 1 27
HELIX 75 AI3 THR D 231 PHE D 235 5 5
HELIX 76 AI4 SER D 245 PHE D 257 1 13
HELIX 77 AI5 ASN D 263 ALA D 290 1 28
HELIX 78 AI6 PHE D 298 ASP D 308 1 11
HELIX 79 AI7 THR D 313 GLN D 334 1 22
HELIX 80 AI8 PRO D 335 ASN D 338 5 4
HELIX 81 AI9 PRO D 342 LEU D 346 5 5
HELIX 82 AJ1 PRO E 9 THR E 15 1 7
HELIX 83 AJ2 SER E 16 THR E 40 1 25
HELIX 84 AJ3 GLY E 41 GLY E 48 1 8
HELIX 85 AJ4 GLU E 71 GLN E 82 1 12
HELIX 86 AJ5 THR F 17 GLN F 41 1 25
HELIX 87 AJ6 THR H 5 ARG H 12 1 8
HELIX 88 AJ7 PRO H 13 SER H 16 5 4
HELIX 89 AJ8 THR H 27 ASN H 50 1 24
HELIX 90 AJ9 SER H 61 LEU H 65 5 5
HELIX 91 AK1 GLU I 2 SER I 25 1 24
HELIX 92 AK2 GLY I 26 ARG I 30 5 5
HELIX 93 AK3 PRO J 9 TYR J 33 1 25
HELIX 94 AK4 PRO K 12 ILE K 17 5 6
HELIX 95 AK5 PHE K 18 LEU K 25 1 8
HELIX 96 AK6 VAL K 27 VAL K 43 1 17
HELIX 97 AK7 ASN L 13 ASN L 37 1 25
HELIX 98 AK8 LEU M 6 SER M 31 1 26
HELIX 99 AK9 THR O 6 VAL O 11 1 6
HELIX 100 AL1 GLY O 14 LYS O 18 5 5
HELIX 101 AL2 GLU O 179 GLU O 181 5 3
HELIX 102 AL3 LEU O 182 VAL O 187 1 6
HELIX 103 AL4 GLU T 2 PHE T 23 1 22
HELIX 104 AL5 ASN U 11 GLY U 18 1 8
HELIX 105 AL6 THR U 19 GLU U 23 5 5
HELIX 106 AL7 ASN U 31 TYR U 38 5 8
HELIX 107 AL8 PRO U 43 ALA U 53 1 11
HELIX 108 AL9 SER U 57 ILE U 64 5 8
HELIX 109 AM1 THR U 68 LEU U 79 1 12
HELIX 110 AM2 GLU U 88 GLU U 93 1 6
HELIX 111 AM3 GLY U 94 ASP U 96 5 3
HELIX 112 AM4 THR V 22 CYS V 37 1 16
HELIX 113 AM5 CYS V 37 VAL V 42 1 6
HELIX 114 AM6 GLY V 43 ILE V 45 5 3
HELIX 115 AM7 ARG V 55 ALA V 62 1 8
HELIX 116 AM8 ASN V 68 ASN V 78 1 11
HELIX 117 AM9 PHE V 101 ARG V 105 5 5
HELIX 118 AN1 THR V 108 GLY V 127 1 20
HELIX 119 AN2 ASP V 128 TRP V 130 5 3
HELIX 120 AN3 GLY V 133 TYR V 137 5 5
HELIX 121 AN4 ILE Y 19 ARG Y 42 1 24
HELIX 122 AN5 THR X 4 ASP X 35 1 32
HELIX 123 AN6 THR Z 2 SER Z 29 1 28
HELIX 124 AN7 ASP Z 32 ASN Z 58 1 27
HELIX 125 AN8 PHE Z 59 VAL Z 61 5 3
HELIX 126 AN9 ASN a 12 THR a 22 1 11
HELIX 127 AO1 VAL a 30 ALA a 55 1 26
HELIX 128 AO2 PRO a 95 ALA a 99 5 5
HELIX 129 AO3 SER a 101 ASN a 108 1 8
HELIX 130 AO4 GLY a 109 LEU a 137 1 29
HELIX 131 AO5 TRP a 142 LEU a 159 1 18
HELIX 132 AO6 LEU a 159 GLY a 166 1 8
HELIX 133 AO7 SER a 167 GLY a 171 5 5
HELIX 134 AO8 ILE a 176 ASN a 191 1 16
HELIX 135 AO9 ILE a 192 MET a 194 5 3
HELIX 136 AP1 HIS a 195 SER a 222 1 28
HELIX 137 AP2 SER a 232 TYR a 237 5 6
HELIX 138 AP3 ASN a 247 ILE a 259 1 13
HELIX 139 AP4 PHE a 260 SER a 264 5 5
HELIX 140 AP5 ASN a 267 ALA a 294 1 28
HELIX 141 AP6 THR a 316 HIS a 332 1 17
HELIX 142 AP7 TYR b 6 ILE b 13 5 8
HELIX 143 AP8 ASP b 15 PHE b 45 1 31
HELIX 144 AP9 PRO b 54 GLN b 58 5 5
HELIX 145 AQ1 VAL b 62 LEU b 69 1 8
HELIX 146 AQ2 SER b 92 TYR b 117 1 26
HELIX 147 AQ3 LEU b 120 ARG b 124 5 5
HELIX 148 AQ4 ASP b 134 PHE b 156 1 23
HELIX 149 AQ5 GLY b 186 ASN b 191 5 6
HELIX 150 AQ6 ASN b 194 VAL b 219 1 26
HELIX 151 AQ7 PRO b 222 LEU b 229 1 8
HELIX 152 AQ8 ASN b 233 GLY b 259 1 27
HELIX 153 AQ9 PRO b 264 GLY b 269 1 6
HELIX 154 AR1 THR b 271 SER b 277 1 7
HELIX 155 AR2 SER b 278 SER b 294 1 17
HELIX 156 AR3 THR b 297 ALA b 304 1 8
HELIX 157 AR4 PRO b 306 ASP b 313 1 8
HELIX 158 AR5 TYR b 314 GLY b 322 5 9
HELIX 159 AR6 PRO b 329 GLY b 333 5 5
HELIX 160 AR7 ASP b 413 ILE b 425 1 13
HELIX 161 AR8 SER b 446 PHE b 475 1 30
HELIX 162 AR9 ARG b 476 PHE b 479 5 4
HELIX 163 AS1 SER b 487 GLU b 492 1 6
HELIX 164 AS2 ASP b 501 ARG b 505 5 5
HELIX 165 AS3 ASP c 27 GLY c 32 1 6
HELIX 166 AS4 ALA c 34 ILE c 43 5 10
HELIX 167 AS5 LEU c 45 PHE c 75 1 31
HELIX 168 AS6 PRO c 80 GLN c 84 5 5
HELIX 169 AS7 ILE c 87 LEU c 95 1 9
HELIX 170 AS8 GLY c 100 GLU c 104 5 5
HELIX 171 AS9 THR c 108 ARG c 135 1 28
HELIX 172 AT1 ASP c 153 PHE c 182 1 30
HELIX 173 AT2 ASP c 205 LEU c 214 1 10
HELIX 174 AT3 GLY c 222 VAL c 227 5 6
HELIX 175 AT4 ASN c 229 THR c 254 1 26
HELIX 176 AT5 PHE c 257 PHE c 264 1 8
HELIX 177 AT6 SER c 267 ASN c 293 1 27
HELIX 178 AT7 PRO c 298 GLY c 303 1 6
HELIX 179 AT8 THR c 305 GLY c 325 1 21
HELIX 180 AT9 GLY c 353 TRP c 359 5 7
HELIX 181 AU1 LEU c 366 PRO c 368 5 3
HELIX 182 AU2 ASP c 376 ASP c 383 1 8
HELIX 183 AU3 GLN c 385 THR c 397 1 13
HELIX 184 AU4 SER c 421 GLY c 454 1 34
HELIX 185 AU5 ASP c 460 MET c 469 5 10
HELIX 186 AU6 GLY d 13 LYS d 23 1 11
HELIX 187 AU7 VAL d 30 VAL d 55 1 26
HELIX 188 AU8 SER d 57 GLY d 62 1 6
HELIX 189 AU9 SER d 66 GLY d 70 5 5
HELIX 190 AV1 ALA d 82 GLY d 86 5 5
HELIX 191 AV2 ASP d 100 LEU d 107 1 8
HELIX 192 AV3 GLY d 108 GLY d 137 1 30
HELIX 193 AV4 PRO d 140 LEU d 158 1 19
HELIX 194 AV5 LEU d 158 GLN d 164 1 7
HELIX 195 AV6 SER d 166 ALA d 170 5 5
HELIX 196 AV7 VAL d 175 ASN d 190 1 16
HELIX 197 AV8 TRP d 191 LEU d 193 5 3
HELIX 198 AV9 ASN d 194 ASN d 220 1 27
HELIX 199 AW1 THR d 231 PHE d 235 5 5
HELIX 200 AW2 SER d 245 PHE d 257 1 13
HELIX 201 AW3 ASN d 263 ALA d 290 1 28
HELIX 202 AW4 PHE d 298 ASP d 308 1 11
HELIX 203 AW5 THR d 313 GLN d 334 1 22
HELIX 204 AW6 PRO d 335 ASN d 338 5 4
HELIX 205 AW7 PRO d 342 LEU d 346 5 5
HELIX 206 AW8 PRO e 9 THR e 15 1 7
HELIX 207 AW9 SER e 16 THR e 40 1 25
HELIX 208 AX1 GLY e 41 GLY e 48 1 8
HELIX 209 AX2 GLU e 71 GLN e 82 1 12
HELIX 210 AX3 THR f 17 GLN f 41 1 25
HELIX 211 AX4 THR h 5 ARG h 12 1 8
HELIX 212 AX5 PRO h 13 SER h 16 5 4
HELIX 213 AX6 THR h 27 ASN h 50 1 24
HELIX 214 AX7 GLU i 2 SER i 25 1 24
HELIX 215 AX8 PRO j 9 ALA j 32 1 24
HELIX 216 AX9 PRO k 12 ILE k 17 5 6
HELIX 217 AY1 PHE k 18 LEU k 25 1 8
HELIX 218 AY2 VAL k 27 VAL k 43 1 17
HELIX 219 AY3 ASN l 13 ASN l 37 1 25
HELIX 220 AY4 LEU m 6 SER m 31 1 26
HELIX 221 AY5 THR o 6 VAL o 11 1 6
HELIX 222 AY6 GLY o 14 LYS o 18 5 5
HELIX 223 AY7 LEU o 182 VAL o 187 1 6
HELIX 224 AY8 GLU t 2 PHE t 23 1 22
HELIX 225 AY9 ASN u 11 GLY u 18 1 8
HELIX 226 AZ1 THR u 19 GLU u 23 5 5
HELIX 227 AZ2 ASN u 31 TYR u 38 5 8
HELIX 228 AZ3 PRO u 43 ALA u 53 1 11
HELIX 229 AZ4 SER u 57 ILE u 64 5 8
HELIX 230 AZ5 THR u 68 LEU u 79 1 12
HELIX 231 AZ6 GLU u 88 GLU u 93 1 6
HELIX 232 AZ7 GLY u 94 ASP u 96 5 3
HELIX 233 AZ8 THR v 22 CYS v 37 1 16
HELIX 234 AZ9 CYS v 37 VAL v 42 1 6
HELIX 235 BA1 GLY v 43 ILE v 45 5 3
HELIX 236 BA2 ARG v 55 ALA v 62 1 8
HELIX 237 BA3 ASN v 68 ASN v 78 1 11
HELIX 238 BA4 PHE v 101 ARG v 105 5 5
HELIX 239 BA5 THR v 108 GLY v 127 1 20
HELIX 240 BA6 ASP v 128 TRP v 130 5 3
HELIX 241 BA7 GLY v 132 TYR v 137 5 6
HELIX 242 BA8 ILE y 19 ARG y 42 1 24
HELIX 243 BA9 THR x 4 ASP x 35 1 32
HELIX 244 BB1 THR z 2 SER z 29 1 28
HELIX 245 BB2 ASP z 32 PHE z 59 1 28
SHEET 1 AA1 2 ALA A 81 VAL A 82 0
SHEET 2 AA1 2 LEU A 174 GLY A 175 -1 O LEU A 174 N VAL A 82
SHEET 1 AA2 2 LEU A 297 ASN A 298 0
SHEET 2 AA2 2 GLY C 402 SER C 403 1 O GLY C 402 N ASN A 298
SHEET 1 AA3 2 LEU B 3 PRO B 4 0
SHEET 2 AA3 2 VAL L 10 GLU L 11 1 O GLU L 11 N LEU B 3
SHEET 1 AA4 2 MET B 166 VAL B 168 0
SHEET 2 AA4 2 SER B 177 GLN B 179 -1 O GLN B 179 N MET B 166
SHEET 1 AA5 6 VAL B 377 ASP B 380 0
SHEET 2 AA5 6 ILE B 369 THR B 371 -1 N LEU B 370 O ALA B 379
SHEET 3 AA5 6 GLU B 353 VAL B 356 -1 N PHE B 355 O THR B 371
SHEET 4 AA5 6 ILE B 336 ARG B 347 -1 N PHE B 346 O LEU B 354
SHEET 5 AA5 6 THR B 398 TYR B 402 -1 O THR B 398 N ARG B 347
SHEET 6 AA5 6 THR B 410 PHE B 411 -1 O PHE B 411 N VAL B 399
SHEET 1 AA6 5 VAL B 377 ASP B 380 0
SHEET 2 AA6 5 ILE B 369 THR B 371 -1 N LEU B 370 O ALA B 379
SHEET 3 AA6 5 GLU B 353 VAL B 356 -1 N PHE B 355 O THR B 371
SHEET 4 AA6 5 ILE B 336 ARG B 347 -1 N PHE B 346 O LEU B 354
SHEET 5 AA6 5 ILE B 429 ASP B 433 -1 O GLU B 431 N GLN B 338
SHEET 1 AA7 2 LEU C 185 ASP C 187 0
SHEET 2 AA7 2 ASP C 195 ARG C 197 -1 O ARG C 197 N LEU C 185
SHEET 1 AA8 2 LEU C 341 ARG C 343 0
SHEET 2 AA8 2 ILE C 349 PHE C 351 -1 O ILE C 350 N MET C 342
SHEET 1 AA9 2 ARG C 370 GLY C 371 0
SHEET 2 AA9 2 GLY C 374 LEU C 375 -1 O GLY C 374 N GLY C 371
SHEET 1 AB1 2 ALA D 77 VAL D 78 0
SHEET 2 AB1 2 PHE D 173 GLY D 174 -1 O PHE D 173 N VAL D 78
SHEET 1 AB2 2 TYR O 30 PRO O 31 0
SHEET 2 AB2 2 SER O 135 ILE O 136 -1 O ILE O 136 N TYR O 30
SHEET 1 AB310 PHE O 65 PRO O 67 0
SHEET 2 AB310 TYR O 38 LYS O 53 -1 N VAL O 52 O VAL O 66
SHEET 3 AB310 GLU O 232 PRO O 245 -1 O GLN O 236 N THR O 48
SHEET 4 AB310 GLU O 210 LEU O 220 -1 N ILE O 211 O ALA O 241
SHEET 5 AB310 LEU O 192 ASP O 205 -1 N ASN O 200 O THR O 214
SHEET 6 AB310 ASP O 141 PRO O 149 -1 N PHE O 142 O LEU O 199
SHEET 7 AB310 VAL O 126 SER O 128 -1 N SER O 128 O LYS O 143
SHEET 8 AB310 LEU O 93 ILE O 101 -1 N PHE O 95 O ALA O 127
SHEET 9 AB310 LEU O 78 VAL O 87 -1 N GLN O 82 O ASP O 99
SHEET 10 AB310 TYR O 38 LYS O 53 -1 N LEU O 45 O LEU O 78
SHEET 1 AB4 3 LYS O 69 LEU O 70 0
SHEET 2 AB4 3 PHE O 103 GLN O 109 -1 O GLN O 109 N LYS O 69
SHEET 3 AB4 3 ARG O 115 THR O 121 -1 O ILE O 116 N VAL O 108
SHEET 1 AB5 2 ILE U 25 ASP U 26 0
SHEET 2 AB5 2 PHE U 82 THR U 83 1 O THR U 83 N ILE U 25
SHEET 1 AB6 2 THR V 9 PRO V 11 0
SHEET 2 AB6 2 THR V 18 THR V 20 -1 O ILE V 19 N VAL V 10
SHEET 1 AB7 2 ALA a 81 VAL a 82 0
SHEET 2 AB7 2 LEU a 174 GLY a 175 -1 O LEU a 174 N VAL a 82
SHEET 1 AB8 2 LEU a 297 ASN a 298 0
SHEET 2 AB8 2 GLY c 402 SER c 403 1 O GLY c 402 N ASN a 298
SHEET 1 AB9 2 LEU b 3 PRO b 4 0
SHEET 2 AB9 2 VAL l 10 GLU l 11 1 O GLU l 11 N LEU b 3
SHEET 1 AC1 2 MET b 166 VAL b 168 0
SHEET 2 AC1 2 SER b 177 GLN b 179 -1 O GLN b 179 N MET b 166
SHEET 1 AC2 6 VAL b 377 ASP b 380 0
SHEET 2 AC2 6 ILE b 369 THR b 371 -1 N LEU b 370 O ALA b 379
SHEET 3 AC2 6 GLU b 353 VAL b 356 -1 N PHE b 355 O THR b 371
SHEET 4 AC2 6 ILE b 336 ARG b 347 -1 N PHE b 346 O LEU b 354
SHEET 5 AC2 6 THR b 398 TYR b 402 -1 O THR b 398 N ARG b 347
SHEET 6 AC2 6 THR b 410 PHE b 411 -1 O PHE b 411 N VAL b 399
SHEET 1 AC3 5 VAL b 377 ASP b 380 0
SHEET 2 AC3 5 ILE b 369 THR b 371 -1 N LEU b 370 O ALA b 379
SHEET 3 AC3 5 GLU b 353 VAL b 356 -1 N PHE b 355 O THR b 371
SHEET 4 AC3 5 ILE b 336 ARG b 347 -1 N PHE b 346 O LEU b 354
SHEET 5 AC3 5 ILE b 429 ASP b 433 -1 O GLU b 431 N GLN b 338
SHEET 1 AC4 2 LEU c 185 ASP c 187 0
SHEET 2 AC4 2 ASP c 195 ARG c 197 -1 O ARG c 197 N LEU c 185
SHEET 1 AC5 2 LEU c 341 ARG c 343 0
SHEET 2 AC5 2 ILE c 349 PHE c 351 -1 O ILE c 350 N MET c 342
SHEET 1 AC6 2 ARG c 370 GLY c 371 0
SHEET 2 AC6 2 GLY c 374 LEU c 375 -1 O GLY c 374 N GLY c 371
SHEET 1 AC7 2 ALA d 77 VAL d 78 0
SHEET 2 AC7 2 PHE d 173 GLY d 174 -1 O PHE d 173 N VAL d 78
SHEET 1 AC8 2 TYR o 30 PRO o 31 0
SHEET 2 AC8 2 SER o 135 ILE o 136 -1 O ILE o 136 N TYR o 30
SHEET 1 AC910 PHE o 65 PRO o 67 0
SHEET 2 AC910 TYR o 38 LYS o 53 -1 N VAL o 52 O VAL o 66
SHEET 3 AC910 GLU o 232 PRO o 245 -1 O GLN o 236 N THR o 48
SHEET 4 AC910 GLU o 210 LEU o 220 -1 N ILE o 211 O ALA o 241
SHEET 5 AC910 LEU o 192 ASP o 205 -1 N GLN o 196 O GLU o 218
SHEET 6 AC910 ASP o 141 PRO o 149 -1 N PHE o 142 O LEU o 199
SHEET 7 AC910 VAL o 126 SER o 128 -1 N SER o 128 O LYS o 143
SHEET 8 AC910 LEU o 93 ILE o 101 -1 N PHE o 95 O ALA o 127
SHEET 9 AC910 LEU o 78 VAL o 87 -1 N GLN o 82 O ASP o 99
SHEET 10 AC910 TYR o 38 LYS o 53 -1 N LEU o 45 O LEU o 78
SHEET 1 AD1 3 LYS o 69 LEU o 70 0
SHEET 2 AD1 3 PHE o 103 GLN o 109 -1 O GLN o 109 N LYS o 69
SHEET 3 AD1 3 ARG o 115 THR o 121 -1 O ILE o 116 N VAL o 108
SHEET 1 AD2 2 ILE u 25 ASP u 26 0
SHEET 2 AD2 2 PHE u 82 THR u 83 1 O THR u 83 N ILE u 25
SHEET 1 AD3 2 THR v 9 PRO v 11 0
SHEET 2 AD3 2 THR v 18 THR v 20 -1 O ILE v 19 N VAL v 10
SSBOND 1 CYS O 19 CYS O 44 1555 1555 2.03
SSBOND 2 CYS o 19 CYS o 44 1555 1555 2.03
LINK OD1 ASP A 170 CA1 OEX A 601 1555 1555 2.92
LINK OD2 ASP A 170 MN4 OEX A 601 1555 1555 2.46
LINK OD2 ASP A 170 CA1 OEX A 601 1555 1555 3.19
LINK OE2 GLU A 189 MN1 OEX A 601 1555 1555 2.24
LINK NE2 HIS A 215 FE FE2 A 613 1555 1555 2.42
LINK NE2 HIS A 272 FE FE2 A 613 1555 1555 2.42
LINK NE2 HIS A 332 MN1 OEX A 601 1555 1555 2.41
LINK OE1 GLU A 333 MN3 OEX A 601 1555 1555 2.33
LINK OE2 GLU A 333 MN4 OEX A 601 1555 1555 2.43
LINK OD1 ASP A 342 MN2 OEX A 601 1555 1555 2.32
LINK OD2 ASP A 342 MN1 OEX A 601 1555 1555 2.36
LINK O ALA A 344 CA1 OEX A 601 1555 1555 2.95
LINK OXT ALA A 344 MN2 OEX A 601 1555 1555 2.34
LINK MN2 OEX A 601 OE1 GLU C 354 1555 1555 2.38
LINK MN3 OEX A 601 OE2 GLU C 354 1555 1555 2.40
LINK O1 BCT A 604 FE FE2 A 613 1555 1555 2.52
LINK O2 BCT A 604 FE FE2 A 613 1555 1555 2.52
LINK FE FE2 A 613 NE2 HIS D 214 1555 1555 2.52
LINK FE FE2 A 613 NE2 HIS D 268 1555 1555 2.42
LINK OD1 ASN C 39 MG CLA C 511 1555 1555 2.78
LINK NE2 HIS E 23 FE HEM E 102 1555 1555 2.37
LINK FE HEM E 102 NE2 HIS F 24 1555 1555 2.37
LINK O GLY J 31 MG MG J 102 1555 1555 2.97
LINK O ALA J 34 MG MG J 102 1555 1555 2.17
LINK O LEU J 36 MG MG J 102 1555 1555 2.38
LINK O4 LMG J 101 MG MG J 102 1555 1555 2.71
LINK O THR O 138 CA CA O 301 1555 1555 2.52
LINK OD1 ASN O 200 CA CA O 301 1555 1555 3.19
LINK NE2 HIS V 41 FE HEM V 202 1555 1555 2.32
LINK NE2 HIS V 92 FE HEM V 202 1555 1555 2.38
LINK OD1 ASP a 170 CA1 OEX a 601 1555 1555 2.95
LINK OD2 ASP a 170 CA1 OEX a 601 1555 1555 3.12
LINK OD2 ASP a 170 MN4 OEX a 601 1555 1555 2.50
LINK OE2 GLU a 189 MN1 OEX a 601 1555 1555 2.22
LINK NE2 HIS a 215 FE FE2 a 615 1555 1555 2.46
LINK NE2 HIS a 272 FE FE2 a 615 1555 1555 2.40
LINK NE2 HIS a 332 MN1 OEX a 601 1555 1555 2.43
LINK OE1 GLU a 333 MN3 OEX a 601 1555 1555 2.29
LINK OE2 GLU a 333 MN4 OEX a 601 1555 1555 2.52
LINK OD1 ASP a 342 MN2 OEX a 601 1555 1555 2.38
LINK OD2 ASP a 342 MN1 OEX a 601 1555 1555 2.34
LINK O ALA a 344 CA1 OEX a 601 1555 1555 2.98
LINK OXT ALA a 344 MN2 OEX a 601 1555 1555 2.34
LINK MN2 OEX a 601 OE1 GLU c 354 1555 1555 2.32
LINK MN3 OEX a 601 OE2 GLU c 354 1555 1555 2.36
LINK O1 BCT a 603 FE FE2 a 615 1555 1555 2.57
LINK O2 BCT a 603 FE FE2 a 615 1555 1555 2.54
LINK FE FE2 a 615 NE2 HIS d 214 1555 1555 2.47
LINK FE FE2 a 615 NE2 HIS d 268 1555 1555 2.40
LINK OD1 ASN c 39 MG CLA c 512 1555 1555 2.75
LINK NE2 HIS e 23 FE HEM e 102 1555 1555 2.42
LINK FE HEM e 102 NE2 HIS f 24 1555 1555 2.40
LINK O ARG f 45 CA CA f 102 1555 1555 3.02
LINK OXT ARG f 45 CA CA f 102 1555 1555 2.75
LINK CA CA f 102 OE1 GLU v 23 1555 1555 3.10
LINK O GLY j 31 MG MG j 102 1555 1555 2.31
LINK O ALA j 34 MG MG j 102 1555 1555 1.98
LINK O LEU j 36 MG MG j 102 1555 1555 2.59
LINK O4 LMG j 101 MG MG j 102 1555 1555 2.37
LINK O THR o 138 CA CA o 301 1555 1555 2.41
LINK OD1 ASN o 200 CA CA o 301 1555 1555 2.57
LINK O VAL o 201 CA CA o 301 1555 1555 2.48
LINK NE2 HIS v 41 FE HEM v 201 1555 1555 2.34
LINK NE2 HIS v 92 FE HEM v 201 1555 1555 2.39
CISPEP 1 TYR U 42 PRO U 43 0 3.67
CISPEP 2 ALA U 53 PRO U 54 0 -2.14
CISPEP 3 THR V 63 PRO V 64 0 -10.81
CISPEP 4 TYR u 42 PRO u 43 0 4.33
CISPEP 5 ALA u 53 PRO u 54 0 5.30
CISPEP 6 THR v 63 PRO v 64 0 -8.08
SITE 1 AC1 9 ASP A 170 GLU A 189 HIS A 332 GLU A 333
SITE 2 AC1 9 HIS A 337 ASP A 342 ALA A 344 GLU C 354
SITE 3 AC1 9 ARG C 357
SITE 1 AC2 4 ASN A 181 HIS A 332 GLU A 333 LYS D 317
SITE 1 AC3 3 ASN A 338 PHE A 339 GLU C 354
SITE 1 AC4 7 GLU A 244 TYR A 246 HIS A 272 FE2 A 613
SITE 2 AC4 7 HIS D 214 TYR D 244 HIS D 268
SITE 1 AC5 22 PHE A 119 TYR A 147 PRO A 150 SER A 153
SITE 2 AC5 22 VAL A 157 MET A 183 PHE A 186 GLN A 187
SITE 3 AC5 22 ILE A 192 LEU A 193 HIS A 198 PHE A 206
SITE 4 AC5 22 ALA A 286 ALA A 287 ILE A 290 CLA A 606
SITE 5 AC5 22 PHO A 607 LEU D 182 LEU D 205 CLA D 402
SITE 6 AC5 22 CLA D 403 PHE T 17
SITE 1 AC6 18 GLN A 199 VAL A 202 ALA A 203 PHE A 206
SITE 2 AC6 18 GLY A 207 LEU A 210 TRP A 278 CLA A 605
SITE 3 AC6 18 PL9 A 610 DGD C 518 PHE D 157 VAL D 175
SITE 4 AC6 18 ILE D 178 PHE D 179 LEU D 182 PHO D 401
SITE 5 AC6 18 CLA D 403 LMG J 101
SITE 1 AC7 20 LEU A 41 ALA A 44 THR A 45 ILE A 115
SITE 2 AC7 20 PHE A 119 TYR A 126 GLN A 130 ALA A 146
SITE 3 AC7 20 TYR A 147 ALA A 149 PRO A 150 GLY A 175
SITE 4 AC7 20 PRO A 279 VAL A 283 CLA A 605 LEU D 205
SITE 5 AC7 20 LEU D 209 ILE D 213 TRP D 253 CLA D 402
SITE 1 AC8 18 ILE A 36 PRO A 39 THR A 40 PHE A 93
SITE 2 AC8 18 PRO A 95 ILE A 96 TRP A 97 LEU A 114
SITE 3 AC8 18 HIS A 118 LEU A 121 BCR A 609 LMG A 612
SITE 4 AC8 18 VAL I 8 TYR I 9 VAL I 11 VAL I 12
SITE 5 AC8 18 PHE I 15 VAL I 20
SITE 1 AC9 12 VAL A 35 PRO A 39 LEU A 42 ALA A 43
SITE 2 AC9 12 CYS A 47 ILE A 50 ILE A 96 TRP A 105
SITE 3 AC9 12 LEU A 106 CLA A 608 PHE I 15 LEU I 18
SITE 1 AD1 20 PHE A 211 MET A 214 HIS A 215 LEU A 218
SITE 2 AD1 20 HIS A 252 PHE A 255 SER A 264 PHE A 265
SITE 3 AD1 20 LEU A 271 PHE A 274 CLA A 606 VAL D 30
SITE 4 AD1 20 PRO D 39 ALA D 41 TYR D 42 PHO D 401
SITE 5 AD1 20 ALA F 22 THR F 25 THR X 24 LEU X 28
SITE 1 AD2 13 GLY A 204 ASN A 267 SER A 270 PHE A 273
SITE 2 AD2 13 TRP A 278 GLY A 282 GLN C 28 ALA C 34
SITE 3 AD2 13 TRP C 36 CLA C 508 ARG D 233 LHG D 408
SITE 4 AD2 13 PHE K 37
SITE 1 AD3 13 PHE A 93 TRP A 97 GLU A 98 LEU A 121
SITE 2 AD3 13 SER A 124 PHE A 155 CLA A 608 LEU C 214
SITE 3 AD3 13 GLU C 221 TRP C 223 CLA C 505 LYS I 5
SITE 4 AD3 13 TYR I 9
SITE 1 AD4 5 HIS A 215 HIS A 272 BCT A 604 HIS D 214
SITE 2 AD4 5 HIS D 268
SITE 1 AD5 2 ASN B 438 GLU O 181
SITE 1 AD6 5 PRO B 187 PHE B 190 CLA B 603 PHE H 41
SITE 2 AD6 5 BCR H 101
SITE 1 AD7 22 GLU B 184 TRP B 185 GLY B 189 PHE B 190
SITE 2 AD7 22 PRO B 192 GLY B 197 ALA B 200 HIS B 201
SITE 3 AD7 22 ALA B 204 ALA B 205 VAL B 208 PHE B 247
SITE 4 AD7 22 PHE B 250 CLA B 602 CLA B 604 CLA B 606
SITE 5 AD7 22 PHE H 41 ILE H 45 LEU H 46 TYR H 49
SITE 6 AD7 22 BCR H 101 DGD H 102
SITE 1 AD8 18 LEU B 69 ALA B 146 LEU B 149 CYS B 150
SITE 2 AD8 18 PHE B 153 LEU B 158 VAL B 198 HIS B 201
SITE 3 AD8 18 HIS B 202 VAL B 252 THR B 262 CLA B 603
SITE 4 AD8 18 CLA B 605 CLA B 606 CLA B 607 MET H 35
SITE 5 AD8 18 PHE H 38 LEU H 39
SITE 1 AD9 17 TRP B 33 PHE B 65 ARG B 68 LEU B 149
SITE 2 AD9 17 VAL B 245 ALA B 248 ALA B 249 VAL B 252
SITE 3 AD9 17 PHE B 451 HIS B 455 PHE B 458 ALA B 459
SITE 4 AD9 17 CLA B 604 CLA B 606 CLA B 608 CLA B 613
SITE 5 AD9 17 CLA B 616
SITE 1 AE1 20 THR B 27 ALA B 34 VAL B 62 MET B 66
SITE 2 AE1 20 LEU B 69 HIS B 100 LEU B 103 ALA B 146
SITE 3 AE1 20 GLY B 147 CYS B 150 ALA B 205 GLY B 209
SITE 4 AE1 20 CLA B 603 CLA B 604 CLA B 605 CLA B 607
SITE 5 AE1 20 CLA B 610 CLA B 611 CLA B 616 BCR B 620
SITE 1 AE2 16 VAL B 71 PHE B 90 TRP B 91 VAL B 96
SITE 2 AE2 16 VAL B 102 GLY B 152 PHE B 153 PHE B 156
SITE 3 AE2 16 HIS B 157 PHE B 162 GLY B 163 PRO B 164
SITE 4 AE2 16 CLA B 604 CLA B 606 BCR B 620 SQD a 612
SITE 1 AE3 18 TRP B 33 TYR B 40 GLN B 58 GLY B 59
SITE 2 AE3 18 MET B 60 PHE B 61 LEU B 324 THR B 327
SITE 3 AE3 18 GLY B 328 PRO B 329 TRP B 450 PHE B 451
SITE 4 AE3 18 CLA B 605 BCR B 619 LMG B 621 LHG B 622
SITE 5 AE3 18 PHE M 14 BCR t 101
SITE 1 AE4 14 THR B 236 SER B 239 SER B 240 ALA B 243
SITE 2 AE4 14 PHE B 246 PHE B 463 HIS B 466 ILE B 467
SITE 3 AE4 14 CLA B 611 PHE D 120 LEU D 127 ILE D 150
SITE 4 AE4 14 LEU H 39 LEU H 43
SITE 1 AE5 17 PHE B 139 LEU B 143 VAL B 208 ALA B 212
SITE 2 AE5 17 PHE B 215 HIS B 216 VAL B 219 PRO B 221
SITE 3 AE5 17 PRO B 222 LEU B 229 CLA B 606 CLA B 611
SITE 4 AE5 17 THR H 27 MET H 31 PHE H 34 LEU H 43
SITE 5 AE5 17 BCR H 101
SITE 1 AE6 14 LEU B 135 MET B 138 PHE B 139 HIS B 142
SITE 2 AE6 14 LEU B 143 LEU B 145 ALA B 146 VAL B 237
SITE 3 AE6 14 SER B 241 CLA B 606 CLA B 609 CLA B 610
SITE 4 AE6 14 CLA B 613 CLA B 616
SITE 1 AE7 18 TYR B 6 ARG B 7 VAL B 8 HIS B 9
SITE 2 AE7 18 THR B 10 LEU B 238 LEU B 461 PHE B 462
SITE 3 AE7 18 PHE B 464 GLY B 465 TRP B 468 HIS B 469
SITE 4 AE7 18 ARG B 472 CLA B 613 CLA B 614 CLA B 615
SITE 5 AE7 18 BCR B 619 LHG B 622
SITE 1 AE8 14 HIS B 9 LEU B 19 HIS B 23 HIS B 26
SITE 2 AE8 14 THR B 27 LEU B 238 SER B 241 VAL B 245
SITE 3 AE8 14 CLA B 605 CLA B 611 CLA B 612 CLA B 614
SITE 4 AE8 14 CLA B 615 CLA B 616
SITE 1 AE9 12 HIS B 9 HIS B 26 VAL B 30 TRP B 33
SITE 2 AE9 12 PHE B 462 CLA B 612 CLA B 613 CLA B 615
SITE 3 AE9 12 BCR B 618 BCR B 619 LMG B 621 LHG B 622
SITE 1 AF1 16 VAL B 8 HIS B 9 VAL B 11 ALA B 22
SITE 2 AF1 16 LEU B 29 TRP B 115 CLA B 612 CLA B 613
SITE 3 AF1 16 CLA B 614 BCR B 618 LMG B 621 SQD B 623
SITE 4 AF1 16 GLN L 8 VAL L 10 PHE M 21 PHE t 8
SITE 1 AF2 12 HIS B 23 LEU B 24 MET B 138 HIS B 142
SITE 2 AF2 12 LEU B 145 CLA B 605 CLA B 606 CLA B 611
SITE 3 AF2 12 CLA B 613 CLA B 617 BCR B 620 LEU H 14
SITE 1 AF3 10 LEU B 24 ALA B 110 TRP B 113 HIS B 114
SITE 2 AF3 10 LEU B 120 CLA B 616 BCR B 620 THR H 5
SITE 3 AF3 10 LEU H 7 GLY H 8
SITE 1 AF4 10 MET B 25 LEU B 29 TRP B 115 CLA B 614
SITE 2 AF4 10 CLA B 615 BCR B 619 LMG B 621 SQD B 623
SITE 3 AF4 10 PHE t 19 BCR t 101
SITE 1 AF5 14 LEU B 29 GLY B 32 TRP B 33 SER B 36
SITE 2 AF5 14 ILE B 101 VAL B 102 SER B 104 GLY B 105
SITE 3 AF5 14 CLA B 608 CLA B 612 CLA B 614 BCR B 618
SITE 4 AF5 14 LMG B 621 BCR t 101
SITE 1 AF6 9 LEU B 106 LEU B 109 TRP B 113 CLA B 606
SITE 2 AF6 9 CLA B 607 CLA B 616 CLA B 617 SQD a 612
SITE 3 AF6 9 PHE t 23
SITE 1 AF7 14 TYR B 40 THR B 327 GLY B 328 PRO B 329
SITE 2 AF7 14 ALA B 454 CLA B 608 CLA B 614 CLA B 615
SITE 3 AF7 14 BCR B 618 BCR B 619 LHG B 622 LHG L 101
SITE 4 AF7 14 ASN M 4 ALA M 10
SITE 1 AF8 18 SER A 232 ASN A 234 TRP B 5 TYR B 6
SITE 2 AF8 18 ARG B 7 LEU B 461 PHE B 464 TRP B 468
SITE 3 AF8 18 CLA B 608 CLA B 612 CLA B 614 LMG B 621
SITE 4 AF8 18 TYR D 141 ILE D 144 TRP D 266 PHE D 269
SITE 5 AF8 18 THR D 277 LHG L 101
SITE 1 AF9 14 ARG B 18 ALA B 28 LEU B 29 SER B 104
SITE 2 AF9 14 PHE B 108 TRP B 115 CLA B 615 BCR B 618
SITE 3 AF9 14 ARG L 7 ARG l 14 TYR l 18 LEU m 16
SITE 4 AF9 14 PHE t 19 PHE t 23
SITE 1 AG1 16 LEU C 95 LEU C 168 GLY C 171 ALA C 172
SITE 2 AG1 16 LEU C 175 VAL C 233 HIS C 237 ILE C 240
SITE 3 AG1 16 MET C 282 VAL C 296 TYR C 297 CLA C 502
SITE 4 AG1 16 CLA C 503 CLA C 506 CLA C 507 BCR C 515
SITE 1 AG2 16 HIS C 91 GLY C 171 LYS C 178 PHE C 182
SITE 2 AG2 16 LEU C 279 MET C 282 ALA C 286 VAL C 290
SITE 3 AG2 16 TYR C 297 HIS C 430 LEU C 433 PHE C 437
SITE 4 AG2 16 CLA C 501 CLA C 503 CLA C 504 CLA C 510
SITE 1 AG3 13 ILE C 60 VAL C 61 THR C 68 LEU C 88
SITE 2 AG3 13 HIS C 91 LEU C 95 VAL C 114 HIS C 118
SITE 3 AG3 13 CLA C 501 CLA C 502 CLA C 510 CLA C 512
SITE 4 AG3 13 LMG C 520
SITE 1 AG4 18 TRP C 63 MET C 67 PHE C 70 GLN C 84
SITE 2 AG4 18 GLY C 85 ILE C 87 TRP C 425 SER C 429
SITE 3 AG4 18 PHE C 436 CLA C 502 CLA C 508 CLA C 510
SITE 4 AG4 18 DGD C 517 DGD C 518 LMG C 519 LHG D 408
SITE 5 AG4 18 PRO K 26 VAL K 30
SITE 1 AG5 16 PHE A 33 MET A 127 TRP A 131 LMG A 612
SITE 2 AG5 16 PHE C 264 SER C 273 TYR C 274 HIS C 441
SITE 3 AG5 16 LEU C 442 ALA C 445 ARG C 449 CLA C 507
SITE 4 AG5 16 BCR C 515 VAL I 12 VAL I 16 PHE I 23
SITE 1 AG6 14 LEU C 161 LEU C 165 LEU C 213 ILE C 243
SITE 2 AG6 14 GLY C 247 TRP C 250 HIS C 251 THR C 254
SITE 3 AG6 14 THR C 255 PHE C 257 TRP C 259 PHE C 264
SITE 4 AG6 14 CLA C 501 CLA C 507
SITE 1 AG7 16 MET C 157 THR C 158 LEU C 161 HIS C 164
SITE 2 AG7 16 LEU C 168 CYS C 244 PHE C 264 TRP C 266
SITE 3 AG7 16 TYR C 271 TYR C 274 SER C 275 CLA C 501
SITE 4 AG7 16 CLA C 505 CLA C 506 CLA C 509 BCR C 515
SITE 1 AG8 23 SQD A 611 TRP C 36 ALA C 37 GLY C 38
SITE 2 AG8 23 ASN C 39 ALA C 40 GLU C 269 LEU C 272
SITE 3 AG8 23 LEU C 276 PHE C 436 PHE C 437 GLY C 440
SITE 4 AG8 23 TRP C 443 HIS C 444 ARG C 447 CLA C 504
SITE 5 AG8 23 CLA C 509 CLA C 510 CLA C 511 DGD C 518
SITE 6 AG8 23 LMG C 519 LHG D 408 VAL K 30
SITE 1 AG9 20 ASN C 39 LEU C 49 ALA C 52 HIS C 53
SITE 2 AG9 20 HIS C 56 TYR C 149 MET C 157 ILE C 160
SITE 3 AG9 20 HIS C 164 GLY C 268 GLU C 269 TYR C 271
SITE 4 AG9 20 LEU C 272 SER C 275 LEU C 279 CLA C 507
SITE 5 AG9 20 CLA C 508 CLA C 510 CLA C 511 CLA C 512
SITE 1 AH1 16 ASN C 39 HIS C 56 LEU C 59 ILE C 60
SITE 2 AH1 16 TRP C 63 LEU C 279 PHE C 436 PHE C 437
SITE 3 AH1 16 CLA C 502 CLA C 503 CLA C 504 CLA C 508
SITE 4 AH1 16 CLA C 509 LHG D 408 PRO K 29 LEU K 33
SITE 1 AH2 28 THR C 24 ARG C 26 TRP C 35 GLY C 38
SITE 2 AH2 28 ASN C 39 ARG C 41 LEU C 42 LEU C 45
SITE 3 AH2 28 LYS C 48 ALA C 52 ALA C 123 PHE C 127
SITE 4 AH2 28 ILE C 134 CLA C 508 CLA C 509 BCR C 521
SITE 5 AH2 28 LEU K 33 ALA K 36 TRP K 39 GLN K 40
SITE 6 AH2 28 LEU Y 39 ASN Y 45 LEU Y 46 MET Z 19
SITE 7 AH2 28 VAL Z 20 VAL Z 23 PRO Z 24 ALA Z 28
SITE 1 AH3 11 HIS C 53 PHE C 146 PHE C 147 PHE C 163
SITE 2 AH3 11 HIS C 164 VAL C 167 ILE C 170 GLY C 171
SITE 3 AH3 11 CLA C 503 CLA C 509 CLA C 513
SITE 1 AH4 9 LEU C 50 GLY C 128 TYR C 131 HIS C 132
SITE 2 AH4 9 TYR C 143 PHE C 147 CLA C 512 BCR C 514
SITE 3 AH4 9 LMG Z 101
SITE 1 AH5 11 PHE C 112 VAL C 116 SER C 121 VAL C 124
SITE 2 AH5 11 LEU C 125 CLA C 513 LMG C 520 TYR K 15
SITE 3 AH5 11 VAL Z 51 GLY Z 55 ASN Z 58
SITE 1 AH6 13 ILE C 209 PHE C 210 LEU C 213 VAL C 227
SITE 2 AH6 13 GLY C 236 HIS C 237 ILE C 240 CLA C 501
SITE 3 AH6 13 CLA C 505 CLA C 507 VAL I 20 PHE I 23
SITE 4 AH6 13 LEU I 24
SITE 1 AH7 22 LEU A 91 SER A 148 PRO C 217 PHE C 218
SITE 2 AH7 22 GLY C 219 GLY C 220 GLU C 221 GLY C 222
SITE 3 AH7 22 TRP C 223 VAL C 225 SER C 226 VAL C 227
SITE 4 AH7 22 ASN C 228 CYS C 288 PHE C 292 ASN C 293
SITE 5 AH7 22 ASN C 294 THR C 295 ASP C 360 PHE C 361
SITE 6 AH7 22 ARG C 362 LEU C 438
SITE 1 AH8 17 HIS A 195 PHE A 197 LEU A 297 GLU C 83
SITE 2 AH8 17 GLN C 84 GLY C 85 SER C 406 ASN C 418
SITE 3 AH8 17 PHE C 419 VAL C 420 TRP C 425 SER C 429
SITE 4 AH8 17 CLA C 504 DGD C 518 LMG C 519 PHE J 29
SITE 5 AH8 17 TYR J 33
SITE 1 AH9 25 GLN A 199 LEU A 200 ALA A 203 ASN A 301
SITE 2 AH9 25 PHE A 302 SER A 305 CLA A 606 ASN C 405
SITE 3 AH9 25 VAL C 407 ASN C 415 SER C 416 VAL C 417
SITE 4 AH9 25 ASN C 418 CLA C 504 CLA C 508 DGD C 517
SITE 5 AH9 25 ASN D 72 PHE J 29 ALA J 32 TYR J 33
SITE 6 AH9 25 GLY J 37 SER J 38 SER J 39 LEU J 40
SITE 7 AH9 25 LMG J 101
SITE 1 AI1 9 PHE C 70 HIS C 74 GLN C 84 CLA C 504
SITE 2 AI1 9 CLA C 508 DGD C 517 ASP K 23 VAL K 27
SITE 3 AI1 9 ILE Y 25
SITE 1 AI2 8 TRP C 97 ASP C 107 VAL C 117 SER C 121
SITE 2 AI2 8 CLA C 503 BCR C 514 PHE Z 59 VAL Z 62
SITE 1 AI3 17 ALA C 55 GLY C 58 LEU C 59 PHE C 62
SITE 2 AI3 17 ILE C 120 SER C 122 ALA C 123 GLY C 126
SITE 3 AI3 17 CLA C 511 TYR K 15 PHE K 32 ALA K 36
SITE 4 AI3 17 TRP K 39 BCR K 101 LEU Z 9 SER Z 16
SITE 5 AI3 17 TRP Z 47
SITE 1 AI4 21 PHE A 206 ALA A 209 LEU A 210 MET A 214
SITE 2 AI4 21 PHE A 255 CLA A 606 PL9 A 610 ALA D 41
SITE 3 AI4 21 TRP D 48 ILE D 114 GLY D 118 GLY D 121
SITE 4 AI4 21 LEU D 122 PHE D 125 GLN D 129 ASN D 142
SITE 5 AI4 21 PHE D 146 PRO D 149 PHE D 153 LEU D 279
SITE 6 AI4 21 CLA D 403
SITE 1 AI5 16 VAL A 157 MET A 172 ILE A 176 THR A 179
SITE 2 AI5 16 MET A 183 CLA A 605 PHO A 607 MET D 198
SITE 3 AI5 16 VAL D 201 ALA D 202 LEU D 205 GLY D 206
SITE 4 AI5 16 CLA D 403 PL9 D 405 LHG L 101 SQD b 601
SITE 1 AI6 21 MET A 183 PHE A 206 CLA A 605 CLA A 606
SITE 2 AI6 21 LEU D 45 LEU D 122 PRO D 149 VAL D 152
SITE 3 AI6 21 VAL D 156 LEU D 182 PHE D 185 GLN D 186
SITE 4 AI6 21 TRP D 191 HIS D 197 VAL D 201 VAL D 204
SITE 5 AI6 21 SER D 282 ALA D 283 VAL D 286 PHO D 401
SITE 6 AI6 21 CLA D 402
SITE 1 AI7 18 ILE D 35 PRO D 39 CYS D 40 LEU D 43
SITE 2 AI7 18 LEU D 89 LEU D 90 LEU D 91 LEU D 92
SITE 3 AI7 18 TRP D 93 TRP D 104 THR D 112 PHE D 113
SITE 4 AI7 18 HIS D 117 BCR F 101 LEU H 39 GLY X 13
SITE 5 AI7 18 LEU X 14 LEU X 21
SITE 1 AI8 22 PHE A 52 ILE A 53 MET D 198 MET D 199
SITE 2 AI8 22 ALA D 202 LEU D 209 HIS D 214 THR D 217
SITE 3 AI8 22 TRP D 253 ALA D 260 PHE D 261 LEU D 267
SITE 4 AI8 22 VAL D 274 GLY D 278 CLA D 402 LHG D 407
SITE 5 AI8 22 LEU L 23 LEU L 27 LEU L 29 LEU L 30
SITE 6 AI8 22 LHG L 101 PHE T 10
SITE 1 AI9 6 GLY D 99 ASP D 100 THR D 102 PHE E 37
SITE 2 AI9 6 ASP E 45 BCR F 101
SITE 1 AJ1 21 MET A 37 ARG A 129 ILE D 256 PHE D 257
SITE 2 AJ1 21 ILE D 259 ALA D 260 PHE D 261 SER D 262
SITE 3 AJ1 21 ASN D 263 TRP D 266 PHE D 270 PL9 D 405
SITE 4 AJ1 21 ASN L 13 THR L 15 SER L 16 TYR L 18
SITE 5 AJ1 21 LEU L 19 LHG L 101 PHE T 10 PHE T 17
SITE 6 AJ1 21 ALA T 20
SITE 1 AJ2 17 ARG A 140 TRP A 142 PHE A 273 SQD A 611
SITE 2 AJ2 17 PHE C 33 TRP C 36 TRP C 443 ARG C 447
SITE 3 AJ2 17 CLA C 504 CLA C 508 CLA C 510 GLU D 219
SITE 4 AJ2 17 ASN D 220 ALA D 229 SER D 230 THR D 231
SITE 5 AJ2 17 PHE D 232
SITE 1 AJ3 12 LEU A 258 PHE A 260 TYR A 262 PHE D 27
SITE 2 AJ3 12 ARG D 128 THR E 4 THR E 5 GLU E 7
SITE 3 AJ3 12 PRO E 9 PHE E 10 SER E 11 ARG F 19
SITE 1 AJ4 15 PHE E 10 ARG E 18 TYR E 19 ILE E 22
SITE 2 AJ4 15 HIS E 23 THR E 26 ILE E 27 LEU E 30
SITE 3 AJ4 15 ILE F 15 ARG F 19 TRP F 20 VAL F 23
SITE 4 AJ4 15 HIS F 24 ALA F 27 ILE F 31
SITE 1 AJ5 14 LEU D 43 GLY D 46 GLY D 47 LEU D 49
SITE 2 AJ5 14 PHE D 101 PHE D 113 CLA D 404 DGD D 406
SITE 3 AJ5 14 PRO F 29 THR F 30 PHE F 33 LEU F 34
SITE 4 AJ5 14 VAL J 21 LMG J 101
SITE 1 AJ6 2 ARG F 45 GLU V 23
SITE 1 AJ7 10 CLA B 602 CLA B 603 CLA B 610 MET H 31
SITE 2 AJ7 10 MET H 35 LEU H 37 PHE H 38 VAL H 40
SITE 3 AJ7 10 PHE H 41 ILE H 44
SITE 1 AJ8 19 TYR B 193 PHE B 250 GLY B 254 TYR B 258
SITE 2 AJ8 19 GLN B 274 SER B 277 TYR B 279 ALA B 456
SITE 3 AJ8 19 PHE B 463 CLA B 603 HIS D 87 ILE D 159
SITE 4 AJ8 19 LEU D 162 LEU H 46 TYR H 49 ASN H 50
SITE 5 AJ8 19 VAL H 60 SER H 61 TRP H 62
SITE 1 AJ9 17 CLA A 606 DGD C 518 TYR D 67 GLY D 70
SITE 2 AJ9 17 CYS D 71 ASN D 72 PHE D 73 THR F 30
SITE 3 AJ9 17 ILE F 37 MET F 40 GLN F 41 BCR F 101
SITE 4 AJ9 17 PHE J 28 GLY J 31 ALA J 32 LEU J 36
SITE 5 AJ9 17 MG J 102
SITE 1 AK1 5 GLY J 31 ALA J 34 GLY J 35 LEU J 36
SITE 2 AK1 5 LMG J 101
SITE 1 AK2 14 PHE C 62 BCR C 521 ALA J 14 THR J 15
SITE 2 AK2 14 GLY J 18 MET J 19 LEU K 31 PHE K 32
SITE 3 AK2 14 ALA K 34 PRO Y 33 VAL Z 13 SER Z 16
SITE 4 AK2 14 PHE Z 17 VAL Z 20
SITE 1 AK3 21 SER A 232 ASN A 234 PRO B 4 TRP B 5
SITE 2 AK3 21 TYR B 6 LMG B 621 LHG B 622 TRP D 266
SITE 3 AK3 21 PHE D 273 CLA D 402 PL9 D 405 LHG D 407
SITE 4 AK3 21 GLU L 11 LEU L 12 ASN L 13 SER L 16
SITE 5 AK3 21 LEU L 19 GLY L 20 LEU L 22 LEU L 23
SITE 6 AK3 21 PHE M 21
SITE 1 AK4 3 THR O 138 ASN O 200 VAL O 201
SITE 1 AK5 17 LEU A 28 PHE T 8 ALA T 11 CYS T 12
SITE 2 AK5 17 ALA T 15 PHE T 18 ILE T 21 PHE T 22
SITE 3 AK5 17 TRP b 33 SER b 36 MET b 37 TYR b 40
SITE 4 AK5 17 LEU b 109 SQD b 601 CLA b 610 BCR b 620
SITE 5 AK5 17 BCR b 621
SITE 1 AK6 18 CYS V 37 CYS V 40 HIS V 41 THR V 46
SITE 2 AK6 18 THR V 48 LEU V 52 ASP V 53 LEU V 54
SITE 3 AK6 18 THR V 58 LEU V 59 ALA V 62 LEU V 72
SITE 4 AK6 18 TYR V 75 MET V 76 THR V 81 TYR V 82
SITE 5 AK6 18 HIS V 92 PRO V 93
SITE 1 AK7 10 TRP D 21 ARG D 24 ARG D 26 PHE F 16
SITE 2 AK7 10 THR F 17 VAL F 18 LEU X 23 VAL X 27
SITE 3 AK7 10 ILE X 31 ASP X 35
SITE 1 AK8 6 CLA C 513 TYR Z 27 TRP Z 33 LYS Z 37
SITE 2 AK8 6 PHE Z 41 TRP Z 47
SITE 1 AK9 10 ASP a 61 ASP a 170 GLU a 189 HIS a 332
SITE 2 AK9 10 GLU a 333 HIS a 337 ASP a 342 ALA a 344
SITE 3 AK9 10 GLU c 354 ARG c 357
SITE 1 AL1 5 ASN a 181 HIS a 332 GLU a 333 LYS d 317
SITE 2 AL1 5 LEU d 321
SITE 1 AL2 7 GLU a 244 TYR a 246 HIS a 272 FE2 a 615
SITE 2 AL2 7 HIS d 214 TYR d 244 HIS d 268
SITE 1 AL3 19 TYR a 147 PRO a 150 SER a 153 VAL a 157
SITE 2 AL3 19 MET a 183 PHE a 186 GLN a 187 ILE a 192
SITE 3 AL3 19 LEU a 193 HIS a 198 ALA a 286 ALA a 287
SITE 4 AL3 19 ILE a 290 CLA a 605 PHO a 606 CLA a 613
SITE 5 AL3 19 LEU d 205 CLA d 402 PHE t 17
SITE 1 AL4 17 GLN a 199 VAL a 202 ALA a 203 PHE a 206
SITE 2 AL4 17 GLY a 207 LEU a 210 TRP a 278 CLA a 604
SITE 3 AL4 17 PL9 a 609 PHE d 157 VAL d 175 ILE d 178
SITE 4 AL4 17 PHE d 179 LEU d 182 PHO d 401 CLA d 402
SITE 5 AL4 17 LMG j 101
SITE 1 AL5 18 LEU a 41 ALA a 44 THR a 45 PHE a 48
SITE 2 AL5 18 TYR a 126 GLN a 130 ALA a 146 TYR a 147
SITE 3 AL5 18 PRO a 150 VAL a 283 CLA a 604 CLA a 613
SITE 4 AL5 18 LEU d 205 ALA d 208 LEU d 209 ILE d 213
SITE 5 AL5 18 TRP d 253 PHE d 257
SITE 1 AL6 17 ILE a 36 PRO a 39 THR a 40 PHE a 93
SITE 2 AL6 17 PRO a 95 ILE a 96 TRP a 97 LEU a 114
SITE 3 AL6 17 HIS a 118 LEU a 121 BCR a 608 LMG a 611
SITE 4 AL6 17 VAL i 8 TYR i 9 VAL i 11 VAL i 12
SITE 5 AL6 17 PHE i 15
SITE 1 AL7 9 PRO a 39 LEU a 42 ALA a 43 CYS a 47
SITE 2 AL7 9 ILE a 50 TRP a 105 LEU a 106 CLA a 607
SITE 3 AL7 9 PHE i 15
SITE 1 AL8 20 PHE a 211 MET a 214 HIS a 215 LEU a 218
SITE 2 AL8 20 PHE a 255 SER a 264 PHE a 265 LEU a 271
SITE 3 AL8 20 PHE a 274 CLA a 605 VAL d 30 PHE d 38
SITE 4 AL8 20 PRO d 39 ALA d 41 TYR d 42 PHO d 401
SITE 5 AL8 20 THR f 25 LEU f 26 THR x 24 LEU x 28
SITE 1 AL9 16 GLY a 204 ASN a 267 SER a 270 PHE a 273
SITE 2 AL9 16 PHE a 274 TRP a 278 VAL a 281 GLY a 282
SITE 3 AL9 16 LHG a 614 GLN c 28 ALA c 34 TRP c 36
SITE 4 AL9 16 CLA c 509 PHE d 232 ARG d 233 PHE k 37
SITE 1 AM1 15 PHE a 93 TRP a 97 GLU a 98 PHE a 117
SITE 2 AM1 15 LEU a 121 SER a 124 PHE a 155 CLA a 607
SITE 3 AM1 15 LEU c 214 GLU c 221 TRP c 223 PHE c 284
SITE 4 AM1 15 DGD c 517 LYS i 5 TYR i 9
SITE 1 AM2 12 VAL B 102 TRP B 113 TYR B 117 CLA B 607
SITE 2 AM2 12 BCR B 620 TRP a 20 ASN a 26 ARG a 27
SITE 3 AM2 12 LEU a 28 ILE a 38 CLA a 613 BCR t 101
SITE 1 AM3 17 VAL a 157 MET a 172 ILE a 176 THR a 179
SITE 2 AM3 17 PHE a 180 MET a 183 CLA a 604 PHO a 606
SITE 3 AM3 17 SQD a 612 MET d 198 VAL d 201 ALA d 202
SITE 4 AM3 17 LEU d 205 GLY d 206 CLA d 402 PL9 d 404
SITE 5 AM3 17 LHG l 101
SITE 1 AM4 17 ARG a 140 TRP a 142 PHE a 273 SQD a 610
SITE 2 AM4 17 TRP c 36 TRP c 443 ARG c 447 CLA c 505
SITE 3 AM4 17 CLA c 509 CLA c 511 DGD c 519 GLU d 219
SITE 4 AM4 17 ASN d 220 ALA d 229 SER d 230 THR d 231
SITE 5 AM4 17 PHE d 232
SITE 1 AM5 5 HIS a 215 HIS a 272 BCT a 603 HIS d 214
SITE 2 AM5 5 HIS d 268
SITE 1 AM6 10 TRP A 20 ASN A 26 ARG A 27 LEU A 28
SITE 2 AM6 10 CLA D 402 BCR T 101 TRP b 113 TYR b 117
SITE 3 AM6 10 CLA b 609 BCR b 622
SITE 1 AM7 14 ARG L 14 TYR L 18 LEU M 16 PHE T 19
SITE 2 AM7 14 PHE T 23 ARG b 18 ALA b 28 LEU b 29
SITE 3 AM7 14 SER b 104 PHE b 108 TRP b 115 CLA b 617
SITE 4 AM7 14 BCR b 620 ARG l 7
SITE 1 AM8 1 ASN b 438
SITE 1 AM9 5 TRP b 185 PRO b 187 PHE b 190 CLA b 605
SITE 2 AM9 5 BCR h 101
SITE 1 AN1 18 TRP b 185 GLY b 189 PHE b 190 GLY b 197
SITE 2 AN1 18 ALA b 200 HIS b 201 ALA b 204 ALA b 205
SITE 3 AN1 18 VAL b 208 PHE b 247 PHE b 250 CLA b 604
SITE 4 AN1 18 CLA b 606 CLA b 608 PHE h 38 PHE h 41
SITE 5 AN1 18 ILE h 45 BCR h 101
SITE 1 AN2 16 ARG b 68 LEU b 69 ALA b 146 LEU b 149
SITE 2 AN2 16 CYS b 150 PHE b 153 HIS b 201 HIS b 202
SITE 3 AN2 16 VAL b 252 THR b 262 CLA b 605 CLA b 607
SITE 4 AN2 16 CLA b 608 CLA b 609 MET h 35 PHE h 38
SITE 1 AN3 17 TRP b 33 PHE b 65 ARG b 68 LEU b 149
SITE 2 AN3 17 VAL b 245 ALA b 248 ALA b 249 VAL b 252
SITE 3 AN3 17 PHE b 451 HIS b 455 PHE b 458 CLA b 606
SITE 4 AN3 17 CLA b 608 CLA b 610 CLA b 615 CLA b 616
SITE 5 AN3 17 CLA b 618
SITE 1 AN4 22 THR b 27 VAL b 30 ALA b 34 VAL b 62
SITE 2 AN4 22 PHE b 65 MET b 66 LEU b 69 HIS b 100
SITE 3 AN4 22 LEU b 103 ALA b 146 GLY b 147 CYS b 150
SITE 4 AN4 22 ALA b 205 GLY b 209 CLA b 605 CLA b 606
SITE 5 AN4 22 CLA b 607 CLA b 609 CLA b 612 CLA b 613
SITE 6 AN4 22 CLA b 618 BCR b 622
SITE 1 AN5 16 PHE b 90 TRP b 91 VAL b 96 VAL b 102
SITE 2 AN5 16 LEU b 106 GLY b 152 PHE b 153 PHE b 156
SITE 3 AN5 16 HIS b 157 PHE b 162 GLY b 163 PRO b 164
SITE 4 AN5 16 SQD b 601 CLA b 606 CLA b 608 BCR b 622
SITE 1 AN6 18 BCR T 101 TRP b 33 TYR b 40 GLN b 58
SITE 2 AN6 18 GLY b 59 MET b 60 PHE b 61 LEU b 324
SITE 3 AN6 18 THR b 327 GLY b 328 PRO b 329 TRP b 450
SITE 4 AN6 18 CLA b 607 BCR b 620 BCR b 621 LMG b 623
SITE 5 AN6 18 LHG b 624 PHE m 14
SITE 1 AN7 12 THR b 236 SER b 239 SER b 240 ALA b 243
SITE 2 AN7 12 PHE b 463 HIS b 466 ILE b 467 GLY b 470
SITE 3 AN7 12 CLA b 613 ILE d 150 LEU h 39 LEU h 43
SITE 1 AN8 19 PHE b 139 LEU b 143 VAL b 208 ALA b 212
SITE 2 AN8 19 PHE b 215 HIS b 216 VAL b 219 ARG b 220
SITE 3 AN8 19 PRO b 221 PRO b 222 LEU b 229 CLA b 608
SITE 4 AN8 19 CLA b 613 THR h 27 MET h 31 PHE h 34
SITE 5 AN8 19 LEU h 42 LEU h 43 BCR h 101
SITE 1 AN9 15 LEU b 135 MET b 138 PHE b 139 HIS b 142
SITE 2 AN9 15 LEU b 143 ALA b 146 MET b 231 VAL b 237
SITE 3 AN9 15 SER b 240 SER b 241 CLA b 608 CLA b 611
SITE 4 AN9 15 CLA b 612 CLA b 615 CLA b 618
SITE 1 AO1 18 TYR b 6 ARG b 7 VAL b 8 HIS b 9
SITE 2 AO1 18 THR b 10 LEU b 238 ILE b 242 LEU b 461
SITE 3 AO1 18 PHE b 462 GLY b 465 TRP b 468 HIS b 469
SITE 4 AO1 18 ARG b 472 CLA b 615 CLA b 616 CLA b 617
SITE 5 AO1 18 LHG b 624 PHE m 21
SITE 1 AO2 15 HIS b 9 LEU b 19 HIS b 23 HIS b 26
SITE 2 AO2 15 THR b 27 ILE b 234 VAL b 237 LEU b 238
SITE 3 AO2 15 SER b 241 CLA b 607 CLA b 613 CLA b 614
SITE 4 AO2 15 CLA b 616 CLA b 617 CLA b 618
SITE 1 AO3 11 HIS b 9 HIS b 26 VAL b 30 TRP b 33
SITE 2 AO3 11 PHE b 462 CLA b 607 CLA b 614 CLA b 615
SITE 3 AO3 11 CLA b 617 BCR b 621 LMG b 623
SITE 1 AO4 16 PHE T 8 VAL b 8 HIS b 9 VAL b 11
SITE 2 AO4 16 ALA b 22 LEU b 29 TRP b 115 SQD b 602
SITE 3 AO4 16 CLA b 614 CLA b 615 CLA b 616 BCR b 620
SITE 4 AO4 16 LMG b 623 GLN l 8 VAL l 10 PHE m 21
SITE 1 AO5 14 HIS b 23 MET b 138 HIS b 142 LEU b 145
SITE 2 AO5 14 CLA b 607 CLA b 608 CLA b 613 CLA b 615
SITE 3 AO5 14 CLA b 619 BCR b 622 LEU h 7 LEU h 11
SITE 4 AO5 14 LEU h 14 ASN h 15
SITE 1 AO6 10 LEU b 24 ALA b 110 TRP b 113 HIS b 114
SITE 2 AO6 10 LEU b 120 CLA b 618 BCR b 622 THR h 5
SITE 3 AO6 10 LEU h 7 GLY h 8
SITE 1 AO7 13 PHE T 19 BCR T 101 MET b 25 LEU b 29
SITE 2 AO7 13 ALA b 111 CYS b 112 TRP b 115 SQD b 602
SITE 3 AO7 13 CLA b 610 CLA b 617 BCR b 621 LMG b 623
SITE 4 AO7 13 ALA m 10
SITE 1 AO8 13 BCR T 101 LEU b 29 GLY b 32 TRP b 33
SITE 2 AO8 13 SER b 36 ILE b 101 VAL b 102 SER b 104
SITE 3 AO8 13 GLY b 105 CLA b 610 CLA b 616 BCR b 620
SITE 4 AO8 13 LMG b 623
SITE 1 AO9 7 LEU b 106 TRP b 113 SQD b 601 CLA b 608
SITE 2 AO9 7 CLA b 609 CLA b 618 CLA b 619
SITE 1 AP1 13 TYR b 40 THR b 327 GLY b 328 PRO b 329
SITE 2 AP1 13 LYS b 332 CLA b 610 CLA b 616 CLA b 617
SITE 3 AP1 13 BCR b 620 BCR b 621 ILE d 284 PHE l 35
SITE 4 AP1 13 ASN m 4
SITE 1 AP2 17 SER a 232 ASN a 234 TRP b 5 TYR b 6
SITE 2 AP2 17 ARG b 7 LEU b 461 PHE b 464 TRP b 468
SITE 3 AP2 17 CLA b 610 CLA b 614 TYR d 141 ILE d 144
SITE 4 AP2 17 TRP d 266 PHE d 269 THR d 277 LEU l 23
SITE 5 AP2 17 LHG l 101
SITE 1 AP3 4 ASN a 338 PHE a 339 GLY c 353 GLU c 354
SITE 1 AP4 17 LEU c 95 LEU c 168 GLY c 171 ALA c 172
SITE 2 AP4 17 LEU c 175 VAL c 233 HIS c 237 ILE c 240
SITE 3 AP4 17 MET c 282 ILE c 285 PHE c 289 VAL c 296
SITE 4 AP4 17 TYR c 297 CLA c 503 CLA c 504 CLA c 507
SITE 5 AP4 17 BCR c 516
SITE 1 AP5 16 TRP c 63 HIS c 91 LYS c 178 PHE c 182
SITE 2 AP5 16 LEU c 279 MET c 282 ALA c 286 TYR c 297
SITE 3 AP5 16 LEU c 426 HIS c 430 LEU c 433 PHE c 437
SITE 4 AP5 16 CLA c 502 CLA c 504 CLA c 505 CLA c 511
SITE 1 AP6 13 ILE c 60 VAL c 61 THR c 68 LEU c 88
SITE 2 AP6 13 HIS c 91 LEU c 95 VAL c 114 HIS c 118
SITE 3 AP6 13 CLA c 502 CLA c 503 CLA c 511 CLA c 513
SITE 4 AP6 13 LMG c 521
SITE 1 AP7 17 LHG a 614 TRP c 63 PHE c 70 GLN c 84
SITE 2 AP7 17 GLY c 85 ILE c 87 TRP c 425 SER c 429
SITE 3 AP7 17 PHE c 436 CLA c 503 CLA c 509 CLA c 511
SITE 4 AP7 17 DGD c 518 DGD c 519 LMG c 520 PRO k 26
SITE 5 AP7 17 VAL k 30
SITE 1 AP8 16 PHE a 33 MET a 127 TRP a 131 PHE c 264
SITE 2 AP8 16 SER c 273 TYR c 274 GLY c 277 ALA c 278
SITE 3 AP8 16 HIS c 441 LEU c 442 ALA c 445 ARG c 449
SITE 4 AP8 16 CLA c 508 BCR c 516 VAL i 16 PHE i 23
SITE 1 AP9 16 LEU c 161 LEU c 165 LEU c 213 ILE c 243
SITE 2 AP9 16 GLY c 247 TRP c 250 HIS c 251 THR c 254
SITE 3 AP9 16 THR c 255 PHE c 257 TRP c 259 PHE c 264
SITE 4 AP9 16 CLA c 502 CLA c 508 BCR c 516 DGD c 517
SITE 1 AQ1 15 MET c 157 THR c 158 LEU c 161 HIS c 164
SITE 2 AQ1 15 LEU c 168 TRP c 259 PHE c 264 TRP c 266
SITE 3 AQ1 15 TYR c 271 TYR c 274 SER c 275 CLA c 506
SITE 4 AQ1 15 CLA c 507 CLA c 510 BCR c 516
SITE 1 AQ2 21 SQD a 610 LHG a 614 TRP c 36 ALA c 37
SITE 2 AQ2 21 GLY c 38 ASN c 39 GLU c 269 LEU c 272
SITE 3 AQ2 21 LEU c 276 PHE c 436 PHE c 437 GLY c 440
SITE 4 AQ2 21 TRP c 443 HIS c 444 ARG c 447 CLA c 505
SITE 5 AQ2 21 CLA c 510 CLA c 511 CLA c 512 DGD c 519
SITE 6 AQ2 21 LMG c 520
SITE 1 AQ3 21 ASN c 39 LEU c 49 ALA c 52 HIS c 53
SITE 2 AQ3 21 HIS c 56 TYR c 149 MET c 157 ILE c 160
SITE 3 AQ3 21 HIS c 164 LEU c 168 GLY c 268 GLU c 269
SITE 4 AQ3 21 TYR c 271 LEU c 272 SER c 275 LEU c 279
SITE 5 AQ3 21 CLA c 508 CLA c 509 CLA c 511 CLA c 512
SITE 6 AQ3 21 CLA c 513
SITE 1 AQ4 17 LHG a 614 ASN c 39 HIS c 56 LEU c 59
SITE 2 AQ4 17 ILE c 60 TRP c 63 LEU c 279 PHE c 436
SITE 3 AQ4 17 PHE c 437 CLA c 503 CLA c 504 CLA c 505
SITE 4 AQ4 17 CLA c 509 CLA c 510 PRO k 29 VAL k 30
SITE 5 AQ4 17 LEU k 33
SITE 1 AQ5 28 ASN c 25 ARG c 26 TRP c 35 GLY c 38
SITE 2 AQ5 28 ASN c 39 ARG c 41 LEU c 42 LEU c 45
SITE 3 AQ5 28 LYS c 48 ALA c 52 ALA c 123 PHE c 127
SITE 4 AQ5 28 ILE c 134 CLA c 509 CLA c 510 BCR c 522
SITE 5 AQ5 28 PHE k 32 LEU k 33 ALA k 36 TRP k 39
SITE 6 AQ5 28 GLN k 40 ILE y 35 ILE y 36 LEU y 39
SITE 7 AQ5 28 ASN y 45 VAL z 20 VAL z 23 ALA z 28
SITE 1 AQ6 14 HIS c 53 LEU c 125 PHE c 146 PHE c 147
SITE 2 AQ6 14 PHE c 163 HIS c 164 VAL c 167 ILE c 170
SITE 3 AQ6 14 GLY c 171 LEU c 174 CLA c 504 CLA c 510
SITE 4 AQ6 14 CLA c 514 BCR c 515
SITE 1 AQ7 9 VAL c 124 GLY c 128 TYR c 131 HIS c 132
SITE 2 AQ7 9 TYR c 143 PHE c 147 CLA c 513 BCR c 515
SITE 3 AQ7 9 LMG z 101
SITE 1 AQ8 13 PHE c 112 VAL c 116 ILE c 120 SER c 121
SITE 2 AQ8 13 VAL c 124 LEU c 125 CLA c 513 CLA c 514
SITE 3 AQ8 13 LMG c 521 TYR k 15 VAL z 51 GLY z 55
SITE 4 AQ8 13 ASN z 58
SITE 1 AQ9 15 ILE c 209 PHE c 210 TYR c 212 LEU c 213
SITE 2 AQ9 15 VAL c 227 ASP c 232 GLY c 236 HIS c 237
SITE 3 AQ9 15 CLA c 502 CLA c 506 CLA c 507 CLA c 508
SITE 4 AQ9 15 VAL i 20 PHE i 23 LEU i 24
SITE 1 AR1 23 LEU a 91 SER a 148 LMG a 611 PRO c 217
SITE 2 AR1 23 GLY c 219 GLY c 220 GLU c 221 GLY c 222
SITE 3 AR1 23 TRP c 223 VAL c 225 SER c 226 VAL c 227
SITE 4 AR1 23 ASN c 228 PHE c 284 CYS c 288 PHE c 292
SITE 5 AR1 23 ASN c 293 ASN c 294 THR c 295 ASP c 360
SITE 6 AR1 23 PHE c 361 ARG c 362 CLA c 507
SITE 1 AR2 17 HIS a 195 PHE a 197 LEU a 297 GLU c 83
SITE 2 AR2 17 GLN c 84 GLY c 85 SER c 406 ASN c 418
SITE 3 AR2 17 PHE c 419 VAL c 420 TRP c 425 SER c 429
SITE 4 AR2 17 CLA c 505 DGD c 519 LMG c 520 PHE j 29
SITE 5 AR2 17 TYR j 33
SITE 1 AR3 24 GLN a 199 LEU a 200 ASN a 301 PHE a 302
SITE 2 AR3 24 SER a 305 LHG a 614 ASN c 405 VAL c 407
SITE 3 AR3 24 ASN c 415 SER c 416 VAL c 417 ASN c 418
SITE 4 AR3 24 CLA c 505 CLA c 509 DGD c 518 LEU d 74
SITE 5 AR3 24 PHE j 29 ALA j 32 TYR j 33 GLY j 37
SITE 6 AR3 24 SER j 38 SER j 39 LMG j 101 GLN v 34
SITE 1 AR4 9 HIS c 74 GLN c 84 CLA c 505 CLA c 509
SITE 2 AR4 9 DGD c 518 ASP k 23 VAL k 30 GLN y 21
SITE 3 AR4 9 ILE y 25
SITE 1 AR5 7 TRP c 97 ASP c 107 SER c 121 CLA c 504
SITE 2 AR5 7 BCR c 515 PHE z 59 VAL z 62
SITE 1 AR6 16 ALA c 55 GLY c 58 LEU c 59 PHE c 62
SITE 2 AR6 16 LEU c 119 SER c 122 ALA c 123 GLY c 126
SITE 3 AR6 16 CLA c 512 TYR k 15 PHE k 32 TRP k 39
SITE 4 AR6 16 BCR k 101 LEU z 9 SER z 16 TRP z 47
SITE 1 AR7 23 PHE a 206 ALA a 209 LEU a 210 MET a 214
SITE 2 AR7 23 PHE a 255 CLA a 605 PL9 a 609 ALA d 41
SITE 3 AR7 23 TRP d 48 ILE d 114 GLY d 118 GLY d 121
SITE 4 AR7 23 LEU d 122 PHE d 125 GLN d 129 ASN d 142
SITE 5 AR7 23 ALA d 145 PHE d 146 PRO d 149 PHE d 153
SITE 6 AR7 23 PRO d 275 LEU d 279 CLA d 402
SITE 1 AR8 22 MET a 183 PHE a 206 CLA a 604 CLA a 605
SITE 2 AR8 22 CLA a 613 LEU d 45 LEU d 122 PRO d 149
SITE 3 AR8 22 VAL d 152 PHE d 153 VAL d 156 LEU d 182
SITE 4 AR8 22 PHE d 185 GLN d 186 TRP d 191 HIS d 197
SITE 5 AR8 22 GLY d 200 VAL d 201 SER d 282 ALA d 283
SITE 6 AR8 22 VAL d 286 PHO d 401
SITE 1 AR9 16 PRO d 39 CYS d 40 LEU d 43 LEU d 89
SITE 2 AR9 16 LEU d 90 LEU d 91 LEU d 92 TRP d 93
SITE 3 AR9 16 THR d 112 PHE d 113 HIS d 117 LEU h 39
SITE 4 AR9 16 GLY x 13 LEU x 14 VAL x 20 LEU x 21
SITE 1 AS1 23 PHE a 52 ILE a 53 CLA a 613 MET d 198
SITE 2 AS1 23 MET d 199 ALA d 202 LEU d 209 HIS d 214
SITE 3 AS1 23 THR d 217 TRP d 253 ALA d 260 PHE d 261
SITE 4 AS1 23 LEU d 267 PHE d 273 VAL d 274 THR d 277
SITE 5 AS1 23 GLY d 278 LHG d 406 LEU l 23 VAL l 26
SITE 6 AS1 23 LEU l 29 LHG l 101 PHE t 10
SITE 1 AS2 5 GLY d 99 ASP d 100 THR d 102 ASP e 45
SITE 2 AS2 5 BCR f 101
SITE 1 AS3 20 MET a 37 PHE d 257 ILE d 259 ALA d 260
SITE 2 AS3 20 PHE d 261 SER d 262 ASN d 263 TRP d 266
SITE 3 AS3 20 PHE d 270 PL9 d 404 ASN l 13 THR l 15
SITE 4 AS3 20 SER l 16 TYR l 18 LEU l 19 LHG l 101
SITE 5 AS3 20 PHE t 10 PHE t 17 ALA t 20 ILE t 21
SITE 1 AS4 11 LEU a 258 PHE a 260 TYR a 262 PHE d 27
SITE 2 AS4 11 THR e 4 THR e 5 GLU e 7 PRO e 9
SITE 3 AS4 11 PHE e 10 SER e 11 ALA f 22
SITE 1 AS5 12 ARG e 18 TYR e 19 HIS e 23 ILE e 27
SITE 2 AS5 12 LEU e 30 ILE f 15 ARG f 19 TRP f 20
SITE 3 AS5 12 VAL f 23 HIS f 24 VAL f 28 ILE f 31
SITE 1 AS6 14 TYR d 42 LEU d 43 GLY d 46 LEU d 49
SITE 2 AS6 14 THR d 50 PHE d 101 DGD d 405 PRO f 29
SITE 3 AS6 14 THR f 30 PHE f 33 LEU f 34 VAL j 21
SITE 4 AS6 14 VAL j 25 LMG j 101
SITE 1 AS7 2 ARG f 45 GLU v 23
SITE 1 AS8 7 CLA b 604 CLA b 605 CLA b 612 MET h 31
SITE 2 AS8 7 LEU h 37 PHE h 38 PHE h 41
SITE 1 AS9 16 TYR b 193 PHE b 250 GLY b 254 TYR b 258
SITE 2 AS9 16 GLN b 274 ALA b 456 PHE b 463 HIS d 87
SITE 3 AS9 16 ILE d 123 LEU d 162 LEU h 46 TYR h 49
SITE 4 AS9 16 ASN h 50 VAL h 60 SER h 61 TRP h 62
SITE 1 AT1 18 CLA a 605 DGD c 519 TYR d 67 GLY d 70
SITE 2 AT1 18 CYS d 71 ASN d 72 PHE d 73 LEU f 26
SITE 3 AT1 18 THR f 30 ILE f 37 MET f 40 GLN f 41
SITE 4 AT1 18 BCR f 101 PHE j 28 GLY j 31 ALA j 32
SITE 5 AT1 18 LEU j 36 MG j 102
SITE 1 AT2 6 GLN f 41 GLY j 31 ALA j 34 GLY j 35
SITE 2 AT2 6 LEU j 36 LMG j 101
SITE 1 AT3 16 PHE c 62 BCR c 522 ALA j 14 THR j 15
SITE 2 AT3 16 GLY j 18 MET j 19 LEU k 21 LEU k 31
SITE 3 AT3 16 PHE k 32 ALA k 34 ALA k 41 ILE y 28
SITE 4 AT3 16 GLY y 29 PRO y 33 VAL z 13 PHE z 17
SITE 1 AT4 21 SER a 232 ASN a 234 CLA a 613 PRO b 4
SITE 2 AT4 21 TRP b 5 TYR b 6 LHG b 624 TRP d 266
SITE 3 AT4 21 PHE d 273 PL9 d 404 LHG d 406 GLU l 11
SITE 4 AT4 21 LEU l 12 ASN l 13 SER l 16 GLY l 20
SITE 5 AT4 21 LEU l 22 LEU l 23 VAL l 26 PHE m 21
SITE 6 AT4 21 LEU m 22
SITE 1 AT5 3 THR o 138 ASN o 200 VAL o 201
SITE 1 AT6 14 TRP B 33 SER B 36 MET B 37 PHE B 108
SITE 2 AT6 14 LEU B 109 CLA B 608 BCR B 618 BCR B 619
SITE 3 AT6 14 LEU a 28 SQD a 612 PHE t 8 ALA t 15
SITE 4 AT6 14 PHE t 18 PHE t 22
SITE 1 AT7 18 ALA v 36 CYS v 37 CYS v 40 HIS v 41
SITE 2 AT7 18 THR v 48 LEU v 52 ASP v 53 LEU v 54
SITE 3 AT7 18 THR v 58 ALA v 62 LEU v 72 TYR v 75
SITE 4 AT7 18 MET v 76 THR v 81 TYR v 82 HIS v 92
SITE 5 AT7 18 PRO v 93 MET v 104
SITE 1 AT8 12 TRP d 21 ARG d 24 ARG d 26 PHE f 16
SITE 2 AT8 12 THR f 17 VAL f 18 LEU x 23 THR x 24
SITE 3 AT8 12 VAL x 27 LEU x 28 ILE x 31 ASP x 35
SITE 1 AT9 9 PHE c 127 TYR c 131 ARG c 135 CLA c 514
SITE 2 AT9 9 TYR z 27 TRP z 33 LYS z 37 PHE z 41
SITE 3 AT9 9 TRP z 47
CRYST1 133.250 226.260 307.090 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007505 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004420 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003256 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
