HEADER CELL ADHESION 09-OCT-09 3K6S
TITLE STRUCTURE OF INTEGRIN ALPHAXBETA2 ECTODOMAIN
CAVEAT 3K6S NAG J 1 HAS WRONG CHIRALITY AT ATOM C1 MAN J 3 HAS WRONG
CAVEAT 2 3K6S CHIRALITY AT ATOM C1 NAG M 1 HAS WRONG CHIRALITY AT ATOM C1
CAVEAT 3 3K6S NAG P 1 HAS WRONG CHIRALITY AT ATOM C1 MAN P 3 HAS WRONG
CAVEAT 4 3K6S CHIRALITY AT ATOM C1 NAG S 1 HAS WRONG CHIRALITY AT ATOM C1
CAVEAT 5 3K6S MAN S 3 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTEGRIN ALPHA-X;
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 FRAGMENT: RESIDUES 20-1103;
COMPND 5 SYNONYM: LEUKOCYTE ADHESION GLYCOPROTEIN P150,95 ALPHA CHAIN,
COMPND 6 LEUKOCYTE ADHESION RECEPTOR P150,95, LEU M5, CD11 ANTIGEN-LIKE FAMILY
COMPND 7 MEMBER C;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: INTEGRIN BETA-2;
COMPND 11 CHAIN: B, D, F, H;
COMPND 12 FRAGMENT: RESIDUES 23-700;
COMPND 13 SYNONYM: CELL SURFACE ADHESION GLYCOPROTEINS LFA-1/CR3/P150,95
COMPND 14 SUBUNIT BETA, COMPLEMENT RECEPTOR C3 SUBUNIT BETA;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CD11C, ITGAX;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: CHO LEC 3.2.8.1;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1(-);
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 GENE: CD18, ITGB2, MFI7;
SOURCE 17 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 18 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 20 EXPRESSION_SYSTEM_STRAIN: CHO LEC 3.2.8.1;
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PEF1/PURO
KEYWDS INTEGRIN, CELL RECEPTOR, ADHESION MOLECULE, CELL ADHESION,
KEYWDS 2 PYRROLIDONE CARBOXYLIC ACID
EXPDTA X-RAY DIFFRACTION
AUTHOR C.XIE,J.ZHU,X.CHEN,L.MI,N.NISHIDA,T.A.SPRINGER
REVDAT 5 29-JUL-20 3K6S 1 CAVEAT COMPND REMARK SEQADV
REVDAT 5 2 1 HETNAM LINK SITE ATOM
REVDAT 4 20-JUN-18 3K6S 1 REMARK
REVDAT 3 13-DEC-17 3K6S 1 SOURCE REMARK
REVDAT 2 02-MAR-10 3K6S 1 JRNL
REVDAT 1 12-JAN-10 3K6S 0
JRNL AUTH C.XIE,J.ZHU,X.CHEN,L.MI,N.NISHIDA,T.A.SPRINGER
JRNL TITL STRUCTURE OF AN INTEGRIN WITH AN ALPHAI DOMAIN, COMPLEMENT
JRNL TITL 2 RECEPTOR TYPE 4.
JRNL REF EMBO J. V. 29 666 2010
JRNL REFN ISSN 0261-4189
JRNL PMID 20033057
JRNL DOI 10.1038/EMBOJ.2009.367
REMARK 2
REMARK 2 RESOLUTION. 3.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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 : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.61
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 147271
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.298
REMARK 3 R VALUE (WORKING SET) : 0.297
REMARK 3 FREE R VALUE : 0.335
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.040
REMARK 3 FREE R VALUE TEST SET COUNT : 1536
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 48.6180 - 7.7743 1.00 13784 135 0.2620 0.2635
REMARK 3 2 7.7743 - 6.1747 1.00 13433 155 0.2602 0.3393
REMARK 3 3 6.1747 - 5.3953 1.00 13319 128 0.2405 0.3151
REMARK 3 4 5.3953 - 4.9025 1.00 13232 135 0.2176 0.2651
REMARK 3 5 4.9025 - 4.5514 1.00 13184 151 0.2176 0.2746
REMARK 3 6 4.5514 - 4.2832 1.00 13148 154 0.2456 0.3073
REMARK 3 7 4.2832 - 4.0688 1.00 13193 141 0.2950 0.3182
REMARK 3 8 4.0688 - 3.8918 1.00 13059 132 0.3173 0.4038
REMARK 3 9 3.8918 - 3.7420 1.00 13180 130 0.3423 0.3701
REMARK 3 10 3.7420 - 3.6129 1.00 13108 133 0.3748 0.3778
REMARK 3 11 3.6129 - 3.5000 1.00 13095 142 0.4335 0.4381
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3 K_SOL : 0.40
REMARK 3 B_SOL : 150.0
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.800
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 80.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 99973
REMARK 3 ANGLE : 0.648 179807
REMARK 3 CHIRALITY : 0.048 7755
REMARK 3 PLANARITY : 0.004 15838
REMARK 3 DIHEDRAL : 13.189 25172
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN H AND RESSEQ 600-676
REMARK 3 ORIGIN FOR THE GROUP (A): -49.2788 66.0624 16.3271
REMARK 3 T TENSOR
REMARK 3 T11: -1.9640 T22: -0.2099
REMARK 3 T33: -0.3532 T12: 0.1416
REMARK 3 T13: -1.3569 T23: 0.2785
REMARK 3 L TENSOR
REMARK 3 L11: 0.0714 L22: 0.4622
REMARK 3 L33: 0.7779 L12: -0.1659
REMARK 3 L13: -0.2894 L23: 0.2831
REMARK 3 S TENSOR
REMARK 3 S11: -0.2078 S12: 0.2931 S13: -0.0089
REMARK 3 S21: -0.1683 S22: -0.6650 S23: -0.1551
REMARK 3 S31: -0.0379 S32: 0.1454 S33: -0.9279
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 14
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 1:126 OR RESSEQ
REMARK 3 330:595 OR RESSEQ 2005-2007)
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 1:126 OR RESSEQ
REMARK 3 330:595 OR RESSEQ 2005-2007)
REMARK 3 ATOM PAIRS NUMBER : 5796
REMARK 3 RMSD : 0.008
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 1:126 OR RESSEQ
REMARK 3 330:595 OR RESSEQ 2005-2007)
REMARK 3 SELECTION : CHAIN E AND (RESSEQ 1:126 OR RESSEQ
REMARK 3 330:595 OR RESSEQ 2005-2007)
REMARK 3 ATOM PAIRS NUMBER : 5796
REMARK 3 RMSD : 0.007
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 1:126 OR RESSEQ
REMARK 3 330:595 OR RESSEQ 2005-2007)
REMARK 3 SELECTION : CHAIN G AND (RESSEQ 1:126 OR RESSEQ
REMARK 3 330:595 OR RESSEQ 2005-2007)
REMARK 3 ATOM PAIRS NUMBER : 5796
REMARK 3 RMSD : 0.008
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 600:617 OR RESSEQ
REMARK 3 627:723 OR RESSEQ 731:750 )
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 600:617 OR RESSEQ
REMARK 3 627:723 OR RESSEQ 731:750 )
REMARK 3 ATOM PAIRS NUMBER : 2150
REMARK 3 RMSD : 0.005
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 600:617 OR RESSEQ
REMARK 3 627:723 OR RESSEQ 731:750 )
REMARK 3 SELECTION : CHAIN E AND (RESSEQ 600:617 OR RESSEQ
REMARK 3 627:723 OR RESSEQ 731:750 )
REMARK 3 ATOM PAIRS NUMBER : 2150
REMARK 3 RMSD : 0.004
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 600:617 OR RESSEQ
REMARK 3 627:723 OR RESSEQ 731:750 )
REMARK 3 SELECTION : CHAIN G AND (RESSEQ 600:617 OR RESSEQ
REMARK 3 627:723 OR RESSEQ 731:750 )
REMARK 3 ATOM PAIRS NUMBER : 2150
REMARK 3 RMSD : 0.005
REMARK 3 NCS GROUP : 3
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 760:812 OR RESSEQ
REMARK 3 827:902 )
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 760:812 OR RESSEQ
REMARK 3 827:902 )
REMARK 3 ATOM PAIRS NUMBER : 1941
REMARK 3 RMSD : 0.005
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 760:812 OR RESSEQ
REMARK 3 827:902 )
REMARK 3 SELECTION : CHAIN E AND (RESSEQ 760:812 OR RESSEQ
REMARK 3 827:902 )
REMARK 3 ATOM PAIRS NUMBER : 1941
REMARK 3 RMSD : 0.005
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 760:812 OR RESSEQ
REMARK 3 827:902 )
REMARK 3 SELECTION : CHAIN G AND (RESSEQ 760:812 OR RESSEQ
REMARK 3 827:902 )
REMARK 3 ATOM PAIRS NUMBER : 1941
REMARK 3 RMSD : 0.004
REMARK 3 NCS GROUP : 4
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 903:986 OR RESSEQ
REMARK 3 995:1081 )
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 903:986 OR RESSEQ
REMARK 3 995:1081 )
REMARK 3 ATOM PAIRS NUMBER : 2709
REMARK 3 RMSD : 0.006
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 903:986 OR RESSEQ
REMARK 3 995:1081 )
REMARK 3 SELECTION : CHAIN E AND (RESSEQ 903:986 OR RESSEQ
REMARK 3 995:1081 )
REMARK 3 ATOM PAIRS NUMBER : 2709
REMARK 3 RMSD : 0.023
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 903:986 OR RESSEQ
REMARK 3 995:1081 )
REMARK 3 SELECTION : CHAIN G AND (RESSEQ 903:986 OR RESSEQ
REMARK 3 995:1081 )
REMARK 3 ATOM PAIRS NUMBER : 2709
REMARK 3 RMSD : 0.005
REMARK 3 NCS GROUP : 5
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 1:56 )
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 1:56 )
REMARK 3 ATOM PAIRS NUMBER : 826
REMARK 3 RMSD : 0.004
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 1:56 )
REMARK 3 SELECTION : CHAIN F AND (RESSEQ 1:56 )
REMARK 3 ATOM PAIRS NUMBER : 826
REMARK 3 RMSD : 0.002
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 1:56 )
REMARK 3 SELECTION : CHAIN H AND (RESSEQ 1:56 )
REMARK 3 ATOM PAIRS NUMBER : 826
REMARK 3 RMSD : 0.003
REMARK 3 NCS GROUP : 6
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 60:67 OR RESSEQ 73:99
REMARK 3 OR RESSEQ 348:423 )
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 60:67 OR RESSEQ 73:99
REMARK 3 OR RESSEQ 348:423 )
REMARK 3 ATOM PAIRS NUMBER : 1721
REMARK 3 RMSD : 0.006
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 60:67 OR RESSEQ 73:99
REMARK 3 OR RESSEQ 348:423 )
REMARK 3 SELECTION : CHAIN F AND (RESSEQ 60:67 OR RESSEQ 73:99
REMARK 3 OR RESSEQ 348:423 )
REMARK 3 ATOM PAIRS NUMBER : 1721
REMARK 3 RMSD : 0.006
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 60:67 OR RESSEQ 73:99
REMARK 3 OR RESSEQ 348:423 )
REMARK 3 SELECTION : CHAIN H AND (RESSEQ 60:67 OR RESSEQ 73:99
REMARK 3 OR RESSEQ 348:423 )
REMARK 3 ATOM PAIRS NUMBER : 1721
REMARK 3 RMSD : 0.009
REMARK 3 NCS GROUP : 7
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 436:449 OR RESSEQ
REMARK 3 456:461 )
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 436:449 OR RESSEQ
REMARK 3 456:461 )
REMARK 3 ATOM PAIRS NUMBER : 283
REMARK 3 RMSD : 0.015
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 436:449 OR RESSEQ
REMARK 3 456:461 )
REMARK 3 SELECTION : CHAIN F AND (RESSEQ 436:449 OR RESSEQ
REMARK 3 456:461 )
REMARK 3 ATOM PAIRS NUMBER : 283
REMARK 3 RMSD : 0.008
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 436:449 OR RESSEQ
REMARK 3 456:461 )
REMARK 3 SELECTION : CHAIN H AND (RESSEQ 436:449 OR RESSEQ
REMARK 3 456:461 )
REMARK 3 ATOM PAIRS NUMBER : 283
REMARK 3 RMSD : 0.004
REMARK 3 NCS GROUP : 8
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 102:342 OR RESID 2002
REMARK 3 )
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 102:342 OR RESID 2002
REMARK 3 )
REMARK 3 ATOM PAIRS NUMBER : 3752
REMARK 3 RMSD : 0.009
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 102:342 OR RESID 2002
REMARK 3 )
REMARK 3 SELECTION : CHAIN F AND (RESSEQ 102:342 OR RESID 2002
REMARK 3 )
REMARK 3 ATOM PAIRS NUMBER : 3752
REMARK 3 RMSD : 0.004
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 102:342 OR RESID 2002
REMARK 3 )
REMARK 3 SELECTION : CHAIN H AND (RESSEQ 102:342 OR RESID 2002
REMARK 3 )
REMARK 3 ATOM PAIRS NUMBER : 3752
REMARK 3 RMSD : 0.005
REMARK 3 NCS GROUP : 9
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 463:473 )
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 463:473 )
REMARK 3 ATOM PAIRS NUMBER : 157
REMARK 3 RMSD : 0.056
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 463:473 )
REMARK 3 SELECTION : CHAIN F AND (RESSEQ 463:473 )
REMARK 3 ATOM PAIRS NUMBER : 157
REMARK 3 RMSD : 0.055
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 463:473 )
REMARK 3 SELECTION : CHAIN H AND (RESSEQ 463:473 )
REMARK 3 ATOM PAIRS NUMBER : 157
REMARK 3 RMSD : 0.053
REMARK 3 NCS GROUP : 10
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 475:512 )
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 475:512 )
REMARK 3 ATOM PAIRS NUMBER : 536
REMARK 3 RMSD : 0.011
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 475:512 )
REMARK 3 SELECTION : CHAIN F AND (RESSEQ 475:512 )
REMARK 3 ATOM PAIRS NUMBER : 536
REMARK 3 RMSD : 0.004
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 475:512 )
REMARK 3 SELECTION : CHAIN H AND (RESSEQ 475:512 )
REMARK 3 ATOM PAIRS NUMBER : 536
REMARK 3 RMSD : 0.004
REMARK 3 NCS GROUP : 11
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 516:550 )
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 516:550 )
REMARK 3 ATOM PAIRS NUMBER : 479
REMARK 3 RMSD : 0.004
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 516:550 )
REMARK 3 SELECTION : CHAIN F AND (RESSEQ 516:550 )
REMARK 3 ATOM PAIRS NUMBER : 479
REMARK 3 RMSD : 0.004
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 516:550 )
REMARK 3 SELECTION : CHAIN H AND (RESSEQ 516:550 )
REMARK 3 ATOM PAIRS NUMBER : 479
REMARK 3 RMSD : 0.003
REMARK 3 NCS GROUP : 12
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 555:592 )
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 555:592 )
REMARK 3 ATOM PAIRS NUMBER : 568
REMARK 3 RMSD : 0.004
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 555:592 )
REMARK 3 SELECTION : CHAIN F AND (RESSEQ 555:592 )
REMARK 3 ATOM PAIRS NUMBER : 568
REMARK 3 RMSD : 0.004
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 555:592 )
REMARK 3 SELECTION : CHAIN H AND (RESSEQ 555:592 )
REMARK 3 ATOM PAIRS NUMBER : 568
REMARK 3 RMSD : 0.003
REMARK 3 NCS GROUP : 13
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 593:597 )
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 593:597 )
REMARK 3 ATOM PAIRS NUMBER : 55
REMARK 3 RMSD : 0.010
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 593:597 )
REMARK 3 SELECTION : CHAIN F AND (RESSEQ 593:597 )
REMARK 3 ATOM PAIRS NUMBER : 55
REMARK 3 RMSD : 0.036
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 593:597 )
REMARK 3 SELECTION : CHAIN H AND (RESSEQ 593:597 )
REMARK 3 ATOM PAIRS NUMBER : 55
REMARK 3 RMSD : 0.020
REMARK 3 NCS GROUP : 14
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 600:673 )
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 600:673 )
REMARK 3 ATOM PAIRS NUMBER : 1114
REMARK 3 RMSD : 0.003
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 600:673 )
REMARK 3 SELECTION : CHAIN F AND (RESSEQ 600:673 )
REMARK 3 ATOM PAIRS NUMBER : 1114
REMARK 3 RMSD : 0.035
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 600:673 )
REMARK 3 SELECTION : CHAIN H AND (RESSEQ 600:673 )
REMARK 3 ATOM PAIRS NUMBER : 1114
REMARK 3 RMSD : 0.035
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: MLHL REFINEMENT
REMARK 4
REMARK 4 3K6S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-OCT-09.
REMARK 100 THE DEPOSITION ID IS D_1000055617.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-DEC-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97926,0.97942,0.96419
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR AND
REMARK 200 K-B PAIR OF BIOMORPH MIRRORS FOR
REMARK 200 VERTICAL AND HORIZONTAL FOCUSING
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.530
REMARK 200 R MERGE (I) : 0.16100
REMARK 200 R SYM (I) : 0.16100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.60
REMARK 200 R MERGE FOR SHELL (I) : 1.37100
REMARK 200 R SYM FOR SHELL (I) : 1.37100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.930
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.55M TRI-SODIUM CITRATE, 0.1M
REMARK 280 IMIDAZOLE, PH 6.5, EVAPORATION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 66.04750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 268.45550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 81.78050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 268.45550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 66.04750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 81.78050
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, 3, 4, 5
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 83870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I, J, K
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 74020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, L, M, N
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 75370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, O, P, Q
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 75460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, R, S, T
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: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 42980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 292170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -128.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L, M, N, O, P, Q, R, S, T
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 VAL A 1083
REMARK 465 HIS A 1084
REMARK 465 GLY A 1085
REMARK 465 CYS A 1086
REMARK 465 GLY A 1087
REMARK 465 GLY A 1088
REMARK 465 LEU A 1089
REMARK 465 GLU A 1090
REMARK 465 ASN A 1091
REMARK 465 LEU A 1092
REMARK 465 TYR A 1093
REMARK 465 PHE A 1094
REMARK 465 GLN A 1095
REMARK 465 ALA B 675
REMARK 465 GLY B 676
REMARK 465 PRO B 677
REMARK 465 ASP B 678
REMARK 465 GLY B 679
REMARK 465 CYS B 680
REMARK 465 GLY B 681
REMARK 465 GLU B 682
REMARK 465 ASN B 683
REMARK 465 LEU B 684
REMARK 465 TYR B 685
REMARK 465 PHE B 686
REMARK 465 GLN B 687
REMARK 465 GLN C 129
REMARK 465 GLU C 130
REMARK 465 GLN C 131
REMARK 465 ASP C 132
REMARK 465 ILE C 133
REMARK 465 VAL C 134
REMARK 465 PHE C 135
REMARK 465 LEU C 136
REMARK 465 ILE C 137
REMARK 465 ASP C 138
REMARK 465 GLY C 139
REMARK 465 SER C 140
REMARK 465 GLY C 141
REMARK 465 SER C 142
REMARK 465 ILE C 143
REMARK 465 SER C 144
REMARK 465 SER C 145
REMARK 465 ARG C 146
REMARK 465 ASN C 147
REMARK 465 PHE C 148
REMARK 465 ALA C 149
REMARK 465 THR C 150
REMARK 465 MET C 151
REMARK 465 MET C 152
REMARK 465 ASN C 153
REMARK 465 PHE C 154
REMARK 465 VAL C 155
REMARK 465 ARG C 156
REMARK 465 ALA C 157
REMARK 465 VAL C 158
REMARK 465 ILE C 159
REMARK 465 SER C 160
REMARK 465 GLN C 161
REMARK 465 PHE C 162
REMARK 465 GLN C 163
REMARK 465 ARG C 164
REMARK 465 PRO C 165
REMARK 465 SER C 166
REMARK 465 THR C 167
REMARK 465 GLN C 168
REMARK 465 PHE C 169
REMARK 465 SER C 170
REMARK 465 LEU C 171
REMARK 465 MET C 172
REMARK 465 GLN C 173
REMARK 465 PHE C 174
REMARK 465 SER C 175
REMARK 465 ASN C 176
REMARK 465 LYS C 177
REMARK 465 PHE C 178
REMARK 465 GLN C 179
REMARK 465 THR C 180
REMARK 465 HIS C 181
REMARK 465 PHE C 182
REMARK 465 THR C 183
REMARK 465 PHE C 184
REMARK 465 GLU C 185
REMARK 465 GLU C 186
REMARK 465 PHE C 187
REMARK 465 ARG C 188
REMARK 465 ARG C 189
REMARK 465 SER C 190
REMARK 465 SER C 191
REMARK 465 ASN C 192
REMARK 465 PRO C 193
REMARK 465 LEU C 194
REMARK 465 SER C 195
REMARK 465 LEU C 196
REMARK 465 LEU C 197
REMARK 465 ALA C 198
REMARK 465 SER C 199
REMARK 465 VAL C 200
REMARK 465 HIS C 201
REMARK 465 GLN C 202
REMARK 465 LEU C 203
REMARK 465 GLN C 204
REMARK 465 GLY C 205
REMARK 465 PHE C 206
REMARK 465 THR C 207
REMARK 465 TYR C 208
REMARK 465 THR C 209
REMARK 465 ALA C 210
REMARK 465 THR C 211
REMARK 465 ALA C 212
REMARK 465 ILE C 213
REMARK 465 GLN C 214
REMARK 465 ASN C 215
REMARK 465 VAL C 216
REMARK 465 VAL C 217
REMARK 465 HIS C 218
REMARK 465 ARG C 219
REMARK 465 LEU C 220
REMARK 465 PHE C 221
REMARK 465 HIS C 222
REMARK 465 ALA C 223
REMARK 465 SER C 224
REMARK 465 TYR C 225
REMARK 465 GLY C 226
REMARK 465 ALA C 227
REMARK 465 ARG C 228
REMARK 465 ARG C 229
REMARK 465 ASP C 230
REMARK 465 ALA C 231
REMARK 465 ALA C 232
REMARK 465 LYS C 233
REMARK 465 ILE C 234
REMARK 465 LEU C 235
REMARK 465 ILE C 236
REMARK 465 VAL C 237
REMARK 465 ILE C 238
REMARK 465 THR C 239
REMARK 465 ASP C 240
REMARK 465 GLY C 241
REMARK 465 LYS C 242
REMARK 465 LYS C 243
REMARK 465 GLU C 244
REMARK 465 GLY C 245
REMARK 465 ASP C 246
REMARK 465 SER C 247
REMARK 465 LEU C 248
REMARK 465 ASP C 249
REMARK 465 TYR C 250
REMARK 465 LYS C 251
REMARK 465 ASP C 252
REMARK 465 VAL C 253
REMARK 465 ILE C 254
REMARK 465 PRO C 255
REMARK 465 MET C 256
REMARK 465 ALA C 257
REMARK 465 ASP C 258
REMARK 465 ALA C 259
REMARK 465 ALA C 260
REMARK 465 GLY C 261
REMARK 465 ILE C 262
REMARK 465 ILE C 263
REMARK 465 ARG C 264
REMARK 465 TYR C 265
REMARK 465 ALA C 266
REMARK 465 ILE C 267
REMARK 465 GLY C 268
REMARK 465 VAL C 269
REMARK 465 GLY C 270
REMARK 465 LEU C 271
REMARK 465 ALA C 272
REMARK 465 PHE C 273
REMARK 465 GLN C 274
REMARK 465 ASN C 275
REMARK 465 ARG C 276
REMARK 465 ASN C 277
REMARK 465 SER C 278
REMARK 465 TRP C 279
REMARK 465 LYS C 280
REMARK 465 GLU C 281
REMARK 465 LEU C 282
REMARK 465 ASN C 283
REMARK 465 ASP C 284
REMARK 465 ILE C 285
REMARK 465 ALA C 286
REMARK 465 SER C 287
REMARK 465 LYS C 288
REMARK 465 PRO C 289
REMARK 465 SER C 290
REMARK 465 GLN C 291
REMARK 465 GLU C 292
REMARK 465 HIS C 293
REMARK 465 ILE C 294
REMARK 465 PHE C 295
REMARK 465 LYS C 296
REMARK 465 VAL C 297
REMARK 465 GLU C 298
REMARK 465 ASP C 299
REMARK 465 PHE C 300
REMARK 465 ASP C 301
REMARK 465 ALA C 302
REMARK 465 LEU C 303
REMARK 465 LYS C 304
REMARK 465 ASP C 305
REMARK 465 ILE C 306
REMARK 465 GLN C 307
REMARK 465 ASN C 308
REMARK 465 GLN C 309
REMARK 465 LEU C 310
REMARK 465 LYS C 311
REMARK 465 GLU C 312
REMARK 465 LYS C 313
REMARK 465 ILE C 314
REMARK 465 PHE C 315
REMARK 465 ALA C 316
REMARK 465 ILE C 317
REMARK 465 GLU C 318
REMARK 465 GLY C 319
REMARK 465 THR C 320
REMARK 465 GLU C 321
REMARK 465 THR C 322
REMARK 465 THR C 323
REMARK 465 SER C 324
REMARK 465 SER C 325
REMARK 465 VAL C 1083
REMARK 465 HIS C 1084
REMARK 465 GLY C 1085
REMARK 465 CYS C 1086
REMARK 465 GLY C 1087
REMARK 465 GLY C 1088
REMARK 465 LEU C 1089
REMARK 465 GLU C 1090
REMARK 465 ASN C 1091
REMARK 465 LEU C 1092
REMARK 465 TYR C 1093
REMARK 465 PHE C 1094
REMARK 465 GLN C 1095
REMARK 465 ALA D 675
REMARK 465 GLY D 676
REMARK 465 PRO D 677
REMARK 465 ASP D 678
REMARK 465 GLY D 679
REMARK 465 CYS D 680
REMARK 465 GLY D 681
REMARK 465 GLU D 682
REMARK 465 ASN D 683
REMARK 465 LEU D 684
REMARK 465 TYR D 685
REMARK 465 PHE D 686
REMARK 465 GLN D 687
REMARK 465 GLN E 129
REMARK 465 GLU E 130
REMARK 465 GLN E 131
REMARK 465 ASP E 132
REMARK 465 ILE E 133
REMARK 465 VAL E 134
REMARK 465 PHE E 135
REMARK 465 LEU E 136
REMARK 465 ILE E 137
REMARK 465 ASP E 138
REMARK 465 GLY E 139
REMARK 465 SER E 140
REMARK 465 GLY E 141
REMARK 465 SER E 142
REMARK 465 ILE E 143
REMARK 465 SER E 144
REMARK 465 SER E 145
REMARK 465 ARG E 146
REMARK 465 ASN E 147
REMARK 465 PHE E 148
REMARK 465 ALA E 149
REMARK 465 THR E 150
REMARK 465 MET E 151
REMARK 465 MET E 152
REMARK 465 ASN E 153
REMARK 465 PHE E 154
REMARK 465 VAL E 155
REMARK 465 ARG E 156
REMARK 465 ALA E 157
REMARK 465 VAL E 158
REMARK 465 ILE E 159
REMARK 465 SER E 160
REMARK 465 GLN E 161
REMARK 465 PHE E 162
REMARK 465 GLN E 163
REMARK 465 ARG E 164
REMARK 465 PRO E 165
REMARK 465 SER E 166
REMARK 465 THR E 167
REMARK 465 GLN E 168
REMARK 465 PHE E 169
REMARK 465 SER E 170
REMARK 465 LEU E 171
REMARK 465 MET E 172
REMARK 465 GLN E 173
REMARK 465 PHE E 174
REMARK 465 SER E 175
REMARK 465 ASN E 176
REMARK 465 LYS E 177
REMARK 465 PHE E 178
REMARK 465 GLN E 179
REMARK 465 THR E 180
REMARK 465 HIS E 181
REMARK 465 PHE E 182
REMARK 465 THR E 183
REMARK 465 PHE E 184
REMARK 465 GLU E 185
REMARK 465 GLU E 186
REMARK 465 PHE E 187
REMARK 465 ARG E 188
REMARK 465 ARG E 189
REMARK 465 SER E 190
REMARK 465 SER E 191
REMARK 465 ASN E 192
REMARK 465 PRO E 193
REMARK 465 LEU E 194
REMARK 465 SER E 195
REMARK 465 LEU E 196
REMARK 465 LEU E 197
REMARK 465 ALA E 198
REMARK 465 SER E 199
REMARK 465 VAL E 200
REMARK 465 HIS E 201
REMARK 465 GLN E 202
REMARK 465 LEU E 203
REMARK 465 GLN E 204
REMARK 465 GLY E 205
REMARK 465 PHE E 206
REMARK 465 THR E 207
REMARK 465 TYR E 208
REMARK 465 THR E 209
REMARK 465 ALA E 210
REMARK 465 THR E 211
REMARK 465 ALA E 212
REMARK 465 ILE E 213
REMARK 465 GLN E 214
REMARK 465 ASN E 215
REMARK 465 VAL E 216
REMARK 465 VAL E 217
REMARK 465 HIS E 218
REMARK 465 ARG E 219
REMARK 465 LEU E 220
REMARK 465 PHE E 221
REMARK 465 HIS E 222
REMARK 465 ALA E 223
REMARK 465 SER E 224
REMARK 465 TYR E 225
REMARK 465 GLY E 226
REMARK 465 ALA E 227
REMARK 465 ARG E 228
REMARK 465 ARG E 229
REMARK 465 ASP E 230
REMARK 465 ALA E 231
REMARK 465 ALA E 232
REMARK 465 LYS E 233
REMARK 465 ILE E 234
REMARK 465 LEU E 235
REMARK 465 ILE E 236
REMARK 465 VAL E 237
REMARK 465 ILE E 238
REMARK 465 THR E 239
REMARK 465 ASP E 240
REMARK 465 GLY E 241
REMARK 465 LYS E 242
REMARK 465 LYS E 243
REMARK 465 GLU E 244
REMARK 465 GLY E 245
REMARK 465 ASP E 246
REMARK 465 SER E 247
REMARK 465 LEU E 248
REMARK 465 ASP E 249
REMARK 465 TYR E 250
REMARK 465 LYS E 251
REMARK 465 ASP E 252
REMARK 465 VAL E 253
REMARK 465 ILE E 254
REMARK 465 PRO E 255
REMARK 465 MET E 256
REMARK 465 ALA E 257
REMARK 465 ASP E 258
REMARK 465 ALA E 259
REMARK 465 ALA E 260
REMARK 465 GLY E 261
REMARK 465 ILE E 262
REMARK 465 ILE E 263
REMARK 465 ARG E 264
REMARK 465 TYR E 265
REMARK 465 ALA E 266
REMARK 465 ILE E 267
REMARK 465 GLY E 268
REMARK 465 VAL E 269
REMARK 465 GLY E 270
REMARK 465 LEU E 271
REMARK 465 ALA E 272
REMARK 465 PHE E 273
REMARK 465 GLN E 274
REMARK 465 ASN E 275
REMARK 465 ARG E 276
REMARK 465 ASN E 277
REMARK 465 SER E 278
REMARK 465 TRP E 279
REMARK 465 LYS E 280
REMARK 465 GLU E 281
REMARK 465 LEU E 282
REMARK 465 ASN E 283
REMARK 465 ASP E 284
REMARK 465 ILE E 285
REMARK 465 ALA E 286
REMARK 465 SER E 287
REMARK 465 LYS E 288
REMARK 465 PRO E 289
REMARK 465 SER E 290
REMARK 465 GLN E 291
REMARK 465 GLU E 292
REMARK 465 HIS E 293
REMARK 465 ILE E 294
REMARK 465 PHE E 295
REMARK 465 LYS E 296
REMARK 465 VAL E 297
REMARK 465 GLU E 298
REMARK 465 ASP E 299
REMARK 465 PHE E 300
REMARK 465 ASP E 301
REMARK 465 ALA E 302
REMARK 465 LEU E 303
REMARK 465 LYS E 304
REMARK 465 ASP E 305
REMARK 465 ILE E 306
REMARK 465 GLN E 307
REMARK 465 ASN E 308
REMARK 465 GLN E 309
REMARK 465 LEU E 310
REMARK 465 LYS E 311
REMARK 465 GLU E 312
REMARK 465 LYS E 313
REMARK 465 ILE E 314
REMARK 465 PHE E 315
REMARK 465 ALA E 316
REMARK 465 ILE E 317
REMARK 465 GLU E 318
REMARK 465 GLY E 319
REMARK 465 THR E 320
REMARK 465 GLU E 321
REMARK 465 THR E 322
REMARK 465 THR E 323
REMARK 465 SER E 324
REMARK 465 SER E 325
REMARK 465 SER E 326
REMARK 465 VAL E 1083
REMARK 465 HIS E 1084
REMARK 465 GLY E 1085
REMARK 465 CYS E 1086
REMARK 465 GLY E 1087
REMARK 465 GLY E 1088
REMARK 465 LEU E 1089
REMARK 465 GLU E 1090
REMARK 465 ASN E 1091
REMARK 465 LEU E 1092
REMARK 465 TYR E 1093
REMARK 465 PHE E 1094
REMARK 465 GLN E 1095
REMARK 465 ALA F 675
REMARK 465 GLY F 676
REMARK 465 PRO F 677
REMARK 465 ASP F 678
REMARK 465 GLY F 679
REMARK 465 CYS F 680
REMARK 465 GLY F 681
REMARK 465 GLU F 682
REMARK 465 ASN F 683
REMARK 465 LEU F 684
REMARK 465 TYR F 685
REMARK 465 PHE F 686
REMARK 465 GLN F 687
REMARK 465 GLN G 129
REMARK 465 GLU G 130
REMARK 465 GLN G 131
REMARK 465 ASP G 132
REMARK 465 ILE G 133
REMARK 465 VAL G 134
REMARK 465 PHE G 135
REMARK 465 LEU G 136
REMARK 465 ILE G 137
REMARK 465 ASP G 138
REMARK 465 GLY G 139
REMARK 465 SER G 140
REMARK 465 GLY G 141
REMARK 465 SER G 142
REMARK 465 ILE G 143
REMARK 465 SER G 144
REMARK 465 SER G 145
REMARK 465 ARG G 146
REMARK 465 ASN G 147
REMARK 465 PHE G 148
REMARK 465 ALA G 149
REMARK 465 THR G 150
REMARK 465 MET G 151
REMARK 465 MET G 152
REMARK 465 ASN G 153
REMARK 465 PHE G 154
REMARK 465 VAL G 155
REMARK 465 ARG G 156
REMARK 465 ALA G 157
REMARK 465 VAL G 158
REMARK 465 ILE G 159
REMARK 465 SER G 160
REMARK 465 GLN G 161
REMARK 465 PHE G 162
REMARK 465 GLN G 163
REMARK 465 ARG G 164
REMARK 465 PRO G 165
REMARK 465 SER G 166
REMARK 465 THR G 167
REMARK 465 GLN G 168
REMARK 465 PHE G 169
REMARK 465 SER G 170
REMARK 465 LEU G 171
REMARK 465 MET G 172
REMARK 465 GLN G 173
REMARK 465 PHE G 174
REMARK 465 SER G 175
REMARK 465 ASN G 176
REMARK 465 LYS G 177
REMARK 465 PHE G 178
REMARK 465 GLN G 179
REMARK 465 THR G 180
REMARK 465 HIS G 181
REMARK 465 PHE G 182
REMARK 465 THR G 183
REMARK 465 PHE G 184
REMARK 465 GLU G 185
REMARK 465 GLU G 186
REMARK 465 PHE G 187
REMARK 465 ARG G 188
REMARK 465 ARG G 189
REMARK 465 SER G 190
REMARK 465 SER G 191
REMARK 465 ASN G 192
REMARK 465 PRO G 193
REMARK 465 LEU G 194
REMARK 465 SER G 195
REMARK 465 LEU G 196
REMARK 465 LEU G 197
REMARK 465 ALA G 198
REMARK 465 SER G 199
REMARK 465 VAL G 200
REMARK 465 HIS G 201
REMARK 465 GLN G 202
REMARK 465 LEU G 203
REMARK 465 GLN G 204
REMARK 465 GLY G 205
REMARK 465 PHE G 206
REMARK 465 THR G 207
REMARK 465 TYR G 208
REMARK 465 THR G 209
REMARK 465 ALA G 210
REMARK 465 THR G 211
REMARK 465 ALA G 212
REMARK 465 ILE G 213
REMARK 465 GLN G 214
REMARK 465 ASN G 215
REMARK 465 VAL G 216
REMARK 465 VAL G 217
REMARK 465 HIS G 218
REMARK 465 ARG G 219
REMARK 465 LEU G 220
REMARK 465 PHE G 221
REMARK 465 HIS G 222
REMARK 465 ALA G 223
REMARK 465 SER G 224
REMARK 465 TYR G 225
REMARK 465 GLY G 226
REMARK 465 ALA G 227
REMARK 465 ARG G 228
REMARK 465 ARG G 229
REMARK 465 ASP G 230
REMARK 465 ALA G 231
REMARK 465 ALA G 232
REMARK 465 LYS G 233
REMARK 465 ILE G 234
REMARK 465 LEU G 235
REMARK 465 ILE G 236
REMARK 465 VAL G 237
REMARK 465 ILE G 238
REMARK 465 THR G 239
REMARK 465 ASP G 240
REMARK 465 GLY G 241
REMARK 465 LYS G 242
REMARK 465 LYS G 243
REMARK 465 GLU G 244
REMARK 465 GLY G 245
REMARK 465 ASP G 246
REMARK 465 SER G 247
REMARK 465 LEU G 248
REMARK 465 ASP G 249
REMARK 465 TYR G 250
REMARK 465 LYS G 251
REMARK 465 ASP G 252
REMARK 465 VAL G 253
REMARK 465 ILE G 254
REMARK 465 PRO G 255
REMARK 465 MET G 256
REMARK 465 ALA G 257
REMARK 465 ASP G 258
REMARK 465 ALA G 259
REMARK 465 ALA G 260
REMARK 465 GLY G 261
REMARK 465 ILE G 262
REMARK 465 ILE G 263
REMARK 465 ARG G 264
REMARK 465 TYR G 265
REMARK 465 ALA G 266
REMARK 465 ILE G 267
REMARK 465 GLY G 268
REMARK 465 VAL G 269
REMARK 465 GLY G 270
REMARK 465 LEU G 271
REMARK 465 ALA G 272
REMARK 465 PHE G 273
REMARK 465 GLN G 274
REMARK 465 ASN G 275
REMARK 465 ARG G 276
REMARK 465 ASN G 277
REMARK 465 SER G 278
REMARK 465 TRP G 279
REMARK 465 LYS G 280
REMARK 465 GLU G 281
REMARK 465 LEU G 282
REMARK 465 ASN G 283
REMARK 465 ASP G 284
REMARK 465 ILE G 285
REMARK 465 ALA G 286
REMARK 465 SER G 287
REMARK 465 LYS G 288
REMARK 465 PRO G 289
REMARK 465 SER G 290
REMARK 465 GLN G 291
REMARK 465 GLU G 292
REMARK 465 HIS G 293
REMARK 465 ILE G 294
REMARK 465 PHE G 295
REMARK 465 LYS G 296
REMARK 465 VAL G 297
REMARK 465 GLU G 298
REMARK 465 ASP G 299
REMARK 465 PHE G 300
REMARK 465 ASP G 301
REMARK 465 ALA G 302
REMARK 465 LEU G 303
REMARK 465 LYS G 304
REMARK 465 ASP G 305
REMARK 465 ILE G 306
REMARK 465 GLN G 307
REMARK 465 ASN G 308
REMARK 465 GLN G 309
REMARK 465 LEU G 310
REMARK 465 LYS G 311
REMARK 465 GLU G 312
REMARK 465 LYS G 313
REMARK 465 ILE G 314
REMARK 465 PHE G 315
REMARK 465 ALA G 316
REMARK 465 ILE G 317
REMARK 465 GLU G 318
REMARK 465 GLY G 319
REMARK 465 THR G 320
REMARK 465 GLU G 321
REMARK 465 THR G 322
REMARK 465 THR G 323
REMARK 465 SER G 324
REMARK 465 SER G 325
REMARK 465 VAL G 1083
REMARK 465 HIS G 1084
REMARK 465 GLY G 1085
REMARK 465 CYS G 1086
REMARK 465 GLY G 1087
REMARK 465 GLY G 1088
REMARK 465 LEU G 1089
REMARK 465 GLU G 1090
REMARK 465 ASN G 1091
REMARK 465 LEU G 1092
REMARK 465 TYR G 1093
REMARK 465 PHE G 1094
REMARK 465 GLN G 1095
REMARK 465 ALA H 675
REMARK 465 GLY H 676
REMARK 465 PRO H 677
REMARK 465 ASP H 678
REMARK 465 GLY H 679
REMARK 465 CYS H 680
REMARK 465 GLY H 681
REMARK 465 GLU H 682
REMARK 465 ASN H 683
REMARK 465 LEU H 684
REMARK 465 TYR H 685
REMARK 465 PHE H 686
REMARK 465 GLN H 687
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 ND2 ASN G 678 C2 NAG G 3678 1.70
REMARK 500 ND2 ASN C 678 C2 NAG C 3678 1.71
REMARK 500 ND2 ASN E 678 C2 NAG E 3678 1.71
REMARK 500 ND2 ASN G 880 C2 NAG G 3880 1.71
REMARK 500 ND2 ASN A 678 C2 NAG A 3678 1.72
REMARK 500 ND2 ASN C 880 C2 NAG C 3880 1.72
REMARK 500 ND2 ASN E 880 C2 NAG E 3880 1.74
REMARK 500 ND2 ASN A 880 C2 NAG A 3880 1.75
REMARK 500 O GLY E 816 N LYS E 818 2.12
REMARK 500 O GLY G 816 N LYS G 818 2.13
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 GLU A 6 -67.49 -149.44
REMARK 500 ARG A 12 74.80 -108.49
REMARK 500 ALA A 16 -111.19 67.00
REMARK 500 ALA A 26 129.07 -37.46
REMARK 500 ASN A 27 -32.61 -33.03
REMARK 500 GLN A 36 34.29 -96.75
REMARK 500 ILE A 38 127.59 -38.68
REMARK 500 ALA A 40 -140.72 66.79
REMARK 500 ASN A 42 54.54 35.40
REMARK 500 GLN A 43 -130.48 -108.87
REMARK 500 ASN A 70 41.96 33.34
REMARK 500 SER A 72 75.62 38.87
REMARK 500 ALA A 78 140.67 -172.87
REMARK 500 SER A 82 -95.04 -31.03
REMARK 500 PRO A 91 28.86 -74.72
REMARK 500 THR A 92 30.79 -145.27
REMARK 500 LEU A 110 -164.16 -106.02
REMARK 500 PRO A 112 45.75 -72.32
REMARK 500 THR A 113 -142.24 -150.36
REMARK 500 ARG A 123 104.62 -36.07
REMARK 500 GLN A 124 98.61 -57.86
REMARK 500 SER A 175 -88.64 -128.17
REMARK 500 LYS A 177 -168.92 -124.56
REMARK 500 GLN A 204 -147.12 57.15
REMARK 500 PHE A 206 -157.26 -78.06
REMARK 500 THR A 209 -76.05 -36.77
REMARK 500 ARG A 219 -65.14 -142.22
REMARK 500 LYS A 242 -169.75 -72.15
REMARK 500 ASP A 246 98.88 -56.23
REMARK 500 LEU A 271 -10.98 72.18
REMARK 500 PHE A 295 73.96 -154.46
REMARK 500 ALA A 316 0.83 -69.21
REMARK 500 GLU A 318 -59.52 -126.25
REMARK 500 GLU A 321 -51.68 -153.46
REMARK 500 THR A 322 57.97 -100.88
REMARK 500 SER A 324 71.65 30.75
REMARK 500 GLU A 329 -84.82 -148.91
REMARK 500 LEU A 330 57.29 -147.03
REMARK 500 GLN A 334 51.37 39.75
REMARK 500 THR A 342 144.56 176.34
REMARK 500 PRO A 343 -31.12 -39.51
REMARK 500 ASP A 344 56.74 -106.62
REMARK 500 PHE A 354 -113.57 62.39
REMARK 500 THR A 355 41.60 -82.24
REMARK 500 PRO A 364 -174.75 -67.18
REMARK 500 ASN A 366 -5.88 68.46
REMARK 500 THR A 370 -164.13 -108.92
REMARK 500 ASN A 373 -156.36 -94.13
REMARK 500 SER A 375 165.68 71.93
REMARK 500 ASP A 380 -159.71 -79.92
REMARK 500
REMARK 500 THIS ENTRY HAS 939 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 SER A 82 PRO A 83 145.13
REMARK 500 ARG A 118 LEU A 119 130.11
REMARK 500 LEU A 119 PRO A 120 55.26
REMARK 500 ASP A 488 ALA A 489 147.57
REMARK 500 VAL A 490 LEU A 491 -135.05
REMARK 500 VAL A 624 VAL A 625 -148.07
REMARK 500 VAL A 625 SER A 626 142.89
REMARK 500 GLY A 816 GLN A 817 -140.25
REMARK 500 GLN A 821 LEU A 822 -144.33
REMARK 500 SER A 824 LEU A 825 -141.74
REMARK 500 THR B 160 HIS B 161 148.68
REMARK 500 ASP B 163 LYS B 164 146.93
REMARK 500 SER C 82 PRO C 83 145.07
REMARK 500 ARG C 118 LEU C 119 131.31
REMARK 500 ASP C 488 ALA C 489 147.57
REMARK 500 VAL C 490 LEU C 491 -135.09
REMARK 500 ARG C 621 GLU C 622 -105.76
REMARK 500 GLU C 622 GLN C 623 144.56
REMARK 500 VAL C 625 SER C 626 145.81
REMARK 500 GLY C 816 GLN C 817 -145.83
REMARK 500 GLN C 817 LYS C 818 149.72
REMARK 500 GLN C 821 LEU C 822 -144.96
REMARK 500 SER C 824 LEU C 825 -142.66
REMARK 500 THR D 160 HIS D 161 148.70
REMARK 500 ASP D 163 LYS D 164 147.00
REMARK 500 GLN D 462 THR D 463 -147.55
REMARK 500 SER E 82 PRO E 83 145.26
REMARK 500 ARG E 118 LEU E 119 131.19
REMARK 500 ASP E 488 ALA E 489 147.55
REMARK 500 VAL E 490 LEU E 491 -135.13
REMARK 500 VAL E 624 VAL E 625 -148.63
REMARK 500 VAL E 625 SER E 626 144.19
REMARK 500 GLY E 816 GLN E 817 -132.86
REMARK 500 GLN E 817 LYS E 818 139.14
REMARK 500 GLN E 821 LEU E 822 -144.69
REMARK 500 SER E 824 LEU E 825 -142.86
REMARK 500 THR F 160 HIS F 161 148.60
REMARK 500 ASP F 163 LYS F 164 146.96
REMARK 500 SER G 82 PRO G 83 145.07
REMARK 500 ARG G 118 LEU G 119 131.49
REMARK 500 ASP G 488 ALA G 489 147.60
REMARK 500 VAL G 490 LEU G 491 -134.99
REMARK 500 VAL G 624 VAL G 625 -148.73
REMARK 500 VAL G 625 SER G 626 143.96
REMARK 500 GLY G 816 GLN G 817 -139.66
REMARK 500 GLN G 817 LYS G 818 148.63
REMARK 500 GLN G 819 GLY G 820 148.71
REMARK 500 GLN G 821 LEU G 822 -142.55
REMARK 500 SER G 824 LEU G 825 -143.26
REMARK 500 ARG H 99 ALA H 100 -145.22
REMARK 500
REMARK 500 THIS ENTRY HAS 52 NON CIS, NON-TRANS OMEGA OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 MAN A 3378
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 MG A2009 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 140 OG
REMARK 620 2 SER A 142 OG 88.4
REMARK 620 3 ASP A 240 OD1 118.9 95.6
REMARK 620 4 HOH A4001 O 111.1 160.3 73.3
REMARK 620 5 HOH A4002 O 133.0 97.2 107.0 71.6
REMARK 620 6 HOH A4003 O 67.5 87.6 172.8 101.7 66.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2005 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 447 OD1
REMARK 620 2 SER A 453 O 150.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2006 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 513 OD1
REMARK 620 2 LEU A 517 O 101.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2007 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 574 OD1
REMARK 620 2 THR A 576 OG1 103.2
REMARK 620 3 ASP A 578 O 70.6 104.9
REMARK 620 4 LEU A 580 O 81.9 173.6 72.9
REMARK 620 5 ASP A 582 OD1 131.1 93.6 147.6 85.7
REMARK 620 6 ASP A 582 OD2 91.7 80.2 162.2 103.7 46.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B2002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 116 O
REMARK 620 2 ASP B 119 OD1 117.5
REMARK 620 3 ASP B 120 OD1 131.9 71.8
REMARK 620 4 GLU B 325 O 158.9 80.8 61.3
REMARK 620 5 GLU B 325 OE2 81.1 154.9 109.4 78.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C2005 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 447 OD1
REMARK 620 2 ASP C 451 OD1 82.6
REMARK 620 3 SER C 453 O 150.7 79.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C2006 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C 513 OD1
REMARK 620 2 LEU C 517 O 102.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C2007 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 574 OD1
REMARK 620 2 THR C 576 OG1 102.8
REMARK 620 3 ASP C 578 O 70.5 104.6
REMARK 620 4 LEU C 580 O 81.9 173.8 73.0
REMARK 620 5 ASP C 582 OD1 131.1 93.7 148.0 86.0
REMARK 620 6 ASP C 582 OD2 91.5 80.1 162.0 103.9 46.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D2002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER D 116 O
REMARK 620 2 ASP D 119 OD1 117.5
REMARK 620 3 ASP D 120 OD1 131.8 71.8
REMARK 620 4 GLU D 325 O 159.0 80.7 61.3
REMARK 620 5 GLU D 325 OE2 81.1 155.0 109.4 78.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E2005 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 447 OD1
REMARK 620 2 ASP E 451 OD1 82.4
REMARK 620 3 SER E 453 O 150.6 79.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E2006 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN E 513 OD1
REMARK 620 2 LEU E 517 O 101.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E2007 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 574 OD1
REMARK 620 2 THR E 576 OG1 102.9
REMARK 620 3 ASP E 578 O 70.7 104.7
REMARK 620 4 LEU E 580 O 82.0 173.9 73.2
REMARK 620 5 ASP E 582 OD1 131.0 93.5 148.0 85.9
REMARK 620 6 ASP E 582 OD2 91.5 80.0 162.1 103.7 46.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F2002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER F 116 O
REMARK 620 2 ASP F 119 OD1 117.5
REMARK 620 3 ASP F 120 OD1 131.8 71.8
REMARK 620 4 GLU F 325 O 159.0 80.6 61.3
REMARK 620 5 GLU F 325 OE2 81.1 154.9 109.5 78.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G2005 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 447 OD1
REMARK 620 2 ASP G 451 OD1 82.6
REMARK 620 3 SER G 453 O 150.9 79.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G2006 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN G 513 OD1
REMARK 620 2 LEU G 517 O 101.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G2007 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 574 OD1
REMARK 620 2 THR G 576 OG1 102.8
REMARK 620 3 ASP G 578 O 70.5 105.0
REMARK 620 4 LEU G 580 O 81.8 174.3 73.1
REMARK 620 5 ASP G 582 OD1 130.6 93.7 148.2 85.8
REMARK 620 6 ASP G 582 OD2 91.2 80.0 161.6 103.5 46.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA H2002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER H 116 O
REMARK 620 2 ASP H 119 OD1 117.5
REMARK 620 3 ASP H 120 OD1 131.8 71.7
REMARK 620 4 GLU H 325 O 159.1 80.6 61.3
REMARK 620 5 GLU H 325 OE2 81.2 155.0 109.5 78.6
REMARK 620 N 1 2 3 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3K72 RELATED DB: PDB
REMARK 900 STRUCTURE OF INTEGRIN ALPHAX BETA2
REMARK 900 RELATED ID: 3K71 RELATED DB: PDB
REMARK 900 STRUCTURE OF INTEGRIN ALPHAX BETA2 ECTODOMAIN
DBREF 3K6S A 1 1084 UNP P20702 ITAX_HUMAN 20 1103
DBREF 3K6S B 1 683 UNP P05107 ITB2_HUMAN 23 700
DBREF 3K6S C 1 1084 UNP P20702 ITAX_HUMAN 20 1103
DBREF 3K6S D 1 683 UNP P05107 ITB2_HUMAN 23 700
DBREF 3K6S E 1 1084 UNP P20702 ITAX_HUMAN 20 1103
DBREF 3K6S F 1 683 UNP P05107 ITB2_HUMAN 23 700
DBREF 3K6S G 1 1084 UNP P20702 ITAX_HUMAN 20 1103
DBREF 3K6S H 1 683 UNP P05107 ITB2_HUMAN 23 700
SEQADV 3K6S GLY A 1085 UNP P20702 EXPRESSION TAG
SEQADV 3K6S CYS A 1086 UNP P20702 EXPRESSION TAG
SEQADV 3K6S GLY A 1087 UNP P20702 EXPRESSION TAG
SEQADV 3K6S GLY A 1088 UNP P20702 EXPRESSION TAG
SEQADV 3K6S LEU A 1089 UNP P20702 EXPRESSION TAG
SEQADV 3K6S GLU A 1090 UNP P20702 EXPRESSION TAG
SEQADV 3K6S ASN A 1091 UNP P20702 EXPRESSION TAG
SEQADV 3K6S LEU A 1092 UNP P20702 EXPRESSION TAG
SEQADV 3K6S TYR A 1093 UNP P20702 EXPRESSION TAG
SEQADV 3K6S PHE A 1094 UNP P20702 EXPRESSION TAG
SEQADV 3K6S GLN A 1095 UNP P20702 EXPRESSION TAG
SEQADV 3K6S ASP B 678 UNP P05107 EXPRESSION TAG
SEQADV 3K6S GLY B 679 UNP P05107 EXPRESSION TAG
SEQADV 3K6S CYS B 680 UNP P05107 EXPRESSION TAG
SEQADV 3K6S GLY B 681 UNP P05107 EXPRESSION TAG
SEQADV 3K6S GLU B 682 UNP P05107 EXPRESSION TAG
SEQADV 3K6S LEU B 684 UNP P05107 EXPRESSION TAG
SEQADV 3K6S TYR B 685 UNP P05107 EXPRESSION TAG
SEQADV 3K6S PHE B 686 UNP P05107 EXPRESSION TAG
SEQADV 3K6S GLN B 687 UNP P05107 EXPRESSION TAG
SEQADV 3K6S GLY C 1085 UNP P20702 EXPRESSION TAG
SEQADV 3K6S CYS C 1086 UNP P20702 EXPRESSION TAG
SEQADV 3K6S GLY C 1087 UNP P20702 EXPRESSION TAG
SEQADV 3K6S GLY C 1088 UNP P20702 EXPRESSION TAG
SEQADV 3K6S LEU C 1089 UNP P20702 EXPRESSION TAG
SEQADV 3K6S GLU C 1090 UNP P20702 EXPRESSION TAG
SEQADV 3K6S ASN C 1091 UNP P20702 EXPRESSION TAG
SEQADV 3K6S LEU C 1092 UNP P20702 EXPRESSION TAG
SEQADV 3K6S TYR C 1093 UNP P20702 EXPRESSION TAG
SEQADV 3K6S PHE C 1094 UNP P20702 EXPRESSION TAG
SEQADV 3K6S GLN C 1095 UNP P20702 EXPRESSION TAG
SEQADV 3K6S ASP D 678 UNP P05107 EXPRESSION TAG
SEQADV 3K6S GLY D 679 UNP P05107 EXPRESSION TAG
SEQADV 3K6S CYS D 680 UNP P05107 EXPRESSION TAG
SEQADV 3K6S GLY D 681 UNP P05107 EXPRESSION TAG
SEQADV 3K6S GLU D 682 UNP P05107 EXPRESSION TAG
SEQADV 3K6S LEU D 684 UNP P05107 EXPRESSION TAG
SEQADV 3K6S TYR D 685 UNP P05107 EXPRESSION TAG
SEQADV 3K6S PHE D 686 UNP P05107 EXPRESSION TAG
SEQADV 3K6S GLN D 687 UNP P05107 EXPRESSION TAG
SEQADV 3K6S GLY E 1085 UNP P20702 EXPRESSION TAG
SEQADV 3K6S CYS E 1086 UNP P20702 EXPRESSION TAG
SEQADV 3K6S GLY E 1087 UNP P20702 EXPRESSION TAG
SEQADV 3K6S GLY E 1088 UNP P20702 EXPRESSION TAG
SEQADV 3K6S LEU E 1089 UNP P20702 EXPRESSION TAG
SEQADV 3K6S GLU E 1090 UNP P20702 EXPRESSION TAG
SEQADV 3K6S ASN E 1091 UNP P20702 EXPRESSION TAG
SEQADV 3K6S LEU E 1092 UNP P20702 EXPRESSION TAG
SEQADV 3K6S TYR E 1093 UNP P20702 EXPRESSION TAG
SEQADV 3K6S PHE E 1094 UNP P20702 EXPRESSION TAG
SEQADV 3K6S GLN E 1095 UNP P20702 EXPRESSION TAG
SEQADV 3K6S ASP F 678 UNP P05107 EXPRESSION TAG
SEQADV 3K6S GLY F 679 UNP P05107 EXPRESSION TAG
SEQADV 3K6S CYS F 680 UNP P05107 EXPRESSION TAG
SEQADV 3K6S GLY F 681 UNP P05107 EXPRESSION TAG
SEQADV 3K6S GLU F 682 UNP P05107 EXPRESSION TAG
SEQADV 3K6S LEU F 684 UNP P05107 EXPRESSION TAG
SEQADV 3K6S TYR F 685 UNP P05107 EXPRESSION TAG
SEQADV 3K6S PHE F 686 UNP P05107 EXPRESSION TAG
SEQADV 3K6S GLN F 687 UNP P05107 EXPRESSION TAG
SEQADV 3K6S GLY G 1085 UNP P20702 EXPRESSION TAG
SEQADV 3K6S CYS G 1086 UNP P20702 EXPRESSION TAG
SEQADV 3K6S GLY G 1087 UNP P20702 EXPRESSION TAG
SEQADV 3K6S GLY G 1088 UNP P20702 EXPRESSION TAG
SEQADV 3K6S LEU G 1089 UNP P20702 EXPRESSION TAG
SEQADV 3K6S GLU G 1090 UNP P20702 EXPRESSION TAG
SEQADV 3K6S ASN G 1091 UNP P20702 EXPRESSION TAG
SEQADV 3K6S LEU G 1092 UNP P20702 EXPRESSION TAG
SEQADV 3K6S TYR G 1093 UNP P20702 EXPRESSION TAG
SEQADV 3K6S PHE G 1094 UNP P20702 EXPRESSION TAG
SEQADV 3K6S GLN G 1095 UNP P20702 EXPRESSION TAG
SEQADV 3K6S ASP H 678 UNP P05107 EXPRESSION TAG
SEQADV 3K6S GLY H 679 UNP P05107 EXPRESSION TAG
SEQADV 3K6S CYS H 680 UNP P05107 EXPRESSION TAG
SEQADV 3K6S GLY H 681 UNP P05107 EXPRESSION TAG
SEQADV 3K6S GLU H 682 UNP P05107 EXPRESSION TAG
SEQADV 3K6S LEU H 684 UNP P05107 EXPRESSION TAG
SEQADV 3K6S TYR H 685 UNP P05107 EXPRESSION TAG
SEQADV 3K6S PHE H 686 UNP P05107 EXPRESSION TAG
SEQADV 3K6S GLN H 687 UNP P05107 EXPRESSION TAG
SEQRES 1 A 1095 PHE ASN LEU ASP THR GLU GLU LEU THR ALA PHE ARG VAL
SEQRES 2 A 1095 ASP SER ALA GLY PHE GLY ASP SER VAL VAL GLN TYR ALA
SEQRES 3 A 1095 ASN SER TRP VAL VAL VAL GLY ALA PRO GLN LYS ILE THR
SEQRES 4 A 1095 ALA ALA ASN GLN THR GLY GLY LEU TYR GLN CYS GLY TYR
SEQRES 5 A 1095 SER THR GLY ALA CYS GLU PRO ILE GLY LEU GLN VAL PRO
SEQRES 6 A 1095 PRO GLU ALA VAL ASN MET SER LEU GLY LEU SER LEU ALA
SEQRES 7 A 1095 SER THR THR SER PRO SER GLN LEU LEU ALA CYS GLY PRO
SEQRES 8 A 1095 THR VAL HIS HIS GLU CYS GLY ARG ASN MET TYR LEU THR
SEQRES 9 A 1095 GLY LEU CYS PHE LEU LEU GLY PRO THR GLN LEU THR GLN
SEQRES 10 A 1095 ARG LEU PRO VAL SER ARG GLN GLU CYS PRO ARG GLN GLU
SEQRES 11 A 1095 GLN ASP ILE VAL PHE LEU ILE ASP GLY SER GLY SER ILE
SEQRES 12 A 1095 SER SER ARG ASN PHE ALA THR MET MET ASN PHE VAL ARG
SEQRES 13 A 1095 ALA VAL ILE SER GLN PHE GLN ARG PRO SER THR GLN PHE
SEQRES 14 A 1095 SER LEU MET GLN PHE SER ASN LYS PHE GLN THR HIS PHE
SEQRES 15 A 1095 THR PHE GLU GLU PHE ARG ARG SER SER ASN PRO LEU SER
SEQRES 16 A 1095 LEU LEU ALA SER VAL HIS GLN LEU GLN GLY PHE THR TYR
SEQRES 17 A 1095 THR ALA THR ALA ILE GLN ASN VAL VAL HIS ARG LEU PHE
SEQRES 18 A 1095 HIS ALA SER TYR GLY ALA ARG ARG ASP ALA ALA LYS ILE
SEQRES 19 A 1095 LEU ILE VAL ILE THR ASP GLY LYS LYS GLU GLY ASP SER
SEQRES 20 A 1095 LEU ASP TYR LYS ASP VAL ILE PRO MET ALA ASP ALA ALA
SEQRES 21 A 1095 GLY ILE ILE ARG TYR ALA ILE GLY VAL GLY LEU ALA PHE
SEQRES 22 A 1095 GLN ASN ARG ASN SER TRP LYS GLU LEU ASN ASP ILE ALA
SEQRES 23 A 1095 SER LYS PRO SER GLN GLU HIS ILE PHE LYS VAL GLU ASP
SEQRES 24 A 1095 PHE ASP ALA LEU LYS ASP ILE GLN ASN GLN LEU LYS GLU
SEQRES 25 A 1095 LYS ILE PHE ALA ILE GLU GLY THR GLU THR THR SER SER
SEQRES 26 A 1095 SER SER PHE GLU LEU GLU MET ALA GLN GLU GLY PHE SER
SEQRES 27 A 1095 ALA VAL PHE THR PRO ASP GLY PRO VAL LEU GLY ALA VAL
SEQRES 28 A 1095 GLY SER PHE THR TRP SER GLY GLY ALA PHE LEU TYR PRO
SEQRES 29 A 1095 PRO ASN MET SER PRO THR PHE ILE ASN MET SER GLN GLU
SEQRES 30 A 1095 ASN VAL ASP MET ARG ASP SER TYR LEU GLY TYR SER THR
SEQRES 31 A 1095 GLU LEU ALA LEU TRP LYS GLY VAL GLN SER LEU VAL LEU
SEQRES 32 A 1095 GLY ALA PRO ARG TYR GLN HIS THR GLY LYS ALA VAL ILE
SEQRES 33 A 1095 PHE THR GLN VAL SER ARG GLN TRP ARG MET LYS ALA GLU
SEQRES 34 A 1095 VAL THR GLY THR GLN ILE GLY SER TYR PHE GLY ALA SER
SEQRES 35 A 1095 LEU CYS SER VAL ASP VAL ASP SER ASP GLY SER THR ASP
SEQRES 36 A 1095 LEU VAL LEU ILE GLY ALA PRO HIS TYR TYR GLU GLN THR
SEQRES 37 A 1095 ARG GLY GLY GLN VAL SER VAL CYS PRO LEU PRO ARG GLY
SEQRES 38 A 1095 TRP ARG ARG TRP TRP CYS ASP ALA VAL LEU TYR GLY GLU
SEQRES 39 A 1095 GLN GLY HIS PRO TRP GLY ARG PHE GLY ALA ALA LEU THR
SEQRES 40 A 1095 VAL LEU GLY ASP VAL ASN GLY ASP LYS LEU THR ASP VAL
SEQRES 41 A 1095 VAL ILE GLY ALA PRO GLY GLU GLU GLU ASN ARG GLY ALA
SEQRES 42 A 1095 VAL TYR LEU PHE HIS GLY VAL LEU GLY PRO SER ILE SER
SEQRES 43 A 1095 PRO SER HIS SER GLN ARG ILE ALA GLY SER GLN LEU SER
SEQRES 44 A 1095 SER ARG LEU GLN TYR PHE GLY GLN ALA LEU SER GLY GLY
SEQRES 45 A 1095 GLN ASP LEU THR GLN ASP GLY LEU VAL ASP LEU ALA VAL
SEQRES 46 A 1095 GLY ALA ARG GLY GLN VAL LEU LEU LEU ARG THR ARG PRO
SEQRES 47 A 1095 VAL LEU TRP VAL GLY VAL SER MET GLN PHE ILE PRO ALA
SEQRES 48 A 1095 GLU ILE PRO ARG SER ALA PHE GLU CYS ARG GLU GLN VAL
SEQRES 49 A 1095 VAL SER GLU GLN THR LEU VAL GLN SER ASN ILE CYS LEU
SEQRES 50 A 1095 TYR ILE ASP LYS ARG SER LYS ASN LEU LEU GLY SER ARG
SEQRES 51 A 1095 ASP LEU GLN SER SER VAL THR LEU ASP LEU ALA LEU ASP
SEQRES 52 A 1095 PRO GLY ARG LEU SER PRO ARG ALA THR PHE GLN GLU THR
SEQRES 53 A 1095 LYS ASN ARG SER LEU SER ARG VAL ARG VAL LEU GLY LEU
SEQRES 54 A 1095 LYS ALA HIS CYS GLU ASN PHE ASN LEU LEU LEU PRO SER
SEQRES 55 A 1095 CYS VAL GLU ASP SER VAL THR PRO ILE THR LEU ARG LEU
SEQRES 56 A 1095 ASN PHE THR LEU VAL GLY LYS PRO LEU LEU ALA PHE ARG
SEQRES 57 A 1095 ASN LEU ARG PRO MET LEU ALA ALA ASP ALA GLN ARG TYR
SEQRES 58 A 1095 PHE THR ALA SER LEU PRO PHE GLU LYS ASN CYS GLY ALA
SEQRES 59 A 1095 ASP HIS ILE CYS GLN ASP ASN LEU GLY ILE SER PHE SER
SEQRES 60 A 1095 PHE PRO GLY LEU LYS SER LEU LEU VAL GLY SER ASN LEU
SEQRES 61 A 1095 GLU LEU ASN ALA GLU VAL MET VAL TRP ASN ASP GLY GLU
SEQRES 62 A 1095 ASP SER TYR GLY THR THR ILE THR PHE SER HIS PRO ALA
SEQRES 63 A 1095 GLY LEU SER TYR ARG TYR VAL ALA GLU GLY GLN LYS GLN
SEQRES 64 A 1095 GLY GLN LEU ARG SER LEU HIS LEU THR CYS ASP SER ALA
SEQRES 65 A 1095 PRO VAL GLY SER GLN GLY THR TRP SER THR SER CYS ARG
SEQRES 66 A 1095 ILE ASN HIS LEU ILE PHE ARG GLY GLY ALA GLN ILE THR
SEQRES 67 A 1095 PHE LEU ALA THR PHE ASP VAL SER PRO LYS ALA VAL LEU
SEQRES 68 A 1095 GLY ASP ARG LEU LEU LEU THR ALA ASN VAL SER SER GLU
SEQRES 69 A 1095 ASN ASN THR PRO ARG THR SER LYS THR THR PHE GLN LEU
SEQRES 70 A 1095 GLU LEU PRO VAL LYS TYR ALA VAL TYR THR VAL VAL SER
SEQRES 71 A 1095 SER HIS GLU GLN PHE THR LYS TYR LEU ASN PHE SER GLU
SEQRES 72 A 1095 SER GLU GLU LYS GLU SER HIS VAL ALA MET HIS ARG TYR
SEQRES 73 A 1095 GLN VAL ASN ASN LEU GLY GLN ARG ASP LEU PRO VAL SER
SEQRES 74 A 1095 ILE ASN PHE TRP VAL PRO VAL GLU LEU ASN GLN GLU ALA
SEQRES 75 A 1095 VAL TRP MET ASP VAL GLU VAL SER HIS PRO GLN ASN PRO
SEQRES 76 A 1095 SER LEU ARG CYS SER SER GLU LYS ILE ALA PRO PRO ALA
SEQRES 77 A 1095 SER ASP PHE LEU ALA HIS ILE GLN LYS ASN PRO VAL LEU
SEQRES 78 A 1095 ASP CYS SER ILE ALA GLY CYS LEU ARG PHE ARG CYS ASP
SEQRES 79 A 1095 VAL PRO SER PHE SER VAL GLN GLU GLU LEU ASP PHE THR
SEQRES 80 A 1095 LEU LYS GLY ASN LEU SER PHE GLY TRP VAL ARG GLN ILE
SEQRES 81 A 1095 LEU GLN LYS LYS VAL SER VAL VAL SER VAL ALA GLU ILE
SEQRES 82 A 1095 THR PHE ASP THR SER VAL TYR SER GLN LEU PRO GLY GLN
SEQRES 83 A 1095 GLU ALA PHE MET ARG ALA GLN THR THR THR VAL LEU GLU
SEQRES 84 A 1095 LYS TYR LYS VAL HIS GLY CYS GLY GLY LEU GLU ASN LEU
SEQRES 85 A 1095 TYR PHE GLN
SEQRES 1 B 687 GLN GLU CYS THR LYS PHE LYS VAL SER SER CYS ARG GLU
SEQRES 2 B 687 CYS ILE GLU SER GLY PRO GLY CYS THR TRP CYS GLN LYS
SEQRES 3 B 687 LEU ASN PHE THR GLY PRO GLY ASP PRO ASP SER ILE ARG
SEQRES 4 B 687 CYS ASP THR ARG PRO GLN LEU LEU MET ARG GLY CYS ALA
SEQRES 5 B 687 ALA ASP ASP ILE MET ASP PRO THR SER LEU ALA GLU THR
SEQRES 6 B 687 GLN GLU ASP HIS ASN GLY GLY GLN LYS GLN LEU SER PRO
SEQRES 7 B 687 GLN LYS VAL THR LEU TYR LEU ARG PRO GLY GLN ALA ALA
SEQRES 8 B 687 ALA PHE ASN VAL THR PHE ARG ARG ALA LYS GLY TYR PRO
SEQRES 9 B 687 ILE ASP LEU TYR TYR LEU MET ASP LEU SER TYR SER MET
SEQRES 10 B 687 LEU ASP ASP LEU ARG ASN VAL LYS LYS LEU GLY GLY ASP
SEQRES 11 B 687 LEU LEU ARG ALA LEU ASN GLU ILE THR GLU SER GLY ARG
SEQRES 12 B 687 ILE GLY PHE GLY SER PHE VAL ASP LYS THR VAL LEU PRO
SEQRES 13 B 687 PHE VAL ASN THR HIS PRO ASP LYS LEU ARG ASN PRO CYS
SEQRES 14 B 687 PRO ASN LYS GLU LYS GLU CYS GLN PRO PRO PHE ALA PHE
SEQRES 15 B 687 ARG HIS VAL LEU LYS LEU THR ASN ASN SER ASN GLN PHE
SEQRES 16 B 687 GLN THR GLU VAL GLY LYS GLN LEU ILE SER GLY ASN LEU
SEQRES 17 B 687 ASP ALA PRO GLU GLY GLY LEU ASP ALA MET MET GLN VAL
SEQRES 18 B 687 ALA ALA CYS PRO GLU GLU ILE GLY TRP ARG ASN VAL THR
SEQRES 19 B 687 ARG LEU LEU VAL PHE ALA THR ASP ASP GLY PHE HIS PHE
SEQRES 20 B 687 ALA GLY ASP GLY LYS LEU GLY ALA ILE LEU THR PRO ASN
SEQRES 21 B 687 ASP GLY ARG CYS HIS LEU GLU ASP ASN LEU TYR LYS ARG
SEQRES 22 B 687 SER ASN GLU PHE ASP TYR PRO SER VAL GLY GLN LEU ALA
SEQRES 23 B 687 HIS LYS LEU ALA GLU ASN ASN ILE GLN PRO ILE PHE ALA
SEQRES 24 B 687 VAL THR SER ARG MET VAL LYS THR TYR GLU LYS LEU THR
SEQRES 25 B 687 GLU ILE ILE PRO LYS SER ALA VAL GLY GLU LEU SER GLU
SEQRES 26 B 687 ASP SER SER ASN VAL VAL GLN LEU ILE LYS ASN ALA TYR
SEQRES 27 B 687 ASN LYS LEU SER SER ARG VAL PHE LEU ASP HIS ASN ALA
SEQRES 28 B 687 LEU PRO ASP THR LEU LYS VAL THR TYR ASP SER PHE CYS
SEQRES 29 B 687 SER ASN GLY VAL THR HIS ARG ASN GLN PRO ARG GLY ASP
SEQRES 30 B 687 CYS ASP GLY VAL GLN ILE ASN VAL PRO ILE THR PHE GLN
SEQRES 31 B 687 VAL LYS VAL THR ALA THR GLU CYS ILE GLN GLU GLN SER
SEQRES 32 B 687 PHE VAL ILE ARG ALA LEU GLY PHE THR ASP ILE VAL THR
SEQRES 33 B 687 VAL GLN VAL LEU PRO GLN CYS GLU CYS ARG CYS ARG ASP
SEQRES 34 B 687 GLN SER ARG ASP ARG SER LEU CYS HIS GLY LYS GLY PHE
SEQRES 35 B 687 LEU GLU CYS GLY ILE CYS ARG CYS ASP THR GLY TYR ILE
SEQRES 36 B 687 GLY LYS ASN CYS GLU CYS GLN THR GLN GLY ARG SER SER
SEQRES 37 B 687 GLN GLU LEU GLU GLY SER CYS ARG LYS ASP ASN ASN SER
SEQRES 38 B 687 ILE ILE CYS SER GLY LEU GLY ASP CYS VAL CYS GLY GLN
SEQRES 39 B 687 CYS LEU CYS HIS THR SER ASP VAL PRO GLY LYS LEU ILE
SEQRES 40 B 687 TYR GLY GLN TYR CYS GLU CYS ASP THR ILE ASN CYS GLU
SEQRES 41 B 687 ARG TYR ASN GLY GLN VAL CYS GLY GLY PRO GLY ARG GLY
SEQRES 42 B 687 LEU CYS PHE CYS GLY LYS CYS ARG CYS HIS PRO GLY PHE
SEQRES 43 B 687 GLU GLY SER ALA CYS GLN CYS GLU ARG THR THR GLU GLY
SEQRES 44 B 687 CYS LEU ASN PRO ARG ARG VAL GLU CYS SER GLY ARG GLY
SEQRES 45 B 687 ARG CYS ARG CYS ASN VAL CYS GLU CYS HIS SER GLY TYR
SEQRES 46 B 687 GLN LEU PRO LEU CYS GLN GLU CYS PRO GLY CYS PRO SER
SEQRES 47 B 687 PRO CYS GLY LYS TYR ILE SER CYS ALA GLU CYS LEU LYS
SEQRES 48 B 687 PHE GLU LYS GLY PRO PHE GLY LYS ASN CYS SER ALA ALA
SEQRES 49 B 687 CYS PRO GLY LEU GLN LEU SER ASN ASN PRO VAL LYS GLY
SEQRES 50 B 687 ARG THR CYS LYS GLU ARG ASP SER GLU GLY CYS TRP VAL
SEQRES 51 B 687 ALA TYR THR LEU GLU GLN GLN ASP GLY MET ASP ARG TYR
SEQRES 52 B 687 LEU ILE TYR VAL ASP GLU SER ARG GLU CYS VAL ALA GLY
SEQRES 53 B 687 PRO ASP GLY CYS GLY GLU ASN LEU TYR PHE GLN
SEQRES 1 C 1095 PHE ASN LEU ASP THR GLU GLU LEU THR ALA PHE ARG VAL
SEQRES 2 C 1095 ASP SER ALA GLY PHE GLY ASP SER VAL VAL GLN TYR ALA
SEQRES 3 C 1095 ASN SER TRP VAL VAL VAL GLY ALA PRO GLN LYS ILE THR
SEQRES 4 C 1095 ALA ALA ASN GLN THR GLY GLY LEU TYR GLN CYS GLY TYR
SEQRES 5 C 1095 SER THR GLY ALA CYS GLU PRO ILE GLY LEU GLN VAL PRO
SEQRES 6 C 1095 PRO GLU ALA VAL ASN MET SER LEU GLY LEU SER LEU ALA
SEQRES 7 C 1095 SER THR THR SER PRO SER GLN LEU LEU ALA CYS GLY PRO
SEQRES 8 C 1095 THR VAL HIS HIS GLU CYS GLY ARG ASN MET TYR LEU THR
SEQRES 9 C 1095 GLY LEU CYS PHE LEU LEU GLY PRO THR GLN LEU THR GLN
SEQRES 10 C 1095 ARG LEU PRO VAL SER ARG GLN GLU CYS PRO ARG GLN GLU
SEQRES 11 C 1095 GLN ASP ILE VAL PHE LEU ILE ASP GLY SER GLY SER ILE
SEQRES 12 C 1095 SER SER ARG ASN PHE ALA THR MET MET ASN PHE VAL ARG
SEQRES 13 C 1095 ALA VAL ILE SER GLN PHE GLN ARG PRO SER THR GLN PHE
SEQRES 14 C 1095 SER LEU MET GLN PHE SER ASN LYS PHE GLN THR HIS PHE
SEQRES 15 C 1095 THR PHE GLU GLU PHE ARG ARG SER SER ASN PRO LEU SER
SEQRES 16 C 1095 LEU LEU ALA SER VAL HIS GLN LEU GLN GLY PHE THR TYR
SEQRES 17 C 1095 THR ALA THR ALA ILE GLN ASN VAL VAL HIS ARG LEU PHE
SEQRES 18 C 1095 HIS ALA SER TYR GLY ALA ARG ARG ASP ALA ALA LYS ILE
SEQRES 19 C 1095 LEU ILE VAL ILE THR ASP GLY LYS LYS GLU GLY ASP SER
SEQRES 20 C 1095 LEU ASP TYR LYS ASP VAL ILE PRO MET ALA ASP ALA ALA
SEQRES 21 C 1095 GLY ILE ILE ARG TYR ALA ILE GLY VAL GLY LEU ALA PHE
SEQRES 22 C 1095 GLN ASN ARG ASN SER TRP LYS GLU LEU ASN ASP ILE ALA
SEQRES 23 C 1095 SER LYS PRO SER GLN GLU HIS ILE PHE LYS VAL GLU ASP
SEQRES 24 C 1095 PHE ASP ALA LEU LYS ASP ILE GLN ASN GLN LEU LYS GLU
SEQRES 25 C 1095 LYS ILE PHE ALA ILE GLU GLY THR GLU THR THR SER SER
SEQRES 26 C 1095 SER SER PHE GLU LEU GLU MET ALA GLN GLU GLY PHE SER
SEQRES 27 C 1095 ALA VAL PHE THR PRO ASP GLY PRO VAL LEU GLY ALA VAL
SEQRES 28 C 1095 GLY SER PHE THR TRP SER GLY GLY ALA PHE LEU TYR PRO
SEQRES 29 C 1095 PRO ASN MET SER PRO THR PHE ILE ASN MET SER GLN GLU
SEQRES 30 C 1095 ASN VAL ASP MET ARG ASP SER TYR LEU GLY TYR SER THR
SEQRES 31 C 1095 GLU LEU ALA LEU TRP LYS GLY VAL GLN SER LEU VAL LEU
SEQRES 32 C 1095 GLY ALA PRO ARG TYR GLN HIS THR GLY LYS ALA VAL ILE
SEQRES 33 C 1095 PHE THR GLN VAL SER ARG GLN TRP ARG MET LYS ALA GLU
SEQRES 34 C 1095 VAL THR GLY THR GLN ILE GLY SER TYR PHE GLY ALA SER
SEQRES 35 C 1095 LEU CYS SER VAL ASP VAL ASP SER ASP GLY SER THR ASP
SEQRES 36 C 1095 LEU VAL LEU ILE GLY ALA PRO HIS TYR TYR GLU GLN THR
SEQRES 37 C 1095 ARG GLY GLY GLN VAL SER VAL CYS PRO LEU PRO ARG GLY
SEQRES 38 C 1095 TRP ARG ARG TRP TRP CYS ASP ALA VAL LEU TYR GLY GLU
SEQRES 39 C 1095 GLN GLY HIS PRO TRP GLY ARG PHE GLY ALA ALA LEU THR
SEQRES 40 C 1095 VAL LEU GLY ASP VAL ASN GLY ASP LYS LEU THR ASP VAL
SEQRES 41 C 1095 VAL ILE GLY ALA PRO GLY GLU GLU GLU ASN ARG GLY ALA
SEQRES 42 C 1095 VAL TYR LEU PHE HIS GLY VAL LEU GLY PRO SER ILE SER
SEQRES 43 C 1095 PRO SER HIS SER GLN ARG ILE ALA GLY SER GLN LEU SER
SEQRES 44 C 1095 SER ARG LEU GLN TYR PHE GLY GLN ALA LEU SER GLY GLY
SEQRES 45 C 1095 GLN ASP LEU THR GLN ASP GLY LEU VAL ASP LEU ALA VAL
SEQRES 46 C 1095 GLY ALA ARG GLY GLN VAL LEU LEU LEU ARG THR ARG PRO
SEQRES 47 C 1095 VAL LEU TRP VAL GLY VAL SER MET GLN PHE ILE PRO ALA
SEQRES 48 C 1095 GLU ILE PRO ARG SER ALA PHE GLU CYS ARG GLU GLN VAL
SEQRES 49 C 1095 VAL SER GLU GLN THR LEU VAL GLN SER ASN ILE CYS LEU
SEQRES 50 C 1095 TYR ILE ASP LYS ARG SER LYS ASN LEU LEU GLY SER ARG
SEQRES 51 C 1095 ASP LEU GLN SER SER VAL THR LEU ASP LEU ALA LEU ASP
SEQRES 52 C 1095 PRO GLY ARG LEU SER PRO ARG ALA THR PHE GLN GLU THR
SEQRES 53 C 1095 LYS ASN ARG SER LEU SER ARG VAL ARG VAL LEU GLY LEU
SEQRES 54 C 1095 LYS ALA HIS CYS GLU ASN PHE ASN LEU LEU LEU PRO SER
SEQRES 55 C 1095 CYS VAL GLU ASP SER VAL THR PRO ILE THR LEU ARG LEU
SEQRES 56 C 1095 ASN PHE THR LEU VAL GLY LYS PRO LEU LEU ALA PHE ARG
SEQRES 57 C 1095 ASN LEU ARG PRO MET LEU ALA ALA ASP ALA GLN ARG TYR
SEQRES 58 C 1095 PHE THR ALA SER LEU PRO PHE GLU LYS ASN CYS GLY ALA
SEQRES 59 C 1095 ASP HIS ILE CYS GLN ASP ASN LEU GLY ILE SER PHE SER
SEQRES 60 C 1095 PHE PRO GLY LEU LYS SER LEU LEU VAL GLY SER ASN LEU
SEQRES 61 C 1095 GLU LEU ASN ALA GLU VAL MET VAL TRP ASN ASP GLY GLU
SEQRES 62 C 1095 ASP SER TYR GLY THR THR ILE THR PHE SER HIS PRO ALA
SEQRES 63 C 1095 GLY LEU SER TYR ARG TYR VAL ALA GLU GLY GLN LYS GLN
SEQRES 64 C 1095 GLY GLN LEU ARG SER LEU HIS LEU THR CYS ASP SER ALA
SEQRES 65 C 1095 PRO VAL GLY SER GLN GLY THR TRP SER THR SER CYS ARG
SEQRES 66 C 1095 ILE ASN HIS LEU ILE PHE ARG GLY GLY ALA GLN ILE THR
SEQRES 67 C 1095 PHE LEU ALA THR PHE ASP VAL SER PRO LYS ALA VAL LEU
SEQRES 68 C 1095 GLY ASP ARG LEU LEU LEU THR ALA ASN VAL SER SER GLU
SEQRES 69 C 1095 ASN ASN THR PRO ARG THR SER LYS THR THR PHE GLN LEU
SEQRES 70 C 1095 GLU LEU PRO VAL LYS TYR ALA VAL TYR THR VAL VAL SER
SEQRES 71 C 1095 SER HIS GLU GLN PHE THR LYS TYR LEU ASN PHE SER GLU
SEQRES 72 C 1095 SER GLU GLU LYS GLU SER HIS VAL ALA MET HIS ARG TYR
SEQRES 73 C 1095 GLN VAL ASN ASN LEU GLY GLN ARG ASP LEU PRO VAL SER
SEQRES 74 C 1095 ILE ASN PHE TRP VAL PRO VAL GLU LEU ASN GLN GLU ALA
SEQRES 75 C 1095 VAL TRP MET ASP VAL GLU VAL SER HIS PRO GLN ASN PRO
SEQRES 76 C 1095 SER LEU ARG CYS SER SER GLU LYS ILE ALA PRO PRO ALA
SEQRES 77 C 1095 SER ASP PHE LEU ALA HIS ILE GLN LYS ASN PRO VAL LEU
SEQRES 78 C 1095 ASP CYS SER ILE ALA GLY CYS LEU ARG PHE ARG CYS ASP
SEQRES 79 C 1095 VAL PRO SER PHE SER VAL GLN GLU GLU LEU ASP PHE THR
SEQRES 80 C 1095 LEU LYS GLY ASN LEU SER PHE GLY TRP VAL ARG GLN ILE
SEQRES 81 C 1095 LEU GLN LYS LYS VAL SER VAL VAL SER VAL ALA GLU ILE
SEQRES 82 C 1095 THR PHE ASP THR SER VAL TYR SER GLN LEU PRO GLY GLN
SEQRES 83 C 1095 GLU ALA PHE MET ARG ALA GLN THR THR THR VAL LEU GLU
SEQRES 84 C 1095 LYS TYR LYS VAL HIS GLY CYS GLY GLY LEU GLU ASN LEU
SEQRES 85 C 1095 TYR PHE GLN
SEQRES 1 D 687 GLN GLU CYS THR LYS PHE LYS VAL SER SER CYS ARG GLU
SEQRES 2 D 687 CYS ILE GLU SER GLY PRO GLY CYS THR TRP CYS GLN LYS
SEQRES 3 D 687 LEU ASN PHE THR GLY PRO GLY ASP PRO ASP SER ILE ARG
SEQRES 4 D 687 CYS ASP THR ARG PRO GLN LEU LEU MET ARG GLY CYS ALA
SEQRES 5 D 687 ALA ASP ASP ILE MET ASP PRO THR SER LEU ALA GLU THR
SEQRES 6 D 687 GLN GLU ASP HIS ASN GLY GLY GLN LYS GLN LEU SER PRO
SEQRES 7 D 687 GLN LYS VAL THR LEU TYR LEU ARG PRO GLY GLN ALA ALA
SEQRES 8 D 687 ALA PHE ASN VAL THR PHE ARG ARG ALA LYS GLY TYR PRO
SEQRES 9 D 687 ILE ASP LEU TYR TYR LEU MET ASP LEU SER TYR SER MET
SEQRES 10 D 687 LEU ASP ASP LEU ARG ASN VAL LYS LYS LEU GLY GLY ASP
SEQRES 11 D 687 LEU LEU ARG ALA LEU ASN GLU ILE THR GLU SER GLY ARG
SEQRES 12 D 687 ILE GLY PHE GLY SER PHE VAL ASP LYS THR VAL LEU PRO
SEQRES 13 D 687 PHE VAL ASN THR HIS PRO ASP LYS LEU ARG ASN PRO CYS
SEQRES 14 D 687 PRO ASN LYS GLU LYS GLU CYS GLN PRO PRO PHE ALA PHE
SEQRES 15 D 687 ARG HIS VAL LEU LYS LEU THR ASN ASN SER ASN GLN PHE
SEQRES 16 D 687 GLN THR GLU VAL GLY LYS GLN LEU ILE SER GLY ASN LEU
SEQRES 17 D 687 ASP ALA PRO GLU GLY GLY LEU ASP ALA MET MET GLN VAL
SEQRES 18 D 687 ALA ALA CYS PRO GLU GLU ILE GLY TRP ARG ASN VAL THR
SEQRES 19 D 687 ARG LEU LEU VAL PHE ALA THR ASP ASP GLY PHE HIS PHE
SEQRES 20 D 687 ALA GLY ASP GLY LYS LEU GLY ALA ILE LEU THR PRO ASN
SEQRES 21 D 687 ASP GLY ARG CYS HIS LEU GLU ASP ASN LEU TYR LYS ARG
SEQRES 22 D 687 SER ASN GLU PHE ASP TYR PRO SER VAL GLY GLN LEU ALA
SEQRES 23 D 687 HIS LYS LEU ALA GLU ASN ASN ILE GLN PRO ILE PHE ALA
SEQRES 24 D 687 VAL THR SER ARG MET VAL LYS THR TYR GLU LYS LEU THR
SEQRES 25 D 687 GLU ILE ILE PRO LYS SER ALA VAL GLY GLU LEU SER GLU
SEQRES 26 D 687 ASP SER SER ASN VAL VAL GLN LEU ILE LYS ASN ALA TYR
SEQRES 27 D 687 ASN LYS LEU SER SER ARG VAL PHE LEU ASP HIS ASN ALA
SEQRES 28 D 687 LEU PRO ASP THR LEU LYS VAL THR TYR ASP SER PHE CYS
SEQRES 29 D 687 SER ASN GLY VAL THR HIS ARG ASN GLN PRO ARG GLY ASP
SEQRES 30 D 687 CYS ASP GLY VAL GLN ILE ASN VAL PRO ILE THR PHE GLN
SEQRES 31 D 687 VAL LYS VAL THR ALA THR GLU CYS ILE GLN GLU GLN SER
SEQRES 32 D 687 PHE VAL ILE ARG ALA LEU GLY PHE THR ASP ILE VAL THR
SEQRES 33 D 687 VAL GLN VAL LEU PRO GLN CYS GLU CYS ARG CYS ARG ASP
SEQRES 34 D 687 GLN SER ARG ASP ARG SER LEU CYS HIS GLY LYS GLY PHE
SEQRES 35 D 687 LEU GLU CYS GLY ILE CYS ARG CYS ASP THR GLY TYR ILE
SEQRES 36 D 687 GLY LYS ASN CYS GLU CYS GLN THR GLN GLY ARG SER SER
SEQRES 37 D 687 GLN GLU LEU GLU GLY SER CYS ARG LYS ASP ASN ASN SER
SEQRES 38 D 687 ILE ILE CYS SER GLY LEU GLY ASP CYS VAL CYS GLY GLN
SEQRES 39 D 687 CYS LEU CYS HIS THR SER ASP VAL PRO GLY LYS LEU ILE
SEQRES 40 D 687 TYR GLY GLN TYR CYS GLU CYS ASP THR ILE ASN CYS GLU
SEQRES 41 D 687 ARG TYR ASN GLY GLN VAL CYS GLY GLY PRO GLY ARG GLY
SEQRES 42 D 687 LEU CYS PHE CYS GLY LYS CYS ARG CYS HIS PRO GLY PHE
SEQRES 43 D 687 GLU GLY SER ALA CYS GLN CYS GLU ARG THR THR GLU GLY
SEQRES 44 D 687 CYS LEU ASN PRO ARG ARG VAL GLU CYS SER GLY ARG GLY
SEQRES 45 D 687 ARG CYS ARG CYS ASN VAL CYS GLU CYS HIS SER GLY TYR
SEQRES 46 D 687 GLN LEU PRO LEU CYS GLN GLU CYS PRO GLY CYS PRO SER
SEQRES 47 D 687 PRO CYS GLY LYS TYR ILE SER CYS ALA GLU CYS LEU LYS
SEQRES 48 D 687 PHE GLU LYS GLY PRO PHE GLY LYS ASN CYS SER ALA ALA
SEQRES 49 D 687 CYS PRO GLY LEU GLN LEU SER ASN ASN PRO VAL LYS GLY
SEQRES 50 D 687 ARG THR CYS LYS GLU ARG ASP SER GLU GLY CYS TRP VAL
SEQRES 51 D 687 ALA TYR THR LEU GLU GLN GLN ASP GLY MET ASP ARG TYR
SEQRES 52 D 687 LEU ILE TYR VAL ASP GLU SER ARG GLU CYS VAL ALA GLY
SEQRES 53 D 687 PRO ASP GLY CYS GLY GLU ASN LEU TYR PHE GLN
SEQRES 1 E 1095 PHE ASN LEU ASP THR GLU GLU LEU THR ALA PHE ARG VAL
SEQRES 2 E 1095 ASP SER ALA GLY PHE GLY ASP SER VAL VAL GLN TYR ALA
SEQRES 3 E 1095 ASN SER TRP VAL VAL VAL GLY ALA PRO GLN LYS ILE THR
SEQRES 4 E 1095 ALA ALA ASN GLN THR GLY GLY LEU TYR GLN CYS GLY TYR
SEQRES 5 E 1095 SER THR GLY ALA CYS GLU PRO ILE GLY LEU GLN VAL PRO
SEQRES 6 E 1095 PRO GLU ALA VAL ASN MET SER LEU GLY LEU SER LEU ALA
SEQRES 7 E 1095 SER THR THR SER PRO SER GLN LEU LEU ALA CYS GLY PRO
SEQRES 8 E 1095 THR VAL HIS HIS GLU CYS GLY ARG ASN MET TYR LEU THR
SEQRES 9 E 1095 GLY LEU CYS PHE LEU LEU GLY PRO THR GLN LEU THR GLN
SEQRES 10 E 1095 ARG LEU PRO VAL SER ARG GLN GLU CYS PRO ARG GLN GLU
SEQRES 11 E 1095 GLN ASP ILE VAL PHE LEU ILE ASP GLY SER GLY SER ILE
SEQRES 12 E 1095 SER SER ARG ASN PHE ALA THR MET MET ASN PHE VAL ARG
SEQRES 13 E 1095 ALA VAL ILE SER GLN PHE GLN ARG PRO SER THR GLN PHE
SEQRES 14 E 1095 SER LEU MET GLN PHE SER ASN LYS PHE GLN THR HIS PHE
SEQRES 15 E 1095 THR PHE GLU GLU PHE ARG ARG SER SER ASN PRO LEU SER
SEQRES 16 E 1095 LEU LEU ALA SER VAL HIS GLN LEU GLN GLY PHE THR TYR
SEQRES 17 E 1095 THR ALA THR ALA ILE GLN ASN VAL VAL HIS ARG LEU PHE
SEQRES 18 E 1095 HIS ALA SER TYR GLY ALA ARG ARG ASP ALA ALA LYS ILE
SEQRES 19 E 1095 LEU ILE VAL ILE THR ASP GLY LYS LYS GLU GLY ASP SER
SEQRES 20 E 1095 LEU ASP TYR LYS ASP VAL ILE PRO MET ALA ASP ALA ALA
SEQRES 21 E 1095 GLY ILE ILE ARG TYR ALA ILE GLY VAL GLY LEU ALA PHE
SEQRES 22 E 1095 GLN ASN ARG ASN SER TRP LYS GLU LEU ASN ASP ILE ALA
SEQRES 23 E 1095 SER LYS PRO SER GLN GLU HIS ILE PHE LYS VAL GLU ASP
SEQRES 24 E 1095 PHE ASP ALA LEU LYS ASP ILE GLN ASN GLN LEU LYS GLU
SEQRES 25 E 1095 LYS ILE PHE ALA ILE GLU GLY THR GLU THR THR SER SER
SEQRES 26 E 1095 SER SER PHE GLU LEU GLU MET ALA GLN GLU GLY PHE SER
SEQRES 27 E 1095 ALA VAL PHE THR PRO ASP GLY PRO VAL LEU GLY ALA VAL
SEQRES 28 E 1095 GLY SER PHE THR TRP SER GLY GLY ALA PHE LEU TYR PRO
SEQRES 29 E 1095 PRO ASN MET SER PRO THR PHE ILE ASN MET SER GLN GLU
SEQRES 30 E 1095 ASN VAL ASP MET ARG ASP SER TYR LEU GLY TYR SER THR
SEQRES 31 E 1095 GLU LEU ALA LEU TRP LYS GLY VAL GLN SER LEU VAL LEU
SEQRES 32 E 1095 GLY ALA PRO ARG TYR GLN HIS THR GLY LYS ALA VAL ILE
SEQRES 33 E 1095 PHE THR GLN VAL SER ARG GLN TRP ARG MET LYS ALA GLU
SEQRES 34 E 1095 VAL THR GLY THR GLN ILE GLY SER TYR PHE GLY ALA SER
SEQRES 35 E 1095 LEU CYS SER VAL ASP VAL ASP SER ASP GLY SER THR ASP
SEQRES 36 E 1095 LEU VAL LEU ILE GLY ALA PRO HIS TYR TYR GLU GLN THR
SEQRES 37 E 1095 ARG GLY GLY GLN VAL SER VAL CYS PRO LEU PRO ARG GLY
SEQRES 38 E 1095 TRP ARG ARG TRP TRP CYS ASP ALA VAL LEU TYR GLY GLU
SEQRES 39 E 1095 GLN GLY HIS PRO TRP GLY ARG PHE GLY ALA ALA LEU THR
SEQRES 40 E 1095 VAL LEU GLY ASP VAL ASN GLY ASP LYS LEU THR ASP VAL
SEQRES 41 E 1095 VAL ILE GLY ALA PRO GLY GLU GLU GLU ASN ARG GLY ALA
SEQRES 42 E 1095 VAL TYR LEU PHE HIS GLY VAL LEU GLY PRO SER ILE SER
SEQRES 43 E 1095 PRO SER HIS SER GLN ARG ILE ALA GLY SER GLN LEU SER
SEQRES 44 E 1095 SER ARG LEU GLN TYR PHE GLY GLN ALA LEU SER GLY GLY
SEQRES 45 E 1095 GLN ASP LEU THR GLN ASP GLY LEU VAL ASP LEU ALA VAL
SEQRES 46 E 1095 GLY ALA ARG GLY GLN VAL LEU LEU LEU ARG THR ARG PRO
SEQRES 47 E 1095 VAL LEU TRP VAL GLY VAL SER MET GLN PHE ILE PRO ALA
SEQRES 48 E 1095 GLU ILE PRO ARG SER ALA PHE GLU CYS ARG GLU GLN VAL
SEQRES 49 E 1095 VAL SER GLU GLN THR LEU VAL GLN SER ASN ILE CYS LEU
SEQRES 50 E 1095 TYR ILE ASP LYS ARG SER LYS ASN LEU LEU GLY SER ARG
SEQRES 51 E 1095 ASP LEU GLN SER SER VAL THR LEU ASP LEU ALA LEU ASP
SEQRES 52 E 1095 PRO GLY ARG LEU SER PRO ARG ALA THR PHE GLN GLU THR
SEQRES 53 E 1095 LYS ASN ARG SER LEU SER ARG VAL ARG VAL LEU GLY LEU
SEQRES 54 E 1095 LYS ALA HIS CYS GLU ASN PHE ASN LEU LEU LEU PRO SER
SEQRES 55 E 1095 CYS VAL GLU ASP SER VAL THR PRO ILE THR LEU ARG LEU
SEQRES 56 E 1095 ASN PHE THR LEU VAL GLY LYS PRO LEU LEU ALA PHE ARG
SEQRES 57 E 1095 ASN LEU ARG PRO MET LEU ALA ALA ASP ALA GLN ARG TYR
SEQRES 58 E 1095 PHE THR ALA SER LEU PRO PHE GLU LYS ASN CYS GLY ALA
SEQRES 59 E 1095 ASP HIS ILE CYS GLN ASP ASN LEU GLY ILE SER PHE SER
SEQRES 60 E 1095 PHE PRO GLY LEU LYS SER LEU LEU VAL GLY SER ASN LEU
SEQRES 61 E 1095 GLU LEU ASN ALA GLU VAL MET VAL TRP ASN ASP GLY GLU
SEQRES 62 E 1095 ASP SER TYR GLY THR THR ILE THR PHE SER HIS PRO ALA
SEQRES 63 E 1095 GLY LEU SER TYR ARG TYR VAL ALA GLU GLY GLN LYS GLN
SEQRES 64 E 1095 GLY GLN LEU ARG SER LEU HIS LEU THR CYS ASP SER ALA
SEQRES 65 E 1095 PRO VAL GLY SER GLN GLY THR TRP SER THR SER CYS ARG
SEQRES 66 E 1095 ILE ASN HIS LEU ILE PHE ARG GLY GLY ALA GLN ILE THR
SEQRES 67 E 1095 PHE LEU ALA THR PHE ASP VAL SER PRO LYS ALA VAL LEU
SEQRES 68 E 1095 GLY ASP ARG LEU LEU LEU THR ALA ASN VAL SER SER GLU
SEQRES 69 E 1095 ASN ASN THR PRO ARG THR SER LYS THR THR PHE GLN LEU
SEQRES 70 E 1095 GLU LEU PRO VAL LYS TYR ALA VAL TYR THR VAL VAL SER
SEQRES 71 E 1095 SER HIS GLU GLN PHE THR LYS TYR LEU ASN PHE SER GLU
SEQRES 72 E 1095 SER GLU GLU LYS GLU SER HIS VAL ALA MET HIS ARG TYR
SEQRES 73 E 1095 GLN VAL ASN ASN LEU GLY GLN ARG ASP LEU PRO VAL SER
SEQRES 74 E 1095 ILE ASN PHE TRP VAL PRO VAL GLU LEU ASN GLN GLU ALA
SEQRES 75 E 1095 VAL TRP MET ASP VAL GLU VAL SER HIS PRO GLN ASN PRO
SEQRES 76 E 1095 SER LEU ARG CYS SER SER GLU LYS ILE ALA PRO PRO ALA
SEQRES 77 E 1095 SER ASP PHE LEU ALA HIS ILE GLN LYS ASN PRO VAL LEU
SEQRES 78 E 1095 ASP CYS SER ILE ALA GLY CYS LEU ARG PHE ARG CYS ASP
SEQRES 79 E 1095 VAL PRO SER PHE SER VAL GLN GLU GLU LEU ASP PHE THR
SEQRES 80 E 1095 LEU LYS GLY ASN LEU SER PHE GLY TRP VAL ARG GLN ILE
SEQRES 81 E 1095 LEU GLN LYS LYS VAL SER VAL VAL SER VAL ALA GLU ILE
SEQRES 82 E 1095 THR PHE ASP THR SER VAL TYR SER GLN LEU PRO GLY GLN
SEQRES 83 E 1095 GLU ALA PHE MET ARG ALA GLN THR THR THR VAL LEU GLU
SEQRES 84 E 1095 LYS TYR LYS VAL HIS GLY CYS GLY GLY LEU GLU ASN LEU
SEQRES 85 E 1095 TYR PHE GLN
SEQRES 1 F 687 GLN GLU CYS THR LYS PHE LYS VAL SER SER CYS ARG GLU
SEQRES 2 F 687 CYS ILE GLU SER GLY PRO GLY CYS THR TRP CYS GLN LYS
SEQRES 3 F 687 LEU ASN PHE THR GLY PRO GLY ASP PRO ASP SER ILE ARG
SEQRES 4 F 687 CYS ASP THR ARG PRO GLN LEU LEU MET ARG GLY CYS ALA
SEQRES 5 F 687 ALA ASP ASP ILE MET ASP PRO THR SER LEU ALA GLU THR
SEQRES 6 F 687 GLN GLU ASP HIS ASN GLY GLY GLN LYS GLN LEU SER PRO
SEQRES 7 F 687 GLN LYS VAL THR LEU TYR LEU ARG PRO GLY GLN ALA ALA
SEQRES 8 F 687 ALA PHE ASN VAL THR PHE ARG ARG ALA LYS GLY TYR PRO
SEQRES 9 F 687 ILE ASP LEU TYR TYR LEU MET ASP LEU SER TYR SER MET
SEQRES 10 F 687 LEU ASP ASP LEU ARG ASN VAL LYS LYS LEU GLY GLY ASP
SEQRES 11 F 687 LEU LEU ARG ALA LEU ASN GLU ILE THR GLU SER GLY ARG
SEQRES 12 F 687 ILE GLY PHE GLY SER PHE VAL ASP LYS THR VAL LEU PRO
SEQRES 13 F 687 PHE VAL ASN THR HIS PRO ASP LYS LEU ARG ASN PRO CYS
SEQRES 14 F 687 PRO ASN LYS GLU LYS GLU CYS GLN PRO PRO PHE ALA PHE
SEQRES 15 F 687 ARG HIS VAL LEU LYS LEU THR ASN ASN SER ASN GLN PHE
SEQRES 16 F 687 GLN THR GLU VAL GLY LYS GLN LEU ILE SER GLY ASN LEU
SEQRES 17 F 687 ASP ALA PRO GLU GLY GLY LEU ASP ALA MET MET GLN VAL
SEQRES 18 F 687 ALA ALA CYS PRO GLU GLU ILE GLY TRP ARG ASN VAL THR
SEQRES 19 F 687 ARG LEU LEU VAL PHE ALA THR ASP ASP GLY PHE HIS PHE
SEQRES 20 F 687 ALA GLY ASP GLY LYS LEU GLY ALA ILE LEU THR PRO ASN
SEQRES 21 F 687 ASP GLY ARG CYS HIS LEU GLU ASP ASN LEU TYR LYS ARG
SEQRES 22 F 687 SER ASN GLU PHE ASP TYR PRO SER VAL GLY GLN LEU ALA
SEQRES 23 F 687 HIS LYS LEU ALA GLU ASN ASN ILE GLN PRO ILE PHE ALA
SEQRES 24 F 687 VAL THR SER ARG MET VAL LYS THR TYR GLU LYS LEU THR
SEQRES 25 F 687 GLU ILE ILE PRO LYS SER ALA VAL GLY GLU LEU SER GLU
SEQRES 26 F 687 ASP SER SER ASN VAL VAL GLN LEU ILE LYS ASN ALA TYR
SEQRES 27 F 687 ASN LYS LEU SER SER ARG VAL PHE LEU ASP HIS ASN ALA
SEQRES 28 F 687 LEU PRO ASP THR LEU LYS VAL THR TYR ASP SER PHE CYS
SEQRES 29 F 687 SER ASN GLY VAL THR HIS ARG ASN GLN PRO ARG GLY ASP
SEQRES 30 F 687 CYS ASP GLY VAL GLN ILE ASN VAL PRO ILE THR PHE GLN
SEQRES 31 F 687 VAL LYS VAL THR ALA THR GLU CYS ILE GLN GLU GLN SER
SEQRES 32 F 687 PHE VAL ILE ARG ALA LEU GLY PHE THR ASP ILE VAL THR
SEQRES 33 F 687 VAL GLN VAL LEU PRO GLN CYS GLU CYS ARG CYS ARG ASP
SEQRES 34 F 687 GLN SER ARG ASP ARG SER LEU CYS HIS GLY LYS GLY PHE
SEQRES 35 F 687 LEU GLU CYS GLY ILE CYS ARG CYS ASP THR GLY TYR ILE
SEQRES 36 F 687 GLY LYS ASN CYS GLU CYS GLN THR GLN GLY ARG SER SER
SEQRES 37 F 687 GLN GLU LEU GLU GLY SER CYS ARG LYS ASP ASN ASN SER
SEQRES 38 F 687 ILE ILE CYS SER GLY LEU GLY ASP CYS VAL CYS GLY GLN
SEQRES 39 F 687 CYS LEU CYS HIS THR SER ASP VAL PRO GLY LYS LEU ILE
SEQRES 40 F 687 TYR GLY GLN TYR CYS GLU CYS ASP THR ILE ASN CYS GLU
SEQRES 41 F 687 ARG TYR ASN GLY GLN VAL CYS GLY GLY PRO GLY ARG GLY
SEQRES 42 F 687 LEU CYS PHE CYS GLY LYS CYS ARG CYS HIS PRO GLY PHE
SEQRES 43 F 687 GLU GLY SER ALA CYS GLN CYS GLU ARG THR THR GLU GLY
SEQRES 44 F 687 CYS LEU ASN PRO ARG ARG VAL GLU CYS SER GLY ARG GLY
SEQRES 45 F 687 ARG CYS ARG CYS ASN VAL CYS GLU CYS HIS SER GLY TYR
SEQRES 46 F 687 GLN LEU PRO LEU CYS GLN GLU CYS PRO GLY CYS PRO SER
SEQRES 47 F 687 PRO CYS GLY LYS TYR ILE SER CYS ALA GLU CYS LEU LYS
SEQRES 48 F 687 PHE GLU LYS GLY PRO PHE GLY LYS ASN CYS SER ALA ALA
SEQRES 49 F 687 CYS PRO GLY LEU GLN LEU SER ASN ASN PRO VAL LYS GLY
SEQRES 50 F 687 ARG THR CYS LYS GLU ARG ASP SER GLU GLY CYS TRP VAL
SEQRES 51 F 687 ALA TYR THR LEU GLU GLN GLN ASP GLY MET ASP ARG TYR
SEQRES 52 F 687 LEU ILE TYR VAL ASP GLU SER ARG GLU CYS VAL ALA GLY
SEQRES 53 F 687 PRO ASP GLY CYS GLY GLU ASN LEU TYR PHE GLN
SEQRES 1 G 1095 PHE ASN LEU ASP THR GLU GLU LEU THR ALA PHE ARG VAL
SEQRES 2 G 1095 ASP SER ALA GLY PHE GLY ASP SER VAL VAL GLN TYR ALA
SEQRES 3 G 1095 ASN SER TRP VAL VAL VAL GLY ALA PRO GLN LYS ILE THR
SEQRES 4 G 1095 ALA ALA ASN GLN THR GLY GLY LEU TYR GLN CYS GLY TYR
SEQRES 5 G 1095 SER THR GLY ALA CYS GLU PRO ILE GLY LEU GLN VAL PRO
SEQRES 6 G 1095 PRO GLU ALA VAL ASN MET SER LEU GLY LEU SER LEU ALA
SEQRES 7 G 1095 SER THR THR SER PRO SER GLN LEU LEU ALA CYS GLY PRO
SEQRES 8 G 1095 THR VAL HIS HIS GLU CYS GLY ARG ASN MET TYR LEU THR
SEQRES 9 G 1095 GLY LEU CYS PHE LEU LEU GLY PRO THR GLN LEU THR GLN
SEQRES 10 G 1095 ARG LEU PRO VAL SER ARG GLN GLU CYS PRO ARG GLN GLU
SEQRES 11 G 1095 GLN ASP ILE VAL PHE LEU ILE ASP GLY SER GLY SER ILE
SEQRES 12 G 1095 SER SER ARG ASN PHE ALA THR MET MET ASN PHE VAL ARG
SEQRES 13 G 1095 ALA VAL ILE SER GLN PHE GLN ARG PRO SER THR GLN PHE
SEQRES 14 G 1095 SER LEU MET GLN PHE SER ASN LYS PHE GLN THR HIS PHE
SEQRES 15 G 1095 THR PHE GLU GLU PHE ARG ARG SER SER ASN PRO LEU SER
SEQRES 16 G 1095 LEU LEU ALA SER VAL HIS GLN LEU GLN GLY PHE THR TYR
SEQRES 17 G 1095 THR ALA THR ALA ILE GLN ASN VAL VAL HIS ARG LEU PHE
SEQRES 18 G 1095 HIS ALA SER TYR GLY ALA ARG ARG ASP ALA ALA LYS ILE
SEQRES 19 G 1095 LEU ILE VAL ILE THR ASP GLY LYS LYS GLU GLY ASP SER
SEQRES 20 G 1095 LEU ASP TYR LYS ASP VAL ILE PRO MET ALA ASP ALA ALA
SEQRES 21 G 1095 GLY ILE ILE ARG TYR ALA ILE GLY VAL GLY LEU ALA PHE
SEQRES 22 G 1095 GLN ASN ARG ASN SER TRP LYS GLU LEU ASN ASP ILE ALA
SEQRES 23 G 1095 SER LYS PRO SER GLN GLU HIS ILE PHE LYS VAL GLU ASP
SEQRES 24 G 1095 PHE ASP ALA LEU LYS ASP ILE GLN ASN GLN LEU LYS GLU
SEQRES 25 G 1095 LYS ILE PHE ALA ILE GLU GLY THR GLU THR THR SER SER
SEQRES 26 G 1095 SER SER PHE GLU LEU GLU MET ALA GLN GLU GLY PHE SER
SEQRES 27 G 1095 ALA VAL PHE THR PRO ASP GLY PRO VAL LEU GLY ALA VAL
SEQRES 28 G 1095 GLY SER PHE THR TRP SER GLY GLY ALA PHE LEU TYR PRO
SEQRES 29 G 1095 PRO ASN MET SER PRO THR PHE ILE ASN MET SER GLN GLU
SEQRES 30 G 1095 ASN VAL ASP MET ARG ASP SER TYR LEU GLY TYR SER THR
SEQRES 31 G 1095 GLU LEU ALA LEU TRP LYS GLY VAL GLN SER LEU VAL LEU
SEQRES 32 G 1095 GLY ALA PRO ARG TYR GLN HIS THR GLY LYS ALA VAL ILE
SEQRES 33 G 1095 PHE THR GLN VAL SER ARG GLN TRP ARG MET LYS ALA GLU
SEQRES 34 G 1095 VAL THR GLY THR GLN ILE GLY SER TYR PHE GLY ALA SER
SEQRES 35 G 1095 LEU CYS SER VAL ASP VAL ASP SER ASP GLY SER THR ASP
SEQRES 36 G 1095 LEU VAL LEU ILE GLY ALA PRO HIS TYR TYR GLU GLN THR
SEQRES 37 G 1095 ARG GLY GLY GLN VAL SER VAL CYS PRO LEU PRO ARG GLY
SEQRES 38 G 1095 TRP ARG ARG TRP TRP CYS ASP ALA VAL LEU TYR GLY GLU
SEQRES 39 G 1095 GLN GLY HIS PRO TRP GLY ARG PHE GLY ALA ALA LEU THR
SEQRES 40 G 1095 VAL LEU GLY ASP VAL ASN GLY ASP LYS LEU THR ASP VAL
SEQRES 41 G 1095 VAL ILE GLY ALA PRO GLY GLU GLU GLU ASN ARG GLY ALA
SEQRES 42 G 1095 VAL TYR LEU PHE HIS GLY VAL LEU GLY PRO SER ILE SER
SEQRES 43 G 1095 PRO SER HIS SER GLN ARG ILE ALA GLY SER GLN LEU SER
SEQRES 44 G 1095 SER ARG LEU GLN TYR PHE GLY GLN ALA LEU SER GLY GLY
SEQRES 45 G 1095 GLN ASP LEU THR GLN ASP GLY LEU VAL ASP LEU ALA VAL
SEQRES 46 G 1095 GLY ALA ARG GLY GLN VAL LEU LEU LEU ARG THR ARG PRO
SEQRES 47 G 1095 VAL LEU TRP VAL GLY VAL SER MET GLN PHE ILE PRO ALA
SEQRES 48 G 1095 GLU ILE PRO ARG SER ALA PHE GLU CYS ARG GLU GLN VAL
SEQRES 49 G 1095 VAL SER GLU GLN THR LEU VAL GLN SER ASN ILE CYS LEU
SEQRES 50 G 1095 TYR ILE ASP LYS ARG SER LYS ASN LEU LEU GLY SER ARG
SEQRES 51 G 1095 ASP LEU GLN SER SER VAL THR LEU ASP LEU ALA LEU ASP
SEQRES 52 G 1095 PRO GLY ARG LEU SER PRO ARG ALA THR PHE GLN GLU THR
SEQRES 53 G 1095 LYS ASN ARG SER LEU SER ARG VAL ARG VAL LEU GLY LEU
SEQRES 54 G 1095 LYS ALA HIS CYS GLU ASN PHE ASN LEU LEU LEU PRO SER
SEQRES 55 G 1095 CYS VAL GLU ASP SER VAL THR PRO ILE THR LEU ARG LEU
SEQRES 56 G 1095 ASN PHE THR LEU VAL GLY LYS PRO LEU LEU ALA PHE ARG
SEQRES 57 G 1095 ASN LEU ARG PRO MET LEU ALA ALA ASP ALA GLN ARG TYR
SEQRES 58 G 1095 PHE THR ALA SER LEU PRO PHE GLU LYS ASN CYS GLY ALA
SEQRES 59 G 1095 ASP HIS ILE CYS GLN ASP ASN LEU GLY ILE SER PHE SER
SEQRES 60 G 1095 PHE PRO GLY LEU LYS SER LEU LEU VAL GLY SER ASN LEU
SEQRES 61 G 1095 GLU LEU ASN ALA GLU VAL MET VAL TRP ASN ASP GLY GLU
SEQRES 62 G 1095 ASP SER TYR GLY THR THR ILE THR PHE SER HIS PRO ALA
SEQRES 63 G 1095 GLY LEU SER TYR ARG TYR VAL ALA GLU GLY GLN LYS GLN
SEQRES 64 G 1095 GLY GLN LEU ARG SER LEU HIS LEU THR CYS ASP SER ALA
SEQRES 65 G 1095 PRO VAL GLY SER GLN GLY THR TRP SER THR SER CYS ARG
SEQRES 66 G 1095 ILE ASN HIS LEU ILE PHE ARG GLY GLY ALA GLN ILE THR
SEQRES 67 G 1095 PHE LEU ALA THR PHE ASP VAL SER PRO LYS ALA VAL LEU
SEQRES 68 G 1095 GLY ASP ARG LEU LEU LEU THR ALA ASN VAL SER SER GLU
SEQRES 69 G 1095 ASN ASN THR PRO ARG THR SER LYS THR THR PHE GLN LEU
SEQRES 70 G 1095 GLU LEU PRO VAL LYS TYR ALA VAL TYR THR VAL VAL SER
SEQRES 71 G 1095 SER HIS GLU GLN PHE THR LYS TYR LEU ASN PHE SER GLU
SEQRES 72 G 1095 SER GLU GLU LYS GLU SER HIS VAL ALA MET HIS ARG TYR
SEQRES 73 G 1095 GLN VAL ASN ASN LEU GLY GLN ARG ASP LEU PRO VAL SER
SEQRES 74 G 1095 ILE ASN PHE TRP VAL PRO VAL GLU LEU ASN GLN GLU ALA
SEQRES 75 G 1095 VAL TRP MET ASP VAL GLU VAL SER HIS PRO GLN ASN PRO
SEQRES 76 G 1095 SER LEU ARG CYS SER SER GLU LYS ILE ALA PRO PRO ALA
SEQRES 77 G 1095 SER ASP PHE LEU ALA HIS ILE GLN LYS ASN PRO VAL LEU
SEQRES 78 G 1095 ASP CYS SER ILE ALA GLY CYS LEU ARG PHE ARG CYS ASP
SEQRES 79 G 1095 VAL PRO SER PHE SER VAL GLN GLU GLU LEU ASP PHE THR
SEQRES 80 G 1095 LEU LYS GLY ASN LEU SER PHE GLY TRP VAL ARG GLN ILE
SEQRES 81 G 1095 LEU GLN LYS LYS VAL SER VAL VAL SER VAL ALA GLU ILE
SEQRES 82 G 1095 THR PHE ASP THR SER VAL TYR SER GLN LEU PRO GLY GLN
SEQRES 83 G 1095 GLU ALA PHE MET ARG ALA GLN THR THR THR VAL LEU GLU
SEQRES 84 G 1095 LYS TYR LYS VAL HIS GLY CYS GLY GLY LEU GLU ASN LEU
SEQRES 85 G 1095 TYR PHE GLN
SEQRES 1 H 687 GLN GLU CYS THR LYS PHE LYS VAL SER SER CYS ARG GLU
SEQRES 2 H 687 CYS ILE GLU SER GLY PRO GLY CYS THR TRP CYS GLN LYS
SEQRES 3 H 687 LEU ASN PHE THR GLY PRO GLY ASP PRO ASP SER ILE ARG
SEQRES 4 H 687 CYS ASP THR ARG PRO GLN LEU LEU MET ARG GLY CYS ALA
SEQRES 5 H 687 ALA ASP ASP ILE MET ASP PRO THR SER LEU ALA GLU THR
SEQRES 6 H 687 GLN GLU ASP HIS ASN GLY GLY GLN LYS GLN LEU SER PRO
SEQRES 7 H 687 GLN LYS VAL THR LEU TYR LEU ARG PRO GLY GLN ALA ALA
SEQRES 8 H 687 ALA PHE ASN VAL THR PHE ARG ARG ALA LYS GLY TYR PRO
SEQRES 9 H 687 ILE ASP LEU TYR TYR LEU MET ASP LEU SER TYR SER MET
SEQRES 10 H 687 LEU ASP ASP LEU ARG ASN VAL LYS LYS LEU GLY GLY ASP
SEQRES 11 H 687 LEU LEU ARG ALA LEU ASN GLU ILE THR GLU SER GLY ARG
SEQRES 12 H 687 ILE GLY PHE GLY SER PHE VAL ASP LYS THR VAL LEU PRO
SEQRES 13 H 687 PHE VAL ASN THR HIS PRO ASP LYS LEU ARG ASN PRO CYS
SEQRES 14 H 687 PRO ASN LYS GLU LYS GLU CYS GLN PRO PRO PHE ALA PHE
SEQRES 15 H 687 ARG HIS VAL LEU LYS LEU THR ASN ASN SER ASN GLN PHE
SEQRES 16 H 687 GLN THR GLU VAL GLY LYS GLN LEU ILE SER GLY ASN LEU
SEQRES 17 H 687 ASP ALA PRO GLU GLY GLY LEU ASP ALA MET MET GLN VAL
SEQRES 18 H 687 ALA ALA CYS PRO GLU GLU ILE GLY TRP ARG ASN VAL THR
SEQRES 19 H 687 ARG LEU LEU VAL PHE ALA THR ASP ASP GLY PHE HIS PHE
SEQRES 20 H 687 ALA GLY ASP GLY LYS LEU GLY ALA ILE LEU THR PRO ASN
SEQRES 21 H 687 ASP GLY ARG CYS HIS LEU GLU ASP ASN LEU TYR LYS ARG
SEQRES 22 H 687 SER ASN GLU PHE ASP TYR PRO SER VAL GLY GLN LEU ALA
SEQRES 23 H 687 HIS LYS LEU ALA GLU ASN ASN ILE GLN PRO ILE PHE ALA
SEQRES 24 H 687 VAL THR SER ARG MET VAL LYS THR TYR GLU LYS LEU THR
SEQRES 25 H 687 GLU ILE ILE PRO LYS SER ALA VAL GLY GLU LEU SER GLU
SEQRES 26 H 687 ASP SER SER ASN VAL VAL GLN LEU ILE LYS ASN ALA TYR
SEQRES 27 H 687 ASN LYS LEU SER SER ARG VAL PHE LEU ASP HIS ASN ALA
SEQRES 28 H 687 LEU PRO ASP THR LEU LYS VAL THR TYR ASP SER PHE CYS
SEQRES 29 H 687 SER ASN GLY VAL THR HIS ARG ASN GLN PRO ARG GLY ASP
SEQRES 30 H 687 CYS ASP GLY VAL GLN ILE ASN VAL PRO ILE THR PHE GLN
SEQRES 31 H 687 VAL LYS VAL THR ALA THR GLU CYS ILE GLN GLU GLN SER
SEQRES 32 H 687 PHE VAL ILE ARG ALA LEU GLY PHE THR ASP ILE VAL THR
SEQRES 33 H 687 VAL GLN VAL LEU PRO GLN CYS GLU CYS ARG CYS ARG ASP
SEQRES 34 H 687 GLN SER ARG ASP ARG SER LEU CYS HIS GLY LYS GLY PHE
SEQRES 35 H 687 LEU GLU CYS GLY ILE CYS ARG CYS ASP THR GLY TYR ILE
SEQRES 36 H 687 GLY LYS ASN CYS GLU CYS GLN THR GLN GLY ARG SER SER
SEQRES 37 H 687 GLN GLU LEU GLU GLY SER CYS ARG LYS ASP ASN ASN SER
SEQRES 38 H 687 ILE ILE CYS SER GLY LEU GLY ASP CYS VAL CYS GLY GLN
SEQRES 39 H 687 CYS LEU CYS HIS THR SER ASP VAL PRO GLY LYS LEU ILE
SEQRES 40 H 687 TYR GLY GLN TYR CYS GLU CYS ASP THR ILE ASN CYS GLU
SEQRES 41 H 687 ARG TYR ASN GLY GLN VAL CYS GLY GLY PRO GLY ARG GLY
SEQRES 42 H 687 LEU CYS PHE CYS GLY LYS CYS ARG CYS HIS PRO GLY PHE
SEQRES 43 H 687 GLU GLY SER ALA CYS GLN CYS GLU ARG THR THR GLU GLY
SEQRES 44 H 687 CYS LEU ASN PRO ARG ARG VAL GLU CYS SER GLY ARG GLY
SEQRES 45 H 687 ARG CYS ARG CYS ASN VAL CYS GLU CYS HIS SER GLY TYR
SEQRES 46 H 687 GLN LEU PRO LEU CYS GLN GLU CYS PRO GLY CYS PRO SER
SEQRES 47 H 687 PRO CYS GLY LYS TYR ILE SER CYS ALA GLU CYS LEU LYS
SEQRES 48 H 687 PHE GLU LYS GLY PRO PHE GLY LYS ASN CYS SER ALA ALA
SEQRES 49 H 687 CYS PRO GLY LEU GLN LEU SER ASN ASN PRO VAL LYS GLY
SEQRES 50 H 687 ARG THR CYS LYS GLU ARG ASP SER GLU GLY CYS TRP VAL
SEQRES 51 H 687 ALA TYR THR LEU GLU GLN GLN ASP GLY MET ASP ARG TYR
SEQRES 52 H 687 LEU ILE TYR VAL ASP GLU SER ARG GLU CYS VAL ALA GLY
SEQRES 53 H 687 PRO ASP GLY CYS GLY GLU ASN LEU TYR PHE GLN
MODRES 3K6S ASN A 42 ASN GLYCOSYLATION SITE
MODRES 3K6S ASN A 373 ASN GLYCOSYLATION SITE
MODRES 3K6S ASN A 678 ASN GLYCOSYLATION SITE
MODRES 3K6S ASN A 716 ASN GLYCOSYLATION SITE
MODRES 3K6S ASN A 880 ASN GLYCOSYLATION SITE
MODRES 3K6S ASN B 94 ASN GLYCOSYLATION SITE
MODRES 3K6S ASN C 42 ASN GLYCOSYLATION SITE
MODRES 3K6S ASN C 373 ASN GLYCOSYLATION SITE
MODRES 3K6S ASN C 678 ASN GLYCOSYLATION SITE
MODRES 3K6S ASN C 716 ASN GLYCOSYLATION SITE
MODRES 3K6S ASN C 880 ASN GLYCOSYLATION SITE
MODRES 3K6S ASN D 94 ASN GLYCOSYLATION SITE
MODRES 3K6S ASN E 42 ASN GLYCOSYLATION SITE
MODRES 3K6S ASN E 373 ASN GLYCOSYLATION SITE
MODRES 3K6S ASN E 678 ASN GLYCOSYLATION SITE
MODRES 3K6S ASN E 716 ASN GLYCOSYLATION SITE
MODRES 3K6S ASN E 880 ASN GLYCOSYLATION SITE
MODRES 3K6S ASN F 94 ASN GLYCOSYLATION SITE
MODRES 3K6S ASN G 42 ASN GLYCOSYLATION SITE
MODRES 3K6S ASN G 373 ASN GLYCOSYLATION SITE
MODRES 3K6S ASN G 678 ASN GLYCOSYLATION SITE
MODRES 3K6S ASN G 716 ASN GLYCOSYLATION SITE
MODRES 3K6S ASN G 880 ASN GLYCOSYLATION SITE
MODRES 3K6S ASN H 94 ASN GLYCOSYLATION SITE
HET NAG I 1 14
HET NAG I 2 14
HET NAG J 1 14
HET NAG J 2 14
HET MAN J 3 11
HET MAN J 4 11
HET MAN J 5 11
HET NAG K 1 14
HET NAG K 2 14
HET NAG L 1 14
HET NAG L 2 14
HET NAG M 1 14
HET NAG M 2 14
HET NAG N 1 14
HET NAG N 2 14
HET NAG O 1 14
HET NAG O 2 14
HET NAG P 1 14
HET NAG P 2 14
HET MAN P 3 11
HET NAG Q 1 14
HET NAG Q 2 14
HET NAG R 1 14
HET NAG R 2 14
HET NAG S 1 14
HET NAG S 2 14
HET MAN S 3 11
HET NAG T 1 14
HET NAG T 2 14
HET MAN A3378 11
HET NAG A3678 14
HET NAG A3880 14
HET CA A2005 1
HET CA A2006 1
HET CA A2007 1
HET MG A2009 1
HET NAG B3094 14
HET CA B2002 1
HET NAG C3678 14
HET NAG C3880 14
HET CA C2005 1
HET CA C2006 1
HET CA C2007 1
HET NAG D3094 14
HET CA D2002 1
HET NAG E3678 14
HET NAG E3880 14
HET CA E2005 1
HET CA E2006 1
HET CA E2007 1
HET NAG F3094 14
HET CA F2002 1
HET NAG G3678 14
HET NAG G3880 14
HET CA G2005 1
HET CA G2006 1
HET CA G2007 1
HET NAG H3094 14
HET CA H2002 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM CA CALCIUM ION
HETNAM MG MAGNESIUM ION
FORMUL 9 NAG 36(C8 H15 N O6)
FORMUL 10 MAN 6(C6 H12 O6)
FORMUL 24 CA 16(CA 2+)
FORMUL 27 MG MG 2+
FORMUL 51 HOH *3(H2 O)
HELIX 1 1 SER A 145 GLN A 161 1 17
HELIX 2 2 PHE A 184 ARG A 189 1 6
HELIX 3 3 ASN A 192 LEU A 197 5 6
HELIX 4 4 TYR A 208 HIS A 218 1 11
HELIX 5 5 ASP A 249 GLY A 261 1 13
HELIX 6 6 LEU A 271 ASN A 275 5 5
HELIX 7 7 TRP A 279 ASP A 284 1 6
HELIX 8 8 PHE A 300 ASP A 305 5 6
HELIX 9 9 GLN A 309 ALA A 316 1 8
HELIX 10 10 ARG A 407 THR A 411 5 5
HELIX 11 11 ASP A 990 ASN A 998 1 9
HELIX 12 12 PHE A 1034 GLN A 1039 5 6
HELIX 13 13 SER B 10 GLU B 16 1 7
HELIX 14 14 ASP B 36 ILE B 38 5 3
HELIX 15 15 THR B 42 GLY B 50 1 9
HELIX 16 16 MET B 117 ASN B 123 1 7
HELIX 17 17 ASP B 130 GLU B 137 1 8
HELIX 18 18 SER B 192 LYS B 201 1 10
HELIX 19 19 GLY B 213 ALA B 222 1 10
HELIX 20 20 CYS B 224 GLY B 229 1 6
HELIX 21 21 GLY B 249 ALA B 255 5 7
HELIX 22 22 ARG B 273 PHE B 277 5 5
HELIX 23 23 SER B 281 GLY B 283 5 3
HELIX 24 24 GLN B 284 ASN B 292 1 9
HELIX 25 25 THR B 301 ARG B 303 5 3
HELIX 26 26 MET B 304 ILE B 315 1 12
HELIX 27 27 VAL B 330 ILE B 334 5 5
HELIX 28 28 ASN B 336 SER B 342 1 7
HELIX 29 29 LEU B 436 GLY B 439 5 4
HELIX 30 30 GLN B 469 GLY B 473 5 5
HELIX 31 31 ILE B 482 GLY B 486 5 5
HELIX 32 32 GLY B 528 ARG B 532 1 5
HELIX 33 33 TYR B 603 GLU B 608 1 6
HELIX 34 34 ARG C 407 THR C 411 5 5
HELIX 35 35 ASP C 990 ASN C 998 1 9
HELIX 36 36 PHE C 1034 GLN C 1039 5 6
HELIX 37 37 SER D 10 GLU D 16 1 7
HELIX 38 38 ASP D 36 ILE D 38 5 3
HELIX 39 39 THR D 42 GLY D 50 1 9
HELIX 40 40 MET D 117 ASN D 123 1 7
HELIX 41 41 ASP D 130 GLU D 137 1 8
HELIX 42 42 SER D 192 LYS D 201 1 10
HELIX 43 43 GLY D 213 ALA D 222 1 10
HELIX 44 44 CYS D 224 GLY D 229 1 6
HELIX 45 45 GLY D 249 ALA D 255 5 7
HELIX 46 46 ARG D 273 PHE D 277 5 5
HELIX 47 47 SER D 281 GLY D 283 5 3
HELIX 48 48 GLN D 284 ASN D 292 1 9
HELIX 49 49 THR D 301 ARG D 303 5 3
HELIX 50 50 MET D 304 ILE D 315 1 12
HELIX 51 51 VAL D 330 ILE D 334 5 5
HELIX 52 52 ASN D 336 SER D 342 1 7
HELIX 53 53 LEU D 436 GLY D 439 5 4
HELIX 54 54 GLN D 469 GLY D 473 5 5
HELIX 55 55 ILE D 482 GLY D 486 5 5
HELIX 56 56 GLY D 528 ARG D 532 1 5
HELIX 57 57 TYR D 603 GLU D 608 1 6
HELIX 58 58 ARG E 407 THR E 411 5 5
HELIX 59 59 ASP E 990 ASN E 998 1 9
HELIX 60 60 PHE E 1034 GLN E 1039 5 6
HELIX 61 61 SER F 10 GLU F 16 1 7
HELIX 62 62 ASP F 36 ILE F 38 5 3
HELIX 63 63 THR F 42 GLY F 50 1 9
HELIX 64 64 MET F 117 ASN F 123 1 7
HELIX 65 65 ASP F 130 GLU F 137 1 8
HELIX 66 66 SER F 192 LYS F 201 1 10
HELIX 67 67 GLY F 213 ALA F 222 1 10
HELIX 68 68 CYS F 224 GLY F 229 1 6
HELIX 69 69 GLY F 249 ALA F 255 5 7
HELIX 70 70 ARG F 273 PHE F 277 5 5
HELIX 71 71 SER F 281 GLY F 283 5 3
HELIX 72 72 GLN F 284 ASN F 292 1 9
HELIX 73 73 THR F 301 ARG F 303 5 3
HELIX 74 74 MET F 304 ILE F 315 1 12
HELIX 75 75 VAL F 330 ILE F 334 5 5
HELIX 76 76 ASN F 336 SER F 342 1 7
HELIX 77 77 LEU F 436 GLY F 439 5 4
HELIX 78 78 GLN F 469 GLY F 473 5 5
HELIX 79 79 ILE F 482 GLY F 486 5 5
HELIX 80 80 GLY F 528 ARG F 532 1 5
HELIX 81 81 TYR F 603 GLU F 608 1 6
HELIX 82 82 ARG G 407 THR G 411 5 5
HELIX 83 83 ASP G 990 ASN G 998 1 9
HELIX 84 84 PHE G 1034 GLN G 1039 5 6
HELIX 85 85 SER H 10 GLU H 16 1 7
HELIX 86 86 ASP H 36 ILE H 38 5 3
HELIX 87 87 THR H 42 GLY H 50 1 9
HELIX 88 88 MET H 117 ASN H 123 1 7
HELIX 89 89 ASP H 130 GLU H 137 1 8
HELIX 90 90 SER H 192 LYS H 201 1 10
HELIX 91 91 GLY H 213 ALA H 222 1 10
HELIX 92 92 CYS H 224 GLY H 229 1 6
HELIX 93 93 GLY H 249 ALA H 255 5 7
HELIX 94 94 ARG H 273 PHE H 277 5 5
HELIX 95 95 SER H 281 GLY H 283 5 3
HELIX 96 96 GLN H 284 ASN H 292 1 9
HELIX 97 97 THR H 301 ARG H 303 5 3
HELIX 98 98 MET H 304 ILE H 315 1 12
HELIX 99 99 VAL H 330 ILE H 334 5 5
HELIX 100 100 ASN H 336 SER H 342 1 7
HELIX 101 101 LEU H 436 GLY H 439 5 4
HELIX 102 102 GLN H 469 GLY H 473 5 5
HELIX 103 103 ILE H 482 GLY H 486 5 5
HELIX 104 104 GLY H 528 ARG H 532 1 5
HELIX 105 105 TYR H 603 GLU H 608 1 6
SHEET 1 A 4 THR A 9 PHE A 11 0
SHEET 2 A 4 VAL A 591 ARG A 595 -1 O VAL A 591 N PHE A 11
SHEET 3 A 4 ASP A 582 ALA A 587 -1 N VAL A 585 O LEU A 592
SHEET 4 A 4 PHE A 565 GLY A 571 -1 N GLY A 566 O GLY A 586
SHEET 1 B 4 SER A 21 GLN A 24 0
SHEET 2 B 4 TRP A 29 GLY A 33 -1 O VAL A 31 N VAL A 23
SHEET 3 B 4 LEU A 47 GLY A 51 -1 O TYR A 48 N VAL A 32
SHEET 4 B 4 ALA A 56 PRO A 59 -1 O GLU A 58 N GLN A 49
SHEET 1 C 3 SER A 76 THR A 80 0
SHEET 2 C 3 GLN A 85 GLY A 90 -1 O GLN A 85 N THR A 80
SHEET 3 C 3 LEU A 106 LEU A 110 -1 O LEU A 106 N GLY A 90
SHEET 1 D 2 HIS A 94 HIS A 95 0
SHEET 2 D 2 TYR A 102 LEU A 103 -1 O TYR A 102 N HIS A 95
SHEET 1 E 5 PHE A 178 PHE A 182 0
SHEET 2 E 5 THR A 167 PHE A 174 -1 N GLN A 173 O GLN A 179
SHEET 3 E 5 GLN A 131 ASP A 138 1 N ILE A 137 O PHE A 174
SHEET 4 E 5 ALA A 232 THR A 239 1 O ILE A 238 N ASP A 138
SHEET 5 E 5 ILE A 262 ARG A 264 1 O ILE A 263 N LEU A 235
SHEET 1 F 5 PHE A 178 PHE A 182 0
SHEET 2 F 5 THR A 167 PHE A 174 -1 N GLN A 173 O GLN A 179
SHEET 3 F 5 GLN A 131 ASP A 138 1 N ILE A 137 O PHE A 174
SHEET 4 F 5 ALA A 232 THR A 239 1 O ILE A 238 N ASP A 138
SHEET 5 F 5 ILE A 267 GLY A 268 1 O ILE A 267 N VAL A 237
SHEET 1 G 4 ALA A 339 VAL A 340 0
SHEET 2 G 4 VAL A 347 ALA A 350 -1 O VAL A 347 N VAL A 340
SHEET 3 G 4 GLY A 359 LEU A 362 -1 O GLY A 359 N ALA A 350
SHEET 4 G 4 THR A 370 ILE A 372 -1 O THR A 370 N LEU A 362
SHEET 1 H 4 THR A 390 GLU A 391 0
SHEET 2 H 4 SER A 400 ALA A 405 -1 O VAL A 402 N GLU A 391
SHEET 3 H 4 LYS A 413 THR A 418 -1 O LYS A 413 N ALA A 405
SHEET 4 H 4 MET A 426 VAL A 430 -1 O ALA A 428 N ILE A 416
SHEET 1 I 3 LEU A 443 VAL A 446 0
SHEET 2 I 3 LEU A 456 GLY A 460 -1 O LEU A 458 N CYS A 444
SHEET 3 I 3 VAL A 473 PRO A 477 -1 O CYS A 476 N VAL A 457
SHEET 1 J 3 LEU A 506 GLY A 510 0
SHEET 2 J 3 ASP A 519 GLY A 523 -1 O ASP A 519 N GLY A 510
SHEET 3 J 3 VAL A 534 HIS A 538 -1 O TYR A 535 N ILE A 522
SHEET 1 K 4 VAL A 602 PHE A 608 0
SHEET 2 K 4 THR A 629 ILE A 639 -1 O TYR A 638 N GLY A 603
SHEET 3 K 4 HIS A 692 LEU A 700 -1 O PHE A 696 N SER A 633
SHEET 4 K 4 THR A 672 PHE A 673 -1 N THR A 672 O LEU A 699
SHEET 1 L 4 SER A 680 LEU A 687 0
SHEET 2 L 4 SER A 654 LEU A 662 -1 N LEU A 660 O LEU A 681
SHEET 3 L 4 ILE A 711 PHE A 717 -1 O ASN A 716 N ASP A 659
SHEET 4 L 4 PHE A 742 LEU A 746 -1 O ALA A 744 N LEU A 713
SHEET 1 M 4 ILE A 764 SER A 767 0
SHEET 2 M 4 GLU A 781 VAL A 788 -1 O MET A 787 N SER A 765
SHEET 3 M 4 ILE A 857 VAL A 865 -1 O ALA A 861 N ALA A 784
SHEET 4 M 4 LEU A 808 ARG A 811 -1 N ARG A 811 O THR A 862
SHEET 1 N 3 LEU A 775 VAL A 776 0
SHEET 2 N 3 LYS A 902 VAL A 905 1 O ALA A 904 N VAL A 776
SHEET 3 N 3 TYR A1060 GLN A1062 1 O SER A1061 N TYR A 903
SHEET 1 O10 THR A 828 PRO A 833 0
SHEET 2 O10 TRP A 840 ARG A 845 -1 O SER A 843 N ASP A 830
SHEET 3 O10 THR A 799 HIS A 804 -1 N HIS A 804 O TRP A 840
SHEET 4 O10 ARG A 874 SER A 882 -1 O ASN A 880 N THR A 801
SHEET 5 O10 GLN A 896 PRO A 900 -1 O LEU A 899 N LEU A 875
SHEET 6 O10 GLN C 896 PRO C 900 -1 O GLU C 898 N GLN A 896
SHEET 7 O10 ARG C 874 SER C 882 -1 N LEU C 875 O LEU C 899
SHEET 8 O10 THR C 799 HIS C 804 -1 N THR C 801 O ASN C 880
SHEET 9 O10 TRP C 840 ARG C 845 -1 O TRP C 840 N HIS C 804
SHEET 10 O10 THR C 828 PRO C 833 -1 N THR C 828 O ARG C 845
SHEET 1 P 4 VAL A 908 SER A 911 0
SHEET 2 P 4 ALA A 932 ASN A 939 -1 O GLN A 937 N SER A 910
SHEET 3 P 4 ASP A1025 GLY A1030 -1 O LEU A1028 N HIS A 934
SHEET 4 P 4 GLU A 968 SER A 970 -1 N GLU A 968 O LYS A1029
SHEET 1 Q 5 CYS A 979 ILE A 984 0
SHEET 2 Q 5 CYS A1008 PHE A1018 -1 O ARG A1010 N GLU A 982
SHEET 3 Q 5 LEU A 946 TRP A 953 -1 N ILE A 950 O CYS A1013
SHEET 4 Q 5 VAL A1045 THR A1054 -1 O THR A1054 N SER A 949
SHEET 5 Q 5 VAL A1000 LEU A1001 1 N LEU A1001 O VAL A1048
SHEET 1 R 5 CYS A 979 ILE A 984 0
SHEET 2 R 5 CYS A1008 PHE A1018 -1 O ARG A1010 N GLU A 982
SHEET 3 R 5 LEU A 946 TRP A 953 -1 N ILE A 950 O CYS A1013
SHEET 4 R 5 VAL A1045 THR A1054 -1 O THR A1054 N SER A 949
SHEET 5 R 5 ARG A1071 LEU A1078 -1 O LEU A1078 N VAL A1045
SHEET 1 S 3 CYS B 40 ASP B 41 0
SHEET 2 S 3 THR B 22 CYS B 24 -1 N THR B 22 O ASP B 41
SHEET 3 S 3 ILE B 56 MET B 57 -1 O MET B 57 N TRP B 23
SHEET 1 T 3 THR B 82 LEU B 85 0
SHEET 2 T 3 THR B 416 PRO B 421 1 O LEU B 420 N LEU B 83
SHEET 3 T 3 GLN B 402 VAL B 405 -1 N GLN B 402 O VAL B 419
SHEET 1 U 3 ALA B 91 PHE B 97 0
SHEET 2 U 3 ILE B 387 ALA B 395 -1 O VAL B 393 N ALA B 91
SHEET 3 U 3 LEU B 356 THR B 359 -1 N LYS B 357 O THR B 394
SHEET 1 V 4 ARG B 183 THR B 189 0
SHEET 2 V 4 ARG B 143 PHE B 149 -1 N SER B 148 O ARG B 183
SHEET 3 V 4 ASP B 106 ASP B 112 1 N TYR B 109 O GLY B 145
SHEET 4 V 4 LEU B 236 ALA B 240 1 O ALA B 240 N ASP B 112
SHEET 1 W 2 PHE B 298 VAL B 300 0
SHEET 2 W 2 VAL B 320 GLU B 322 1 O GLY B 321 N VAL B 300
SHEET 1 X 2 GLY B 441 LEU B 443 0
SHEET 2 X 2 CYS B 448 CYS B 450 -1 O ARG B 449 N PHE B 442
SHEET 1 Y 2 TYR B 454 ILE B 455 0
SHEET 2 Y 2 CYS B 461 GLN B 462 -1 O CYS B 461 N ILE B 455
SHEET 1 Z 2 GLY B 488 VAL B 491 0
SHEET 2 Z 2 GLN B 494 CYS B 497 -1 O GLN B 494 N VAL B 491
SHEET 1 AA 2 ILE B 507 TYR B 508 0
SHEET 2 AA 2 CYS B 514 ASP B 515 -1 O CYS B 514 N TYR B 508
SHEET 1 AB 2 ARG B 521 TYR B 522 0
SHEET 2 AB 2 GLN B 525 VAL B 526 -1 O GLN B 525 N TYR B 522
SHEET 1 AC 2 GLY B 533 PHE B 536 0
SHEET 2 AC 2 LYS B 539 CYS B 542 -1 O LYS B 539 N PHE B 536
SHEET 1 AD 3 CYS B 640 ARG B 643 0
SHEET 2 AD 3 TRP B 649 LEU B 654 -1 O TYR B 652 N CYS B 640
SHEET 3 AD 3 ILE B 665 VAL B 667 -1 O TYR B 666 N THR B 653
SHEET 1 AE 4 THR C 9 PHE C 11 0
SHEET 2 AE 4 VAL C 591 ARG C 595 -1 O VAL C 591 N PHE C 11
SHEET 3 AE 4 ASP C 582 ALA C 587 -1 N VAL C 585 O LEU C 592
SHEET 4 AE 4 PHE C 565 GLY C 571 -1 N GLY C 566 O GLY C 586
SHEET 1 AF 4 SER C 21 GLN C 24 0
SHEET 2 AF 4 TRP C 29 GLY C 33 -1 O VAL C 31 N VAL C 23
SHEET 3 AF 4 LEU C 47 GLY C 51 -1 O TYR C 48 N VAL C 32
SHEET 4 AF 4 ALA C 56 PRO C 59 -1 O GLU C 58 N GLN C 49
SHEET 1 AG 3 SER C 76 THR C 80 0
SHEET 2 AG 3 GLN C 85 GLY C 90 -1 O GLN C 85 N THR C 80
SHEET 3 AG 3 LEU C 106 LEU C 110 -1 O LEU C 106 N GLY C 90
SHEET 1 AH 2 HIS C 94 HIS C 95 0
SHEET 2 AH 2 TYR C 102 LEU C 103 -1 O TYR C 102 N HIS C 95
SHEET 1 AI 4 ALA C 339 VAL C 340 0
SHEET 2 AI 4 VAL C 347 ALA C 350 -1 O VAL C 347 N VAL C 340
SHEET 3 AI 4 GLY C 359 LEU C 362 -1 O GLY C 359 N ALA C 350
SHEET 4 AI 4 THR C 370 ILE C 372 -1 O THR C 370 N LEU C 362
SHEET 1 AJ 4 THR C 390 GLU C 391 0
SHEET 2 AJ 4 SER C 400 ALA C 405 -1 O VAL C 402 N GLU C 391
SHEET 3 AJ 4 LYS C 413 THR C 418 -1 O LYS C 413 N ALA C 405
SHEET 4 AJ 4 MET C 426 VAL C 430 -1 O ALA C 428 N ILE C 416
SHEET 1 AK 3 LEU C 443 VAL C 446 0
SHEET 2 AK 3 LEU C 456 GLY C 460 -1 O LEU C 458 N CYS C 444
SHEET 3 AK 3 VAL C 473 PRO C 477 -1 O CYS C 476 N VAL C 457
SHEET 1 AL 3 LEU C 506 GLY C 510 0
SHEET 2 AL 3 ASP C 519 GLY C 523 -1 O ASP C 519 N GLY C 510
SHEET 3 AL 3 VAL C 534 HIS C 538 -1 O TYR C 535 N ILE C 522
SHEET 1 AM 4 VAL C 602 PHE C 608 0
SHEET 2 AM 4 THR C 629 ILE C 639 -1 O TYR C 638 N GLY C 603
SHEET 3 AM 4 HIS C 692 LEU C 700 -1 O LEU C 698 N VAL C 631
SHEET 4 AM 4 THR C 672 PHE C 673 -1 N THR C 672 O LEU C 699
SHEET 1 AN 4 SER C 680 LEU C 687 0
SHEET 2 AN 4 SER C 654 LEU C 662 -1 N LEU C 660 O LEU C 681
SHEET 3 AN 4 ILE C 711 PHE C 717 -1 O ASN C 716 N ASP C 659
SHEET 4 AN 4 PHE C 742 LEU C 746 -1 O ALA C 744 N LEU C 713
SHEET 1 AO 4 ILE C 764 SER C 767 0
SHEET 2 AO 4 GLU C 781 VAL C 788 -1 O MET C 787 N SER C 765
SHEET 3 AO 4 ILE C 857 VAL C 865 -1 O ALA C 861 N ALA C 784
SHEET 4 AO 4 LEU C 808 ARG C 811 -1 N ARG C 811 O THR C 862
SHEET 1 AP 3 LEU C 775 VAL C 776 0
SHEET 2 AP 3 LYS C 902 VAL C 905 1 O ALA C 904 N VAL C 776
SHEET 3 AP 3 TYR C1060 GLN C1062 1 O SER C1061 N TYR C 903
SHEET 1 AQ 4 VAL C 908 SER C 911 0
SHEET 2 AQ 4 ALA C 932 ASN C 939 -1 O GLN C 937 N SER C 910
SHEET 3 AQ 4 ASP C1025 GLY C1030 -1 O LEU C1028 N HIS C 934
SHEET 4 AQ 4 GLU C 968 SER C 970 -1 N GLU C 968 O LYS C1029
SHEET 1 AR 5 CYS C 979 ILE C 984 0
SHEET 2 AR 5 CYS C1008 PHE C1018 -1 O ARG C1010 N GLU C 982
SHEET 3 AR 5 LEU C 946 TRP C 953 -1 N ILE C 950 O CYS C1013
SHEET 4 AR 5 VAL C1045 THR C1054 -1 O THR C1054 N SER C 949
SHEET 5 AR 5 VAL C1000 LEU C1001 1 N LEU C1001 O VAL C1048
SHEET 1 AS 5 CYS C 979 ILE C 984 0
SHEET 2 AS 5 CYS C1008 PHE C1018 -1 O ARG C1010 N GLU C 982
SHEET 3 AS 5 LEU C 946 TRP C 953 -1 N ILE C 950 O CYS C1013
SHEET 4 AS 5 VAL C1045 THR C1054 -1 O THR C1054 N SER C 949
SHEET 5 AS 5 ARG C1071 LEU C1078 -1 O LEU C1078 N VAL C1045
SHEET 1 AT 3 CYS D 40 ASP D 41 0
SHEET 2 AT 3 THR D 22 CYS D 24 -1 N THR D 22 O ASP D 41
SHEET 3 AT 3 ILE D 56 MET D 57 -1 O MET D 57 N TRP D 23
SHEET 1 AU 3 LEU D 83 LEU D 85 0
SHEET 2 AU 3 THR D 416 PRO D 421 1 O LEU D 420 N LEU D 83
SHEET 3 AU 3 GLN D 402 VAL D 405 -1 N GLN D 402 O VAL D 419
SHEET 1 AV 3 ALA D 91 PHE D 97 0
SHEET 2 AV 3 ILE D 387 ALA D 395 -1 O VAL D 393 N ALA D 91
SHEET 3 AV 3 LEU D 356 THR D 359 -1 N LYS D 357 O THR D 394
SHEET 1 AW 4 ARG D 183 THR D 189 0
SHEET 2 AW 4 ARG D 143 PHE D 149 -1 N SER D 148 O ARG D 183
SHEET 3 AW 4 ASP D 106 ASP D 112 1 N TYR D 109 O GLY D 145
SHEET 4 AW 4 LEU D 236 ALA D 240 1 O ALA D 240 N ASP D 112
SHEET 1 AX 2 PHE D 298 VAL D 300 0
SHEET 2 AX 2 VAL D 320 GLU D 322 1 O GLY D 321 N VAL D 300
SHEET 1 AY 2 GLY D 441 LEU D 443 0
SHEET 2 AY 2 CYS D 448 CYS D 450 -1 O ARG D 449 N PHE D 442
SHEET 1 AZ 2 TYR D 454 ILE D 455 0
SHEET 2 AZ 2 CYS D 461 GLN D 462 -1 O CYS D 461 N ILE D 455
SHEET 1 BA 2 GLY D 488 VAL D 491 0
SHEET 2 BA 2 GLN D 494 CYS D 497 -1 O GLN D 494 N VAL D 491
SHEET 1 BB 2 ARG D 521 TYR D 522 0
SHEET 2 BB 2 GLN D 525 VAL D 526 -1 O GLN D 525 N TYR D 522
SHEET 1 BC 2 GLY D 533 PHE D 536 0
SHEET 2 BC 2 LYS D 539 CYS D 542 -1 O LYS D 539 N PHE D 536
SHEET 1 BD 3 CYS D 640 ARG D 643 0
SHEET 2 BD 3 TRP D 649 LEU D 654 -1 O TYR D 652 N CYS D 640
SHEET 3 BD 3 ILE D 665 VAL D 667 -1 O TYR D 666 N THR D 653
SHEET 1 BE 4 THR E 9 PHE E 11 0
SHEET 2 BE 4 VAL E 591 ARG E 595 -1 O VAL E 591 N PHE E 11
SHEET 3 BE 4 ASP E 582 ALA E 587 -1 N VAL E 585 O LEU E 592
SHEET 4 BE 4 PHE E 565 GLY E 571 -1 N GLY E 566 O GLY E 586
SHEET 1 BF 4 SER E 21 GLN E 24 0
SHEET 2 BF 4 TRP E 29 GLY E 33 -1 O VAL E 31 N VAL E 23
SHEET 3 BF 4 LEU E 47 GLY E 51 -1 O TYR E 48 N VAL E 32
SHEET 4 BF 4 ALA E 56 PRO E 59 -1 O GLU E 58 N GLN E 49
SHEET 1 BG 3 SER E 76 THR E 80 0
SHEET 2 BG 3 GLN E 85 GLY E 90 -1 O GLN E 85 N THR E 80
SHEET 3 BG 3 LEU E 106 LEU E 110 -1 O LEU E 106 N GLY E 90
SHEET 1 BH 2 HIS E 94 HIS E 95 0
SHEET 2 BH 2 TYR E 102 LEU E 103 -1 O TYR E 102 N HIS E 95
SHEET 1 BI 4 ALA E 339 VAL E 340 0
SHEET 2 BI 4 VAL E 347 ALA E 350 -1 O VAL E 347 N VAL E 340
SHEET 3 BI 4 GLY E 359 LEU E 362 -1 O GLY E 359 N ALA E 350
SHEET 4 BI 4 THR E 370 ILE E 372 -1 O THR E 370 N LEU E 362
SHEET 1 BJ 4 THR E 390 GLU E 391 0
SHEET 2 BJ 4 SER E 400 ALA E 405 -1 O VAL E 402 N GLU E 391
SHEET 3 BJ 4 LYS E 413 THR E 418 -1 O LYS E 413 N ALA E 405
SHEET 4 BJ 4 MET E 426 VAL E 430 -1 O ALA E 428 N ILE E 416
SHEET 1 BK 3 LEU E 443 VAL E 446 0
SHEET 2 BK 3 LEU E 456 GLY E 460 -1 O LEU E 458 N CYS E 444
SHEET 3 BK 3 VAL E 473 PRO E 477 -1 O CYS E 476 N VAL E 457
SHEET 1 BL 3 LEU E 506 GLY E 510 0
SHEET 2 BL 3 ASP E 519 GLY E 523 -1 O ASP E 519 N GLY E 510
SHEET 3 BL 3 VAL E 534 HIS E 538 -1 O TYR E 535 N ILE E 522
SHEET 1 BM 4 VAL E 602 PHE E 608 0
SHEET 2 BM 4 THR E 629 ILE E 639 -1 O TYR E 638 N GLY E 603
SHEET 3 BM 4 HIS E 692 LEU E 700 -1 O PHE E 696 N SER E 633
SHEET 4 BM 4 THR E 672 PHE E 673 -1 N THR E 672 O LEU E 699
SHEET 1 BN 4 SER E 680 LEU E 687 0
SHEET 2 BN 4 SER E 654 LEU E 662 -1 N LEU E 660 O LEU E 681
SHEET 3 BN 4 ILE E 711 PHE E 717 -1 O ASN E 716 N ASP E 659
SHEET 4 BN 4 PHE E 742 LEU E 746 -1 O ALA E 744 N LEU E 713
SHEET 1 BO 4 ILE E 764 SER E 767 0
SHEET 2 BO 4 GLU E 781 VAL E 788 -1 O MET E 787 N SER E 765
SHEET 3 BO 4 ILE E 857 VAL E 865 -1 O ALA E 861 N ALA E 784
SHEET 4 BO 4 LEU E 808 ARG E 811 -1 N ARG E 811 O THR E 862
SHEET 1 BP 3 LEU E 775 VAL E 776 0
SHEET 2 BP 3 LYS E 902 VAL E 905 1 O ALA E 904 N VAL E 776
SHEET 3 BP 3 TYR E1060 GLN E1062 1 O SER E1061 N TYR E 903
SHEET 1 BQ10 THR E 828 PRO E 833 0
SHEET 2 BQ10 TRP E 840 ARG E 845 -1 O ARG E 845 N THR E 828
SHEET 3 BQ10 THR E 799 HIS E 804 -1 N HIS E 804 O TRP E 840
SHEET 4 BQ10 ARG E 874 SER E 882 -1 O ASN E 880 N THR E 801
SHEET 5 BQ10 GLN E 896 PRO E 900 -1 O LEU E 899 N LEU E 875
SHEET 6 BQ10 GLN G 896 PRO G 900 -1 O GLN G 896 N GLU E 898
SHEET 7 BQ10 ARG G 874 SER G 882 -1 N LEU G 875 O LEU G 899
SHEET 8 BQ10 THR G 799 HIS G 804 -1 N THR G 801 O ASN G 880
SHEET 9 BQ10 TRP G 840 ARG G 845 -1 O TRP G 840 N HIS G 804
SHEET 10 BQ10 THR G 828 PRO G 833 -1 N ASP G 830 O SER G 843
SHEET 1 BR 4 VAL E 908 SER E 911 0
SHEET 2 BR 4 ALA E 932 ASN E 939 -1 O GLN E 937 N SER E 910
SHEET 3 BR 4 ASP E1025 GLY E1030 -1 O LEU E1028 N HIS E 934
SHEET 4 BR 4 GLU E 968 SER E 970 -1 N GLU E 968 O LYS E1029
SHEET 1 BS 5 CYS E 979 ILE E 984 0
SHEET 2 BS 5 CYS E1008 PHE E1018 -1 O ARG E1010 N GLU E 982
SHEET 3 BS 5 LEU E 946 TRP E 953 -1 N ILE E 950 O CYS E1013
SHEET 4 BS 5 VAL E1045 THR E1054 -1 O THR E1054 N SER E 949
SHEET 5 BS 5 VAL E1000 LEU E1001 1 N LEU E1001 O VAL E1048
SHEET 1 BT 5 CYS E 979 ILE E 984 0
SHEET 2 BT 5 CYS E1008 PHE E1018 -1 O ARG E1010 N GLU E 982
SHEET 3 BT 5 LEU E 946 TRP E 953 -1 N ILE E 950 O CYS E1013
SHEET 4 BT 5 VAL E1045 THR E1054 -1 O THR E1054 N SER E 949
SHEET 5 BT 5 ARG E1071 LEU E1078 -1 O LEU E1078 N VAL E1045
SHEET 1 BU 3 CYS F 40 ASP F 41 0
SHEET 2 BU 3 THR F 22 CYS F 24 -1 N THR F 22 O ASP F 41
SHEET 3 BU 3 ILE F 56 MET F 57 -1 O MET F 57 N TRP F 23
SHEET 1 BV 3 LEU F 83 LEU F 85 0
SHEET 2 BV 3 THR F 416 PRO F 421 1 O LEU F 420 N LEU F 83
SHEET 3 BV 3 GLN F 402 VAL F 405 -1 N GLN F 402 O VAL F 419
SHEET 1 BW 3 ALA F 91 PHE F 97 0
SHEET 2 BW 3 ILE F 387 ALA F 395 -1 O VAL F 393 N ALA F 91
SHEET 3 BW 3 LEU F 356 THR F 359 -1 N LYS F 357 O THR F 394
SHEET 1 BX 4 ARG F 183 THR F 189 0
SHEET 2 BX 4 ILE F 144 PHE F 149 -1 N SER F 148 O ARG F 183
SHEET 3 BX 4 LEU F 107 ASP F 112 1 N TYR F 109 O GLY F 145
SHEET 4 BX 4 LEU F 236 ALA F 240 1 O ALA F 240 N ASP F 112
SHEET 1 BY 2 PHE F 298 VAL F 300 0
SHEET 2 BY 2 VAL F 320 GLU F 322 1 O GLY F 321 N VAL F 300
SHEET 1 BZ 2 GLY F 441 LEU F 443 0
SHEET 2 BZ 2 CYS F 448 CYS F 450 -1 O ARG F 449 N PHE F 442
SHEET 1 CA 2 TYR F 454 ILE F 455 0
SHEET 2 CA 2 CYS F 461 GLN F 462 -1 O CYS F 461 N ILE F 455
SHEET 1 CB 2 GLY F 488 VAL F 491 0
SHEET 2 CB 2 GLN F 494 CYS F 497 -1 O GLN F 494 N VAL F 491
SHEET 1 CC 2 ILE F 507 TYR F 508 0
SHEET 2 CC 2 CYS F 514 ASP F 515 -1 O CYS F 514 N TYR F 508
SHEET 1 CD 2 ARG F 521 TYR F 522 0
SHEET 2 CD 2 GLN F 525 VAL F 526 -1 O GLN F 525 N TYR F 522
SHEET 1 CE 2 GLY F 533 PHE F 536 0
SHEET 2 CE 2 LYS F 539 CYS F 542 -1 O LYS F 539 N PHE F 536
SHEET 1 CF 3 CYS F 640 ARG F 643 0
SHEET 2 CF 3 TRP F 649 LEU F 654 -1 O TYR F 652 N CYS F 640
SHEET 3 CF 3 ILE F 665 VAL F 667 -1 O TYR F 666 N THR F 653
SHEET 1 CG 4 THR G 9 PHE G 11 0
SHEET 2 CG 4 VAL G 591 ARG G 595 -1 O VAL G 591 N PHE G 11
SHEET 3 CG 4 ASP G 582 ALA G 587 -1 N VAL G 585 O LEU G 592
SHEET 4 CG 4 PHE G 565 GLY G 571 -1 N GLY G 566 O GLY G 586
SHEET 1 CH 4 SER G 21 GLN G 24 0
SHEET 2 CH 4 TRP G 29 GLY G 33 -1 O VAL G 31 N VAL G 23
SHEET 3 CH 4 LEU G 47 GLY G 51 -1 O TYR G 48 N VAL G 32
SHEET 4 CH 4 ALA G 56 PRO G 59 -1 O GLU G 58 N GLN G 49
SHEET 1 CI 3 SER G 76 THR G 80 0
SHEET 2 CI 3 GLN G 85 GLY G 90 -1 O GLN G 85 N THR G 80
SHEET 3 CI 3 LEU G 106 LEU G 110 -1 O LEU G 106 N GLY G 90
SHEET 1 CJ 2 HIS G 94 HIS G 95 0
SHEET 2 CJ 2 TYR G 102 LEU G 103 -1 O TYR G 102 N HIS G 95
SHEET 1 CK 4 ALA G 339 VAL G 340 0
SHEET 2 CK 4 VAL G 347 ALA G 350 -1 O VAL G 347 N VAL G 340
SHEET 3 CK 4 GLY G 359 LEU G 362 -1 O GLY G 359 N ALA G 350
SHEET 4 CK 4 THR G 370 ILE G 372 -1 O THR G 370 N LEU G 362
SHEET 1 CL 4 THR G 390 GLU G 391 0
SHEET 2 CL 4 SER G 400 ALA G 405 -1 O VAL G 402 N GLU G 391
SHEET 3 CL 4 LYS G 413 THR G 418 -1 O LYS G 413 N ALA G 405
SHEET 4 CL 4 MET G 426 VAL G 430 -1 O ALA G 428 N ILE G 416
SHEET 1 CM 3 LEU G 443 VAL G 446 0
SHEET 2 CM 3 LEU G 456 GLY G 460 -1 O LEU G 458 N CYS G 444
SHEET 3 CM 3 VAL G 473 PRO G 477 -1 O CYS G 476 N VAL G 457
SHEET 1 CN 3 LEU G 506 GLY G 510 0
SHEET 2 CN 3 ASP G 519 GLY G 523 -1 O ASP G 519 N GLY G 510
SHEET 3 CN 3 VAL G 534 HIS G 538 -1 O TYR G 535 N ILE G 522
SHEET 1 CO 4 VAL G 602 PHE G 608 0
SHEET 2 CO 4 THR G 629 ILE G 639 -1 O TYR G 638 N GLY G 603
SHEET 3 CO 4 HIS G 692 LEU G 700 -1 O PHE G 696 N SER G 633
SHEET 4 CO 4 THR G 672 PHE G 673 -1 N THR G 672 O LEU G 699
SHEET 1 CP 4 SER G 680 LEU G 687 0
SHEET 2 CP 4 SER G 654 LEU G 662 -1 N LEU G 660 O LEU G 681
SHEET 3 CP 4 ILE G 711 PHE G 717 -1 O ASN G 716 N ASP G 659
SHEET 4 CP 4 PHE G 742 LEU G 746 -1 O ALA G 744 N LEU G 713
SHEET 1 CQ 4 ILE G 764 SER G 767 0
SHEET 2 CQ 4 GLU G 781 VAL G 788 -1 O MET G 787 N SER G 765
SHEET 3 CQ 4 ILE G 857 VAL G 865 -1 O ALA G 861 N ALA G 784
SHEET 4 CQ 4 LEU G 808 ARG G 811 -1 N ARG G 811 O THR G 862
SHEET 1 CR 3 LEU G 775 VAL G 776 0
SHEET 2 CR 3 LYS G 902 VAL G 905 1 O ALA G 904 N VAL G 776
SHEET 3 CR 3 TYR G1060 GLN G1062 1 O SER G1061 N TYR G 903
SHEET 1 CS 4 VAL G 908 SER G 911 0
SHEET 2 CS 4 ALA G 932 ASN G 939 -1 O GLN G 937 N SER G 910
SHEET 3 CS 4 ASP G1025 GLY G1030 -1 O LEU G1028 N HIS G 934
SHEET 4 CS 4 GLU G 968 SER G 970 -1 N GLU G 968 O LYS G1029
SHEET 1 CT 5 CYS G 979 ILE G 984 0
SHEET 2 CT 5 CYS G1008 PHE G1018 -1 O ARG G1010 N GLU G 982
SHEET 3 CT 5 LEU G 946 TRP G 953 -1 N ILE G 950 O CYS G1013
SHEET 4 CT 5 VAL G1045 THR G1054 -1 O GLU G1052 N ASN G 951
SHEET 5 CT 5 VAL G1000 LEU G1001 1 N LEU G1001 O VAL G1048
SHEET 1 CU 5 CYS G 979 ILE G 984 0
SHEET 2 CU 5 CYS G1008 PHE G1018 -1 O ARG G1010 N GLU G 982
SHEET 3 CU 5 LEU G 946 TRP G 953 -1 N ILE G 950 O CYS G1013
SHEET 4 CU 5 VAL G1045 THR G1054 -1 O GLU G1052 N ASN G 951
SHEET 5 CU 5 ARG G1071 LEU G1078 -1 O LEU G1078 N VAL G1045
SHEET 1 CV 3 CYS H 40 ASP H 41 0
SHEET 2 CV 3 THR H 22 CYS H 24 -1 N THR H 22 O ASP H 41
SHEET 3 CV 3 ILE H 56 MET H 57 -1 O MET H 57 N TRP H 23
SHEET 1 CW 3 THR H 82 LEU H 85 0
SHEET 2 CW 3 THR H 416 PRO H 421 1 O LEU H 420 N LEU H 83
SHEET 3 CW 3 GLN H 402 VAL H 405 -1 N GLN H 402 O VAL H 419
SHEET 1 CX 3 ALA H 91 PHE H 97 0
SHEET 2 CX 3 ILE H 387 ALA H 395 -1 O VAL H 393 N ALA H 91
SHEET 3 CX 3 LEU H 356 THR H 359 -1 N LYS H 357 O THR H 394
SHEET 1 CY 4 ARG H 183 THR H 189 0
SHEET 2 CY 4 ARG H 143 PHE H 149 -1 N SER H 148 O ARG H 183
SHEET 3 CY 4 ASP H 106 ASP H 112 1 N TYR H 109 O GLY H 145
SHEET 4 CY 4 LEU H 236 ALA H 240 1 O ALA H 240 N ASP H 112
SHEET 1 CZ 2 PHE H 298 VAL H 300 0
SHEET 2 CZ 2 VAL H 320 GLU H 322 1 O GLY H 321 N VAL H 300
SHEET 1 DA 2 GLY H 441 LEU H 443 0
SHEET 2 DA 2 CYS H 448 CYS H 450 -1 O ARG H 449 N PHE H 442
SHEET 1 DB 2 TYR H 454 ILE H 455 0
SHEET 2 DB 2 CYS H 461 GLN H 462 -1 O CYS H 461 N ILE H 455
SHEET 1 DC 2 GLY H 488 VAL H 491 0
SHEET 2 DC 2 GLN H 494 CYS H 497 -1 O GLN H 494 N VAL H 491
SHEET 1 DD 2 ILE H 507 TYR H 508 0
SHEET 2 DD 2 CYS H 514 ASP H 515 -1 O CYS H 514 N TYR H 508
SHEET 1 DE 2 ARG H 521 TYR H 522 0
SHEET 2 DE 2 GLN H 525 VAL H 526 -1 O GLN H 525 N TYR H 522
SHEET 1 DF 2 GLY H 533 PHE H 536 0
SHEET 2 DF 2 LYS H 539 CYS H 542 -1 O LYS H 539 N PHE H 536
SHEET 1 DG 3 CYS H 640 ARG H 643 0
SHEET 2 DG 3 TRP H 649 LEU H 654 -1 O TYR H 652 N CYS H 640
SHEET 3 DG 3 ILE H 665 VAL H 667 -1 O TYR H 666 N THR H 653
SSBOND 1 CYS A 50 CYS A 57 1555 1555 2.03
SSBOND 2 CYS A 89 CYS A 107 1555 1555 2.03
SSBOND 3 CYS A 97 CYS A 126 1555 1555 2.03
SSBOND 4 CYS A 476 CYS A 487 1555 1555 2.04
SSBOND 5 CYS A 620 CYS A 703 1555 1555 2.03
SSBOND 6 CYS A 636 CYS A 693 1555 1555 2.03
SSBOND 7 CYS A 752 CYS A 758 1555 1555 2.03
SSBOND 8 CYS A 829 CYS A 844 1555 1555 2.03
SSBOND 9 CYS A 979 CYS A 1013 1555 1555 2.03
SSBOND 10 CYS A 1003 CYS A 1008 1555 1555 2.03
SSBOND 11 CYS B 3 CYS B 21 1555 1555 2.03
SSBOND 12 CYS B 11 CYS B 425 1555 1555 2.03
SSBOND 13 CYS B 14 CYS B 40 1555 1555 2.03
SSBOND 14 CYS B 24 CYS B 51 1555 1555 2.03
SSBOND 15 CYS B 169 CYS B 176 1555 1555 2.03
SSBOND 16 CYS B 224 CYS B 264 1555 1555 2.03
SSBOND 17 CYS B 364 CYS B 378 1555 1555 2.03
SSBOND 18 CYS B 398 CYS B 423 1555 1555 2.03
SSBOND 19 CYS B 427 CYS B 445 1555 1555 2.03
SSBOND 20 CYS B 437 CYS B 448 1555 1555 2.03
SSBOND 21 CYS B 450 CYS B 459 1555 1555 2.03
SSBOND 22 CYS B 461 CYS B 492 1555 1555 2.03
SSBOND 23 CYS B 475 CYS B 490 1555 1555 2.03
SSBOND 24 CYS B 484 CYS B 495 1555 1555 2.03
SSBOND 25 CYS B 497 CYS B 512 1555 1555 2.03
SSBOND 26 CYS B 514 CYS B 537 1555 1555 2.03
SSBOND 27 CYS B 519 CYS B 535 1555 1555 2.03
SSBOND 28 CYS B 527 CYS B 540 1555 1555 2.03
SSBOND 29 CYS B 542 CYS B 551 1555 1555 2.04
SSBOND 30 CYS B 553 CYS B 576 1555 1555 2.04
SSBOND 31 CYS B 560 CYS B 574 1555 1555 2.03
SSBOND 32 CYS B 568 CYS B 579 1555 1555 2.03
SSBOND 33 CYS B 581 CYS B 590 1555 1555 2.03
SSBOND 34 CYS B 593 CYS B 596 1555 1555 2.04
SSBOND 35 CYS B 600 CYS B 640 1555 1555 2.03
SSBOND 36 CYS B 606 CYS B 625 1555 1555 2.03
SSBOND 37 CYS B 609 CYS B 621 1555 1555 2.03
SSBOND 38 CYS B 648 CYS B 673 1555 1555 2.03
SSBOND 39 CYS C 50 CYS C 57 1555 1555 2.03
SSBOND 40 CYS C 89 CYS C 107 1555 1555 2.03
SSBOND 41 CYS C 97 CYS C 126 1555 1555 2.03
SSBOND 42 CYS C 476 CYS C 487 1555 1555 2.04
SSBOND 43 CYS C 620 CYS C 703 1555 1555 2.02
SSBOND 44 CYS C 636 CYS C 693 1555 1555 2.03
SSBOND 45 CYS C 752 CYS C 758 1555 1555 2.03
SSBOND 46 CYS C 829 CYS C 844 1555 1555 2.03
SSBOND 47 CYS C 979 CYS C 1013 1555 1555 2.03
SSBOND 48 CYS C 1003 CYS C 1008 1555 1555 2.03
SSBOND 49 CYS D 3 CYS D 21 1555 1555 2.03
SSBOND 50 CYS D 11 CYS D 425 1555 1555 2.02
SSBOND 51 CYS D 14 CYS D 40 1555 1555 2.03
SSBOND 52 CYS D 24 CYS D 51 1555 1555 2.03
SSBOND 53 CYS D 169 CYS D 176 1555 1555 2.03
SSBOND 54 CYS D 224 CYS D 264 1555 1555 2.03
SSBOND 55 CYS D 364 CYS D 378 1555 1555 2.03
SSBOND 56 CYS D 398 CYS D 423 1555 1555 2.03
SSBOND 57 CYS D 427 CYS D 445 1555 1555 2.03
SSBOND 58 CYS D 437 CYS D 448 1555 1555 2.03
SSBOND 59 CYS D 450 CYS D 459 1555 1555 2.03
SSBOND 60 CYS D 461 CYS D 492 1555 1555 2.02
SSBOND 61 CYS D 475 CYS D 490 1555 1555 2.03
SSBOND 62 CYS D 484 CYS D 495 1555 1555 2.03
SSBOND 63 CYS D 497 CYS D 512 1555 1555 2.04
SSBOND 64 CYS D 514 CYS D 537 1555 1555 2.03
SSBOND 65 CYS D 519 CYS D 535 1555 1555 2.03
SSBOND 66 CYS D 527 CYS D 540 1555 1555 2.03
SSBOND 67 CYS D 542 CYS D 551 1555 1555 2.04
SSBOND 68 CYS D 553 CYS D 576 1555 1555 2.03
SSBOND 69 CYS D 560 CYS D 574 1555 1555 2.03
SSBOND 70 CYS D 568 CYS D 579 1555 1555 2.03
SSBOND 71 CYS D 581 CYS D 590 1555 1555 2.03
SSBOND 72 CYS D 593 CYS D 596 1555 1555 2.05
SSBOND 73 CYS D 600 CYS D 640 1555 1555 2.03
SSBOND 74 CYS D 606 CYS D 625 1555 1555 2.03
SSBOND 75 CYS D 609 CYS D 621 1555 1555 2.03
SSBOND 76 CYS D 648 CYS D 673 1555 1555 2.03
SSBOND 77 CYS E 50 CYS E 57 1555 1555 2.03
SSBOND 78 CYS E 89 CYS E 107 1555 1555 2.03
SSBOND 79 CYS E 97 CYS E 126 1555 1555 2.03
SSBOND 80 CYS E 476 CYS E 487 1555 1555 2.04
SSBOND 81 CYS E 620 CYS E 703 1555 1555 2.02
SSBOND 82 CYS E 636 CYS E 693 1555 1555 2.03
SSBOND 83 CYS E 752 CYS E 758 1555 1555 2.03
SSBOND 84 CYS E 829 CYS E 844 1555 1555 2.03
SSBOND 85 CYS E 979 CYS E 1013 1555 1555 2.04
SSBOND 86 CYS E 1003 CYS E 1008 1555 1555 2.03
SSBOND 87 CYS F 3 CYS F 21 1555 1555 2.03
SSBOND 88 CYS F 11 CYS F 425 1555 1555 2.03
SSBOND 89 CYS F 14 CYS F 40 1555 1555 2.03
SSBOND 90 CYS F 24 CYS F 51 1555 1555 2.03
SSBOND 91 CYS F 169 CYS F 176 1555 1555 2.03
SSBOND 92 CYS F 224 CYS F 264 1555 1555 2.03
SSBOND 93 CYS F 364 CYS F 378 1555 1555 2.03
SSBOND 94 CYS F 398 CYS F 423 1555 1555 2.03
SSBOND 95 CYS F 427 CYS F 445 1555 1555 2.03
SSBOND 96 CYS F 437 CYS F 448 1555 1555 2.03
SSBOND 97 CYS F 450 CYS F 459 1555 1555 2.03
SSBOND 98 CYS F 461 CYS F 492 1555 1555 2.02
SSBOND 99 CYS F 475 CYS F 490 1555 1555 2.03
SSBOND 100 CYS F 484 CYS F 495 1555 1555 2.03
SSBOND 101 CYS F 497 CYS F 512 1555 1555 2.04
SSBOND 102 CYS F 514 CYS F 537 1555 1555 2.03
SSBOND 103 CYS F 519 CYS F 535 1555 1555 2.03
SSBOND 104 CYS F 527 CYS F 540 1555 1555 2.03
SSBOND 105 CYS F 542 CYS F 551 1555 1555 2.04
SSBOND 106 CYS F 553 CYS F 576 1555 1555 2.04
SSBOND 107 CYS F 560 CYS F 574 1555 1555 2.03
SSBOND 108 CYS F 568 CYS F 579 1555 1555 2.03
SSBOND 109 CYS F 581 CYS F 590 1555 1555 2.03
SSBOND 110 CYS F 593 CYS F 596 1555 1555 2.03
SSBOND 111 CYS F 600 CYS F 640 1555 1555 2.03
SSBOND 112 CYS F 606 CYS F 625 1555 1555 2.03
SSBOND 113 CYS F 609 CYS F 621 1555 1555 2.03
SSBOND 114 CYS F 648 CYS F 673 1555 1555 2.03
SSBOND 115 CYS G 50 CYS G 57 1555 1555 2.03
SSBOND 116 CYS G 89 CYS G 107 1555 1555 2.03
SSBOND 117 CYS G 97 CYS G 126 1555 1555 2.03
SSBOND 118 CYS G 476 CYS G 487 1555 1555 2.04
SSBOND 119 CYS G 620 CYS G 703 1555 1555 2.02
SSBOND 120 CYS G 636 CYS G 693 1555 1555 2.03
SSBOND 121 CYS G 752 CYS G 758 1555 1555 2.03
SSBOND 122 CYS G 829 CYS G 844 1555 1555 2.03
SSBOND 123 CYS G 979 CYS G 1013 1555 1555 2.03
SSBOND 124 CYS G 1003 CYS G 1008 1555 1555 2.03
SSBOND 125 CYS H 3 CYS H 21 1555 1555 2.03
SSBOND 126 CYS H 11 CYS H 425 1555 1555 2.03
SSBOND 127 CYS H 14 CYS H 40 1555 1555 2.03
SSBOND 128 CYS H 24 CYS H 51 1555 1555 2.03
SSBOND 129 CYS H 169 CYS H 176 1555 1555 2.03
SSBOND 130 CYS H 224 CYS H 264 1555 1555 2.03
SSBOND 131 CYS H 364 CYS H 378 1555 1555 2.03
SSBOND 132 CYS H 398 CYS H 423 1555 1555 2.03
SSBOND 133 CYS H 427 CYS H 445 1555 1555 2.03
SSBOND 134 CYS H 437 CYS H 448 1555 1555 2.03
SSBOND 135 CYS H 450 CYS H 459 1555 1555 2.03
SSBOND 136 CYS H 461 CYS H 492 1555 1555 2.03
SSBOND 137 CYS H 475 CYS H 490 1555 1555 2.03
SSBOND 138 CYS H 484 CYS H 495 1555 1555 2.03
SSBOND 139 CYS H 497 CYS H 512 1555 1555 2.03
SSBOND 140 CYS H 514 CYS H 537 1555 1555 2.03
SSBOND 141 CYS H 519 CYS H 535 1555 1555 2.03
SSBOND 142 CYS H 527 CYS H 540 1555 1555 2.03
SSBOND 143 CYS H 542 CYS H 551 1555 1555 2.04
SSBOND 144 CYS H 553 CYS H 576 1555 1555 2.04
SSBOND 145 CYS H 560 CYS H 574 1555 1555 2.03
SSBOND 146 CYS H 568 CYS H 579 1555 1555 2.03
SSBOND 147 CYS H 581 CYS H 590 1555 1555 2.03
SSBOND 148 CYS H 593 CYS H 596 1555 1555 2.05
SSBOND 149 CYS H 600 CYS H 640 1555 1555 2.03
SSBOND 150 CYS H 606 CYS H 625 1555 1555 2.03
SSBOND 151 CYS H 609 CYS H 621 1555 1555 2.03
SSBOND 152 CYS H 648 CYS H 673 1555 1555 2.03
LINK ND2 ASN A 42 C1 NAG I 1 1555 1555 1.44
LINK ND2 ASN A 373 C1 NAG J 1 1555 1555 1.44
LINK ND2 ASN A 678 C1 NAG A3678 1555 1555 1.44
LINK ND2 ASN A 716 C1 NAG K 1 1555 1555 1.43
LINK ND2 ASN A 880 C1 NAG A3880 1555 1555 1.45
LINK ND2 ASN B 94 C1 NAG B3094 1555 1555 1.44
LINK ND2 ASN C 42 C1 NAG L 1 1555 1555 1.44
LINK ND2 ASN C 373 C1 NAG M 1 1555 1555 1.44
LINK ND2 ASN C 678 C1 NAG C3678 1555 1555 1.44
LINK ND2 ASN C 716 C1 NAG N 1 1555 1555 1.44
LINK ND2 ASN C 880 C1 NAG C3880 1555 1555 1.45
LINK ND2 ASN D 94 C1 NAG D3094 1555 1555 1.44
LINK ND2 ASN E 42 C1 NAG O 1 1555 1555 1.44
LINK ND2 ASN E 373 C1 NAG P 1 1555 1555 1.44
LINK ND2 ASN E 678 C1 NAG E3678 1555 1555 1.44
LINK ND2 ASN E 716 C1 NAG Q 1 1555 1555 1.43
LINK ND2 ASN E 880 C1 NAG E3880 1555 1555 1.45
LINK ND2 ASN F 94 C1 NAG F3094 1555 1555 1.44
LINK ND2 ASN G 42 C1 NAG R 1 1555 1555 1.44
LINK ND2 ASN G 373 C1 NAG S 1 1555 1555 1.44
LINK ND2 ASN G 678 C1 NAG G3678 1555 1555 1.44
LINK ND2 ASN G 716 C1 NAG T 1 1555 1555 1.44
LINK ND2 ASN G 880 C1 NAG G3880 1555 1555 1.45
LINK ND2 ASN H 94 C1 NAG H3094 1555 1555 1.44
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.45
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.44
LINK O4 NAG J 2 C1 MAN J 3 1555 1555 1.45
LINK O3 MAN J 3 C1 MAN J 4 1555 1555 1.44
LINK O6 MAN J 3 C1 MAN J 5 1555 1555 1.44
LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.45
LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.45
LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.45
LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.45
LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.45
LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.44
LINK O4 NAG P 2 C1 MAN P 3 1555 1555 1.45
LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.45
LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.45
LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.44
LINK O4 NAG S 2 C1 MAN S 3 1555 1555 1.45
LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.45
LINK OG SER A 140 MG MG A2009 1555 1555 2.18
LINK OG SER A 142 MG MG A2009 1555 1555 1.82
LINK OD1 ASP A 240 MG MG A2009 1555 1555 2.20
LINK OD1 ASP A 447 CA CA A2005 1555 1555 2.91
LINK O SER A 453 CA CA A2005 1555 1555 2.85
LINK OD1 ASN A 513 CA CA A2006 1555 1555 3.00
LINK O LEU A 517 CA CA A2006 1555 1555 2.81
LINK OD1 ASP A 574 CA CA A2007 1555 1555 2.97
LINK OG1 THR A 576 CA CA A2007 1555 1555 2.70
LINK O ASP A 578 CA CA A2007 1555 1555 2.61
LINK O LEU A 580 CA CA A2007 1555 1555 2.73
LINK OD1 ASP A 582 CA CA A2007 1555 1555 2.82
LINK OD2 ASP A 582 CA CA A2007 1555 1555 2.80
LINK MG MG A2009 O HOH A4001 1555 1555 1.98
LINK MG MG A2009 O HOH A4002 1555 1555 2.03
LINK MG MG A2009 O HOH A4003 1555 1555 2.20
LINK O SER B 116 CA CA B2002 1555 1555 2.43
LINK OD1 ASP B 119 CA CA B2002 1555 1555 2.36
LINK OD1 ASP B 120 CA CA B2002 1555 1555 2.10
LINK O GLU B 325 CA CA B2002 1555 1555 2.70
LINK OE2 GLU B 325 CA CA B2002 1555 1555 2.30
LINK OD1 ASP C 447 CA CA C2005 1555 1555 2.93
LINK OD1 ASP C 451 CA CA C2005 1555 1555 2.99
LINK O SER C 453 CA CA C2005 1555 1555 2.85
LINK OD1 ASN C 513 CA CA C2006 1555 1555 2.97
LINK O LEU C 517 CA CA C2006 1555 1555 2.80
LINK OD1 ASP C 574 CA CA C2007 1555 1555 2.97
LINK OG1 THR C 576 CA CA C2007 1555 1555 2.71
LINK O ASP C 578 CA CA C2007 1555 1555 2.62
LINK O LEU C 580 CA CA C2007 1555 1555 2.71
LINK OD1 ASP C 582 CA CA C2007 1555 1555 2.81
LINK OD2 ASP C 582 CA CA C2007 1555 1555 2.81
LINK O SER D 116 CA CA D2002 1555 1555 2.44
LINK OD1 ASP D 119 CA CA D2002 1555 1555 2.36
LINK OD1 ASP D 120 CA CA D2002 1555 1555 2.10
LINK O GLU D 325 CA CA D2002 1555 1555 2.70
LINK OE2 GLU D 325 CA CA D2002 1555 1555 2.30
LINK OD1 ASP E 447 CA CA E2005 1555 1555 2.93
LINK OD1 ASP E 451 CA CA E2005 1555 1555 3.00
LINK O SER E 453 CA CA E2005 1555 1555 2.84
LINK OD1 ASN E 513 CA CA E2006 1555 1555 2.99
LINK O LEU E 517 CA CA E2006 1555 1555 2.81
LINK OD1 ASP E 574 CA CA E2007 1555 1555 2.97
LINK OG1 THR E 576 CA CA E2007 1555 1555 2.71
LINK O ASP E 578 CA CA E2007 1555 1555 2.61
LINK O LEU E 580 CA CA E2007 1555 1555 2.72
LINK OD1 ASP E 582 CA CA E2007 1555 1555 2.81
LINK OD2 ASP E 582 CA CA E2007 1555 1555 2.81
LINK O SER F 116 CA CA F2002 1555 1555 2.44
LINK OD1 ASP F 119 CA CA F2002 1555 1555 2.36
LINK OD1 ASP F 120 CA CA F2002 1555 1555 2.10
LINK O GLU F 325 CA CA F2002 1555 1555 2.70
LINK OE2 GLU F 325 CA CA F2002 1555 1555 2.30
LINK OD1 ASP G 447 CA CA G2005 1555 1555 2.92
LINK OD1 ASP G 451 CA CA G2005 1555 1555 3.00
LINK O SER G 453 CA CA G2005 1555 1555 2.85
LINK OD1 ASN G 513 CA CA G2006 1555 1555 2.99
LINK O LEU G 517 CA CA G2006 1555 1555 2.80
LINK OD1 ASP G 574 CA CA G2007 1555 1555 2.98
LINK OG1 THR G 576 CA CA G2007 1555 1555 2.70
LINK O ASP G 578 CA CA G2007 1555 1555 2.61
LINK O LEU G 580 CA CA G2007 1555 1555 2.72
LINK OD1 ASP G 582 CA CA G2007 1555 1555 2.81
LINK OD2 ASP G 582 CA CA G2007 1555 1555 2.82
LINK O SER H 116 CA CA H2002 1555 1555 2.43
LINK OD1 ASP H 119 CA CA H2002 1555 1555 2.37
LINK OD1 ASP H 120 CA CA H2002 1555 1555 2.10
LINK O GLU H 325 CA CA H2002 1555 1555 2.70
LINK OE2 GLU H 325 CA CA H2002 1555 1555 2.30
CISPEP 1 ARG A 164 PRO A 165 0 4.31
CISPEP 2 LYS A 288 PRO A 289 0 -5.46
CISPEP 3 SER B 77 PRO B 78 0 0.28
CISPEP 4 LEU B 155 PRO B 156 0 0.14
CISPEP 5 HIS B 161 PRO B 162 0 -19.87
CISPEP 6 LEU B 587 PRO B 588 0 2.56
CISPEP 7 LEU C 119 PRO C 120 0 13.54
CISPEP 8 SER D 77 PRO D 78 0 0.27
CISPEP 9 LEU D 155 PRO D 156 0 0.21
CISPEP 10 HIS D 161 PRO D 162 0 -20.06
CISPEP 11 LEU D 587 PRO D 588 0 2.65
CISPEP 12 LEU E 119 PRO E 120 0 13.60
CISPEP 13 SER F 77 PRO F 78 0 0.16
CISPEP 14 LEU F 155 PRO F 156 0 0.26
CISPEP 15 HIS F 161 PRO F 162 0 -20.02
CISPEP 16 LEU F 587 PRO F 588 0 2.58
CISPEP 17 LEU G 119 PRO G 120 0 13.52
CISPEP 18 SER H 77 PRO H 78 0 0.11
CISPEP 19 LEU H 155 PRO H 156 0 0.16
CISPEP 20 HIS H 161 PRO H 162 0 -19.97
CISPEP 21 LEU H 587 PRO H 588 0 2.68
CRYST1 132.095 163.561 536.911 90.00 90.00 90.00 P 21 21 21 16
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 0.007570 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006114 0.000000 0.00000
SCALE3 0.000000 0.000000 0.001863 0.00000
(ATOM LINES ARE NOT SHOWN.)
END