HEADER OXIDOREDUCTASE 20-JAN-17 5MX2
TITLE PHOTOSYSTEM II DEPLETED OF THE MN4CAO5 CLUSTER AT 2.55 A RESOLUTION
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 MOL_ID: 2;
COMPND 7 MOLECULE: PHOTOSYSTEM II CP47 REACTION CENTER PROTEIN;
COMPND 8 CHAIN: B, b;
COMPND 9 SYNONYM: PSII 47 KDA PROTEIN,PROTEIN CP-47;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: PHOTOSYSTEM II CP43 REACTION CENTER PROTEIN;
COMPND 12 CHAIN: C, c;
COMPND 13 SYNONYM: PSII 43 KDA PROTEIN,PROTEIN CP-43;
COMPND 14 MOL_ID: 4;
COMPND 15 MOLECULE: PHOTOSYSTEM II D2 PROTEIN;
COMPND 16 CHAIN: D, d;
COMPND 17 SYNONYM: PSII D2 PROTEIN,PHOTOSYSTEM II Q(A) PROTEIN;
COMPND 18 EC: 1.10.3.9;
COMPND 19 MOL_ID: 5;
COMPND 20 MOLECULE: CYTOCHROME B559 SUBUNIT ALPHA;
COMPND 21 CHAIN: E, e;
COMPND 22 SYNONYM: PSII REACTION CENTER SUBUNIT V;
COMPND 23 MOL_ID: 6;
COMPND 24 MOLECULE: CYTOCHROME B559 SUBUNIT BETA;
COMPND 25 CHAIN: F, f;
COMPND 26 SYNONYM: PSII REACTION CENTER SUBUNIT VI;
COMPND 27 MOL_ID: 7;
COMPND 28 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN H;
COMPND 29 CHAIN: H, h;
COMPND 30 SYNONYM: PSII-H;
COMPND 31 MOL_ID: 8;
COMPND 32 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN I;
COMPND 33 CHAIN: I, i;
COMPND 34 SYNONYM: PSII-I,PSII 4.4 KDA PROTEIN;
COMPND 35 MOL_ID: 9;
COMPND 36 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN J;
COMPND 37 CHAIN: J, j;
COMPND 38 SYNONYM: PSII-J;
COMPND 39 MOL_ID: 10;
COMPND 40 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN K;
COMPND 41 CHAIN: K, k;
COMPND 42 SYNONYM: PSII-K;
COMPND 43 MOL_ID: 11;
COMPND 44 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN L;
COMPND 45 CHAIN: L, l;
COMPND 46 SYNONYM: PSII-L;
COMPND 47 MOL_ID: 12;
COMPND 48 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN M;
COMPND 49 CHAIN: M, m;
COMPND 50 SYNONYM: PSII-M;
COMPND 51 MOL_ID: 13;
COMPND 52 MOLECULE: PHOTOSYSTEM II MANGANESE-STABILIZING POLYPEPTIDE;
COMPND 53 CHAIN: O, o;
COMPND 54 SYNONYM: MSP;
COMPND 55 MOL_ID: 14;
COMPND 56 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN T;
COMPND 57 CHAIN: T, t;
COMPND 58 SYNONYM: PSII-TC;
COMPND 59 MOL_ID: 15;
COMPND 60 MOLECULE: PHOTOSYSTEM II 12 KDA EXTRINSIC PROTEIN;
COMPND 61 CHAIN: U, u;
COMPND 62 SYNONYM: PS II COMPLEX 12 KDA EXTRINSIC PROTEIN,PSII-U;
COMPND 63 MOL_ID: 16;
COMPND 64 MOLECULE: CYTOCHROME C-550;
COMPND 65 CHAIN: V, v;
COMPND 66 SYNONYM: CYTOCHROME C-549,CYTOCHROME C550,LOW-POTENTIAL CYTOCHROME C;
COMPND 67 MOL_ID: 17;
COMPND 68 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN YCF12;
COMPND 69 CHAIN: Y, y;
COMPND 70 MOL_ID: 18;
COMPND 71 MOLECULE: PHOTOSYSTEM II REACTION CENTER X PROTEIN;
COMPND 72 CHAIN: X, x;
COMPND 73 MOL_ID: 19;
COMPND 74 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN Z;
COMPND 75 CHAIN: Z, z;
COMPND 76 SYNONYM: PSII-Z;
COMPND 77 MOL_ID: 20;
COMPND 78 MOLECULE: PHOTOSYSTEM II PROTEIN Y;
COMPND 79 CHAIN: R, r
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 3 ORGANISM_TAXID: 197221;
SOURCE 4 STRAIN: BP-1;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 7 ORGANISM_TAXID: 197221;
SOURCE 8 STRAIN: BP-1;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 11 ORGANISM_TAXID: 197221;
SOURCE 12 STRAIN: BP-1;
SOURCE 13 MOL_ID: 4;
SOURCE 14 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 15 ORGANISM_TAXID: 197221;
SOURCE 16 STRAIN: BP-1;
SOURCE 17 MOL_ID: 5;
SOURCE 18 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 19 ORGANISM_TAXID: 197221;
SOURCE 20 STRAIN: BP-1;
SOURCE 21 MOL_ID: 6;
SOURCE 22 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 23 ORGANISM_TAXID: 197221;
SOURCE 24 STRAIN: BP-1;
SOURCE 25 MOL_ID: 7;
SOURCE 26 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 27 ORGANISM_TAXID: 197221;
SOURCE 28 STRAIN: BP-1;
SOURCE 29 MOL_ID: 8;
SOURCE 30 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (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;
SOURCE 77 MOL_ID: 20;
SOURCE 78 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 79 ORGANISM_TAXID: 197221;
SOURCE 80 STRAIN: BP-1
KEYWDS PHOTOSYNTHESIS, METAL CLUSTER, EDTA, HYDROXYLAMINE, OXIDOREDUCTASE,
KEYWDS 2 THERMOSYNECHOCOCCUS ELONGATUS
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ZHANG,M.BOMMER,R.CHATTERJEE,R.HUSSAIN,J.KERN,J.YANO,H.DAU,H.DOBBEK,
AUTHOR 2 A.ZOUNI
REVDAT 5 20-NOV-19 5MX2 1 LINK
REVDAT 4 25-SEP-19 5MX2 1 REMARK LINK SITE
REVDAT 3 28-MAR-18 5MX2 1 JRNL
REVDAT 2 21-FEB-18 5MX2 1 JRNL
REVDAT 1 02-AUG-17 5MX2 0
JRNL AUTH M.ZHANG,M.BOMMER,R.CHATTERJEE,R.HUSSEIN,J.YANO,H.DAU,J.KERN,
JRNL AUTH 2 H.DOBBEK,A.ZOUNI
JRNL TITL STRUCTURAL INSIGHTS INTO THE LIGHT-DRIVEN AUTO-ASSEMBLY
JRNL TITL 2 PROCESS OF THE WATER-OXIDIZING MN4CAO5-CLUSTER IN
JRNL TITL 3 PHOTOSYSTEM II.
JRNL REF ELIFE V. 6 2017
JRNL REFN ESSN 2050-084X
JRNL PMID 28718766
JRNL DOI 10.7554/ELIFE.26933
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.65
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.6
REMARK 3 NUMBER OF REFLECTIONS : 364474
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 18225
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 49.6643 - 6.8221 1.00 13093 690 0.1599 0.1898
REMARK 3 2 6.8221 - 5.4170 1.00 12739 670 0.1607 0.2080
REMARK 3 3 5.4170 - 4.7329 1.00 12637 665 0.1502 0.1977
REMARK 3 4 4.7329 - 4.3004 1.00 12570 662 0.1505 0.2016
REMARK 3 5 4.3004 - 3.9923 1.00 12535 660 0.1583 0.2064
REMARK 3 6 3.9923 - 3.7570 1.00 12516 658 0.1685 0.2230
REMARK 3 7 3.7570 - 3.5689 1.00 12547 661 0.1794 0.2370
REMARK 3 8 3.5689 - 3.4136 1.00 12448 655 0.1891 0.2648
REMARK 3 9 3.4136 - 3.2822 1.00 12478 657 0.2001 0.2512
REMARK 3 10 3.2822 - 3.1690 1.00 12454 655 0.2120 0.2720
REMARK 3 11 3.1690 - 3.0699 1.00 12395 653 0.2284 0.2843
REMARK 3 12 3.0699 - 2.9822 1.00 12470 656 0.2304 0.2835
REMARK 3 13 2.9822 - 2.9037 1.00 12409 653 0.2309 0.2913
REMARK 3 14 2.9037 - 2.8328 1.00 12448 655 0.2367 0.3071
REMARK 3 15 2.8328 - 2.7684 1.00 12401 653 0.2418 0.2881
REMARK 3 16 2.7684 - 2.7095 1.00 12389 652 0.2495 0.3053
REMARK 3 17 2.7095 - 2.6553 1.00 12424 654 0.2587 0.3131
REMARK 3 18 2.6553 - 2.6052 1.00 12379 651 0.2765 0.3163
REMARK 3 19 2.6052 - 2.5587 1.00 12417 654 0.2872 0.3294
REMARK 3 20 2.5587 - 2.5153 0.99 12169 641 0.3024 0.3242
REMARK 3 21 2.5153 - 2.4748 0.96 11876 625 0.3152 0.3462
REMARK 3 22 2.4748 - 2.4367 0.90 11183 589 0.3241 0.3456
REMARK 3 23 2.4367 - 2.4009 0.87 10766 567 0.3420 0.3663
REMARK 3 24 2.4009 - 2.3670 0.83 10233 538 0.3514 0.3857
REMARK 3 25 2.3670 - 2.3351 0.79 9764 515 0.3664 0.3880
REMARK 3 26 2.3351 - 2.3047 0.76 9430 496 0.3748 0.4044
REMARK 3 27 2.3047 - 2.2759 0.73 8946 470 0.3824 0.4108
REMARK 3 28 2.2759 - 2.2485 0.69 8598 452 0.3936 0.4361
REMARK 3 29 2.2485 - 2.2223 0.66 8174 431 0.3979 0.4037
REMARK 3 30 2.2223 - 2.1974 0.60 7361 387 0.4098 0.4521
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.900
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.11
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.05
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 : 0.013 51587
REMARK 3 ANGLE : 1.179 70715
REMARK 3 CHIRALITY : 0.067 7098
REMARK 3 PLANARITY : 0.007 10859
REMARK 3 DIHEDRAL : 17.133 30460
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 5MX2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-JAN-17.
REMARK 100 THE DEPOSITION ID IS D_1200003131.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAY-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : SI-111 CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS VERSION OCT 15, 2015
REMARK 200 DATA SCALING SOFTWARE : XDS VERSION OCT 15, 2015
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 364603
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.197
REMARK 200 RESOLUTION RANGE LOW (A) : 49.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 11.20
REMARK 200 R MERGE (I) : 0.25000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.3400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 65.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : 3.27000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.440
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: 4PJ0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: EQUAL VOLUMES OF BUFFER: 0.1 M TRIS
REMARK 280 -HCL PH 7.5, 0.1 M (NH4)2SO4, 14-18 % PEG 5000 MME AND PROTEIN:
REMARK 280 2 MM CHLOROPHYLL EQUIVALENT OF PSII IN C12E8 DETERGENT, POST
REMARK 280 CRYSTALLISATION TREATMENT, MICROBATCH, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 58.16300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 152.02150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 109.80850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 152.02150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 58.16300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 109.80850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: EICOSAMERIC
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, R
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: EICOSAMERIC
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, x, r, y, z
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 THR A 3
REMARK 465 THR A 4
REMARK 465 LEU A 5
REMARK 465 GLN A 6
REMARK 465 ARG A 7
REMARK 465 ARG A 8
REMARK 465 GLU A 9
REMARK 465 SER A 10
REMARK 465 ALA A 11
REMARK 465 MET B 1
REMARK 465 LYS B 507
REMARK 465 GLU B 508
REMARK 465 ALA B 509
REMARK 465 VAL B 510
REMARK 465 MET C 13
REMARK 465 VAL C 14
REMARK 465 THR C 15
REMARK 465 LEU C 16
REMARK 465 SER C 17
REMARK 465 SER C 18
REMARK 465 ASN C 19
REMARK 465 SER C 20
REMARK 465 ILE C 21
REMARK 465 PHE C 22
REMARK 465 ALA C 23
REMARK 465 THR C 24
REMARK 465 ASN C 25
REMARK 465 ARG C 26
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 ILE D 3
REMARK 465 ALA D 4
REMARK 465 ILE D 5
REMARK 465 GLY D 6
REMARK 465 ARG D 7
REMARK 465 ALA D 8
REMARK 465 PRO D 9
REMARK 465 ALA D 10
REMARK 465 GLU D 11
REMARK 465 ARG D 12
REMARK 465 MET E 1
REMARK 465 ALA E 2
REMARK 465 LYS E 84
REMARK 465 MET F 1
REMARK 465 THR F 2
REMARK 465 SER F 3
REMARK 465 ASN F 4
REMARK 465 THR F 5
REMARK 465 PRO F 6
REMARK 465 ASN F 7
REMARK 465 GLN F 8
REMARK 465 GLU F 9
REMARK 465 PRO F 10
REMARK 465 VAL F 11
REMARK 465 SER F 12
REMARK 465 MET H 1
REMARK 465 ALA H 64
REMARK 465 LEU H 65
REMARK 465 GLY H 66
REMARK 465 ARG I 34
REMARK 465 LYS I 35
REMARK 465 ASP I 36
REMARK 465 LEU I 37
REMARK 465 GLU I 38
REMARK 465 MET J 1
REMARK 465 MET J 2
REMARK 465 SER J 3
REMARK 465 GLU J 4
REMARK 465 GLY J 5
REMARK 465 GLY J 6
REMARK 465 ARG J 7
REMARK 465 MET K 1
REMARK 465 ILE K 2
REMARK 465 ASP K 3
REMARK 465 ALA K 4
REMARK 465 LEU K 5
REMARK 465 VAL K 6
REMARK 465 LEU K 7
REMARK 465 VAL K 8
REMARK 465 ALA K 9
REMARK 465 LYS K 10
REMARK 465 ARG K 46
REMARK 465 MET L 1
REMARK 465 GLN M 33
REMARK 465 LYS M 34
REMARK 465 SER M 35
REMARK 465 SER M 36
REMARK 465 MET O -25
REMARK 465 LYS O -24
REMARK 465 TYR O -23
REMARK 465 ARG O -22
REMARK 465 ILE O -21
REMARK 465 LEU O -20
REMARK 465 MET O -19
REMARK 465 ALA O -18
REMARK 465 THR O -17
REMARK 465 LEU O -16
REMARK 465 LEU O -15
REMARK 465 ALA O -14
REMARK 465 VAL O -13
REMARK 465 CYS O -12
REMARK 465 LEU O -11
REMARK 465 GLY O -10
REMARK 465 ILE O -9
REMARK 465 PHE O -8
REMARK 465 SER O -7
REMARK 465 LEU O -6
REMARK 465 SER O -5
REMARK 465 ALA O -4
REMARK 465 PRO O -3
REMARK 465 ALA O -2
REMARK 465 PHE O -1
REMARK 465 ALA O 0
REMARK 465 ALA O 1
REMARK 465 LYS O 2
REMARK 465 GLN O 3
REMARK 465 ALA O 246
REMARK 465 ILE T 29
REMARK 465 THR T 30
REMARK 465 LYS T 31
REMARK 465 LYS T 32
REMARK 465 MET U -29
REMARK 465 GLN U -28
REMARK 465 ARG U -27
REMARK 465 LEU U -26
REMARK 465 GLY U -25
REMARK 465 ARG U -24
REMARK 465 TRP U -23
REMARK 465 LEU U -22
REMARK 465 ALA U -21
REMARK 465 LEU U -20
REMARK 465 ALA U -19
REMARK 465 TYR U -18
REMARK 465 PHE U -17
REMARK 465 VAL U -16
REMARK 465 GLY U -15
REMARK 465 VAL U -14
REMARK 465 SER U -13
REMARK 465 LEU U -12
REMARK 465 LEU U -11
REMARK 465 GLY U -10
REMARK 465 TRP U -9
REMARK 465 ILE U -8
REMARK 465 ASN U -7
REMARK 465 TRP U -6
REMARK 465 SER U -5
REMARK 465 ALA U -4
REMARK 465 PRO U -3
REMARK 465 THR U -2
REMARK 465 LEU U -1
REMARK 465 ALA U 0
REMARK 465 ALA U 1
REMARK 465 THR U 2
REMARK 465 ALA U 3
REMARK 465 SER U 4
REMARK 465 THR U 5
REMARK 465 GLU U 6
REMARK 465 GLU U 7
REMARK 465 GLU U 8
REMARK 465 MET V -25
REMARK 465 LEU V -24
REMARK 465 LYS V -23
REMARK 465 LYS V -22
REMARK 465 CYS V -21
REMARK 465 VAL V -20
REMARK 465 TRP V -19
REMARK 465 LEU V -18
REMARK 465 ALA V -17
REMARK 465 VAL V -16
REMARK 465 ALA V -15
REMARK 465 LEU V -14
REMARK 465 CYS V -13
REMARK 465 LEU V -12
REMARK 465 CYS V -11
REMARK 465 LEU V -10
REMARK 465 TRP V -9
REMARK 465 GLN V -8
REMARK 465 PHE V -7
REMARK 465 THR V -6
REMARK 465 MET V -5
REMARK 465 GLY V -4
REMARK 465 THR V -3
REMARK 465 ALA V -2
REMARK 465 LEU V -1
REMARK 465 ALA V 0
REMARK 465 MET Y 1
REMARK 465 GLY Y 2
REMARK 465 ILE Y 3
REMARK 465 PHE Y 4
REMARK 465 ASN Y 5
REMARK 465 GLY Y 6
REMARK 465 ILE Y 7
REMARK 465 ILE Y 8
REMARK 465 GLU Y 9
REMARK 465 PHE Y 10
REMARK 465 LEU Y 11
REMARK 465 SER Y 12
REMARK 465 ASN Y 13
REMARK 465 ILE Y 14
REMARK 465 ASN Y 15
REMARK 465 PHE Y 16
REMARK 465 GLU Y 17
REMARK 465 VAL Y 18
REMARK 465 ILE Y 19
REMARK 465 ALA Y 20
REMARK 465 GLN Y 21
REMARK 465 LEU Y 22
REMARK 465 THR Y 23
REMARK 465 MET Y 24
REMARK 465 ILE Y 25
REMARK 465 MET X 1
REMARK 465 ARG X 39
REMARK 465 SER X 40
REMARK 465 LEU X 41
REMARK 465 VAL Z 62
REMARK 465 MET a 1
REMARK 465 THR a 2
REMARK 465 THR a 3
REMARK 465 THR a 4
REMARK 465 LEU a 5
REMARK 465 GLN a 6
REMARK 465 ARG a 7
REMARK 465 ARG a 8
REMARK 465 GLU a 9
REMARK 465 SER a 10
REMARK 465 ALA a 11
REMARK 465 MET b 1
REMARK 465 ARG b 505
REMARK 465 ARG b 506
REMARK 465 LYS b 507
REMARK 465 GLU b 508
REMARK 465 ALA b 509
REMARK 465 VAL b 510
REMARK 465 MET c 13
REMARK 465 VAL c 14
REMARK 465 THR c 15
REMARK 465 LEU c 16
REMARK 465 SER c 17
REMARK 465 SER c 18
REMARK 465 ASN c 19
REMARK 465 SER c 20
REMARK 465 ILE c 21
REMARK 465 PHE c 22
REMARK 465 ALA c 23
REMARK 465 THR c 24
REMARK 465 ASN c 25
REMARK 465 MET d 1
REMARK 465 THR d 2
REMARK 465 ILE d 3
REMARK 465 ALA d 4
REMARK 465 ILE d 5
REMARK 465 GLY d 6
REMARK 465 ARG d 7
REMARK 465 ALA d 8
REMARK 465 PRO d 9
REMARK 465 ALA d 10
REMARK 465 GLU d 11
REMARK 465 ARG d 12
REMARK 465 MET e 1
REMARK 465 ALA e 2
REMARK 465 GLY e 3
REMARK 465 THR e 4
REMARK 465 LYS e 84
REMARK 465 MET f 1
REMARK 465 THR f 2
REMARK 465 SER f 3
REMARK 465 ASN f 4
REMARK 465 THR f 5
REMARK 465 PRO f 6
REMARK 465 ASN f 7
REMARK 465 GLN f 8
REMARK 465 GLU f 9
REMARK 465 PRO f 10
REMARK 465 VAL f 11
REMARK 465 SER f 12
REMARK 465 MET h 1
REMARK 465 LEU h 65
REMARK 465 GLY h 66
REMARK 465 ARG i 34
REMARK 465 LYS i 35
REMARK 465 ASP i 36
REMARK 465 LEU i 37
REMARK 465 GLU i 38
REMARK 465 MET j 1
REMARK 465 MET j 2
REMARK 465 SER j 3
REMARK 465 GLU j 4
REMARK 465 GLY j 5
REMARK 465 GLY j 6
REMARK 465 ARG j 7
REMARK 465 MET k 1
REMARK 465 ILE k 2
REMARK 465 ASP k 3
REMARK 465 ALA k 4
REMARK 465 LEU k 5
REMARK 465 VAL k 6
REMARK 465 LEU k 7
REMARK 465 VAL k 8
REMARK 465 ALA k 9
REMARK 465 LYS k 10
REMARK 465 MET l 1
REMARK 465 GLN m 33
REMARK 465 LYS m 34
REMARK 465 SER m 35
REMARK 465 SER m 36
REMARK 465 MET o -25
REMARK 465 LYS o -24
REMARK 465 TYR o -23
REMARK 465 ARG o -22
REMARK 465 ILE o -21
REMARK 465 LEU o -20
REMARK 465 MET o -19
REMARK 465 ALA o -18
REMARK 465 THR o -17
REMARK 465 LEU o -16
REMARK 465 LEU o -15
REMARK 465 ALA o -14
REMARK 465 VAL o -13
REMARK 465 CYS o -12
REMARK 465 LEU o -11
REMARK 465 GLY o -10
REMARK 465 ILE o -9
REMARK 465 PHE o -8
REMARK 465 SER o -7
REMARK 465 LEU o -6
REMARK 465 SER o -5
REMARK 465 ALA o -4
REMARK 465 PRO o -3
REMARK 465 ALA o -2
REMARK 465 PHE o -1
REMARK 465 ALA o 0
REMARK 465 ALA o 1
REMARK 465 LYS o 2
REMARK 465 GLN o 3
REMARK 465 THR o 4
REMARK 465 ALA o 246
REMARK 465 THR t 30
REMARK 465 LYS t 31
REMARK 465 LYS t 32
REMARK 465 MET u -29
REMARK 465 GLN u -28
REMARK 465 ARG u -27
REMARK 465 LEU u -26
REMARK 465 GLY u -25
REMARK 465 ARG u -24
REMARK 465 TRP u -23
REMARK 465 LEU u -22
REMARK 465 ALA u -21
REMARK 465 LEU u -20
REMARK 465 ALA u -19
REMARK 465 TYR u -18
REMARK 465 PHE u -17
REMARK 465 VAL u -16
REMARK 465 GLY u -15
REMARK 465 VAL u -14
REMARK 465 SER u -13
REMARK 465 LEU u -12
REMARK 465 LEU u -11
REMARK 465 GLY u -10
REMARK 465 TRP u -9
REMARK 465 ILE u -8
REMARK 465 ASN u -7
REMARK 465 TRP u -6
REMARK 465 SER u -5
REMARK 465 ALA u -4
REMARK 465 PRO u -3
REMARK 465 THR u -2
REMARK 465 LEU u -1
REMARK 465 ALA u 0
REMARK 465 ALA u 1
REMARK 465 THR u 2
REMARK 465 ALA u 3
REMARK 465 SER u 4
REMARK 465 THR u 5
REMARK 465 GLU u 6
REMARK 465 GLU u 7
REMARK 465 GLU u 8
REMARK 465 MET v -25
REMARK 465 LEU v -24
REMARK 465 LYS v -23
REMARK 465 LYS v -22
REMARK 465 CYS v -21
REMARK 465 VAL v -20
REMARK 465 TRP v -19
REMARK 465 LEU v -18
REMARK 465 ALA v -17
REMARK 465 VAL v -16
REMARK 465 ALA v -15
REMARK 465 LEU v -14
REMARK 465 CYS v -13
REMARK 465 LEU v -12
REMARK 465 CYS v -11
REMARK 465 LEU v -10
REMARK 465 TRP v -9
REMARK 465 GLN v -8
REMARK 465 PHE v -7
REMARK 465 THR v -6
REMARK 465 MET v -5
REMARK 465 GLY v -4
REMARK 465 THR v -3
REMARK 465 ALA v -2
REMARK 465 LEU v -1
REMARK 465 ALA v 0
REMARK 465 MET x 1
REMARK 465 SER x 40
REMARK 465 LEU x 41
REMARK 465 MET R 1
REMARK 465 LYS R 37
REMARK 465 ALA R 38
REMARK 465 LYS R 39
REMARK 465 ALA R 40
REMARK 465 ALA R 41
REMARK 465 MET r 1
REMARK 465 ASP r 2
REMARK 465 LEU r 35
REMARK 465 GLN r 36
REMARK 465 LYS r 37
REMARK 465 ALA r 38
REMARK 465 LYS r 39
REMARK 465 ALA r 40
REMARK 465 ALA r 41
REMARK 465 MET y 1
REMARK 465 GLY y 2
REMARK 465 ILE y 3
REMARK 465 PHE y 4
REMARK 465 ASN y 5
REMARK 465 GLY y 6
REMARK 465 ILE y 7
REMARK 465 ILE y 8
REMARK 465 GLU y 9
REMARK 465 PHE y 10
REMARK 465 LEU y 11
REMARK 465 SER y 12
REMARK 465 ASN y 13
REMARK 465 ILE y 14
REMARK 465 ASN y 15
REMARK 465 PHE y 16
REMARK 465 GLU y 17
REMARK 465 VAL y 18
REMARK 465 ILE y 19
REMARK 465 ALA y 20
REMARK 465 GLN y 21
REMARK 465 LEU y 22
REMARK 465 THR y 23
REMARK 465 VAL z 62
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 OH TYR d 141 O4 LHG b 628 1.99
REMARK 500 O HOH c 657 O HOH c 665 2.01
REMARK 500 O ALA b 155 OG1 THR b 159 2.03
REMARK 500 O ILE D 144 OG SER D 147 2.03
REMARK 500 O ALA B 155 OG1 THR B 159 2.04
REMARK 500 OG1 THR a 286 O1D CLA a 404 2.06
REMARK 500 NH2 ARG b 357 O GLU d 337 2.07
REMARK 500 O ALA c 411 O HOH c 601 2.07
REMARK 500 OD1 ASP B 119 O HOH B 701 2.08
REMARK 500 OG1 THR O 75 O HOH O 301 2.08
REMARK 500 NH2 ARG L 7 O8 SQD L 101 2.09
REMARK 500 O ASP Z 32 OG SER Z 36 2.10
REMARK 500 NH2 ARG U 39 O ALA V 60 2.10
REMARK 500 OE1 GLU D 302 OH TYR D 315 2.11
REMARK 500 OH TYR D 296 O HOH D 501 2.11
REMARK 500 O ALA o 111 O HOH o 301 2.11
REMARK 500 OG1 THR v 56 O HOH v 301 2.11
REMARK 500 O GLY a 299 O HOH a 501 2.12
REMARK 500 OD2 ASP v 83 O HOH v 302 2.12
REMARK 500 OG SER a 232 O5 LHG l 101 2.13
REMARK 500 OD2 ASP U 26 OG1 THR U 85 2.13
REMARK 500 O GLU L 2 O HOH L 201 2.13
REMARK 500 O ASN o 155 O HOH o 302 2.14
REMARK 500 O TRP c 359 O HOH c 602 2.14
REMARK 500 OG SER a 86 O HOH a 502 2.14
REMARK 500 OE1 GLU D 344 O HOH D 502 2.14
REMARK 500 O5E DGD c 517 O3 LMG c 519 2.14
REMARK 500 O GLU a 231 O HOH a 503 2.14
REMARK 500 OG SER B 74 OE2 GLU B 94 2.16
REMARK 500 O HOH A 558 O HOH C 651 2.16
REMARK 500 OD1 ASP B 276 O HOH B 702 2.16
REMARK 500 OG1 THR D 316 O HOH D 503 2.16
REMARK 500 O GLN Z 31 N TRP Z 33 2.16
REMARK 500 OE1 GLN f 41 O4 LMG f 101 2.16
REMARK 500 O ASP c 27 OG SER c 31 2.16
REMARK 500 OD2 ASP B 433 OG1 THR B 436 2.17
REMARK 500 OG SER a 101 O HOH a 504 2.17
REMARK 500 NH2 ARG o 189 O HOH o 303 2.17
REMARK 500 O ASP c 360 O2E DGD c 516 2.17
REMARK 500 OH TYR D 141 O4 LHG D 406 2.17
REMARK 500 O ARG b 124 NH2 ARG h 12 2.17
REMARK 500 O GLY o 28 O HOH o 304 2.18
REMARK 500 O TYR c 82 O HOH c 603 2.18
REMARK 500 O HOH b 756 O HOH b 767 2.18
REMARK 500 OD2 ASP C 473 O HOH C 601 2.18
REMARK 500 OE2 GLU c 300 O HOH c 604 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ALA c 399 C PRO c 400 N -0.145
REMARK 500 ILE e 63 C PRO e 64 N -0.206
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 B 476 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG D 233 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG c 135 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG r 4 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 LEU z 39 CA - CB - CG ANGL. DEV. = 21.0 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 -79.54 -91.80
REMARK 500 SER A 167 132.28 -175.14
REMARK 500 TYR A 235 2.07 -68.99
REMARK 500 PHE A 239 106.71 -51.79
REMARK 500 ILE A 259 -95.75 -108.67
REMARK 500 TYR B 117 53.96 -112.65
REMARK 500 PHE B 162 72.69 -163.82
REMARK 500 THR B 175 51.83 -142.70
REMARK 500 ASP B 188 6.41 -65.09
REMARK 500 ASP B 313 47.42 -93.26
REMARK 500 ALA B 320 44.72 -100.61
REMARK 500 LYS B 321 21.27 -148.02
REMARK 500 ARG B 326 91.80 -68.25
REMARK 500 ASP C 205 108.78 -46.50
REMARK 500 GLU C 221 -87.12 -113.25
REMARK 500 TRP C 223 -143.42 49.27
REMARK 500 THR C 295 -66.30 -102.55
REMARK 500 PRO C 400 73.36 -67.94
REMARK 500 SER C 416 -50.99 167.88
REMARK 500 ARG D 26 -166.41 -119.79
REMARK 500 VAL D 30 -73.43 -105.40
REMARK 500 SER D 57 22.36 -146.98
REMARK 500 SER D 65 7.86 -161.47
REMARK 500 LEU D 158 -62.10 -109.98
REMARK 500 ALA D 234 31.98 -83.50
REMARK 500 ALA D 351 -61.82 72.37
REMARK 500 PRO E 52 -17.97 -49.78
REMARK 500 ASN H 15 64.27 -116.41
REMARK 500 SER I 25 44.67 -79.17
REMARK 500 SER J 39 -12.82 75.64
REMARK 500 ARG O 42 118.07 -167.38
REMARK 500 LYS O 57 -93.79 -57.19
REMARK 500 ASN O 58 34.83 -144.69
REMARK 500 ARG O 60 18.53 57.33
REMARK 500 GLU O 62 100.12 -37.38
REMARK 500 ARG O 73 -159.44 60.86
REMARK 500 GLU O 98 -61.61 -124.17
REMARK 500 ILE O 101 77.12 -67.22
REMARK 500 ASN O 132 77.10 54.52
REMARK 500 LEU O 164 -68.46 -104.90
REMARK 500 LEU O 192 97.70 -160.88
REMARK 500 THR O 193 -169.22 -101.58
REMARK 500 SER O 221 -157.89 -87.13
REMARK 500 LEU U 27 2.51 -66.87
REMARK 500 ASN U 99 89.80 -167.41
REMARK 500 TYR U 103 -89.18 -108.99
REMARK 500 LEU V 12 -67.37 -91.67
REMARK 500 ASN V 13 -161.38 -110.54
REMARK 500 ASN V 49 80.69 -170.61
REMARK 500 ASN V 78 77.08 -157.82
REMARK 500
REMARK 500 THIS ENTRY HAS 122 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA a 81 VAL a 82 149.42
REMARK 500 ARG z 35 SER z 36 -145.75
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 LFA A 410
REMARK 610 LFA A 413
REMARK 610 LMG B 619
REMARK 610 LFA B 620
REMARK 610 LMG B 621
REMARK 610 LFA B 622
REMARK 610 LFA B 623
REMARK 610 LFA B 624
REMARK 610 LFA B 625
REMARK 610 LFA B 626
REMARK 610 LFA B 627
REMARK 610 LFA B 628
REMARK 610 LMG C 501
REMARK 610 DGD C 517
REMARK 610 DGD C 518
REMARK 610 DGD C 519
REMARK 610 LMG C 520
REMARK 610 LFA C 521
REMARK 610 LMG C 522
REMARK 610 LMG D 409
REMARK 610 LFA D 410
REMARK 610 SQD D 411
REMARK 610 LFA D 412
REMARK 610 LFA D 413
REMARK 610 LHG E 101
REMARK 610 DGD H 103
REMARK 610 LFA I 101
REMARK 610 LFA J 101
REMARK 610 SQD L 101
REMARK 610 LFA M 101
REMARK 610 LFA M 102
REMARK 610 LFA T 102
REMARK 610 LFA a 411
REMARK 610 SQD a 412
REMARK 610 LFA b 602
REMARK 610 LFA b 622
REMARK 610 LFA b 623
REMARK 610 LMG b 624
REMARK 610 LFA b 625
REMARK 610 LFA b 626
REMARK 610 LFA b 627
REMARK 610 LFA b 629
REMARK 610 LFA b 630
REMARK 610 LMG c 501
REMARK 610 DGD c 516
REMARK 610 DGD c 517
REMARK 610 DGD c 518
REMARK 610 LMG c 519
REMARK 610 LFA c 520
REMARK 610 LFA c 521
REMARK 610 LMG c 522
REMARK 610 LFA d 408
REMARK 610 LFA d 409
REMARK 610 LFA d 410
REMARK 610 LHG e 101
REMARK 610 LMG f 101
REMARK 610 SQD f 102
REMARK 610 DGD h 102
REMARK 610 LFA i 101
REMARK 610 LFA i 102
REMARK 610 LFA j 101
REMARK 610 LFA m 101
REMARK 610 LFA m 102
REMARK 610 LMG m 103
REMARK 610 LFA t 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 FE A 414 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 215 NE2
REMARK 620 2 HIS A 272 NE2 95.8
REMARK 620 3 HIS D 214 NE2 104.5 91.1
REMARK 620 4 HIS D 268 NE2 86.6 170.4 97.4
REMARK 620 5 BCT A 415 O1 102.2 75.7 151.2 94.7
REMARK 620 6 BCT A 415 O2 158.1 94.2 94.8 80.5 61.6
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 104.9
REMARK 620 3 CLA C 512 NB 99.2 89.6
REMARK 620 4 CLA C 512 NC 89.8 165.0 90.8
REMARK 620 5 CLA C 512 ND 94.7 92.7 164.8 83.1
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 88.2
REMARK 620 3 HEM E 102 NB 91.3 90.2
REMARK 620 4 HEM E 102 NC 86.6 174.7 90.8
REMARK 620 5 HEM E 102 ND 83.9 88.9 175.1 89.6
REMARK 620 6 HIS F 24 NE2 175.1 87.3 90.6 97.9 94.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM V 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS V 41 NE2
REMARK 620 2 HEM V 201 NA 99.3
REMARK 620 3 HEM V 201 NB 91.8 91.0
REMARK 620 4 HEM V 201 NC 85.7 174.1 91.9
REMARK 620 5 HEM V 201 ND 93.1 88.3 175.1 88.4
REMARK 620 6 HIS V 92 NE2 174.0 84.2 93.1 90.6 82.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE a 401 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS a 215 NE2
REMARK 620 2 HIS a 272 NE2 93.0
REMARK 620 3 HIS d 214 NE2 104.5 92.3
REMARK 620 4 HIS d 268 NE2 85.7 167.2 100.3
REMARK 620 5 BCT a 413 O1 156.0 95.2 97.7 81.3
REMARK 620 6 BCT a 413 O2 98.9 73.1 153.0 94.5 62.3
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 108.4
REMARK 620 3 CLA c 512 NB 100.6 89.6
REMARK 620 4 CLA c 512 NC 87.1 164.2 90.9
REMARK 620 5 CLA c 512 ND 94.0 92.6 163.8 82.7
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 94.4
REMARK 620 3 HEM e 102 NB 100.8 90.5
REMARK 620 4 HEM e 102 NC 89.5 173.9 93.3
REMARK 620 5 HEM e 102 ND 83.6 87.1 175.1 88.8
REMARK 620 6 HIS f 24 NE2 170.4 82.8 88.4 92.6 87.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM v 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS v 41 NE2
REMARK 620 2 HEM v 201 NA 105.9
REMARK 620 3 HEM v 201 NB 90.6 90.2
REMARK 620 4 HEM v 201 NC 78.6 174.4 93.1
REMARK 620 5 HEM v 201 ND 94.4 86.8 174.7 89.6
REMARK 620 6 HIS v 92 NE2 170.9 81.7 94.5 93.5 80.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA A 404 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 531 O
REMARK 620 2 CLA A 404 NA 97.5
REMARK 620 3 CLA A 404 NB 108.9 88.8
REMARK 620 4 CLA A 404 NC 92.3 169.4 91.9
REMARK 620 5 CLA A 404 ND 82.3 94.0 168.0 83.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA A 412 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 540 O
REMARK 620 2 CLA A 412 NA 99.1
REMARK 620 3 CLA A 412 NB 96.0 89.5
REMARK 620 4 CLA A 412 NC 91.4 169.2 92.1
REMARK 620 5 CLA A 412 ND 95.7 93.5 167.3 82.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B 606 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 762 O
REMARK 620 2 CLA B 606 NA 97.6
REMARK 620 3 CLA B 606 NB 104.5 88.7
REMARK 620 4 CLA B 606 NC 96.7 165.2 91.5
REMARK 620 5 CLA B 606 ND 92.9 93.2 162.1 82.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B 609 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 748 O
REMARK 620 2 CLA B 609 NA 92.5
REMARK 620 3 CLA B 609 NB 100.9 89.6
REMARK 620 4 CLA B 609 NC 96.1 170.8 92.0
REMARK 620 5 CLA B 609 ND 89.5 93.7 169.1 83.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C 505 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 649 O
REMARK 620 2 CLA C 505 NA 90.7
REMARK 620 3 CLA C 505 NB 96.3 88.5
REMARK 620 4 CLA C 505 NC 103.8 165.3 92.2
REMARK 620 5 CLA C 505 ND 95.3 94.5 168.0 81.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C 508 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 604 O
REMARK 620 2 CLA C 508 NA 80.7
REMARK 620 3 CLA C 508 NB 104.1 89.4
REMARK 620 4 CLA C 508 NC 110.4 168.1 92.1
REMARK 620 5 CLA C 508 ND 91.8 93.3 164.1 82.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA H 101 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 755 O
REMARK 620 2 CLA H 101 NA 94.1
REMARK 620 3 CLA H 101 NB 98.1 89.8
REMARK 620 4 CLA H 101 NC 97.1 168.3 91.9
REMARK 620 5 CLA H 101 ND 95.0 93.2 166.4 82.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA a 405 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH a 544 O
REMARK 620 2 CLA a 405 NA 86.1
REMARK 620 3 CLA a 405 NB 98.6 88.6
REMARK 620 4 CLA a 405 NC 106.8 166.9 91.5
REMARK 620 5 CLA a 405 ND 93.9 93.7 167.4 83.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA b 603 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH b 734 O
REMARK 620 2 CLA b 603 NA 95.8
REMARK 620 3 CLA b 603 NB 107.7 89.2
REMARK 620 4 CLA b 603 NC 94.2 169.0 92.1
REMARK 620 5 CLA b 603 ND 86.2 93.8 165.3 82.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA b 609 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH b 756 O
REMARK 620 2 CLA b 609 NA 90.8
REMARK 620 3 CLA b 609 NB 100.5 87.9
REMARK 620 4 CLA b 609 NC 103.1 165.8 92.5
REMARK 620 5 CLA b 609 ND 93.7 93.8 165.7 82.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA b 612 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH b 723 O
REMARK 620 2 CLA b 612 NA 97.2
REMARK 620 3 CLA b 612 NB 97.0 89.2
REMARK 620 4 CLA b 612 NC 95.9 166.6 91.9
REMARK 620 5 CLA b 612 ND 99.5 92.2 163.1 83.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA c 505 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH c 655 O
REMARK 620 2 CLA c 505 NA 98.8
REMARK 620 3 CLA c 505 NB 101.8 88.6
REMARK 620 4 CLA c 505 NC 96.2 164.6 91.5
REMARK 620 5 CLA c 505 ND 92.1 93.5 165.4 82.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA c 508 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH c 637 O
REMARK 620 2 CLA c 508 NA 92.7
REMARK 620 3 CLA c 508 NB 109.3 89.9
REMARK 620 4 CLA c 508 NC 98.0 168.2 91.3
REMARK 620 5 CLA c 508 ND 84.9 92.8 165.4 83.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA d 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH d 542 O
REMARK 620 2 CLA d 401 NA 95.0
REMARK 620 3 CLA d 401 NB 97.9 89.4
REMARK 620 4 CLA d 401 NC 95.6 169.0 92.1
REMARK 620 5 CLA d 401 ND 93.0 94.2 168.2 82.3
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA A 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE A 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT A 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA B 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA B 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA B 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA B 624
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA B 625
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA B 626
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA B 627
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA B 628
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA C 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 522
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 D 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG D 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG D 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG D 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG D 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA D 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD D 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA D 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA D 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG E 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM E 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA H 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR H 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD H 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA I 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA J 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR K 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR K 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD L 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG L 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA M 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA M 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR T 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA T 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM V 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE a 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO a 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR a 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 a 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD a 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA a 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD a 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT a 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO a 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD b 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA b 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA b 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA b 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG b 624
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA b 625
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA b 626
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA b 627
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG b 628
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA b 629
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA b 630
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA c 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA c 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 522
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 523
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 524
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR d 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 d 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG d 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG d 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA d 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA d 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG e 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM e 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG f 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD f 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR h 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD h 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA i 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA j 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR k 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AW1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG l 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AW2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA m 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AW3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA m 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AW4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG m 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AW5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA t 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AW6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR t 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AW7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide HEM v 201 and CYS v
REMARK 800 40
REMARK 800
REMARK 800 SITE_IDENTIFIER: AW8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide HEM v 201 and CYS v
REMARK 800 37
DBREF 5MX2 A 1 344 UNP P0A444 PSBA1_THEEB 1 344
DBREF 5MX2 B 1 510 UNP Q8DIQ1 PSBB_THEEB 1 510
DBREF 5MX2 C 13 473 UNP Q8DIF8 PSBC_THEEB 1 461
DBREF 5MX2 D 1 352 UNP Q8CM25 PSBD_THEEB 1 352
DBREF 5MX2 E 1 84 UNP Q8DIP0 PSBE_THEEB 1 84
DBREF 5MX2 F 1 45 UNP Q8DIN9 PSBF_THEEB 1 45
DBREF 5MX2 H 1 66 UNP Q8DJ43 PSBH_THEEB 1 66
DBREF 5MX2 I 1 38 UNP Q8DJZ6 PSBI_THEEB 1 38
DBREF 5MX2 J 1 40 UNP P59087 PSBJ_THEEB 1 40
DBREF 5MX2 K 1 46 UNP Q9F1K9 PSBK_THEEB 1 46
DBREF 5MX2 L 1 37 UNP Q8DIN8 PSBL_THEEB 1 37
DBREF 5MX2 M 1 36 UNP Q8DHA7 PSBM_THEEB 1 36
DBREF 5MX2 O -25 246 UNP P0A431 PSBO_THEEB 1 272
DBREF 5MX2 T 1 32 UNP Q8DIQ0 PSBT_THEEB 1 32
DBREF 5MX2 U -29 104 UNP Q9F1L5 PSBU_THEEB 1 134
DBREF 5MX2 V -25 137 UNP P0A386 CY550_THEEB 1 163
DBREF 5MX2 Y 1 46 UNP Q8DJI1 YCF12_THEEB 1 46
DBREF 5MX2 X 1 41 UNP Q9F1R6 PSBX_THEEB 1 41
DBREF 5MX2 Z 1 62 UNP Q8DHJ2 PSBZ_THEEB 1 62
DBREF 5MX2 a 1 344 UNP P0A444 PSBA1_THEEB 1 344
DBREF 5MX2 b 1 510 UNP Q8DIQ1 PSBB_THEEB 1 510
DBREF 5MX2 c 13 473 UNP Q8DIF8 PSBC_THEEB 1 461
DBREF 5MX2 d 1 352 UNP Q8CM25 PSBD_THEEB 1 352
DBREF 5MX2 e 1 84 UNP Q8DIP0 PSBE_THEEB 1 84
DBREF 5MX2 f 1 45 UNP Q8DIN9 PSBF_THEEB 1 45
DBREF 5MX2 h 1 66 UNP Q8DJ43 PSBH_THEEB 1 66
DBREF 5MX2 i 1 38 UNP Q8DJZ6 PSBI_THEEB 1 38
DBREF 5MX2 j 1 40 UNP P59087 PSBJ_THEEB 1 40
DBREF 5MX2 k 1 46 UNP Q9F1K9 PSBK_THEEB 1 46
DBREF 5MX2 l 1 37 UNP Q8DIN8 PSBL_THEEB 1 37
DBREF 5MX2 m 1 36 UNP Q8DHA7 PSBM_THEEB 1 36
DBREF 5MX2 o -25 246 UNP P0A431 PSBO_THEEB 1 272
DBREF 5MX2 t 1 32 UNP Q8DIQ0 PSBT_THEEB 1 32
DBREF 5MX2 u -29 104 UNP Q9F1L5 PSBU_THEEB 1 134
DBREF 5MX2 v -25 137 UNP P0A386 CY550_THEEB 1 163
DBREF 5MX2 x 1 41 UNP Q9F1R6 PSBX_THEEB 1 41
DBREF 5MX2 R 1 41 UNP Q8DKM3 PSBY_THEEB 1 41
DBREF 5MX2 r 1 41 UNP Q8DKM3 PSBY_THEEB 1 41
DBREF 5MX2 y 1 46 UNP Q8DJI1 YCF12_THEEB 1 46
DBREF 5MX2 z 1 62 UNP Q8DHJ2 PSBZ_THEEB 1 62
SEQRES 1 A 344 MET THR THR THR LEU GLN ARG ARG GLU SER ALA ASN LEU
SEQRES 2 A 344 TRP GLU ARG PHE CYS ASN TRP VAL THR SER THR ASP ASN
SEQRES 3 A 344 ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE MET ILE PRO
SEQRES 4 A 344 THR LEU LEU ALA ALA THR ILE CYS PHE VAL ILE ALA PHE
SEQRES 5 A 344 ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY ILE ARG GLU
SEQRES 6 A 344 PRO VAL SER GLY SER LEU LEU TYR GLY ASN ASN ILE ILE
SEQRES 7 A 344 THR GLY ALA VAL VAL PRO SER SER ASN ALA ILE GLY LEU
SEQRES 8 A 344 HIS PHE TYR PRO ILE TRP GLU ALA ALA SER LEU ASP GLU
SEQRES 9 A 344 TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU ILE ILE PHE
SEQRES 10 A 344 HIS PHE LEU LEU GLY ALA SER CYS TYR MET GLY ARG GLN
SEQRES 11 A 344 TRP GLU LEU SER TYR ARG LEU GLY MET ARG PRO TRP ILE
SEQRES 12 A 344 CYS VAL ALA TYR SER ALA PRO LEU ALA SER ALA PHE ALA
SEQRES 13 A 344 VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY SER PHE SER
SEQRES 14 A 344 ASP GLY MET PRO LEU GLY ILE SER GLY THR PHE ASN PHE
SEQRES 15 A 344 MET ILE VAL PHE GLN ALA GLU HIS ASN ILE LEU MET HIS
SEQRES 16 A 344 PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL PHE GLY GLY
SEQRES 17 A 344 ALA LEU PHE CYS ALA MET HIS GLY SER LEU VAL THR SER
SEQRES 18 A 344 SER LEU ILE ARG GLU THR THR GLU THR GLU SER ALA ASN
SEQRES 19 A 344 TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU THR TYR ASN
SEQRES 20 A 344 ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG LEU ILE PHE
SEQRES 21 A 344 GLN TYR ALA SER PHE ASN ASN SER ARG SER LEU HIS PHE
SEQRES 22 A 344 PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL TRP PHE THR
SEQRES 23 A 344 ALA LEU GLY ILE SER THR MET ALA PHE ASN LEU ASN GLY
SEQRES 24 A 344 PHE ASN PHE ASN HIS SER VAL ILE ASP ALA LYS GLY ASN
SEQRES 25 A 344 VAL ILE ASN THR TRP ALA ASP ILE ILE ASN ARG ALA ASN
SEQRES 26 A 344 LEU GLY MET GLU VAL MET HIS GLU ARG ASN ALA HIS ASN
SEQRES 27 A 344 PHE PRO LEU ASP LEU ALA
SEQRES 1 B 510 MET GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE
SEQRES 2 B 510 ASN ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS
SEQRES 3 B 510 THR ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU
SEQRES 4 B 510 TYR GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU
SEQRES 5 B 510 ASN PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE
SEQRES 6 B 510 MET ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP
SEQRES 7 B 510 SER ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP
SEQRES 8 B 510 SER PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER
SEQRES 9 B 510 GLY LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR
SEQRES 10 B 510 TRP ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU
SEQRES 11 B 510 PRO ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU
SEQRES 12 B 510 PHE LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE
SEQRES 13 B 510 HIS LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER
SEQRES 14 B 510 ASP PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA
SEQRES 15 B 510 PRO GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO
SEQRES 16 B 510 GLY GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL
SEQRES 17 B 510 GLY ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO
SEQRES 18 B 510 PRO GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE
SEQRES 19 B 510 GLU THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE
SEQRES 20 B 510 ALA ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER
SEQRES 21 B 510 ALA THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR
SEQRES 22 B 510 GLN TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG
SEQRES 23 B 510 ARG VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU
SEQRES 24 B 510 GLU ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR
SEQRES 25 B 510 ASP TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE
SEQRES 26 B 510 ARG THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN
SEQRES 27 B 510 ALA TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY
SEQRES 28 B 510 GLU GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU
SEQRES 29 B 510 SER PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL
SEQRES 30 B 510 LYS ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR
SEQRES 31 B 510 SER PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY
SEQRES 32 B 510 GLY GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR
SEQRES 33 B 510 VAL LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE
SEQRES 34 B 510 PHE GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE
SEQRES 35 B 510 PHE ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS
SEQRES 36 B 510 ALA VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP
SEQRES 37 B 510 HIS GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY
SEQRES 38 B 510 ILE ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY
SEQRES 39 B 510 PHE TYR GLN LYS VAL GLY ASP VAL THR THR ARG ARG LYS
SEQRES 40 B 510 GLU ALA VAL
SEQRES 1 C 461 MET VAL THR LEU SER SER ASN SER ILE PHE ALA THR ASN
SEQRES 2 C 461 ARG ASP GLN GLU SER SER GLY PHE ALA TRP TRP ALA GLY
SEQRES 3 C 461 ASN ALA ARG LEU ILE ASN LEU SER GLY LYS LEU LEU GLY
SEQRES 4 C 461 ALA HIS VAL ALA HIS ALA GLY LEU ILE VAL PHE TRP ALA
SEQRES 5 C 461 GLY ALA MET THR LEU PHE GLU LEU ALA HIS PHE ILE PRO
SEQRES 6 C 461 GLU LYS PRO MET TYR GLU GLN GLY LEU ILE LEU ILE PRO
SEQRES 7 C 461 HIS ILE ALA THR LEU GLY TRP GLY VAL GLY PRO GLY GLY
SEQRES 8 C 461 GLU VAL VAL ASP THR PHE PRO PHE PHE VAL VAL GLY VAL
SEQRES 9 C 461 VAL HIS LEU ILE SER SER ALA VAL LEU GLY PHE GLY GLY
SEQRES 10 C 461 VAL TYR HIS ALA ILE ARG GLY PRO GLU THR LEU GLU GLU
SEQRES 11 C 461 TYR SER SER PHE PHE GLY TYR ASP TRP LYS ASP LYS ASN
SEQRES 12 C 461 LYS MET THR THR ILE LEU GLY PHE HIS LEU ILE VAL LEU
SEQRES 13 C 461 GLY ILE GLY ALA LEU LEU LEU VAL ALA LYS ALA MET PHE
SEQRES 14 C 461 PHE GLY GLY LEU TYR ASP THR TRP ALA PRO GLY GLY GLY
SEQRES 15 C 461 ASP VAL ARG VAL ILE THR ASN PRO THR LEU ASP PRO ARG
SEQRES 16 C 461 VAL ILE PHE GLY TYR LEU LEU LYS SER PRO PHE GLY GLY
SEQRES 17 C 461 GLU GLY TRP ILE VAL SER VAL ASN ASN LEU GLU ASP VAL
SEQRES 18 C 461 VAL GLY GLY HIS ILE TRP ILE GLY LEU ILE CYS ILE ALA
SEQRES 19 C 461 GLY GLY ILE TRP HIS ILE LEU THR THR PRO PHE GLY TRP
SEQRES 20 C 461 ALA ARG ARG ALA PHE ILE TRP SER GLY GLU ALA TYR LEU
SEQRES 21 C 461 SER TYR SER LEU GLY ALA LEU SER MET MET GLY PHE ILE
SEQRES 22 C 461 ALA THR CYS PHE VAL TRP PHE ASN ASN THR VAL TYR PRO
SEQRES 23 C 461 SER GLU PHE TYR GLY PRO THR GLY PRO GLU ALA SER GLN
SEQRES 24 C 461 ALA GLN ALA MET THR PHE LEU ILE ARG ASP GLN LYS LEU
SEQRES 25 C 461 GLY ALA ASN VAL GLY SER ALA GLN GLY PRO THR GLY LEU
SEQRES 26 C 461 GLY LYS TYR LEU MET ARG SER PRO THR GLY GLU ILE ILE
SEQRES 27 C 461 PHE GLY GLY GLU THR MET ARG PHE TRP ASP PHE ARG GLY
SEQRES 28 C 461 PRO TRP LEU GLU PRO LEU ARG GLY PRO ASN GLY LEU ASP
SEQRES 29 C 461 LEU ASN LYS ILE LYS ASN ASP ILE GLN PRO TRP GLN GLU
SEQRES 30 C 461 ARG ARG ALA ALA GLU TYR MET THR HIS ALA PRO LEU GLY
SEQRES 31 C 461 SER LEU ASN SER VAL GLY GLY VAL ALA THR GLU ILE ASN
SEQRES 32 C 461 SER VAL ASN PHE VAL SER PRO ARG SER TRP LEU ALA THR
SEQRES 33 C 461 SER HIS PHE VAL LEU ALA PHE PHE PHE LEU VAL GLY HIS
SEQRES 34 C 461 LEU TRP HIS ALA GLY ARG ALA ARG ALA ALA ALA ALA GLY
SEQRES 35 C 461 PHE GLU LYS GLY ILE ASP ARG GLU SER GLU PRO VAL LEU
SEQRES 36 C 461 SER MET PRO SER LEU ASP
SEQRES 1 D 352 MET THR ILE ALA ILE GLY ARG ALA PRO ALA GLU ARG GLY
SEQRES 2 D 352 TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS ARG ASP ARG
SEQRES 3 D 352 PHE VAL PHE VAL GLY TRP SER GLY ILE LEU LEU PHE PRO
SEQRES 4 D 352 CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU THR GLY THR
SEQRES 5 D 352 THR PHE VAL THR SER TRP TYR THR HIS GLY LEU ALA SER
SEQRES 6 D 352 SER TYR LEU GLU GLY CYS ASN PHE LEU THR VAL ALA VAL
SEQRES 7 D 352 SER THR PRO ALA ASN SER MET GLY HIS SER LEU LEU LEU
SEQRES 8 D 352 LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE THR ARG TRP
SEQRES 9 D 352 CYS GLN LEU GLY GLY LEU TRP THR PHE ILE ALA LEU HIS
SEQRES 10 D 352 GLY ALA PHE GLY LEU ILE GLY PHE MET LEU ARG GLN PHE
SEQRES 11 D 352 GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO TYR ASN ALA
SEQRES 12 D 352 ILE ALA PHE SER ALA PRO ILE ALA VAL PHE VAL SER VAL
SEQRES 13 D 352 PHE LEU ILE TYR PRO LEU GLY GLN SER SER TRP PHE PHE
SEQRES 14 D 352 ALA PRO SER PHE GLY VAL ALA ALA ILE PHE ARG PHE LEU
SEQRES 15 D 352 LEU PHE PHE GLN GLY PHE HIS ASN TRP THR LEU ASN PRO
SEQRES 16 D 352 PHE HIS MET MET GLY VAL ALA GLY VAL LEU GLY GLY ALA
SEQRES 17 D 352 LEU LEU CYS ALA ILE HIS GLY ALA THR VAL GLU ASN THR
SEQRES 18 D 352 LEU PHE GLN ASP GLY GLU GLY ALA SER THR PHE ARG ALA
SEQRES 19 D 352 PHE ASN PRO THR GLN ALA GLU GLU THR TYR SER MET VAL
SEQRES 20 D 352 THR ALA ASN ARG PHE TRP SER GLN ILE PHE GLY ILE ALA
SEQRES 21 D 352 PHE SER ASN LYS ARG TRP LEU HIS PHE PHE MET LEU PHE
SEQRES 22 D 352 VAL PRO VAL THR GLY LEU TRP MET SER ALA ILE GLY VAL
SEQRES 23 D 352 VAL GLY LEU ALA LEU ASN LEU ARG SER TYR ASP PHE ILE
SEQRES 24 D 352 SER GLN GLU ILE ARG ALA ALA GLU ASP PRO GLU PHE GLU
SEQRES 25 D 352 THR PHE TYR THR LYS ASN LEU LEU LEU ASN GLU GLY ILE
SEQRES 26 D 352 ARG ALA TRP MET ALA PRO GLN ASP GLN PRO HIS GLU ASN
SEQRES 27 D 352 PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG GLY ASN ALA
SEQRES 28 D 352 LEU
SEQRES 1 E 84 MET ALA GLY THR THR GLY GLU ARG PRO PHE SER ASP ILE
SEQRES 2 E 84 ILE THR SER VAL ARG TYR TRP VAL ILE HIS SER ILE THR
SEQRES 3 E 84 ILE PRO ALA LEU PHE ILE ALA GLY TRP LEU PHE VAL SER
SEQRES 4 E 84 THR GLY LEU ALA TYR ASP VAL PHE GLY THR PRO ARG PRO
SEQRES 5 E 84 ASP SER TYR TYR ALA GLN GLU GLN ARG SER ILE PRO LEU
SEQRES 6 E 84 VAL THR ASP ARG PHE GLU ALA LYS GLN GLN VAL GLU THR
SEQRES 7 E 84 PHE LEU GLU GLN LEU LYS
SEQRES 1 F 45 MET THR SER ASN THR PRO ASN GLN GLU PRO VAL SER TYR
SEQRES 2 F 45 PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR LEU
SEQRES 3 F 45 ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA ALA
SEQRES 4 F 45 MET GLN PHE ILE GLN ARG
SEQRES 1 H 66 MET ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO
SEQRES 2 H 66 LEU ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY
SEQRES 3 H 66 THR THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU
SEQRES 4 H 66 VAL PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR
SEQRES 5 H 66 LEU ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU
SEQRES 6 H 66 GLY
SEQRES 1 I 38 MET GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR
SEQRES 2 I 38 PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY
SEQRES 3 I 38 ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP LEU GLU
SEQRES 1 J 40 MET MET SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL
SEQRES 2 J 40 ALA THR VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY
SEQRES 3 J 40 LEU PHE PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER
SEQRES 4 J 40 LEU
SEQRES 1 K 46 MET ILE ASP ALA LEU VAL LEU VAL ALA LYS LEU PRO GLU
SEQRES 2 K 46 ALA TYR ALA ILE PHE ASP PRO LEU VAL ASP VAL LEU PRO
SEQRES 3 K 46 VAL ILE PRO VAL LEU PHE LEU ALA LEU ALA PHE VAL TRP
SEQRES 4 K 46 GLN ALA ALA VAL GLY PHE ARG
SEQRES 1 L 37 MET GLU PRO ASN PRO ASN ARG GLN PRO VAL GLU LEU ASN
SEQRES 2 L 37 ARG THR SER LEU TYR LEU GLY LEU LEU LEU ILE LEU VAL
SEQRES 3 L 37 LEU ALA LEU LEU PHE SER SER TYR PHE PHE ASN
SEQRES 1 M 36 MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU
SEQRES 2 M 36 PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR
SEQRES 3 M 36 VAL GLN THR GLU SER GLN GLN LYS SER SER
SEQRES 1 O 272 MET LYS TYR ARG ILE LEU MET ALA THR LEU LEU ALA VAL
SEQRES 2 O 272 CYS LEU GLY ILE PHE SER LEU SER ALA PRO ALA PHE ALA
SEQRES 3 O 272 ALA LYS GLN THR LEU THR TYR ASP ASP ILE VAL GLY THR
SEQRES 4 O 272 GLY LEU ALA ASN LYS CYS PRO THR LEU ASP ASP THR ALA
SEQRES 5 O 272 ARG GLY ALA TYR PRO ILE ASP SER SER GLN THR TYR ARG
SEQRES 6 O 272 ILE ALA ARG LEU CYS LEU GLN PRO THR THR PHE LEU VAL
SEQRES 7 O 272 LYS GLU GLU PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE
SEQRES 8 O 272 VAL PRO THR LYS LEU VAL THR ARG GLU THR THR SER LEU
SEQRES 9 O 272 ASP GLN ILE GLN GLY GLU LEU LYS VAL ASN SER ASP GLY
SEQRES 10 O 272 SER LEU THR PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN
SEQRES 11 O 272 PRO VAL THR VAL GLN MET ALA GLY GLY GLU ARG ILE PRO
SEQRES 12 O 272 LEU LEU PHE THR VAL LYS ASN LEU VAL ALA SER THR GLN
SEQRES 13 O 272 PRO ASN VAL THR SER ILE THR THR SER THR ASP PHE LYS
SEQRES 14 O 272 GLY GLU PHE ASN VAL PRO SER TYR ARG THR ALA ASN PHE
SEQRES 15 O 272 LEU ASP PRO LYS GLY ARG GLY LEU ALA SER GLY TYR ASP
SEQRES 16 O 272 SER ALA ILE ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU
SEQRES 17 O 272 ALA ARG ALA ASN VAL LYS ARG PHE SER LEU THR LYS GLY
SEQRES 18 O 272 GLN ILE SER LEU ASN VAL ALA LYS VAL ASP GLY ARG THR
SEQRES 19 O 272 GLY GLU ILE ALA GLY THR PHE GLU SER GLU GLN LEU SER
SEQRES 20 O 272 ASP ASP ASP MET GLY ALA HIS GLU PRO HIS GLU VAL LYS
SEQRES 21 O 272 ILE GLN GLY VAL PHE TYR ALA SER ILE GLU PRO ALA
SEQRES 1 T 32 MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE
SEQRES 2 T 32 ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO
SEQRES 3 T 32 PRO ARG ILE THR LYS LYS
SEQRES 1 U 134 MET GLN ARG LEU GLY ARG TRP LEU ALA LEU ALA TYR PHE
SEQRES 2 U 134 VAL GLY VAL SER LEU LEU GLY TRP ILE ASN TRP SER ALA
SEQRES 3 U 134 PRO THR LEU ALA ALA THR ALA SER THR GLU GLU GLU LEU
SEQRES 4 U 134 VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA TYR GLY
SEQRES 5 U 134 GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA ALA PHE
SEQRES 6 U 134 ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA LYS LEU
SEQRES 7 U 134 ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU ASP VAL
SEQRES 8 U 134 LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS GLN ILE
SEQRES 9 U 134 LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR GLU VAL
SEQRES 10 U 134 GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR ASN ASN
SEQRES 11 U 134 GLY LEU TYR LYS
SEQRES 1 V 163 MET LEU LYS LYS CYS VAL TRP LEU ALA VAL ALA LEU CYS
SEQRES 2 V 163 LEU CYS LEU TRP GLN PHE THR MET GLY THR ALA LEU ALA
SEQRES 3 V 163 ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN
SEQRES 4 V 163 SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR
SEQRES 5 V 163 LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER
SEQRES 6 V 163 CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU
SEQRES 7 V 163 ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO
SEQRES 8 V 163 ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN
SEQRES 9 V 163 PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL
SEQRES 10 V 163 HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET
SEQRES 11 V 163 ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY
SEQRES 12 V 163 HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP
SEQRES 13 V 163 GLY GLY GLY LYS VAL TYR TYR
SEQRES 1 Y 46 MET GLY ILE PHE ASN GLY ILE ILE GLU PHE LEU SER ASN
SEQRES 2 Y 46 ILE ASN PHE GLU VAL ILE ALA GLN LEU THR MET ILE ALA
SEQRES 3 Y 46 MET ILE GLY ILE ALA GLY PRO MET ILE ILE PHE LEU LEU
SEQRES 4 Y 46 ALA VAL ARG ARG GLY ASN LEU
SEQRES 1 X 41 MET THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY
SEQRES 2 X 41 LEU LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA
SEQRES 3 X 41 VAL LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG
SEQRES 4 X 41 SER LEU
SEQRES 1 Z 62 MET THR ILE LEU PHE GLN LEU ALA LEU ALA ALA LEU VAL
SEQRES 2 Z 62 ILE LEU SER PHE VAL MET VAL ILE GLY VAL PRO VAL ALA
SEQRES 3 Z 62 TYR ALA SER PRO GLN ASP TRP ASP ARG SER LYS GLN LEU
SEQRES 4 Z 62 ILE PHE LEU GLY SER GLY LEU TRP ILE ALA LEU VAL LEU
SEQRES 5 Z 62 VAL VAL GLY VAL LEU ASN PHE PHE VAL VAL
SEQRES 1 a 344 MET THR THR THR LEU GLN ARG ARG GLU SER ALA ASN LEU
SEQRES 2 a 344 TRP GLU ARG PHE CYS ASN TRP VAL THR SER THR ASP ASN
SEQRES 3 a 344 ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE MET ILE PRO
SEQRES 4 a 344 THR LEU LEU ALA ALA THR ILE CYS PHE VAL ILE ALA PHE
SEQRES 5 a 344 ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY ILE ARG GLU
SEQRES 6 a 344 PRO VAL SER GLY SER LEU LEU TYR GLY ASN ASN ILE ILE
SEQRES 7 a 344 THR GLY ALA VAL VAL PRO SER SER ASN ALA ILE GLY LEU
SEQRES 8 a 344 HIS PHE TYR PRO ILE TRP GLU ALA ALA SER LEU ASP GLU
SEQRES 9 a 344 TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU ILE ILE PHE
SEQRES 10 a 344 HIS PHE LEU LEU GLY ALA SER CYS TYR MET GLY ARG GLN
SEQRES 11 a 344 TRP GLU LEU SER TYR ARG LEU GLY MET ARG PRO TRP ILE
SEQRES 12 a 344 CYS VAL ALA TYR SER ALA PRO LEU ALA SER ALA PHE ALA
SEQRES 13 a 344 VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY SER PHE SER
SEQRES 14 a 344 ASP GLY MET PRO LEU GLY ILE SER GLY THR PHE ASN PHE
SEQRES 15 a 344 MET ILE VAL PHE GLN ALA GLU HIS ASN ILE LEU MET HIS
SEQRES 16 a 344 PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL PHE GLY GLY
SEQRES 17 a 344 ALA LEU PHE CYS ALA MET HIS GLY SER LEU VAL THR SER
SEQRES 18 a 344 SER LEU ILE ARG GLU THR THR GLU THR GLU SER ALA ASN
SEQRES 19 a 344 TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU THR TYR ASN
SEQRES 20 a 344 ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG LEU ILE PHE
SEQRES 21 a 344 GLN TYR ALA SER PHE ASN ASN SER ARG SER LEU HIS PHE
SEQRES 22 a 344 PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL TRP PHE THR
SEQRES 23 a 344 ALA LEU GLY ILE SER THR MET ALA PHE ASN LEU ASN GLY
SEQRES 24 a 344 PHE ASN PHE ASN HIS SER VAL ILE ASP ALA LYS GLY ASN
SEQRES 25 a 344 VAL ILE ASN THR TRP ALA ASP ILE ILE ASN ARG ALA ASN
SEQRES 26 a 344 LEU GLY MET GLU VAL MET HIS GLU ARG ASN ALA HIS ASN
SEQRES 27 a 344 PHE PRO LEU ASP LEU ALA
SEQRES 1 b 510 MET GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE
SEQRES 2 b 510 ASN ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS
SEQRES 3 b 510 THR ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU
SEQRES 4 b 510 TYR GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU
SEQRES 5 b 510 ASN PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE
SEQRES 6 b 510 MET ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP
SEQRES 7 b 510 SER ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP
SEQRES 8 b 510 SER PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER
SEQRES 9 b 510 GLY LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR
SEQRES 10 b 510 TRP ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU
SEQRES 11 b 510 PRO ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU
SEQRES 12 b 510 PHE LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE
SEQRES 13 b 510 HIS LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER
SEQRES 14 b 510 ASP PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA
SEQRES 15 b 510 PRO GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO
SEQRES 16 b 510 GLY GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL
SEQRES 17 b 510 GLY ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO
SEQRES 18 b 510 PRO GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE
SEQRES 19 b 510 GLU THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE
SEQRES 20 b 510 ALA ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER
SEQRES 21 b 510 ALA THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR
SEQRES 22 b 510 GLN TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG
SEQRES 23 b 510 ARG VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU
SEQRES 24 b 510 GLU ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR
SEQRES 25 b 510 ASP TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE
SEQRES 26 b 510 ARG THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN
SEQRES 27 b 510 ALA TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY
SEQRES 28 b 510 GLU GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU
SEQRES 29 b 510 SER PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL
SEQRES 30 b 510 LYS ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR
SEQRES 31 b 510 SER PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY
SEQRES 32 b 510 GLY GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR
SEQRES 33 b 510 VAL LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE
SEQRES 34 b 510 PHE GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE
SEQRES 35 b 510 PHE ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS
SEQRES 36 b 510 ALA VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP
SEQRES 37 b 510 HIS GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY
SEQRES 38 b 510 ILE ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY
SEQRES 39 b 510 PHE TYR GLN LYS VAL GLY ASP VAL THR THR ARG ARG LYS
SEQRES 40 b 510 GLU ALA VAL
SEQRES 1 c 461 MET VAL THR LEU SER SER ASN SER ILE PHE ALA THR ASN
SEQRES 2 c 461 ARG ASP GLN GLU SER SER GLY PHE ALA TRP TRP ALA GLY
SEQRES 3 c 461 ASN ALA ARG LEU ILE ASN LEU SER GLY LYS LEU LEU GLY
SEQRES 4 c 461 ALA HIS VAL ALA HIS ALA GLY LEU ILE VAL PHE TRP ALA
SEQRES 5 c 461 GLY ALA MET THR LEU PHE GLU LEU ALA HIS PHE ILE PRO
SEQRES 6 c 461 GLU LYS PRO MET TYR GLU GLN GLY LEU ILE LEU ILE PRO
SEQRES 7 c 461 HIS ILE ALA THR LEU GLY TRP GLY VAL GLY PRO GLY GLY
SEQRES 8 c 461 GLU VAL VAL ASP THR PHE PRO PHE PHE VAL VAL GLY VAL
SEQRES 9 c 461 VAL HIS LEU ILE SER SER ALA VAL LEU GLY PHE GLY GLY
SEQRES 10 c 461 VAL TYR HIS ALA ILE ARG GLY PRO GLU THR LEU GLU GLU
SEQRES 11 c 461 TYR SER SER PHE PHE GLY TYR ASP TRP LYS ASP LYS ASN
SEQRES 12 c 461 LYS MET THR THR ILE LEU GLY PHE HIS LEU ILE VAL LEU
SEQRES 13 c 461 GLY ILE GLY ALA LEU LEU LEU VAL ALA LYS ALA MET PHE
SEQRES 14 c 461 PHE GLY GLY LEU TYR ASP THR TRP ALA PRO GLY GLY GLY
SEQRES 15 c 461 ASP VAL ARG VAL ILE THR ASN PRO THR LEU ASP PRO ARG
SEQRES 16 c 461 VAL ILE PHE GLY TYR LEU LEU LYS SER PRO PHE GLY GLY
SEQRES 17 c 461 GLU GLY TRP ILE VAL SER VAL ASN ASN LEU GLU ASP VAL
SEQRES 18 c 461 VAL GLY GLY HIS ILE TRP ILE GLY LEU ILE CYS ILE ALA
SEQRES 19 c 461 GLY GLY ILE TRP HIS ILE LEU THR THR PRO PHE GLY TRP
SEQRES 20 c 461 ALA ARG ARG ALA PHE ILE TRP SER GLY GLU ALA TYR LEU
SEQRES 21 c 461 SER TYR SER LEU GLY ALA LEU SER MET MET GLY PHE ILE
SEQRES 22 c 461 ALA THR CYS PHE VAL TRP PHE ASN ASN THR VAL TYR PRO
SEQRES 23 c 461 SER GLU PHE TYR GLY PRO THR GLY PRO GLU ALA SER GLN
SEQRES 24 c 461 ALA GLN ALA MET THR PHE LEU ILE ARG ASP GLN LYS LEU
SEQRES 25 c 461 GLY ALA ASN VAL GLY SER ALA GLN GLY PRO THR GLY LEU
SEQRES 26 c 461 GLY LYS TYR LEU MET ARG SER PRO THR GLY GLU ILE ILE
SEQRES 27 c 461 PHE GLY GLY GLU THR MET ARG PHE TRP ASP PHE ARG GLY
SEQRES 28 c 461 PRO TRP LEU GLU PRO LEU ARG GLY PRO ASN GLY LEU ASP
SEQRES 29 c 461 LEU ASN LYS ILE LYS ASN ASP ILE GLN PRO TRP GLN GLU
SEQRES 30 c 461 ARG ARG ALA ALA GLU TYR MET THR HIS ALA PRO LEU GLY
SEQRES 31 c 461 SER LEU ASN SER VAL GLY GLY VAL ALA THR GLU ILE ASN
SEQRES 32 c 461 SER VAL ASN PHE VAL SER PRO ARG SER TRP LEU ALA THR
SEQRES 33 c 461 SER HIS PHE VAL LEU ALA PHE PHE PHE LEU VAL GLY HIS
SEQRES 34 c 461 LEU TRP HIS ALA GLY ARG ALA ARG ALA ALA ALA ALA GLY
SEQRES 35 c 461 PHE GLU LYS GLY ILE ASP ARG GLU SER GLU PRO VAL LEU
SEQRES 36 c 461 SER MET PRO SER LEU ASP
SEQRES 1 d 352 MET THR ILE ALA ILE GLY ARG ALA PRO ALA GLU ARG GLY
SEQRES 2 d 352 TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS ARG ASP ARG
SEQRES 3 d 352 PHE VAL PHE VAL GLY TRP SER GLY ILE LEU LEU PHE PRO
SEQRES 4 d 352 CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU THR GLY THR
SEQRES 5 d 352 THR PHE VAL THR SER TRP TYR THR HIS GLY LEU ALA SER
SEQRES 6 d 352 SER TYR LEU GLU GLY CYS ASN PHE LEU THR VAL ALA VAL
SEQRES 7 d 352 SER THR PRO ALA ASN SER MET GLY HIS SER LEU LEU LEU
SEQRES 8 d 352 LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE THR ARG TRP
SEQRES 9 d 352 CYS GLN LEU GLY GLY LEU TRP THR PHE ILE ALA LEU HIS
SEQRES 10 d 352 GLY ALA PHE GLY LEU ILE GLY PHE MET LEU ARG GLN PHE
SEQRES 11 d 352 GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO TYR ASN ALA
SEQRES 12 d 352 ILE ALA PHE SER ALA PRO ILE ALA VAL PHE VAL SER VAL
SEQRES 13 d 352 PHE LEU ILE TYR PRO LEU GLY GLN SER SER TRP PHE PHE
SEQRES 14 d 352 ALA PRO SER PHE GLY VAL ALA ALA ILE PHE ARG PHE LEU
SEQRES 15 d 352 LEU PHE PHE GLN GLY PHE HIS ASN TRP THR LEU ASN PRO
SEQRES 16 d 352 PHE HIS MET MET GLY VAL ALA GLY VAL LEU GLY GLY ALA
SEQRES 17 d 352 LEU LEU CYS ALA ILE HIS GLY ALA THR VAL GLU ASN THR
SEQRES 18 d 352 LEU PHE GLN ASP GLY GLU GLY ALA SER THR PHE ARG ALA
SEQRES 19 d 352 PHE ASN PRO THR GLN ALA GLU GLU THR TYR SER MET VAL
SEQRES 20 d 352 THR ALA ASN ARG PHE TRP SER GLN ILE PHE GLY ILE ALA
SEQRES 21 d 352 PHE SER ASN LYS ARG TRP LEU HIS PHE PHE MET LEU PHE
SEQRES 22 d 352 VAL PRO VAL THR GLY LEU TRP MET SER ALA ILE GLY VAL
SEQRES 23 d 352 VAL GLY LEU ALA LEU ASN LEU ARG SER TYR ASP PHE ILE
SEQRES 24 d 352 SER GLN GLU ILE ARG ALA ALA GLU ASP PRO GLU PHE GLU
SEQRES 25 d 352 THR PHE TYR THR LYS ASN LEU LEU LEU ASN GLU GLY ILE
SEQRES 26 d 352 ARG ALA TRP MET ALA PRO GLN ASP GLN PRO HIS GLU ASN
SEQRES 27 d 352 PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG GLY ASN ALA
SEQRES 28 d 352 LEU
SEQRES 1 e 84 MET ALA GLY THR THR GLY GLU ARG PRO PHE SER ASP ILE
SEQRES 2 e 84 ILE THR SER VAL ARG TYR TRP VAL ILE HIS SER ILE THR
SEQRES 3 e 84 ILE PRO ALA LEU PHE ILE ALA GLY TRP LEU PHE VAL SER
SEQRES 4 e 84 THR GLY LEU ALA TYR ASP VAL PHE GLY THR PRO ARG PRO
SEQRES 5 e 84 ASP SER TYR TYR ALA GLN GLU GLN ARG SER ILE PRO LEU
SEQRES 6 e 84 VAL THR ASP ARG PHE GLU ALA LYS GLN GLN VAL GLU THR
SEQRES 7 e 84 PHE LEU GLU GLN LEU LYS
SEQRES 1 f 45 MET THR SER ASN THR PRO ASN GLN GLU PRO VAL SER TYR
SEQRES 2 f 45 PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR LEU
SEQRES 3 f 45 ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA ALA
SEQRES 4 f 45 MET GLN PHE ILE GLN ARG
SEQRES 1 h 66 MET ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO
SEQRES 2 h 66 LEU ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY
SEQRES 3 h 66 THR THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU
SEQRES 4 h 66 VAL PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR
SEQRES 5 h 66 LEU ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU
SEQRES 6 h 66 GLY
SEQRES 1 i 38 MET GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR
SEQRES 2 i 38 PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY
SEQRES 3 i 38 ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP LEU GLU
SEQRES 1 j 40 MET MET SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL
SEQRES 2 j 40 ALA THR VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY
SEQRES 3 j 40 LEU PHE PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER
SEQRES 4 j 40 LEU
SEQRES 1 k 46 MET ILE ASP ALA LEU VAL LEU VAL ALA LYS LEU PRO GLU
SEQRES 2 k 46 ALA TYR ALA ILE PHE ASP PRO LEU VAL ASP VAL LEU PRO
SEQRES 3 k 46 VAL ILE PRO VAL LEU PHE LEU ALA LEU ALA PHE VAL TRP
SEQRES 4 k 46 GLN ALA ALA VAL GLY PHE ARG
SEQRES 1 l 37 MET GLU PRO ASN PRO ASN ARG GLN PRO VAL GLU LEU ASN
SEQRES 2 l 37 ARG THR SER LEU TYR LEU GLY LEU LEU LEU ILE LEU VAL
SEQRES 3 l 37 LEU ALA LEU LEU PHE SER SER TYR PHE PHE ASN
SEQRES 1 m 36 MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU
SEQRES 2 m 36 PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR
SEQRES 3 m 36 VAL GLN THR GLU SER GLN GLN LYS SER SER
SEQRES 1 o 272 MET LYS TYR ARG ILE LEU MET ALA THR LEU LEU ALA VAL
SEQRES 2 o 272 CYS LEU GLY ILE PHE SER LEU SER ALA PRO ALA PHE ALA
SEQRES 3 o 272 ALA LYS GLN THR LEU THR TYR ASP ASP ILE VAL GLY THR
SEQRES 4 o 272 GLY LEU ALA ASN LYS CYS PRO THR LEU ASP ASP THR ALA
SEQRES 5 o 272 ARG GLY ALA TYR PRO ILE ASP SER SER GLN THR TYR ARG
SEQRES 6 o 272 ILE ALA ARG LEU CYS LEU GLN PRO THR THR PHE LEU VAL
SEQRES 7 o 272 LYS GLU GLU PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE
SEQRES 8 o 272 VAL PRO THR LYS LEU VAL THR ARG GLU THR THR SER LEU
SEQRES 9 o 272 ASP GLN ILE GLN GLY GLU LEU LYS VAL ASN SER ASP GLY
SEQRES 10 o 272 SER LEU THR PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN
SEQRES 11 o 272 PRO VAL THR VAL GLN MET ALA GLY GLY GLU ARG ILE PRO
SEQRES 12 o 272 LEU LEU PHE THR VAL LYS ASN LEU VAL ALA SER THR GLN
SEQRES 13 o 272 PRO ASN VAL THR SER ILE THR THR SER THR ASP PHE LYS
SEQRES 14 o 272 GLY GLU PHE ASN VAL PRO SER TYR ARG THR ALA ASN PHE
SEQRES 15 o 272 LEU ASP PRO LYS GLY ARG GLY LEU ALA SER GLY TYR ASP
SEQRES 16 o 272 SER ALA ILE ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU
SEQRES 17 o 272 ALA ARG ALA ASN VAL LYS ARG PHE SER LEU THR LYS GLY
SEQRES 18 o 272 GLN ILE SER LEU ASN VAL ALA LYS VAL ASP GLY ARG THR
SEQRES 19 o 272 GLY GLU ILE ALA GLY THR PHE GLU SER GLU GLN LEU SER
SEQRES 20 o 272 ASP ASP ASP MET GLY ALA HIS GLU PRO HIS GLU VAL LYS
SEQRES 21 o 272 ILE GLN GLY VAL PHE TYR ALA SER ILE GLU PRO ALA
SEQRES 1 t 32 MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE
SEQRES 2 t 32 ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO
SEQRES 3 t 32 PRO ARG ILE THR LYS LYS
SEQRES 1 u 134 MET GLN ARG LEU GLY ARG TRP LEU ALA LEU ALA TYR PHE
SEQRES 2 u 134 VAL GLY VAL SER LEU LEU GLY TRP ILE ASN TRP SER ALA
SEQRES 3 u 134 PRO THR LEU ALA ALA THR ALA SER THR GLU GLU GLU LEU
SEQRES 4 u 134 VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA TYR GLY
SEQRES 5 u 134 GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA ALA PHE
SEQRES 6 u 134 ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA LYS LEU
SEQRES 7 u 134 ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU ASP VAL
SEQRES 8 u 134 LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS GLN ILE
SEQRES 9 u 134 LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR GLU VAL
SEQRES 10 u 134 GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR ASN ASN
SEQRES 11 u 134 GLY LEU TYR LYS
SEQRES 1 v 163 MET LEU LYS LYS CYS VAL TRP LEU ALA VAL ALA LEU CYS
SEQRES 2 v 163 LEU CYS LEU TRP GLN PHE THR MET GLY THR ALA LEU ALA
SEQRES 3 v 163 ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN
SEQRES 4 v 163 SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR
SEQRES 5 v 163 LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER
SEQRES 6 v 163 CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU
SEQRES 7 v 163 ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO
SEQRES 8 v 163 ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN
SEQRES 9 v 163 PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL
SEQRES 10 v 163 HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET
SEQRES 11 v 163 ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY
SEQRES 12 v 163 HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP
SEQRES 13 v 163 GLY GLY GLY LYS VAL TYR TYR
SEQRES 1 x 41 MET THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY
SEQRES 2 x 41 LEU LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA
SEQRES 3 x 41 VAL LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG
SEQRES 4 x 41 SER LEU
SEQRES 1 R 41 MET ASP TRP ARG VAL LEU VAL VAL LEU LEU PRO VAL LEU
SEQRES 2 R 41 LEU ALA ALA GLY TRP ALA VAL ARG ASN ILE LEU PRO TYR
SEQRES 3 R 41 ALA VAL LYS GLN VAL GLN LYS LEU LEU GLN LYS ALA LYS
SEQRES 4 R 41 ALA ALA
SEQRES 1 r 41 MET ASP TRP ARG VAL LEU VAL VAL LEU LEU PRO VAL LEU
SEQRES 2 r 41 LEU ALA ALA GLY TRP ALA VAL ARG ASN ILE LEU PRO TYR
SEQRES 3 r 41 ALA VAL LYS GLN VAL GLN LYS LEU LEU GLN LYS ALA LYS
SEQRES 4 r 41 ALA ALA
SEQRES 1 y 46 MET GLY ILE PHE ASN GLY ILE ILE GLU PHE LEU SER ASN
SEQRES 2 y 46 ILE ASN PHE GLU VAL ILE ALA GLN LEU THR MET ILE ALA
SEQRES 3 y 46 MET ILE GLY ILE ALA GLY PRO MET ILE ILE PHE LEU LEU
SEQRES 4 y 46 ALA VAL ARG ARG GLY ASN LEU
SEQRES 1 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 CL A 401 1
HET CL A 402 1
HET CLA A 403 65
HET CLA A 404 65
HET PHO A 405 64
HET CLA A 406 65
HET BCR A 407 40
HET PL9 A 408 55
HET SQD A 409 54
HET LFA A 410 14
HET SQD A 411 54
HET CLA A 412 65
HET LFA A 413 11
HET FE A 414 1
HET BCT A 415 4
HET CLA B 601 65
HET CLA B 602 65
HET CLA B 603 65
HET CLA B 604 65
HET CLA B 605 65
HET CLA B 606 65
HET CLA B 607 65
HET CLA B 608 65
HET CLA B 609 65
HET CLA B 610 65
HET CLA B 611 65
HET CLA B 612 65
HET CLA B 613 65
HET CLA B 614 65
HET CLA B 615 65
HET BCR B 616 40
HET BCR B 617 40
HET BCR B 618 40
HET LMG B 619 51
HET LFA B 620 10
HET LMG B 621 36
HET LFA B 622 16
HET LFA B 623 13
HET LFA B 624 15
HET LFA B 625 9
HET LFA B 626 10
HET LFA B 627 14
HET LFA B 628 12
HET LMG C 501 51
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 56
HET DGD C 519 62
HET LMG C 520 48
HET LFA C 521 15
HET LMG C 522 44
HET PHO D 401 64
HET CLA D 402 65
HET CLA D 403 65
HET BCR D 404 40
HET PL9 D 405 55
HET LHG D 406 49
HET LHG D 407 49
HET LHG D 408 49
HET LMG D 409 51
HET LFA D 410 15
HET SQD D 411 43
HET LFA D 412 8
HET LFA D 413 10
HET LHG E 101 42
HET HEM E 102 43
HET CLA H 101 65
HET BCR H 102 40
HET DGD H 103 60
HET LFA I 101 14
HET LFA J 101 11
HET BCR K 101 40
HET BCR K 102 40
HET SQD L 101 48
HET LHG L 102 49
HET LFA M 101 10
HET LFA M 102 16
HET BCR T 101 40
HET LFA T 102 12
HET HEM V 201 43
HET FE a 401 1
HET CL a 402 1
HET CL a 403 1
HET CLA a 404 65
HET CLA a 405 65
HET PHO a 406 64
HET CLA a 407 65
HET BCR a 408 40
HET PL9 a 409 55
HET SQD a 410 54
HET LFA a 411 7
HET SQD a 412 50
HET BCT a 413 4
HET PHO a 414 64
HET SQD b 601 54
HET LFA b 602 15
HET CLA b 603 65
HET CLA b 604 65
HET CLA b 605 65
HET CLA b 606 65
HET CLA b 607 65
HET CLA b 608 65
HET CLA b 609 65
HET CLA b 610 65
HET CLA b 611 65
HET CLA b 612 65
HET CLA b 613 65
HET CLA b 614 65
HET CLA b 615 65
HET CLA b 616 65
HET CLA b 617 65
HET CLA b 618 65
HET BCR b 619 40
HET BCR b 620 40
HET BCR b 621 40
HET LFA b 622 10
HET LFA b 623 12
HET LMG b 624 39
HET LFA b 625 16
HET LFA b 626 12
HET LFA b 627 11
HET LHG b 628 49
HET LFA b 629 9
HET LFA b 630 15
HET LMG c 501 51
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 DGD c 516 62
HET DGD c 517 55
HET DGD c 518 62
HET LMG c 519 51
HET LFA c 520 9
HET LFA c 521 15
HET LMG c 522 41
HET BCR c 523 40
HET BCR c 524 40
HET CLA d 401 65
HET CLA d 402 65
HET CLA d 403 65
HET BCR d 404 40
HET PL9 d 405 55
HET LHG d 406 49
HET LHG d 407 49
HET LFA d 408 15
HET LFA d 409 9
HET LFA d 410 16
HET LHG e 101 42
HET HEM e 102 43
HET LMG f 101 51
HET SQD f 102 43
HET BCR h 101 40
HET DGD h 102 62
HET LFA i 101 16
HET LFA i 102 7
HET LFA j 101 15
HET BCR k 101 40
HET LHG l 101 49
HET LFA m 101 10
HET LFA m 102 15
HET LMG m 103 51
HET LFA t 101 15
HET BCR t 102 40
HET HEM v 201 43
HETNAM CL CHLORIDE 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 LFA EICOSANE
HETNAM FE FE (III) ION
HETNAM BCT BICARBONATE ION
HETNAM LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE
HETNAM DGD DIGALACTOSYL DIACYL GLYCEROL (DGDG)
HETNAM LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN PL9 PLASTOQUINONE 9
HETSYN SQD SULFOQUINOVOSYLDIACYLGLYCEROL
HETSYN LFA LIPID FRAGMENT
HETSYN HEM HEME
FORMUL 41 CL 4(CL 1-)
FORMUL 43 CLA 70(C55 H72 MG N4 O5 2+)
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 LFA 39(C20 H42)
FORMUL 54 FE 2(FE 3+)
FORMUL 55 BCT 2(C H O3 1-)
FORMUL 74 LMG 12(C45 H86 O10)
FORMUL 00 DGD 8(C51 H96 O15)
FORMUL 11 LHG 10(C38 H75 O10 P)
FORMUL 20 HEM 4(C34 H32 FE N4 O4)
FORMUL 30 HOH *703(H2 O)
HELIX 1 AA1 ASN A 12 THR A 22 1 11
HELIX 2 AA2 VAL A 30 ALA A 55 1 26
HELIX 3 AA3 SER A 70 GLY A 74 5 5
HELIX 4 AA4 SER A 101 GLY A 109 1 9
HELIX 5 AA5 GLY A 109 GLY A 138 1 30
HELIX 6 AA6 TRP A 142 LEU A 159 1 18
HELIX 7 AA7 LEU A 159 GLY A 166 1 8
HELIX 8 AA8 SER A 167 GLY A 171 5 5
HELIX 9 AA9 ILE A 176 ASN A 191 1 16
HELIX 10 AB1 ILE A 192 MET A 194 5 3
HELIX 11 AB2 HIS A 195 SER A 222 1 28
HELIX 12 AB3 SER A 232 TYR A 237 5 6
HELIX 13 AB4 ASN A 247 ILE A 259 1 13
HELIX 14 AB5 PHE A 260 SER A 264 5 5
HELIX 15 AB6 ASN A 267 ALA A 294 1 28
HELIX 16 AB7 THR A 316 VAL A 330 1 15
HELIX 17 AB8 PRO B 4 ILE B 13 5 10
HELIX 18 AB9 ASP B 15 PHE B 45 1 31
HELIX 19 AC1 PRO B 54 GLN B 58 5 5
HELIX 20 AC2 VAL B 62 LEU B 69 1 8
HELIX 21 AC3 SER B 92 TYR B 117 1 26
HELIX 22 AC4 LEU B 120 ARG B 124 5 5
HELIX 23 AC5 ASP B 134 PHE B 156 1 23
HELIX 24 AC6 GLY B 186 PHE B 190 5 5
HELIX 25 AC7 ASN B 194 VAL B 219 1 26
HELIX 26 AC8 PRO B 222 LEU B 229 1 8
HELIX 27 AC9 ASN B 233 GLY B 259 1 27
HELIX 28 AD1 PRO B 264 GLY B 269 1 6
HELIX 29 AD2 THR B 271 SER B 277 1 7
HELIX 30 AD3 SER B 278 SER B 294 1 17
HELIX 31 AD4 THR B 297 ALA B 304 1 8
HELIX 32 AD5 PRO B 306 ASP B 313 1 8
HELIX 33 AD6 TYR B 314 ASN B 318 5 5
HELIX 34 AD7 PRO B 329 GLY B 333 5 5
HELIX 35 AD8 SER B 391 GLY B 396 1 6
HELIX 36 AD9 GLY B 403 ASN B 407 5 5
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 GLN C 28 GLY C 32 1 5
HELIX 42 AE6 ALA C 34 ILE C 43 5 10
HELIX 43 AE7 LEU C 45 PHE C 75 1 31
HELIX 44 AE8 PRO C 80 GLN C 84 5 5
HELIX 45 AE9 ILE C 87 LEU C 95 1 9
HELIX 46 AF1 GLY C 100 GLU C 104 5 5
HELIX 47 AF2 THR C 108 ARG C 135 1 28
HELIX 48 AF3 ASP C 153 PHE C 181 1 29
HELIX 49 AF4 ASP C 205 LEU C 213 1 9
HELIX 50 AF5 GLY C 222 VAL C 227 5 6
HELIX 51 AF6 ASN C 229 THR C 254 1 26
HELIX 52 AF7 PHE C 257 ARG C 262 1 6
HELIX 53 AF8 SER C 267 ASN C 293 1 27
HELIX 54 AF9 PRO C 298 GLY C 303 1 6
HELIX 55 AG1 THR C 305 GLY C 325 1 21
HELIX 56 AG2 GLY C 353 TRP C 359 5 7
HELIX 57 AG3 LEU C 366 PRO C 368 5 3
HELIX 58 AG4 ASP C 376 ASP C 383 1 8
HELIX 59 AG5 GLN C 385 THR C 397 1 13
HELIX 60 AG6 SER C 421 GLY C 454 1 34
HELIX 61 AG7 ASP C 460 GLU C 464 5 5
HELIX 62 AG8 PRO C 465 MET C 469 5 5
HELIX 63 AG9 TRP D 14 LYS D 23 1 10
HELIX 64 AH1 TRP D 32 VAL D 55 1 24
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 PHE D 146 1 7
HELIX 70 AH7 PHE D 146 LEU D 158 1 13
HELIX 71 AH8 LEU D 158 GLN D 164 1 7
HELIX 72 AH9 SER D 166 ALA D 170 5 5
HELIX 73 AI1 VAL D 175 PHE D 188 1 14
HELIX 74 AI2 ASN D 190 LEU D 193 5 4
HELIX 75 AI3 ASN D 194 ASN D 220 1 27
HELIX 76 AI4 SER D 230 PHE D 235 5 6
HELIX 77 AI5 SER D 245 GLY D 258 1 14
HELIX 78 AI6 ASN D 263 LEU D 291 1 29
HELIX 79 AI7 PHE D 298 ASP D 308 1 11
HELIX 80 AI8 THR D 313 GLN D 334 1 22
HELIX 81 AI9 PRO D 335 ASN D 338 5 4
HELIX 82 AJ1 PRO D 342 LEU D 346 5 5
HELIX 83 AJ2 PRO E 9 SER E 16 1 8
HELIX 84 AJ3 SER E 16 THR E 40 1 25
HELIX 85 AJ4 GLY E 41 GLY E 48 1 8
HELIX 86 AJ5 GLU E 71 GLN E 82 1 12
HELIX 87 AJ6 THR F 17 GLN F 41 1 25
HELIX 88 AJ7 THR H 5 ARG H 12 1 8
HELIX 89 AJ8 PRO H 13 SER H 16 5 4
HELIX 90 AJ9 THR H 27 ASN H 50 1 24
HELIX 91 AK1 GLU I 2 SER I 25 1 24
HELIX 92 AK2 PRO J 9 ALA J 32 1 24
HELIX 93 AK3 PRO K 12 ILE K 17 5 6
HELIX 94 AK4 PHE K 18 LEU K 25 1 8
HELIX 95 AK5 VAL K 27 VAL K 43 1 17
HELIX 96 AK6 ASN L 13 ASN L 37 1 25
HELIX 97 AK7 LEU M 6 SER M 31 1 26
HELIX 98 AK8 THR O 6 VAL O 11 1 6
HELIX 99 AK9 GLY O 14 LYS O 18 5 5
HELIX 100 AL1 LEU O 182 VAL O 187 1 6
HELIX 101 AL2 GLU T 2 PHE T 23 1 22
HELIX 102 AL3 ASN U 11 LEU U 17 1 7
HELIX 103 AL4 GLY U 18 GLU U 23 5 6
HELIX 104 AL5 ASN U 31 TYR U 38 5 8
HELIX 105 AL6 PRO U 43 ASN U 52 1 10
HELIX 106 AL7 SER U 57 ILE U 64 5 8
HELIX 107 AL8 THR U 68 GLU U 77 1 10
HELIX 108 AL9 ASN U 78 GLU U 80 5 3
HELIX 109 AM1 GLU U 88 GLU U 93 1 6
HELIX 110 AM2 GLY U 94 ASP U 96 5 3
HELIX 111 AM3 THR V 22 CYS V 37 1 16
HELIX 112 AM4 CYS V 37 VAL V 42 1 6
HELIX 113 AM5 GLY V 43 ILE V 45 5 3
HELIX 114 AM6 ARG V 55 ALA V 62 1 8
HELIX 115 AM7 ASN V 68 ASN V 78 1 11
HELIX 116 AM8 PHE V 101 ARG V 105 5 5
HELIX 117 AM9 THR V 108 GLY V 127 1 20
HELIX 118 AN1 ASP V 128 TRP V 130 5 3
HELIX 119 AN2 GLY V 132 TYR V 137 5 6
HELIX 120 AN3 MET Y 27 ARG Y 42 1 16
HELIX 121 AN4 THR X 4 ASP X 35 1 32
HELIX 122 AN5 THR Z 2 ALA Z 28 1 27
HELIX 123 AN6 ASP Z 32 ASN Z 58 1 27
HELIX 124 AN7 PHE Z 59 VAL Z 61 5 3
HELIX 125 AN8 LEU a 13 THR a 22 1 10
HELIX 126 AN9 VAL a 30 ALA a 55 1 26
HELIX 127 AO1 SER a 70 GLY a 74 5 5
HELIX 128 AO2 PRO a 95 ALA a 99 5 5
HELIX 129 AO3 SER a 101 ASN a 108 1 8
HELIX 130 AO4 GLY a 109 GLY a 138 1 30
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 221 1 27
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 VAL a 330 1 15
HELIX 142 AP7 PRO b 4 ILE b 13 5 10
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 GLY b 295 1 18
HELIX 156 AR3 THR b 297 ALA b 304 1 8
HELIX 157 AR4 PRO b 306 ASP b 313 1 8
HELIX 158 AR5 TYR b 314 ASN b 318 5 5
HELIX 159 AR6 PRO b 329 GLY b 333 5 5
HELIX 160 AR7 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 VAL b 491 5 5
HELIX 164 AS2 ASP c 27 GLY c 32 1 6
HELIX 165 AS3 ALA c 34 ILE c 43 5 10
HELIX 166 AS4 LEU c 45 HIS c 74 1 30
HELIX 167 AS5 PRO c 80 GLY c 85 5 6
HELIX 168 AS6 LEU c 88 LEU c 95 1 8
HELIX 169 AS7 GLY c 100 GLU c 104 5 5
HELIX 170 AS8 THR c 108 ARG c 135 1 28
HELIX 171 AS9 ASP c 153 PHE c 182 1 30
HELIX 172 AT1 ASP c 205 LEU c 213 1 9
HELIX 173 AT2 GLY c 222 VAL c 227 5 6
HELIX 174 AT3 ASN c 229 THR c 254 1 26
HELIX 175 AT4 PHE c 257 PHE c 264 1 8
HELIX 176 AT5 SER c 267 ASN c 293 1 27
HELIX 177 AT6 PRO c 298 GLY c 303 1 6
HELIX 178 AT7 THR c 305 GLY c 325 1 21
HELIX 179 AT8 GLY c 353 TRP c 359 5 7
HELIX 180 AT9 LEU c 366 PRO c 368 5 3
HELIX 181 AU1 ASP c 376 ASP c 383 1 8
HELIX 182 AU2 GLN c 385 THR c 397 1 13
HELIX 183 AU3 SER c 421 GLY c 454 1 34
HELIX 184 AU4 ASP c 460 MET c 469 5 10
HELIX 185 AU5 TRP d 14 LYS d 23 1 10
HELIX 186 AU6 SER d 33 VAL d 55 1 23
HELIX 187 AU7 SER d 66 GLY d 70 5 5
HELIX 188 AU8 ALA d 82 GLY d 86 5 5
HELIX 189 AU9 ASP d 100 LEU d 107 1 8
HELIX 190 AV1 GLY d 108 GLY d 137 1 30
HELIX 191 AV2 PRO d 140 PHE d 146 1 7
HELIX 192 AV3 PHE d 146 LEU d 158 1 13
HELIX 193 AV4 LEU d 158 GLN d 164 1 7
HELIX 194 AV5 SER d 166 ALA d 170 5 5
HELIX 195 AV6 GLY d 174 ASN d 190 1 17
HELIX 196 AV7 TRP d 191 LEU d 193 5 3
HELIX 197 AV8 ASN d 194 ASN d 220 1 27
HELIX 198 AV9 SER d 245 GLY d 258 1 14
HELIX 199 AW1 ASN d 263 LEU d 291 1 29
HELIX 200 AW2 PHE d 298 ASP d 308 1 11
HELIX 201 AW3 THR d 313 GLN d 334 1 22
HELIX 202 AW4 PRO d 335 ASN d 338 5 4
HELIX 203 AW5 PRO d 342 LEU d 346 5 5
HELIX 204 AW6 PRO e 9 ILE e 14 1 6
HELIX 205 AW7 SER e 16 THR e 40 1 25
HELIX 206 AW8 GLY e 41 GLY e 48 1 8
HELIX 207 AW9 GLU e 71 GLN e 82 1 12
HELIX 208 AX1 THR f 17 GLN f 41 1 25
HELIX 209 AX2 THR h 5 ARG h 12 1 8
HELIX 210 AX3 THR h 27 ASN h 50 1 24
HELIX 211 AX4 GLU i 2 SER i 25 1 24
HELIX 212 AX5 GLY i 26 ARG i 30 5 5
HELIX 213 AX6 PRO j 9 ALA j 32 1 24
HELIX 214 AX7 PRO k 12 ILE k 17 5 6
HELIX 215 AX8 PHE k 18 ASP k 23 1 6
HELIX 216 AX9 VAL k 24 PRO k 26 5 3
HELIX 217 AY1 VAL k 27 VAL k 43 1 17
HELIX 218 AY2 ASN l 13 ASN l 37 1 25
HELIX 219 AY3 LEU m 6 SER m 31 1 26
HELIX 220 AY4 THR o 6 VAL o 11 1 6
HELIX 221 AY5 GLY o 14 LYS o 18 5 5
HELIX 222 AY6 LEU o 182 VAL o 187 1 6
HELIX 223 AY7 GLU t 2 PHE t 23 1 22
HELIX 224 AY8 ASN u 11 LEU u 17 1 7
HELIX 225 AY9 GLY u 18 GLU u 23 5 6
HELIX 226 AZ1 ASN u 31 TYR u 38 5 8
HELIX 227 AZ2 PRO u 43 ALA u 53 1 11
HELIX 228 AZ3 SER u 57 ILE u 64 5 8
HELIX 229 AZ4 THR u 68 ASN u 78 1 11
HELIX 230 AZ5 GLU u 88 GLU u 93 1 6
HELIX 231 AZ6 THR v 22 CYS v 37 1 16
HELIX 232 AZ7 CYS v 37 VAL v 42 1 6
HELIX 233 AZ8 GLY v 43 ILE v 45 5 3
HELIX 234 AZ9 ARG v 55 ALA v 60 1 6
HELIX 235 BA1 ASN v 68 ASN v 78 1 11
HELIX 236 BA2 PHE v 101 ARG v 105 5 5
HELIX 237 BA3 THR v 108 GLY v 127 1 20
HELIX 238 BA4 ASP v 128 TRP v 130 5 3
HELIX 239 BA5 GLY v 133 TYR v 137 5 5
HELIX 240 BA6 THR x 4 ASP x 35 1 32
HELIX 241 BA7 TRP R 3 LEU R 35 1 33
HELIX 242 BA8 ARG r 4 LEU r 34 1 31
HELIX 243 BA9 ILE y 25 ARG y 42 1 18
HELIX 244 BB1 THR z 2 SER z 29 1 28
HELIX 245 BB2 ASP z 32 ASN z 58 1 27
HELIX 246 BB3 PHE z 59 VAL z 61 5 3
SHEET 1 AA1 2 ALA A 81 VAL A 82 0
SHEET 2 AA1 2 LEU A 174 GLY A 175 -1 O LEU A 174 N VAL A 82
SHEET 1 AA2 2 LEU A 297 ASN A 298 0
SHEET 2 AA2 2 GLY C 402 SER C 403 1 O GLY C 402 N ASN A 298
SHEET 1 AA3 2 MET B 166 VAL B 168 0
SHEET 2 AA3 2 SER B 177 GLN B 179 -1 O SER B 177 N VAL B 168
SHEET 1 AA4 6 VAL B 377 ASP B 380 0
SHEET 2 AA4 6 ILE B 369 THR B 371 -1 N LEU B 370 O ALA B 379
SHEET 3 AA4 6 GLU B 353 VAL B 356 -1 N PHE B 355 O THR B 371
SHEET 4 AA4 6 ILE B 336 ARG B 347 -1 N PHE B 346 O LEU B 354
SHEET 5 AA4 6 THR B 398 TYR B 402 -1 O SER B 400 N VAL B 345
SHEET 6 AA4 6 THR B 410 PHE B 411 -1 O PHE B 411 N VAL B 399
SHEET 1 AA5 5 VAL B 377 ASP B 380 0
SHEET 2 AA5 5 ILE B 369 THR B 371 -1 N LEU B 370 O ALA B 379
SHEET 3 AA5 5 GLU B 353 VAL B 356 -1 N PHE B 355 O THR B 371
SHEET 4 AA5 5 ILE B 336 ARG B 347 -1 N PHE B 346 O LEU B 354
SHEET 5 AA5 5 ILE B 429 ASP B 433 -1 O GLU B 431 N GLN B 338
SHEET 1 AA6 2 LEU C 185 ASP C 187 0
SHEET 2 AA6 2 ASP C 195 ARG C 197 -1 O ASP C 195 N ASP C 187
SHEET 1 AA7 2 LEU C 341 ARG C 343 0
SHEET 2 AA7 2 ILE C 349 PHE C 351 -1 O ILE C 350 N MET C 342
SHEET 1 AA8 2 ARG C 370 GLY C 371 0
SHEET 2 AA8 2 GLY C 374 LEU C 375 -1 O GLY C 374 N GLY C 371
SHEET 1 AA9 2 ALA D 77 VAL D 78 0
SHEET 2 AA9 2 PHE D 173 GLY D 174 -1 O PHE D 173 N VAL D 78
SHEET 1 AB1 2 TYR O 30 PRO O 31 0
SHEET 2 AB1 2 SER O 135 ILE O 136 -1 O ILE O 136 N TYR O 30
SHEET 1 AB210 PHE O 65 PRO O 67 0
SHEET 2 AB210 TYR O 38 LYS O 53 -1 N VAL O 52 O VAL O 66
SHEET 3 AB210 GLU O 232 GLU O 244 -1 O LYS O 234 N LEU O 51
SHEET 4 AB210 GLU O 210 LEU O 220 -1 N GLN O 219 O VAL O 233
SHEET 5 AB210 LEU O 192 ASP O 205 -1 N ALA O 202 O ALA O 212
SHEET 6 AB210 ASP O 141 PRO O 149 -1 N PHE O 146 O GLY O 195
SHEET 7 AB210 VAL O 126 SER O 128 -1 N SER O 128 O LYS O 143
SHEET 8 AB210 LEU O 93 ILE O 101 -1 N PHE O 95 O ALA O 127
SHEET 9 AB210 LEU O 78 VAL O 87 -1 N LYS O 86 O THR O 94
SHEET 10 AB210 TYR O 38 LYS O 53 -1 N LEU O 45 O LEU O 78
SHEET 1 AB3 3 LYS O 69 LEU O 70 0
SHEET 2 AB3 3 PHE O 103 GLN O 109 -1 O GLN O 109 N LYS O 69
SHEET 3 AB3 3 ARG O 115 THR O 121 -1 O LEU O 118 N VAL O 106
SHEET 1 AB4 2 ILE U 25 ASP U 26 0
SHEET 2 AB4 2 PHE U 82 THR U 83 1 O THR U 83 N ILE U 25
SHEET 1 AB5 2 THR V 9 PRO V 11 0
SHEET 2 AB5 2 THR V 18 THR V 20 -1 O ILE V 19 N VAL V 10
SHEET 1 AB6 2 ALA a 81 VAL a 82 0
SHEET 2 AB6 2 LEU a 174 GLY a 175 -1 O LEU a 174 N VAL a 82
SHEET 1 AB7 2 LEU a 297 ASN a 298 0
SHEET 2 AB7 2 GLY c 402 SER c 403 1 O GLY c 402 N ASN a 298
SHEET 1 AB8 2 MET b 166 VAL b 168 0
SHEET 2 AB8 2 SER b 177 GLN b 179 -1 O GLN b 179 N MET b 166
SHEET 1 AB9 6 VAL b 377 ASP b 380 0
SHEET 2 AB9 6 ILE b 369 THR b 371 -1 N LEU b 370 O ALA b 379
SHEET 3 AB9 6 GLU b 353 VAL b 356 -1 N PHE b 355 O THR b 371
SHEET 4 AB9 6 ILE b 336 ARG b 347 -1 N PHE b 346 O LEU b 354
SHEET 5 AB9 6 THR b 398 TYR b 402 -1 O SER b 400 N VAL b 345
SHEET 6 AB9 6 GLN b 409 PHE b 411 -1 O GLN b 409 N PHE b 401
SHEET 1 AC1 5 VAL b 377 ASP b 380 0
SHEET 2 AC1 5 ILE b 369 THR b 371 -1 N LEU b 370 O ALA b 379
SHEET 3 AC1 5 GLU b 353 VAL b 356 -1 N PHE b 355 O THR b 371
SHEET 4 AC1 5 ILE b 336 ARG b 347 -1 N PHE b 346 O LEU b 354
SHEET 5 AC1 5 ILE b 429 ASP b 433 -1 O ILE b 429 N LYS b 341
SHEET 1 AC2 2 LEU c 185 ASP c 187 0
SHEET 2 AC2 2 ASP c 195 ARG c 197 -1 O ASP c 195 N ASP c 187
SHEET 1 AC3 2 LEU c 341 ARG c 343 0
SHEET 2 AC3 2 ILE c 349 PHE c 351 -1 O ILE c 350 N MET c 342
SHEET 1 AC4 2 ARG c 370 GLY c 371 0
SHEET 2 AC4 2 GLY c 374 LEU c 375 -1 O GLY c 374 N GLY c 371
SHEET 1 AC5 2 TYR o 30 PRO o 31 0
SHEET 2 AC5 2 SER o 135 ILE o 136 -1 O ILE o 136 N TYR o 30
SHEET 1 AC610 PHE o 65 PRO o 67 0
SHEET 2 AC610 TYR o 38 LYS o 53 -1 N VAL o 52 O VAL o 66
SHEET 3 AC610 GLU o 232 GLU o 244 -1 O GLN o 236 N THR o 48
SHEET 4 AC610 GLU o 210 LEU o 220 -1 N SER o 217 O ILE o 235
SHEET 5 AC610 THR o 193 ASP o 205 -1 N ALA o 202 O ALA o 212
SHEET 6 AC610 ASP o 141 VAL o 148 -1 N VAL o 148 O THR o 193
SHEET 7 AC610 VAL o 126 SER o 128 -1 N SER o 128 O LYS o 143
SHEET 8 AC610 LEU o 93 ILE o 101 -1 N PHE o 95 O ALA o 127
SHEET 9 AC610 LEU o 78 VAL o 87 -1 N LYS o 86 O THR o 94
SHEET 10 AC610 TYR o 38 LYS o 53 -1 N LEU o 45 O LEU o 78
SHEET 1 AC7 3 LYS o 69 LEU o 70 0
SHEET 2 AC7 3 PHE o 103 GLN o 109 -1 O GLN o 109 N LYS o 69
SHEET 3 AC7 3 ARG o 115 THR o 121 -1 O ILE o 116 N VAL o 108
SHEET 1 AC8 2 ILE u 25 ASP u 26 0
SHEET 2 AC8 2 PHE u 82 THR u 83 1 O THR u 83 N ILE u 25
SHEET 1 AC9 2 THR v 9 PRO v 11 0
SHEET 2 AC9 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 2.02
SSBOND 2 CYS o 19 CYS o 44 1555 1555 2.03
LINK NE2 HIS A 215 FE FE A 414 1555 1555 2.16
LINK NE2 HIS A 272 FE FE A 414 1555 1555 2.50
LINK OD1 ASN C 39 MG CLA C 512 1555 1555 2.16
LINK NE2 HIS D 214 FE FE A 414 1555 1555 2.16
LINK NE2 HIS D 268 FE FE A 414 1555 1555 2.40
LINK NE2 HIS E 23 FE HEM E 102 1555 1555 2.03
LINK NE2 HIS F 24 FE HEM E 102 1555 1555 2.06
LINK SG CYS V 37 CAB HEM V 201 1555 1555 1.77
LINK SG CYS V 40 CAC HEM V 201 1555 1555 1.81
LINK NE2 HIS V 41 FE HEM V 201 1555 1555 1.88
LINK NE2 HIS V 92 FE HEM V 201 1555 1555 2.09
LINK NE2 HIS a 215 FE FE a 401 1555 1555 2.16
LINK NE2 HIS a 272 FE FE a 401 1555 1555 2.44
LINK OD1 ASN c 39 MG CLA c 512 1555 1555 2.13
LINK NE2 HIS d 214 FE FE a 401 1555 1555 2.07
LINK NE2 HIS d 268 FE FE a 401 1555 1555 2.39
LINK NE2 HIS e 23 FE HEM e 102 1555 1555 1.85
LINK NE2 HIS f 24 FE HEM e 102 1555 1555 2.19
LINK SG CYS v 37 CAB HEM v 201 1555 1555 1.77
LINK SG CYS v 40 CAC HEM v 201 1555 1555 1.83
LINK NE2 HIS v 41 FE HEM v 201 1555 1555 1.89
LINK NE2 HIS v 92 FE HEM v 201 1555 1555 2.06
LINK MG CLA A 404 O HOH A 531 1555 1555 2.13
LINK MG CLA A 412 O HOH A 540 1555 1555 2.13
LINK FE FE A 414 O1 BCT A 415 1555 1555 2.05
LINK FE FE A 414 O2 BCT A 415 1555 1555 2.04
LINK MG CLA B 606 O HOH B 762 1555 1555 2.16
LINK MG CLA B 609 O HOH B 748 1555 1555 2.14
LINK MG CLA C 505 O HOH C 649 1555 1555 2.14
LINK MG CLA C 508 O HOH C 604 1555 1555 2.14
LINK MG CLA H 101 O HOH B 755 1555 1555 2.14
LINK FE FE a 401 O1 BCT a 413 1555 1555 2.05
LINK FE FE a 401 O2 BCT a 413 1555 1555 2.03
LINK MG CLA a 405 O HOH a 544 1555 1555 2.12
LINK MG CLA b 603 O HOH b 734 1555 1555 2.13
LINK MG CLA b 609 O HOH b 756 1555 1555 2.17
LINK MG CLA b 612 O HOH b 723 1555 1555 2.14
LINK MG CLA c 505 O HOH c 655 1555 1555 2.14
LINK MG CLA c 508 O HOH c 637 1555 1555 2.13
LINK MG CLA d 401 O HOH d 542 1555 1555 2.13
CISPEP 1 TYR U 42 PRO U 43 0 0.53
CISPEP 2 ALA U 53 PRO U 54 0 1.08
CISPEP 3 THR V 63 PRO V 64 0 -9.47
CISPEP 4 TYR u 42 PRO u 43 0 8.72
CISPEP 5 ALA u 53 PRO u 54 0 6.48
CISPEP 6 THR v 63 PRO v 64 0 -5.62
SITE 1 AC1 3 ASN A 181 HIS A 332 GLU A 333
SITE 1 AC2 4 HIS A 337 ASN A 338 PHE A 339 GLU C 354
SITE 1 AC3 18 PRO A 150 SER A 153 VAL A 157 MET A 183
SITE 2 AC3 18 PHE A 186 GLN A 187 LEU A 193 HIS A 198
SITE 3 AC3 18 GLY A 201 THR A 286 ALA A 287 ILE A 290
SITE 4 AC3 18 CLA A 404 CLA A 412 PHO D 401 CLA D 402
SITE 5 AC3 18 LHG D 407 PHE T 17
SITE 1 AC4 16 GLN A 199 VAL A 202 ALA A 203 GLY A 207
SITE 2 AC4 16 TRP A 278 CLA A 403 PHO A 405 PL9 A 408
SITE 3 AC4 16 HOH A 531 VAL D 175 ILE D 178 PHE D 179
SITE 4 AC4 16 PHE D 181 LEU D 182 CLA D 402 LMG D 409
SITE 1 AC5 19 ALA A 209 LEU A 210 MET A 214 CLA A 404
SITE 2 AC5 19 PL9 A 408 ALA D 41 TRP D 48 ILE D 114
SITE 3 AC5 19 GLY D 121 LEU D 122 PHE D 125 GLN D 129
SITE 4 AC5 19 ASN D 142 PHE D 146 PHE D 153 GLY D 174
SITE 5 AC5 19 PRO D 275 LEU D 279 CLA D 402
SITE 1 AC6 18 THR A 40 PHE A 93 PRO A 95 ILE A 96
SITE 2 AC6 18 TRP A 97 LEU A 114 HIS A 118 LMG C 501
SITE 3 AC6 18 CLA C 506 CLA C 507 BCR C 516 DGD C 517
SITE 4 AC6 18 VAL I 8 TYR I 9 VAL I 11 VAL I 12
SITE 5 AC6 18 THR I 13 PHE I 15
SITE 1 AC7 6 ALA A 43 TRP A 105 LEU A 106 PHE I 15
SITE 2 AC7 6 LFA I 101 LFA b 622
SITE 1 AC8 20 PHE A 211 HIS A 215 LEU A 218 ILE A 248
SITE 2 AC8 20 HIS A 252 PHE A 255 SER A 264 PHE A 265
SITE 3 AC8 20 LEU A 271 LEU A 275 CLA A 404 PHO A 405
SITE 4 AC8 20 PHE D 38 PRO D 39 LEU D 45 SQD D 411
SITE 5 AC8 20 LHG E 101 THR F 25 LEU F 26 THR X 24
SITE 1 AC9 10 LEU A 200 ASN A 267 SER A 270 GLN C 28
SITE 2 AC9 10 ALA C 34 TRP C 36 CLA C 509 PHE D 232
SITE 3 AC9 10 LHG D 408 PHE K 37
SITE 1 AD1 1 TRP A 20
SITE 1 AD2 12 TRP A 20 ASN A 26 ARG A 27 LEU A 28
SITE 2 AD2 12 ILE A 38 LEU A 42 CLA A 412 PHE T 22
SITE 3 AD2 12 BCR T 101 TRP b 113 TYR b 117 BCR b 621
SITE 1 AD3 17 MET A 172 ILE A 176 THR A 179 PHE A 180
SITE 2 AD3 17 MET A 183 CLA A 403 SQD A 411 HOH A 504
SITE 3 AD3 17 HOH A 540 MET D 198 VAL D 201 ALA D 202
SITE 4 AD3 17 LEU D 205 GLY D 206 PHO D 401 PL9 D 405
SITE 5 AD3 17 LHG D 407
SITE 1 AD4 4 LEU A 102 ASP A 103 TRP b 75 ASP b 87
SITE 1 AD5 5 HIS A 215 HIS A 272 BCT A 415 HIS D 214
SITE 2 AD5 5 HIS D 268
SITE 1 AD6 8 HIS A 215 TYR A 246 HIS A 272 FE A 414
SITE 2 AD6 8 HIS D 214 TYR D 244 LYS D 264 HIS D 268
SITE 1 AD7 15 GLY B 189 PHE B 190 GLY B 197 HIS B 201
SITE 2 AD7 15 VAL B 208 PHE B 247 PHE B 250 CLA B 602
SITE 3 AD7 15 CLA B 608 LEU D 162 PHE H 38 ILE H 45
SITE 4 AD7 15 TYR H 49 CLA H 101 DGD H 103
SITE 1 AD8 17 ARG B 68 LEU B 69 ALA B 146 CYS B 150
SITE 2 AD8 17 HIS B 201 HIS B 202 PHE B 247 VAL B 252
SITE 3 AD8 17 THR B 262 CLA B 601 CLA B 603 CLA B 604
SITE 4 AD8 17 CLA B 605 CLA B 607 CLA B 608 HOH B 725
SITE 5 AD8 17 MET H 35
SITE 1 AD9 19 TRP B 33 PHE B 61 PHE B 65 ARG B 68
SITE 2 AD9 19 LEU B 149 VAL B 245 ALA B 248 ALA B 249
SITE 3 AD9 19 VAL B 252 PHE B 451 HIS B 455 PHE B 458
SITE 4 AD9 19 PHE B 462 CLA B 602 CLA B 604 CLA B 606
SITE 5 AD9 19 CLA B 611 CLA B 612 CLA B 614
SITE 1 AE1 20 THR B 27 VAL B 30 ALA B 31 ALA B 34
SITE 2 AE1 20 VAL B 62 MET B 66 ARG B 68 LEU B 69
SITE 3 AE1 20 VAL B 96 HIS B 100 LEU B 103 LEU B 143
SITE 4 AE1 20 ALA B 146 ALA B 205 CLA B 602 CLA B 603
SITE 5 AE1 20 CLA B 605 CLA B 609 CLA B 611 HOH B 707
SITE 1 AE2 15 LEU B 69 TRP B 91 VAL B 96 ALA B 99
SITE 2 AE2 15 LEU B 149 GLY B 152 PHE B 156 HIS B 157
SITE 3 AE2 15 PHE B 162 PRO B 164 CLA B 602 CLA B 604
SITE 4 AE2 15 BCR B 618 LFA B 622 HOH B 777
SITE 1 AE3 18 TRP B 33 MET B 37 TYR B 40 GLN B 58
SITE 2 AE3 18 GLY B 59 PHE B 61 LEU B 324 THR B 327
SITE 3 AE3 18 GLY B 328 PRO B 329 TRP B 450 CLA B 603
SITE 4 AE3 18 CLA B 612 BCR B 617 LMG B 619 HOH B 762
SITE 5 AE3 18 LHG D 406 BCR t 102
SITE 1 AE4 19 THR B 236 SER B 239 SER B 240 ALA B 243
SITE 2 AE4 19 PHE B 463 HIS B 466 ILE B 467 LEU B 474
SITE 3 AE4 19 CLA B 602 CLA B 608 CLA B 609 LFA B 625
SITE 4 AE4 19 PHE D 120 ILE D 123 MET D 126 LEU D 127
SITE 5 AE4 19 PHE D 130 CLA D 403 LEU H 46
SITE 1 AE5 17 PHE B 139 ALA B 212 PHE B 215 HIS B 216
SITE 2 AE5 17 VAL B 219 PRO B 221 PRO B 222 LEU B 225
SITE 3 AE5 17 LEU B 229 CLA B 601 CLA B 602 CLA B 607
SITE 4 AE5 17 CLA B 609 THR H 27 MET H 31 PHE H 34
SITE 5 AE5 17 BCR H 102
SITE 1 AE6 14 LEU B 135 PHE B 139 HIS B 142 LEU B 143
SITE 2 AE6 14 MET B 231 VAL B 237 SER B 240 SER B 241
SITE 3 AE6 14 CLA B 604 CLA B 607 CLA B 608 CLA B 611
SITE 4 AE6 14 CLA B 614 HOH B 748
SITE 1 AE7 18 TRP B 5 TYR B 6 ARG B 7 VAL B 8
SITE 2 AE7 18 HIS B 9 THR B 10 LEU B 238 LEU B 461
SITE 3 AE7 18 PHE B 462 GLY B 465 TRP B 468 HIS B 469
SITE 4 AE7 18 ARG B 472 CLA B 611 CLA B 612 CLA B 613
SITE 5 AE7 18 HOH B 729 LHG D 406
SITE 1 AE8 17 HIS B 9 LEU B 19 HIS B 23 HIS B 26
SITE 2 AE8 17 THR B 27 VAL B 237 LEU B 238 SER B 241
SITE 3 AE8 17 VAL B 245 CLA B 603 CLA B 604 CLA B 609
SITE 4 AE8 17 CLA B 610 CLA B 612 CLA B 613 CLA B 614
SITE 5 AE8 17 HOH B 738
SITE 1 AE9 10 HIS B 9 HIS B 26 PHE B 462 CLA B 603
SITE 2 AE9 10 CLA B 606 CLA B 610 CLA B 611 CLA B 613
SITE 3 AE9 10 BCR B 616 LMG B 619
SITE 1 AF1 12 VAL B 8 HIS B 9 TRP B 115 CLA B 610
SITE 2 AF1 12 CLA B 611 CLA B 612 BCR B 616 LMG B 619
SITE 3 AF1 12 VAL L 10 PHE M 21 LFA M 102 LFA m 101
SITE 1 AF2 11 HIS B 23 MET B 138 ILE B 141 HIS B 142
SITE 2 AF2 11 LEU B 145 CLA B 603 CLA B 609 CLA B 611
SITE 3 AF2 11 CLA B 615 LEU H 11 LEU H 14
SITE 1 AF3 6 LEU B 24 TRP B 113 HIS B 114 CLA B 614
SITE 2 AF3 6 BCR B 618 THR H 5
SITE 1 AF4 8 MET B 25 LEU B 29 CLA B 612 CLA B 613
SITE 2 AF4 8 BCR B 617 LMG B 619 SQD L 101 BCR t 102
SITE 1 AF5 7 LEU B 29 GLY B 32 TRP B 33 SER B 36
SITE 2 AF5 7 CLA B 606 BCR B 616 BCR t 102
SITE 1 AF6 5 LEU B 109 TRP B 113 CLA B 605 CLA B 615
SITE 2 AF6 5 LFA B 622
SITE 1 AF7 15 TYR B 40 THR B 327 PRO B 329 LYS B 332
SITE 2 AF7 15 CLA B 606 CLA B 612 CLA B 613 BCR B 616
SITE 3 AF7 15 HOH B 710 HOH B 732 LHG L 102 ASN M 4
SITE 4 AF7 15 LEU M 6 HOH M 203 LFA t 101
SITE 1 AF8 5 TRP B 75 LEU B 98 LFA B 623 LEU a 102
SITE 2 AF8 5 SQD a 412
SITE 1 AF9 10 PRO B 183 GLU B 184 TRP B 185 ILE B 207
SITE 2 AF9 10 MET C 180 PHE C 181 THR C 200 LEU C 204
SITE 3 AF9 10 ILE C 238 CLA H 101
SITE 1 AG1 4 TRP B 91 LEU B 149 CLA B 605 BCR B 618
SITE 1 AG2 5 TRP B 75 LFA B 620 LFA B 627 LEU a 102
SITE 2 AG2 5 ASP a 103
SITE 1 AG3 5 ARG B 224 ALA B 228 LFA B 625 PHE D 15
SITE 2 AG3 5 LFA D 412
SITE 1 AG4 4 ALA B 228 CLA B 607 LFA B 624 LFA D 412
SITE 1 AG5 1 LEU B 98
SITE 1 AG6 5 LEU B 39 LEU B 42 LFA B 623 LEU a 72
SITE 2 AG6 5 TYR a 73
SITE 1 AG7 2 LEU a 72 ILE t 4
SITE 1 AG8 15 TRP A 97 GLU A 98 PHE A 117 CLA A 406
SITE 2 AG8 15 LEU C 214 LYS C 215 PRO C 217 PHE C 218
SITE 3 AG8 15 GLU C 221 TRP C 223 MET C 281 CLA C 506
SITE 4 AG8 15 DGD C 517 LYS I 5 TYR I 9
SITE 1 AG9 18 THR C 94 LEU C 95 LEU C 168 GLY C 171
SITE 2 AG9 18 ALA C 172 LEU C 175 VAL C 233 HIS C 237
SITE 3 AG9 18 ILE C 240 ALA C 278 MET C 282 PHE C 289
SITE 4 AG9 18 VAL C 296 TYR C 297 CLA C 503 CLA C 504
SITE 5 AG9 18 CLA C 508 BCR C 516
SITE 1 AH1 19 TRP C 63 HIS C 91 LEU C 95 GLY C 171
SITE 2 AH1 19 LEU C 174 PHE C 182 LEU C 279 MET C 282
SITE 3 AH1 19 ALA C 286 VAL C 290 TYR C 297 LEU C 426
SITE 4 AH1 19 HIS C 430 LEU C 433 PHE C 437 CLA C 502
SITE 5 AH1 19 CLA C 504 CLA C 511 CLA C 513
SITE 1 AH2 16 ILE C 60 VAL C 61 THR C 68 LEU C 88
SITE 2 AH2 16 HIS C 91 VAL C 114 HIS C 118 LEU C 279
SITE 3 AH2 16 CLA C 502 CLA C 503 CLA C 508 CLA C 510
SITE 4 AH2 16 CLA C 511 CLA C 513 CLA C 514 LFA C 521
SITE 1 AH3 15 TRP C 63 PHE C 70 GLN C 84 GLY C 85
SITE 2 AH3 15 ILE C 87 TRP C 425 SER C 429 PHE C 436
SITE 3 AH3 15 DGD C 518 DGD C 519 LMG C 520 HOH C 649
SITE 4 AH3 15 LHG D 408 PRO K 26 VAL K 30
SITE 1 AH4 15 PHE A 33 LEU A 121 TRP A 131 CLA A 406
SITE 2 AH4 15 PHE C 264 TYR C 274 GLY C 277 HIS C 441
SITE 3 AH4 15 ALA C 445 ARG C 449 LMG C 501 CLA C 508
SITE 4 AH4 15 BCR C 516 VAL I 16 PHE I 23
SITE 1 AH5 15 CLA A 406 LEU C 165 LEU C 213 ILE C 243
SITE 2 AH5 15 GLY C 247 TRP C 250 HIS C 251 THR C 255
SITE 3 AH5 15 PRO C 256 PHE C 257 TRP C 259 PHE C 264
SITE 4 AH5 15 CLA C 508 BCR C 516 DGD C 517
SITE 1 AH6 17 MET C 157 LEU C 161 HIS C 164 LEU C 165
SITE 2 AH6 17 LEU C 168 TRP C 266 TYR C 271 TYR C 274
SITE 3 AH6 17 SER C 275 MET C 282 CLA C 502 CLA C 504
SITE 4 AH6 17 CLA C 506 CLA C 507 CLA C 510 BCR C 516
SITE 5 AH6 17 HOH C 604
SITE 1 AH7 19 SQD A 409 PHE C 33 TRP C 36 ALA C 37
SITE 2 AH7 19 GLY C 38 ASN C 39 LEU C 272 LEU C 276
SITE 3 AH7 19 PHE C 436 GLY C 440 TRP C 443 HIS C 444
SITE 4 AH7 19 ARG C 447 CLA C 510 CLA C 511 CLA C 512
SITE 5 AH7 19 DGD C 518 DGD C 519 LHG D 408
SITE 1 AH8 18 ASN C 39 LEU C 42 LEU C 49 ALA C 52
SITE 2 AH8 18 HIS C 53 HIS C 56 TYR C 149 GLY C 268
SITE 3 AH8 18 TYR C 271 LEU C 272 SER C 275 LEU C 279
SITE 4 AH8 18 CLA C 504 CLA C 508 CLA C 509 CLA C 511
SITE 5 AH8 18 CLA C 512 CLA C 513
SITE 1 AH9 16 ASN C 39 HIS C 56 TRP C 63 LEU C 279
SITE 2 AH9 16 PHE C 436 PHE C 437 CLA C 503 CLA C 504
SITE 3 AH9 16 CLA C 509 CLA C 510 CLA C 512 LMG C 520
SITE 4 AH9 16 LHG D 408 PRO K 29 VAL K 30 LEU K 33
SITE 1 AI1 20 TRP C 35 GLY C 38 ASN C 39 ARG C 41
SITE 2 AI1 20 LEU C 42 LEU C 45 LYS C 48 PHE C 127
SITE 3 AI1 20 ILE C 134 CLA C 509 CLA C 510 CLA C 511
SITE 4 AI1 20 PHE K 32 TRP K 39 GLN K 40 BCR K 102
SITE 5 AI1 20 LEU Y 39 ASN Y 45 VAL Z 20 ALA Z 28
SITE 1 AI2 12 LEU C 50 HIS C 53 LEU C 125 PHE C 147
SITE 2 AI2 12 PHE C 163 HIS C 164 ILE C 166 VAL C 167
SITE 3 AI2 12 CLA C 503 CLA C 504 CLA C 510 CLA C 514
SITE 1 AI3 10 LEU C 50 VAL C 124 GLY C 128 TYR C 131
SITE 2 AI3 10 HIS C 132 TYR C 143 CLA C 504 CLA C 513
SITE 3 AI3 10 BCR C 515 LFA C 521
SITE 1 AI4 5 PHE C 112 SER C 121 CLA C 514 TYR K 15
SITE 2 AI4 5 GLY Z 55
SITE 1 AI5 12 CLA A 406 ILE C 209 LEU C 213 ASP C 232
SITE 2 AI5 12 GLY C 236 ILE C 240 PHE C 264 CLA C 502
SITE 3 AI5 12 CLA C 506 CLA C 507 CLA C 508 LEU I 24
SITE 1 AI6 20 PHE A 155 ILE A 163 CLA A 406 PRO C 217
SITE 2 AI6 20 GLY C 219 GLY C 220 GLU C 221 GLY C 222
SITE 3 AI6 20 TRP C 223 CYS C 288 ASN C 293 ASN C 294
SITE 4 AI6 20 THR C 295 ASP C 360 PHE C 361 ARG C 362
SITE 5 AI6 20 LEU C 438 LMG C 501 CLA C 507 HOH C 653
SITE 1 AI7 16 PHE A 197 GLU C 83 GLN C 84 GLY C 85
SITE 2 AI7 16 SER C 406 ASN C 418 PHE C 419 VAL C 420
SITE 3 AI7 16 TRP C 425 THR C 428 CLA C 505 CLA C 509
SITE 4 AI7 16 DGD C 519 LMG C 520 TYR J 33 LFA J 101
SITE 1 AI8 19 GLN A 199 PHE A 300 SER A 305 ASN C 405
SITE 2 AI8 19 ASN C 415 SER C 416 ASN C 418 CLA C 505
SITE 3 AI8 19 CLA C 509 DGD C 518 HOH C 637 LHG D 408
SITE 4 AI8 19 PHE J 29 ALA J 32 TYR J 33 GLY J 37
SITE 5 AI8 19 SER J 38 SER J 39 GLN V 34
SITE 1 AI9 6 HIS C 74 CLA C 505 CLA C 511 DGD C 518
SITE 2 AI9 6 LFA J 101 ASP K 23
SITE 1 AJ1 5 TRP C 97 VAL C 117 HIS C 118 CLA C 504
SITE 2 AJ1 5 CLA C 514
SITE 1 AJ2 7 THR B 159 LEU B 161 ALA B 182 PRO B 183
SITE 2 AJ2 7 TRP B 185 LEU C 204 PRO C 206
SITE 1 AJ3 16 LEU A 41 THR A 45 TYR A 126 GLN A 130
SITE 2 AJ3 16 TYR A 147 GLY A 175 VAL A 283 CLA A 403
SITE 3 AJ3 16 CLA A 412 ALA D 208 LEU D 209 ILE D 213
SITE 4 AJ3 16 TRP D 253 PHE D 257 PL9 D 405 LHG D 407
SITE 1 AJ4 19 PHE A 206 CLA A 403 CLA A 404 PHO A 405
SITE 2 AJ4 19 PRO D 149 VAL D 152 VAL D 156 PHE D 181
SITE 3 AJ4 19 LEU D 182 PHE D 185 GLN D 186 TRP D 191
SITE 4 AJ4 19 THR D 192 HIS D 197 GLY D 200 VAL D 204
SITE 5 AJ4 19 SER D 282 ALA D 283 VAL D 286
SITE 1 AJ5 19 CLA B 607 ILE D 35 CYS D 40 LEU D 43
SITE 2 AJ5 19 LEU D 89 LEU D 90 LEU D 91 LEU D 92
SITE 3 AJ5 19 TRP D 93 THR D 112 PHE D 113 LEU D 116
SITE 4 AJ5 19 HIS D 117 LFA D 413 PHE X 11 GLY X 13
SITE 5 AJ5 19 LEU X 14 ALA X 18 VAL X 20
SITE 1 AJ6 12 TYR D 42 LEU D 43 GLY D 46 LEU D 49
SITE 2 AJ6 12 THR D 50 PHE D 101 LMG D 409 PRO F 29
SITE 3 AJ6 12 PHE F 33 LEU F 34 VAL J 21 VAL J 25
SITE 1 AJ7 19 ILE A 77 ILE A 176 CLA A 412 MET D 199
SITE 2 AJ7 19 ALA D 202 LEU D 210 HIS D 214 THR D 217
SITE 3 AJ7 19 MET D 246 TRP D 253 ALA D 260 PHE D 261
SITE 4 AJ7 19 LEU D 267 VAL D 274 PHO D 401 VAL L 26
SITE 5 AJ7 19 LEU L 29 LHG L 102 PHE T 10
SITE 1 AJ8 14 SER A 232 ASN A 234 TYR B 6 ARG B 7
SITE 2 AJ8 14 PHE B 464 TRP B 468 CLA B 606 CLA B 610
SITE 3 AJ8 14 HOH B 729 TYR D 141 TRP D 266 PHE D 269
SITE 4 AJ8 14 LHG L 102 PRO M 18
SITE 1 AJ9 23 MET A 37 CLA A 403 CLA A 412 ILE D 256
SITE 2 AJ9 23 PHE D 257 ILE D 259 ALA D 260 PHE D 261
SITE 3 AJ9 23 SER D 262 ASN D 263 TRP D 266 PHO D 401
SITE 4 AJ9 23 HOH D 538 ASN L 13 THR L 15 SER L 16
SITE 5 AJ9 23 TYR L 18 LEU L 19 LHG L 102 HOH L 202
SITE 6 AJ9 23 PHE T 17 ALA T 20 ILE T 21
SITE 1 AK1 15 ARG A 140 TRP A 142 PHE A 273 SQD A 409
SITE 2 AK1 15 TRP C 36 ARG C 447 CLA C 505 CLA C 509
SITE 3 AK1 15 CLA C 511 DGD C 519 ASN D 220 ALA D 229
SITE 4 AK1 15 SER D 230 THR D 231 PHE D 232
SITE 1 AK2 16 CLA A 404 HOH C 637 TYR D 67 GLY D 70
SITE 2 AK2 16 ASN D 72 PHE D 73 BCR D 404 HOH D 515
SITE 3 AK2 16 ALA F 27 THR F 30 MET F 40 GLN F 41
SITE 4 AK2 16 PHE J 28 GLY J 31 ALA J 32 LEU J 36
SITE 1 AK3 1 LYS D 23
SITE 1 AK4 12 PL9 A 408 ARG D 24 ARG D 26 HOH D 522
SITE 2 AK4 12 HOH D 548 PHE F 16 THR F 17 VAL F 18
SITE 3 AK4 12 VAL F 21 GLN R 30 ILE X 31 ASP X 35
SITE 1 AK5 5 LFA B 624 LFA B 625 ASP D 19 LYS D 23
SITE 2 AK5 5 TRP D 32
SITE 1 AK6 3 TRP D 93 CLA D 403 LEU X 21
SITE 1 AK7 8 LEU A 258 TYR A 262 ALA A 263 PL9 A 408
SITE 2 AK7 8 PRO E 9 PHE E 10 SER E 11 VAL F 23
SITE 1 AK8 17 PHE E 10 ILE E 13 ARG E 18 TYR E 19
SITE 2 AK8 17 HIS E 23 THR E 26 ILE E 27 LEU E 30
SITE 3 AK8 17 ILE F 15 PHE F 16 ARG F 19 TRP F 20
SITE 4 AK8 17 HIS F 24 ALA F 27 ILE F 31 ALA R 19
SITE 5 AK8 17 ILE R 23
SITE 1 AK9 8 TRP B 185 GLY B 186 PHE B 190 CLA B 601
SITE 2 AK9 8 LMG B 621 HOH B 755 PHE H 41 BCR H 102
SITE 1 AL1 6 CLA B 608 PHE H 38 PHE H 41 CLA H 101
SITE 2 AL1 6 THR X 2 LEU X 7
SITE 1 AL2 15 TYR B 193 TYR B 258 TYR B 273 GLN B 274
SITE 2 AL2 15 SER B 277 PHE B 463 CLA B 601 HOH B 720
SITE 3 AL2 15 HIS D 87 LEU D 162 TYR H 49 ASN H 50
SITE 4 AL2 15 VAL H 60 SER H 61 TRP H 62
SITE 1 AL3 1 BCR A 407
SITE 1 AL4 2 DGD C 518 LMG C 520
SITE 1 AL5 12 PHE C 62 ALA J 14 THR J 15 LEU K 31
SITE 2 AL5 12 ALA K 34 VAL K 38 BCR K 102 ILE Y 28
SITE 3 AL5 12 GLY Y 29 GLY Y 32 SER Z 16 PHE Z 17
SITE 1 AL6 9 ALA C 55 LEU C 59 ALA C 123 VAL C 130
SITE 2 AL6 9 CLA C 512 PHE K 32 BCR K 101 LEU Z 12
SITE 3 AL6 9 SER Z 16
SITE 1 AL7 10 ARG B 18 SER B 104 TRP B 115 BCR B 616
SITE 2 AL7 10 ARG L 7 ARG l 14 TYR l 18 TYR m 26
SITE 3 AL7 10 PHE t 23 BCR t 102
SITE 1 AL8 17 SER A 232 ASN A 234 PRO B 4 TRP B 5
SITE 2 AL8 17 TYR B 6 LMG B 619 TRP D 266 PHE D 273
SITE 3 AL8 17 PL9 D 405 LHG D 406 LHG D 407 GLU L 11
SITE 4 AL8 17 LEU L 12 ASN L 13 SER L 16 VAL L 26
SITE 5 AL8 17 PHE M 21
SITE 1 AL9 2 SQD b 601 LFA m 102
SITE 1 AM1 4 CLA B 613 ILE M 24 VAL m 27 LFA m 101
SITE 1 AM2 12 SQD A 411 ALA T 11 ALA T 15 PHE T 18
SITE 2 AM2 12 PHE T 22 SER b 36 TYR b 40 SQD b 601
SITE 3 AM2 12 LFA b 602 CLA b 609 BCR b 619 BCR b 620
SITE 1 AM3 3 LEU M 8 ALA M 12 CLA b 616
SITE 1 AM4 18 ALA V 36 CYS V 37 SER V 39 CYS V 40
SITE 2 AM4 18 HIS V 41 THR V 46 THR V 48 LEU V 52
SITE 3 AM4 18 ASP V 53 THR V 58 LEU V 59 LEU V 72
SITE 4 AM4 18 TYR V 75 MET V 76 TYR V 82 HIS V 92
SITE 5 AM4 18 HOH V 301 HOH V 308
SITE 1 AM5 5 HIS a 215 HIS a 272 BCT a 413 HIS d 214
SITE 2 AM5 5 HIS d 268
SITE 1 AM6 2 ASN a 181 GLU a 333
SITE 1 AM7 4 HIS a 337 ASN a 338 PHE a 339 GLU c 354
SITE 1 AM8 18 TYR a 147 PRO a 150 SER a 153 VAL a 157
SITE 2 AM8 18 MET a 183 PHE a 186 GLN a 187 HIS a 198
SITE 3 AM8 18 GLY a 201 VAL a 202 THR a 286 ALA a 287
SITE 4 AM8 18 ILE a 290 CLA a 405 PHO a 406 CLA d 401
SITE 5 AM8 18 CLA d 402 LHG d 406
SITE 1 AM9 18 PHE a 158 MET a 172 ILE a 176 THR a 179
SITE 2 AM9 18 PHE a 180 MET a 183 CLA a 404 PHO a 406
SITE 3 AM9 18 HOH a 544 MET d 198 VAL d 201 ALA d 202
SITE 4 AM9 18 LEU d 205 GLY d 206 CLA d 402 PL9 d 405
SITE 5 AM9 18 LHG l 101 PHE t 10
SITE 1 AN1 16 LEU a 41 ALA a 44 THR a 45 TYR a 126
SITE 2 AN1 16 GLN a 130 ALA a 146 TYR a 147 PRO a 150
SITE 3 AN1 16 GLY a 175 CLA a 404 CLA a 405 SQD a 412
SITE 4 AN1 16 ALA d 208 LEU d 209 ILE d 213 TRP d 253
SITE 1 AN2 18 THR a 40 PHE a 93 PRO a 95 ILE a 96
SITE 2 AN2 18 TRP a 97 LEU a 114 HIS a 118 LMG c 501
SITE 3 AN2 18 CLA c 506 CLA c 507 BCR c 515 DGD c 516
SITE 4 AN2 18 VAL i 8 TYR i 9 VAL i 11 VAL i 12
SITE 5 AN2 18 THR i 13 PHE i 15
SITE 1 AN3 4 LEU a 42 ALA a 43 ILE a 50 LFA i 101
SITE 1 AN4 17 PHE a 211 HIS a 215 LEU a 218 ILE a 248
SITE 2 AN4 17 PHE a 255 ILE a 259 SER a 264 PHE a 265
SITE 3 AN4 17 LEU a 271 PHO a 414 PHE d 38 PRO d 39
SITE 4 AN4 17 CLA d 402 LHG e 101 THR f 25 SQD f 102
SITE 5 AN4 17 THR x 24
SITE 1 AN5 17 LEU a 200 ALA a 203 GLY a 204 ASN a 267
SITE 2 AN5 17 SER a 270 PHE a 274 ALA a 277 TRP a 278
SITE 3 AN5 17 VAL a 281 GLN c 28 TRP c 36 LMG c 519
SITE 4 AN5 17 BCR c 523 PHE d 232 ARG d 233 LHG d 407
SITE 5 AN5 17 PHE k 37
SITE 1 AN6 1 TRP a 20
SITE 1 AN7 8 TRP B 113 TYR B 117 LFA B 620 ASN a 26
SITE 2 AN7 8 ARG a 27 LEU a 28 THR a 45 PHO a 406
SITE 1 AN8 8 HIS a 215 GLU a 244 TYR a 246 HIS a 272
SITE 2 AN8 8 FE a 401 HIS d 214 TYR d 244 HIS d 268
SITE 1 AN9 19 ALA a 209 LEU a 210 MET a 214 LEU a 258
SITE 2 AN9 19 PL9 a 409 TRP d 48 ILE d 114 GLY d 121
SITE 3 AN9 19 PHE d 125 GLN d 129 ASN d 142 PHE d 146
SITE 4 AN9 19 PHE d 153 PHE d 173 GLY d 174 PRO d 275
SITE 5 AN9 19 LEU d 279 CLA d 401 CLA d 402
SITE 1 AO1 14 ARG L 14 TYR L 18 LEU L 21 TYR M 26
SITE 2 AO1 14 LFA M 101 PHE T 23 BCR T 101 ARG b 18
SITE 3 AO1 14 SER b 104 PHE b 108 TRP b 115 CLA b 616
SITE 4 AO1 14 BCR b 619 ARG l 7
SITE 1 AO2 1 BCR T 101
SITE 1 AO3 8 TRP b 185 PHE b 190 CLA b 604 LMG b 624
SITE 2 AO3 8 HOH b 734 PHE h 41 LEU h 55 BCR h 101
SITE 1 AO4 16 GLY b 189 PHE b 190 PRO b 192 GLY b 197
SITE 2 AO4 16 HIS b 201 PHE b 247 PHE b 250 CLA b 603
SITE 3 AO4 16 CLA b 605 CLA b 611 LEU d 162 PHE h 38
SITE 4 AO4 16 ILE h 45 TYR h 49 BCR h 101 DGD h 102
SITE 1 AO5 17 ARG b 68 LEU b 69 ALA b 146 CYS b 150
SITE 2 AO5 17 PHE b 153 HIS b 201 HIS b 202 PHE b 247
SITE 3 AO5 17 VAL b 252 THR b 262 CLA b 604 CLA b 606
SITE 4 AO5 17 CLA b 607 CLA b 608 CLA b 611 HOH b 713
SITE 5 AO5 17 PHE h 38
SITE 1 AO6 18 TRP b 33 PHE b 61 PHE b 65 ARG b 68
SITE 2 AO6 18 LEU b 149 VAL b 245 ALA b 248 ALA b 249
SITE 3 AO6 18 VAL b 252 PHE b 451 HIS b 455 PHE b 458
SITE 4 AO6 18 PHE b 462 CLA b 605 CLA b 607 CLA b 609
SITE 5 AO6 18 CLA b 614 CLA b 615
SITE 1 AO7 16 THR b 27 VAL b 30 TRP b 33 ALA b 34
SITE 2 AO7 16 VAL b 62 MET b 66 ARG b 68 VAL b 96
SITE 3 AO7 16 HIS b 100 ALA b 205 CLA b 605 CLA b 606
SITE 4 AO7 16 CLA b 608 CLA b 611 CLA b 612 CLA b 614
SITE 1 AO8 15 LEU b 69 PHE b 90 TRP b 91 VAL b 96
SITE 2 AO8 15 ALA b 99 GLY b 152 PHE b 153 HIS b 157
SITE 3 AO8 15 PHE b 162 PRO b 164 CLA b 605 CLA b 607
SITE 4 AO8 15 LFA b 625 LFA b 627 HOH b 729
SITE 1 AO9 17 BCR T 101 TRP b 33 MET b 37 TYR b 40
SITE 2 AO9 17 GLN b 58 GLY b 59 PHE b 61 LEU b 324
SITE 3 AO9 17 THR b 327 GLY b 328 TRP b 450 CLA b 606
SITE 4 AO9 17 BCR b 620 LHG b 628 HOH b 756 MET d 281
SITE 5 AO9 17 LMG m 103
SITE 1 AP1 18 THR b 236 SER b 239 SER b 240 ALA b 243
SITE 2 AP1 18 PHE b 463 HIS b 466 THR b 473 LEU b 474
SITE 3 AP1 18 CLA b 611 CLA b 612 LFA b 629 LEU d 89
SITE 4 AP1 18 PHE d 120 ILE d 123 MET d 126 LEU h 39
SITE 5 AP1 18 LEU h 43 DGD h 102
SITE 1 AP2 18 PHE b 139 ALA b 212 PHE b 215 HIS b 216
SITE 2 AP2 18 VAL b 219 PRO b 221 PRO b 222 LEU b 229
SITE 3 AP2 18 CLA b 604 CLA b 605 CLA b 607 CLA b 610
SITE 4 AP2 18 CLA b 612 LFA b 629 THR h 27 MET h 31
SITE 5 AP2 18 PHE h 34 BCR h 101
SITE 1 AP3 13 PHE b 139 HIS b 142 LEU b 143 MET b 231
SITE 2 AP3 13 VAL b 237 SER b 240 SER b 241 CLA b 607
SITE 3 AP3 13 CLA b 610 CLA b 611 CLA b 614 CLA b 617
SITE 4 AP3 13 HOH b 723
SITE 1 AP4 16 TRP b 5 TYR b 6 ARG b 7 VAL b 8
SITE 2 AP4 16 HIS b 9 LEU b 461 GLY b 465 TRP b 468
SITE 3 AP4 16 HIS b 469 ARG b 472 CLA b 614 CLA b 615
SITE 4 AP4 16 CLA b 616 LHG b 628 HOH b 712 LHG l 101
SITE 1 AP5 16 HIS b 9 LEU b 19 HIS b 23 HIS b 26
SITE 2 AP5 16 THR b 27 VAL b 237 LEU b 238 SER b 241
SITE 3 AP5 16 CLA b 606 CLA b 607 CLA b 612 CLA b 613
SITE 4 AP5 16 CLA b 615 CLA b 616 CLA b 617 HOH b 753
SITE 1 AP6 10 HIS b 9 HIS b 26 PHE b 462 CLA b 606
SITE 2 AP6 10 CLA b 613 CLA b 614 CLA b 616 BCR b 619
SITE 3 AP6 10 PHE m 14 LMG m 103
SITE 1 AP7 13 PHE T 8 LFA T 102 VAL b 8 HIS b 9
SITE 2 AP7 13 SQD b 601 CLA b 613 CLA b 614 CLA b 615
SITE 3 AP7 13 BCR b 619 GLN l 8 VAL l 10 PHE m 21
SITE 4 AP7 13 LMG m 103
SITE 1 AP8 11 ILE b 20 HIS b 23 LEU b 24 MET b 138
SITE 2 AP8 11 ILE b 141 HIS b 142 LEU b 145 CLA b 612
SITE 3 AP8 11 CLA b 614 CLA b 618 LEU h 14
SITE 1 AP9 11 ILE b 20 LEU b 24 TRP b 113 HIS b 114
SITE 2 AP9 11 LEU b 120 LEU b 122 PHE b 123 CLA b 617
SITE 3 AP9 11 BCR b 621 THR h 5 LEU h 7
SITE 1 AQ1 9 PHE T 19 BCR T 101 MET b 25 LEU b 29
SITE 2 AQ1 9 TRP b 115 SQD b 601 CLA b 615 CLA b 616
SITE 3 AQ1 9 BCR b 620
SITE 1 AQ2 9 BCR T 101 LEU b 29 GLY b 32 TRP b 33
SITE 2 AQ2 9 SER b 36 VAL b 102 GLY b 105 CLA b 609
SITE 3 AQ2 9 BCR b 619
SITE 1 AQ3 6 SQD A 411 PHE T 22 LEU b 106 LEU b 109
SITE 2 AQ3 6 ALA b 110 CLA b 618
SITE 1 AQ4 4 BCR A 407 TRP b 75 LEU b 98 LFA b 627
SITE 1 AQ5 3 LEU A 72 LEU b 39 ALA b 43
SITE 1 AQ6 7 GLU b 184 TRP b 185 CLA b 603 ASN c 201
SITE 2 AQ6 7 PRO c 202 ILE c 238 LMG c 522
SITE 1 AQ7 3 PHE b 90 TRP b 91 CLA b 608
SITE 1 AQ8 1 LEU b 98
SITE 1 AQ9 2 CLA b 608 LFA b 622
SITE 1 AR1 13 ASN a 234 TYR b 6 ARG b 7 PHE b 464
SITE 2 AR1 13 TRP b 468 CLA b 609 CLA b 613 HOH b 712
SITE 3 AR1 13 TYR d 141 TRP d 266 PHE d 269 PHE d 273
SITE 4 AR1 13 LHG l 101
SITE 1 AR2 3 CLA b 610 CLA b 611 LFA d 409
SITE 1 AR3 4 ARG b 224 LEU b 225 ASP d 16 LFA d 409
SITE 1 AR4 11 TRP a 97 PHE a 117 CLA a 407 LEU c 214
SITE 2 AR4 11 LYS c 215 SER c 216 PHE c 218 TRP c 223
SITE 3 AR4 11 CLA c 506 LYS i 5 TYR i 9
SITE 1 AR5 16 LEU c 95 LEU c 168 GLY c 171 ALA c 172
SITE 2 AR5 16 HIS c 237 ILE c 240 ALA c 278 MET c 282
SITE 3 AR5 16 PHE c 289 VAL c 296 TYR c 297 CLA c 503
SITE 4 AR5 16 CLA c 504 CLA c 507 CLA c 508 BCR c 515
SITE 1 AR6 15 TRP c 63 HIS c 91 LEU c 95 LEU c 174
SITE 2 AR6 15 LEU c 279 ALA c 286 VAL c 290 TYR c 297
SITE 3 AR6 15 HIS c 430 PHE c 437 CLA c 502 CLA c 504
SITE 4 AR6 15 CLA c 511 CLA c 513 HOH c 627
SITE 1 AR7 15 VAL c 61 ALA c 64 THR c 68 LEU c 88
SITE 2 AR7 15 HIS c 91 HIS c 118 LEU c 279 CLA c 502
SITE 3 AR7 15 CLA c 503 CLA c 508 CLA c 510 CLA c 511
SITE 4 AR7 15 CLA c 513 CLA c 514 LFA c 521
SITE 1 AR8 17 TRP c 63 MET c 67 PHE c 70 GLN c 84
SITE 2 AR8 17 GLY c 85 ILE c 87 TRP c 425 SER c 429
SITE 3 AR8 17 PHE c 436 CLA c 509 CLA c 511 DGD c 517
SITE 4 AR8 17 DGD c 518 LMG c 519 HOH c 655 LHG d 407
SITE 5 AR8 17 PRO k 26
SITE 1 AR9 16 LEU a 121 TRP a 131 CLA a 407 PHE c 264
SITE 2 AR9 16 SER c 273 TYR c 274 GLY c 277 MET c 281
SITE 3 AR9 16 HIS c 441 LEU c 442 ALA c 445 ARG c 449
SITE 4 AR9 16 LMG c 501 CLA c 508 BCR c 515 PHE i 23
SITE 1 AS1 15 CLA a 407 LEU c 161 LEU c 165 ILE c 243
SITE 2 AS1 15 GLY c 247 TRP c 250 HIS c 251 THR c 255
SITE 3 AS1 15 PRO c 256 PHE c 257 TRP c 259 PHE c 264
SITE 4 AS1 15 CLA c 502 CLA c 508 BCR c 515
SITE 1 AS2 15 LEU c 161 HIS c 164 LEU c 165 LEU c 168
SITE 2 AS2 15 TRP c 266 TYR c 271 TYR c 274 MET c 282
SITE 3 AS2 15 CLA c 502 CLA c 504 CLA c 506 CLA c 507
SITE 4 AS2 15 CLA c 510 BCR c 515 HOH c 637
SITE 1 AS3 18 PHE c 33 TRP c 36 ALA c 37 GLY c 38
SITE 2 AS3 18 ASN c 39 LEU c 272 LEU c 276 PHE c 436
SITE 3 AS3 18 GLY c 440 TRP c 443 HIS c 444 ARG c 447
SITE 4 AS3 18 CLA c 505 CLA c 510 CLA c 511 CLA c 512
SITE 5 AS3 18 LMG c 519 LHG d 407
SITE 1 AS4 16 ASN c 39 LEU c 49 ALA c 52 HIS c 53
SITE 2 AS4 16 HIS c 56 TYR c 149 ILE c 160 LEU c 272
SITE 3 AS4 16 SER c 275 LEU c 279 CLA c 504 CLA c 508
SITE 4 AS4 16 CLA c 509 CLA c 511 CLA c 512 CLA c 513
SITE 1 AS5 15 ASN c 39 HIS c 56 LEU c 433 PHE c 437
SITE 2 AS5 15 CLA c 503 CLA c 504 CLA c 505 CLA c 509
SITE 3 AS5 15 CLA c 510 CLA c 512 LMG c 519 LHG d 407
SITE 4 AS5 15 PRO k 29 VAL k 30 LEU k 33
SITE 1 AS6 20 ARG c 26 TRP c 35 GLY c 38 ASN c 39
SITE 2 AS6 20 ARG c 41 LEU c 42 LEU c 45 LYS c 48
SITE 3 AS6 20 ALA c 52 ILE c 134 CLA c 509 CLA c 510
SITE 4 AS6 20 CLA c 511 PHE k 32 LEU k 33 TRP k 39
SITE 5 AS6 20 GLN k 40 BCR k 101 VAL z 20 ALA z 28
SITE 1 AS7 11 HIS c 53 PHE c 147 PHE c 163 HIS c 164
SITE 2 AS7 11 VAL c 167 GLY c 171 CLA c 503 CLA c 504
SITE 3 AS7 11 CLA c 510 CLA c 514 BCR c 524
SITE 1 AS8 10 GLY c 128 TYR c 131 HIS c 132 PRO c 137
SITE 2 AS8 10 LEU c 140 TYR c 143 PHE c 147 CLA c 504
SITE 3 AS8 10 CLA c 513 BCR c 524
SITE 1 AS9 12 CLA a 407 ILE c 209 LEU c 213 GLY c 236
SITE 2 AS9 12 HIS c 237 ILE c 240 PHE c 264 CLA c 502
SITE 3 AS9 12 CLA c 506 CLA c 507 CLA c 508 LEU i 24
SITE 1 AT1 24 PHE a 155 ILE a 160 ILE a 163 CLA a 407
SITE 2 AT1 24 PRO c 217 PHE c 218 GLY c 219 GLY c 220
SITE 3 AT1 24 GLU c 221 GLY c 222 VAL c 225 MET c 281
SITE 4 AT1 24 PHE c 284 CYS c 288 PHE c 292 ASN c 293
SITE 5 AT1 24 ASN c 294 THR c 295 ASP c 360 PHE c 361
SITE 6 AT1 24 ARG c 362 HOH c 613 HOH c 644 HOH c 656
SITE 1 AT2 19 HIS a 195 PHE a 197 HOH a 507 GLU c 83
SITE 2 AT2 19 GLN c 84 GLY c 85 SER c 406 ASN c 418
SITE 3 AT2 19 PHE c 419 VAL c 420 TRP c 425 THR c 428
SITE 4 AT2 19 SER c 429 CLA c 505 DGD c 518 LMG c 519
SITE 5 AT2 19 HOH c 603 TYR j 33 LFA j 101
SITE 1 AT3 21 LEU a 200 ALA a 203 PHE a 300 PHE a 302
SITE 2 AT3 21 SER a 305 ASN c 405 ASN c 415 SER c 416
SITE 3 AT3 21 ASN c 418 CLA c 505 DGD c 517 CLA d 401
SITE 4 AT3 21 LHG d 407 LMG f 101 HOH f 202 PHE j 29
SITE 5 AT3 21 ALA j 32 TYR j 33 GLY j 37 SER j 38
SITE 6 AT3 21 GLN v 34
SITE 1 AT4 11 SQD a 410 HIS c 74 CLA c 505 CLA c 509
SITE 2 AT4 11 CLA c 511 DGD c 517 HOH c 633 ILE j 22
SITE 3 AT4 11 LFA j 101 ASP k 23 ILE y 25
SITE 1 AT5 2 TRP c 35 PHE k 45
SITE 1 AT6 5 TRP c 97 VAL c 113 VAL c 117 SER c 121
SITE 2 AT6 5 CLA c 504
SITE 1 AT7 9 ALA b 155 THR b 159 LEU b 161 ALA b 182
SITE 2 AT7 9 LMG b 624 LEU c 204 ASP c 205 PRO c 206
SITE 3 AT7 9 ALA c 246
SITE 1 AT8 15 SQD a 410 PHE c 62 THR j 15 GLY j 18
SITE 2 AT8 15 MET j 19 ILE k 28 LEU k 31 ALA k 34
SITE 3 AT8 15 VAL k 38 BCR k 101 GLY y 29 GLY y 32
SITE 4 AT8 15 SER z 16 PHE z 17 VAL z 20
SITE 1 AT9 7 PHE c 112 VAL c 116 SER c 121 PHE c 147
SITE 2 AT9 7 CLA c 513 CLA c 514 TYR k 15
SITE 1 AU1 14 GLN a 199 VAL a 202 GLY a 207 TRP a 278
SITE 2 AU1 14 CLA a 404 PHO a 414 DGD c 518 VAL d 175
SITE 3 AU1 14 ILE d 178 PHE d 179 PHE d 181 CLA d 402
SITE 4 AU1 14 HOH d 542 LMG f 101
SITE 1 AU2 20 PHE a 206 CLA a 404 CLA a 405 PL9 a 409
SITE 2 AU2 20 PHO a 414 VAL d 152 VAL d 156 LEU d 182
SITE 3 AU2 20 PHE d 185 GLN d 186 TRP d 191 THR d 192
SITE 4 AU2 20 HIS d 197 GLY d 200 VAL d 204 SER d 282
SITE 5 AU2 20 ALA d 283 VAL d 286 CLA d 401 LMG f 101
SITE 1 AU3 18 ILE d 35 CYS d 40 LEU d 43 LEU d 89
SITE 2 AU3 18 LEU d 90 LEU d 91 LEU d 92 TRP d 93
SITE 3 AU3 18 TRP d 104 THR d 112 PHE d 113 LEU d 116
SITE 4 AU3 18 HIS d 117 LFA d 410 LEU h 37 VAL h 40
SITE 5 AU3 18 LEU x 14 VAL x 20
SITE 1 AU4 12 TYR d 42 LEU d 43 GLY d 46 GLY d 47
SITE 2 AU4 12 LEU d 49 THR d 50 PRO f 29 THR f 30
SITE 3 AU4 12 PHE f 33 LMG f 101 VAL j 21 VAL j 25
SITE 1 AU5 18 ILE a 53 ILE a 77 ILE a 176 CLA a 405
SITE 2 AU5 18 MET d 198 MET d 199 HIS d 214 THR d 217
SITE 3 AU5 18 MET d 246 TRP d 253 ALA d 260 PHE d 261
SITE 4 AU5 18 VAL d 274 LHG d 406 VAL l 26 LEU l 29
SITE 5 AU5 18 LHG l 101 PHE t 10
SITE 1 AU6 17 MET a 37 CLA a 404 PHE d 257 PHE d 261
SITE 2 AU6 17 SER d 262 ASN d 263 TRP d 266 PL9 d 405
SITE 3 AU6 17 ASN l 13 THR l 15 SER l 16 TYR l 18
SITE 4 AU6 17 LHG l 101 HOH l 202 PHE t 17 ALA t 20
SITE 5 AU6 17 ILE t 21
SITE 1 AU7 18 ARG a 140 TRP a 142 PHE a 273 TRP a 284
SITE 2 AU7 18 SQD a 410 TRP c 36 TRP c 443 ARG c 447
SITE 3 AU7 18 CLA c 505 CLA c 509 CLA c 511 DGD c 518
SITE 4 AU7 18 GLU d 219 ASN d 220 ALA d 229 SER d 230
SITE 5 AU7 18 THR d 231 PHE d 232
SITE 1 AU8 3 LFA b 629 LFA b 630 TRP d 32
SITE 1 AU9 6 TRP d 93 GLN d 98 GLY d 99 CLA d 403
SITE 2 AU9 6 ILE x 12 SER x 16
SITE 1 AV1 7 TYR a 262 PL9 a 409 LEU d 37 PRO e 9
SITE 2 AV1 7 PHE e 10 SER e 11 VAL f 23
SITE 1 AV2 15 ILE e 13 ARG e 18 TYR e 19 HIS e 23
SITE 2 AV2 15 THR e 26 LEU e 30 HOH e 202 ILE f 15
SITE 3 AV2 15 ARG f 19 TRP f 20 HIS f 24 ALA f 27
SITE 4 AV2 15 ILE f 31 ALA r 19 ILE r 23
SITE 1 AV3 18 DGD c 518 TYR d 67 GLY d 70 CYS d 71
SITE 2 AV3 18 ASN d 72 PHE d 73 CLA d 401 CLA d 402
SITE 3 AV3 18 BCR d 404 THR f 30 MET f 40 GLN f 41
SITE 4 AV3 18 HOH f 201 HOH f 202 PHE j 28 GLY j 31
SITE 5 AV3 18 ALA j 32 LEU j 36
SITE 1 AV4 11 PL9 a 409 ARG d 26 PHE f 16 THR f 17
SITE 2 AV4 11 VAL f 18 VAL f 21 GLN r 30 LEU r 34
SITE 3 AV4 11 THR x 24 VAL x 27 ASP x 35
SITE 1 AV5 9 CLA b 603 CLA b 604 CLA b 611 LEU h 37
SITE 2 AV5 9 PHE h 38 PHE h 41 LEU h 55 ILE x 3
SITE 3 AV5 9 LEU x 7
SITE 1 AV6 16 TYR b 193 PHE b 250 TYR b 258 TYR b 273
SITE 2 AV6 16 TYR b 279 CLA b 604 CLA b 610 HOH b 726
SITE 3 AV6 16 HIS d 87 LEU d 162 LEU d 291 TYR h 49
SITE 4 AV6 16 ASN h 50 VAL h 60 SER h 61 TRP h 62
SITE 1 AV7 1 BCR a 408
SITE 1 AV8 5 DGD c 517 LMG c 519 GLY j 26 TYR j 30
SITE 2 AV8 5 TYR j 33
SITE 1 AV9 9 ALA c 55 LEU c 59 ALA c 123 CLA c 512
SITE 2 AV9 9 BCR c 523 PHE k 32 LEU k 35 VAL z 13
SITE 3 AV9 9 SER z 16
SITE 1 AW1 17 SER a 232 ASN a 234 CLA a 405 PRO b 4
SITE 2 AW1 17 TRP b 5 TYR b 6 CLA b 613 LHG b 628
SITE 3 AW1 17 TRP d 266 PL9 d 405 LHG d 406 GLU l 11
SITE 4 AW1 17 LEU l 12 ASN l 13 SER l 16 PHE m 21
SITE 5 AW1 17 LMG m 103
SITE 1 AW2 3 CLA B 613 LFA M 102 ILE m 23
SITE 1 AW3 3 VAL M 27 LFA M 101 GLN m 28
SITE 1 AW4 14 THR b 327 GLY b 328 PRO b 329 LYS b 332
SITE 2 AW4 14 PHE b 453 CLA b 609 CLA b 615 CLA b 616
SITE 3 AW4 14 HOH b 760 PHE l 35 LHG l 101 ASN m 4
SITE 4 AW4 14 LEU m 6 ALA m 10
SITE 1 AW5 5 TYR B 40 LMG B 619 ALA m 12 MET t 1
SITE 2 AW5 5 PHE t 8
SITE 1 AW6 12 TYR B 40 CLA B 606 BCR B 616 BCR B 617
SITE 2 AW6 12 SQD L 101 LEU a 28 ILE t 4 PHE t 8
SITE 3 AW6 12 ALA t 11 ALA t 15 PHE t 18 PHE t 22
SITE 1 AW7 16 ALA v 36 CYS v 37 ALA v 38 SER v 39
SITE 2 AW7 16 HIS v 41 ILE v 45 THR v 46 LYS v 47
SITE 3 AW7 16 THR v 48 ASN v 49 LEU v 52 ASP v 53
SITE 4 AW7 16 LEU v 72 TYR v 75 TYR v 82 HIS v 92
SITE 1 AW8 15 PHE v 33 ALA v 36 ALA v 38 SER v 39
SITE 2 AW8 15 CYS v 40 HIS v 41 THR v 46 THR v 48
SITE 3 AW8 15 ASN v 49 LEU v 52 ASP v 53 LEU v 72
SITE 4 AW8 15 TYR v 75 TYR v 82 HIS v 92
CRYST1 116.326 219.617 304.043 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 0.008597 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004553 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003289 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
