HEADER SIGNALING PROTEIN 06-SEP-12 4GZA
TITLE COMPLEX OF MOUSE PLEXIN A2 - SEMAPHORIN 3A - NEUROPILIN-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLEXIN-A2;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: UNP RESIDUES 33-703;
COMPND 5 SYNONYM: PLEX 2, PLEXIN-2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: SEMAPHORIN-3A;
COMPND 9 CHAIN: G;
COMPND 10 FRAGMENT: UNP RESIDUES 21-555;
COMPND 11 SYNONYM: SEMAPHORIN III, SEMA III, SEMAPHORIN-D, SEMA D;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: NEUROPILIN-1;
COMPND 15 CHAIN: H;
COMPND 16 FRAGMENT: UNP RESIDUES 22-586;
COMPND 17 SYNONYM: A5 PROTEIN;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: PLXNA2, KIAA0463;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 12 ORGANISM_COMMON: MOUSE;
SOURCE 13 ORGANISM_TAXID: 10090;
SOURCE 14 GENE: SEMA3A, SEMAD, SEMD;
SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 16 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: HEK293;
SOURCE 19 MOL_ID: 3;
SOURCE 20 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 21 ORGANISM_COMMON: MOUSE;
SOURCE 22 ORGANISM_TAXID: 10090;
SOURCE 23 GENE: NRP1, NRP;
SOURCE 24 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 25 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 26 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 27 EXPRESSION_SYSTEM_CELL_LINE: HEK293
KEYWDS TERNARY COMPLEX, MULTI-DOMAIN, MAMMALIAN, CELL-CELL SIGNALING,
KEYWDS 2 GLYCOSILATION, TRANSMEMBRANE, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR B.J.C.JANSSEN,T.MALINAUSKAS,C.SIEBOLD,E.Y.JONES
REVDAT 4 08-NOV-23 4GZA 1 REMARK SEQADV LINK
REVDAT 3 26-DEC-12 4GZA 1 JRNL
REVDAT 2 07-NOV-12 4GZA 1 JRNL
REVDAT 1 17-OCT-12 4GZA 0
JRNL AUTH B.J.C.JANSSEN,T.MALINAUSKAS,G.A.WEIR,M.Z.CADER,C.SIEBOLD,
JRNL AUTH 2 E.Y.JONES
JRNL TITL NEUROPILINS LOCK SECRETED SEMAPHORINS ONTO PLEXINS IN A
JRNL TITL 2 TERNARY SIGNALING COMPLEX.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 19 1293 2012
JRNL REFN ISSN 1545-9993
JRNL PMID 23104057
JRNL DOI 10.1038/NSMB.2416
REMARK 2
REMARK 2 RESOLUTION. 7.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
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) : 7.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 125.51
REMARK 3 MIN(FOBS/SIGMA_FOBS) : -3.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 20176
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.285
REMARK 3 R VALUE (WORKING SET) : 0.285
REMARK 3 FREE R VALUE : 0.285
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 1009
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1125.5263 - 16.8594 0.91 2575 141 0.2832 0.2739
REMARK 3 2 16.8594 - 13.3867 0.88 2455 130 0.2752 0.2800
REMARK 3 3 13.3867 - 11.6959 0.93 2643 121 0.2530 0.2764
REMARK 3 4 11.6959 - 10.6272 0.95 2731 127 0.2403 0.2518
REMARK 3 5 10.6272 - 9.8658 0.95 2667 150 0.2527 0.2287
REMARK 3 6 9.8658 - 9.2843 0.95 2657 132 0.2596 0.2691
REMARK 3 7 9.2843 - 8.8195 0.95 2700 139 0.2803 0.2878
REMARK 3 8 8.8195 - 8.4357 0.85 2394 133 0.2921 0.3188
REMARK 3 9 8.4357 - 8.1110 0.81 2287 121 0.3213 0.3209
REMARK 3 10 8.1110 - 7.8311 0.90 2565 134 0.3312 0.3185
REMARK 3 11 7.8311 - 7.5863 0.93 2583 158 0.3451 0.3061
REMARK 3 12 7.5863 - 7.3695 0.94 2631 149 0.3447 0.3188
REMARK 3 13 7.3695 - 7.1755 0.94 2660 168 0.3578 0.3668
REMARK 3 14 7.1755 - 7.0004 0.94 2608 119 0.3727 0.3619
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.11
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 283.5
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 1.030
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.140
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 84.12440
REMARK 3 B22 (A**2) : 17.45580
REMARK 3 B33 (A**2) : 22.67680
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 119.00390
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.014 36622
REMARK 3 ANGLE : 1.202 49584
REMARK 3 CHIRALITY : 0.063 5452
REMARK 3 PLANARITY : 0.008 6434
REMARK 3 DIHEDRAL : 13.074 13337
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 AUTHORS STATE THAT DUE TO THE LOW RESOLUTION OF THE DIFFRACTION
REMARK 3 DATA THE STRUCTURE WAS ONLY SUBJECTED TO RIGID BODY REFINEMENT
REMARK 3 WITH EACH DOMAIN AS RIGID BODY USING (PARTS OF) THE COORDINATES OF
REMARK 3 PDB ENTRIES 3OKT, 1Q47 AND 4GZ9.
REMARK 3 AUTHORS HAVE NOT FURTHER REFINED THE RESULTING COORDINATES NOR
REMARK 3 CORRECTED RESULTING CLASHES BETWEEN ATOMS AND DEVIATING PEPTIDE
REMARK 3 LINKAGES BETWEEN DOMAINS.
REMARK 4
REMARK 4 4GZA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-SEP-12.
REMARK 100 THE DEPOSITION ID IS D_1000074820.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-11; 20-APR-11; 05-MAY-11
REMARK 200 TEMPERATURE (KELVIN) : 100; 100; 100
REMARK 200 PH : 7.5; 7.5; 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 3
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y; Y
REMARK 200 RADIATION SOURCE : DIAMOND; DIAMOND; DIAMOND
REMARK 200 BEAMLINE : I04-1; I03; I02
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91730; 1.07190; 0.9795
REMARK 200 MONOCHROMATOR : SINGLE BOUNCE MONOCHROMATOR;
REMARK 200 DOUBLE CRYSTAL MONOCHROMATOR;
REMARK 200 DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL; NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL; PIXEL; CCD
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M; DECTRIS
REMARK 200 PILATUS 6M; ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20176
REMARK 200 RESOLUTION RANGE HIGH (A) : 7.000
REMARK 200 RESOLUTION RANGE LOW (A) : 126.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH; SINGLE
REMARK 200 WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3OKT, 1Q47, 4GZ9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 78.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 70MM HEPES, PH 7.5, 1.4% W/V PEG 400,
REMARK 280 12% V/V GLYCEROL, 1.4M AMMONIUM SULPHATE, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K. 70MM HEPES, PH 7.5, 1.4% W/V PEG
REMARK 280 400, 12% V/V GLYCEROL, 1.4M AMMONIUM SULPHATE, 1% V/V ETHYL
REMARK 280 ACETATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K. 70MM
REMARK 280 HEPES, PH 7.5, 1.4% W/V PEG 400, 12% V/V GLYCEROL, 1.4M AMMONIUM
REMARK 280 SULPHATE, 8% V/V ACETONITRILE , VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 95.81600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 146.80200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 95.81600
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 146.80200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXADECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H
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 BIOMT1 2 -1.000000 0.000000 0.000000 71.11529
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -241.94080
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 GLU A 32
REMARK 465 THR A 33
REMARK 465 GLY A 34
REMARK 465 MET A 35
REMARK 465 ASP A 264
REMARK 465 GLY A 265
REMARK 465 MET A 266
REMARK 465 ALA A 267
REMARK 465 ILE A 268
REMARK 465 ASN A 269
REMARK 465 SER A 270
REMARK 465 ALA A 271
REMARK 465 GLY A 272
REMARK 465 ASP A 627
REMARK 465 GLN A 628
REMARK 465 GLN A 703
REMARK 465 GLY A 704
REMARK 465 THR A 705
REMARK 465 LYS A 706
REMARK 465 HIS A 707
REMARK 465 HIS A 708
REMARK 465 HIS A 709
REMARK 465 HIS A 710
REMARK 465 HIS A 711
REMARK 465 HIS A 712
REMARK 465 GLU B 32
REMARK 465 THR B 33
REMARK 465 GLY B 34
REMARK 465 MET B 35
REMARK 465 ASP B 264
REMARK 465 GLY B 265
REMARK 465 MET B 266
REMARK 465 ALA B 267
REMARK 465 ILE B 268
REMARK 465 ASN B 269
REMARK 465 SER B 270
REMARK 465 ALA B 271
REMARK 465 GLY B 272
REMARK 465 ASP B 627
REMARK 465 GLN B 628
REMARK 465 GLN B 703
REMARK 465 GLY B 704
REMARK 465 THR B 705
REMARK 465 LYS B 706
REMARK 465 HIS B 707
REMARK 465 HIS B 708
REMARK 465 HIS B 709
REMARK 465 HIS B 710
REMARK 465 HIS B 711
REMARK 465 HIS B 712
REMARK 465 GLU C 32
REMARK 465 THR C 33
REMARK 465 GLY C 34
REMARK 465 MET C 35
REMARK 465 ASP C 264
REMARK 465 GLY C 265
REMARK 465 MET C 266
REMARK 465 ALA C 267
REMARK 465 ILE C 268
REMARK 465 ASN C 269
REMARK 465 SER C 270
REMARK 465 ALA C 271
REMARK 465 GLY C 272
REMARK 465 ASP C 627
REMARK 465 GLN C 628
REMARK 465 GLN C 703
REMARK 465 GLY C 704
REMARK 465 THR C 705
REMARK 465 LYS C 706
REMARK 465 HIS C 707
REMARK 465 HIS C 708
REMARK 465 HIS C 709
REMARK 465 HIS C 710
REMARK 465 HIS C 711
REMARK 465 HIS C 712
REMARK 465 GLU D 32
REMARK 465 THR D 33
REMARK 465 GLY D 34
REMARK 465 MET D 35
REMARK 465 ASP D 264
REMARK 465 GLY D 265
REMARK 465 MET D 266
REMARK 465 ALA D 267
REMARK 465 ILE D 268
REMARK 465 ASN D 269
REMARK 465 SER D 270
REMARK 465 ALA D 271
REMARK 465 GLY D 272
REMARK 465 ASP D 627
REMARK 465 GLN D 628
REMARK 465 GLN D 703
REMARK 465 GLY D 704
REMARK 465 THR D 705
REMARK 465 LYS D 706
REMARK 465 HIS D 707
REMARK 465 HIS D 708
REMARK 465 HIS D 709
REMARK 465 HIS D 710
REMARK 465 HIS D 711
REMARK 465 HIS D 712
REMARK 465 GLU E 32
REMARK 465 THR E 33
REMARK 465 GLY E 34
REMARK 465 MET E 35
REMARK 465 ASP E 264
REMARK 465 GLY E 265
REMARK 465 MET E 266
REMARK 465 ALA E 267
REMARK 465 ILE E 268
REMARK 465 ASN E 269
REMARK 465 SER E 270
REMARK 465 ALA E 271
REMARK 465 GLY E 272
REMARK 465 ASP E 627
REMARK 465 GLN E 628
REMARK 465 GLN E 703
REMARK 465 GLY E 704
REMARK 465 THR E 705
REMARK 465 LYS E 706
REMARK 465 HIS E 707
REMARK 465 HIS E 708
REMARK 465 HIS E 709
REMARK 465 HIS E 710
REMARK 465 HIS E 711
REMARK 465 HIS E 712
REMARK 465 GLU F 32
REMARK 465 THR F 33
REMARK 465 GLY F 34
REMARK 465 MET F 35
REMARK 465 ASP F 264
REMARK 465 GLY F 265
REMARK 465 MET F 266
REMARK 465 ALA F 267
REMARK 465 ILE F 268
REMARK 465 ASN F 269
REMARK 465 SER F 270
REMARK 465 ALA F 271
REMARK 465 GLY F 272
REMARK 465 ASP F 627
REMARK 465 GLN F 628
REMARK 465 GLN F 703
REMARK 465 GLY F 704
REMARK 465 THR F 705
REMARK 465 LYS F 706
REMARK 465 HIS F 707
REMARK 465 HIS F 708
REMARK 465 HIS F 709
REMARK 465 HIS F 710
REMARK 465 HIS F 711
REMARK 465 HIS F 712
REMARK 465 GLU G 18
REMARK 465 THR G 19
REMARK 465 GLY G 20
REMARK 465 ASN G 21
REMARK 465 TYR G 22
REMARK 465 ALA G 23
REMARK 465 ASN G 24
REMARK 465 GLY G 25
REMARK 465 PRO G 465
REMARK 465 LYS G 466
REMARK 465 GLU G 467
REMARK 465 THR G 468
REMARK 465 TRP G 469
REMARK 465 HIS G 470
REMARK 465 ASP G 471
REMARK 465 LEU G 472
REMARK 465 GLU G 473
REMARK 465 GLU G 474
REMARK 465 VAL G 475
REMARK 465 GLY G 521
REMARK 465 LYS G 522
REMARK 465 ALA G 523
REMARK 465 CYS G 524
REMARK 465 ALA G 525
REMARK 465 GLU G 526
REMARK 465 CYS G 527
REMARK 465 CYS G 528
REMARK 465 LEU G 529
REMARK 465 ALA G 530
REMARK 465 ARG G 531
REMARK 465 ASP G 532
REMARK 465 PRO G 533
REMARK 465 TYR G 534
REMARK 465 CYS G 535
REMARK 465 ALA G 536
REMARK 465 TRP G 537
REMARK 465 ASP G 538
REMARK 465 GLY G 539
REMARK 465 SER G 540
REMARK 465 SER G 541
REMARK 465 CYS G 542
REMARK 465 SER G 543
REMARK 465 ARG G 544
REMARK 465 TYR G 545
REMARK 465 PHE G 546
REMARK 465 PRO G 547
REMARK 465 THR G 548
REMARK 465 ALA G 549
REMARK 465 LYS G 550
REMARK 465 ARG G 551
REMARK 465 ARG G 552
REMARK 465 THR G 553
REMARK 465 ARG G 554
REMARK 465 ARG G 555
REMARK 465 GLU H 19
REMARK 465 THR H 20
REMARK 465 GLY H 21
REMARK 465 PHE H 22
REMARK 465 ARG H 23
REMARK 465 SER H 24
REMARK 465 LYS H 142
REMARK 465 ARG H 143
REMARK 465 GLY H 144
REMARK 465 PRO H 145
REMARK 465 GLU H 146
REMARK 465 CYS H 147
REMARK 465 SER H 148
REMARK 465 GLN H 149
REMARK 465 ASN H 150
REMARK 465 TYR H 151
REMARK 465 THR H 152
REMARK 465 ALA H 153
REMARK 465 PRO H 154
REMARK 465 THR H 155
REMARK 465 GLY H 156
REMARK 465 VAL H 157
REMARK 465 ILE H 158
REMARK 465 LYS H 159
REMARK 465 SER H 160
REMARK 465 PRO H 161
REMARK 465 GLY H 162
REMARK 465 PHE H 163
REMARK 465 PRO H 164
REMARK 465 GLU H 165
REMARK 465 LYS H 166
REMARK 465 TYR H 167
REMARK 465 PRO H 168
REMARK 465 ASN H 169
REMARK 465 SER H 170
REMARK 465 LEU H 171
REMARK 465 GLU H 172
REMARK 465 CYS H 173
REMARK 465 THR H 174
REMARK 465 TYR H 175
REMARK 465 ILE H 176
REMARK 465 ILE H 177
REMARK 465 PHE H 178
REMARK 465 ALA H 179
REMARK 465 PRO H 180
REMARK 465 LYS H 181
REMARK 465 MET H 182
REMARK 465 SER H 183
REMARK 465 GLU H 184
REMARK 465 ILE H 185
REMARK 465 ILE H 186
REMARK 465 LEU H 187
REMARK 465 GLU H 188
REMARK 465 PHE H 189
REMARK 465 GLU H 190
REMARK 465 SER H 191
REMARK 465 PHE H 192
REMARK 465 ASP H 193
REMARK 465 LEU H 194
REMARK 465 GLU H 195
REMARK 465 GLN H 196
REMARK 465 ASP H 197
REMARK 465 SER H 198
REMARK 465 ASN H 199
REMARK 465 PRO H 200
REMARK 465 PRO H 201
REMARK 465 GLY H 202
REMARK 465 GLY H 203
REMARK 465 MET H 204
REMARK 465 PHE H 205
REMARK 465 CYS H 206
REMARK 465 ARG H 207
REMARK 465 TYR H 208
REMARK 465 ASP H 209
REMARK 465 ARG H 210
REMARK 465 LEU H 211
REMARK 465 GLU H 212
REMARK 465 ILE H 213
REMARK 465 TRP H 214
REMARK 465 ASP H 215
REMARK 465 GLY H 216
REMARK 465 PHE H 217
REMARK 465 PRO H 218
REMARK 465 GLU H 219
REMARK 465 VAL H 220
REMARK 465 GLY H 221
REMARK 465 PRO H 222
REMARK 465 HIS H 223
REMARK 465 ILE H 224
REMARK 465 GLY H 225
REMARK 465 ARG H 226
REMARK 465 TYR H 227
REMARK 465 CYS H 228
REMARK 465 GLY H 229
REMARK 465 GLN H 230
REMARK 465 LYS H 231
REMARK 465 THR H 232
REMARK 465 PRO H 233
REMARK 465 GLY H 234
REMARK 465 ARG H 235
REMARK 465 ILE H 236
REMARK 465 ARG H 237
REMARK 465 SER H 238
REMARK 465 SER H 239
REMARK 465 SER H 240
REMARK 465 GLY H 241
REMARK 465 VAL H 242
REMARK 465 LEU H 243
REMARK 465 SER H 244
REMARK 465 MET H 245
REMARK 465 VAL H 246
REMARK 465 PHE H 247
REMARK 465 TYR H 248
REMARK 465 THR H 249
REMARK 465 ASP H 250
REMARK 465 SER H 251
REMARK 465 ALA H 252
REMARK 465 ILE H 253
REMARK 465 ALA H 254
REMARK 465 LYS H 255
REMARK 465 GLU H 256
REMARK 465 GLY H 257
REMARK 465 PHE H 258
REMARK 465 SER H 259
REMARK 465 ALA H 260
REMARK 465 ASN H 261
REMARK 465 TYR H 262
REMARK 465 SER H 263
REMARK 465 VAL H 264
REMARK 465 LEU H 265
REMARK 465 GLN H 266
REMARK 465 SER H 267
REMARK 465 SER H 268
REMARK 465 ILE H 269
REMARK 465 SER H 270
REMARK 465 GLU H 271
REMARK 465 ASP H 272
REMARK 465 PHE H 273
REMARK 465 LYS H 274
REMARK 465 CYS H 275
REMARK 465 MET H 276
REMARK 465 GLU H 277
REMARK 465 ALA H 278
REMARK 465 LEU H 279
REMARK 465 GLY H 280
REMARK 465 MET H 281
REMARK 465 GLU H 282
REMARK 465 SER H 283
REMARK 465 GLY H 284
REMARK 465 GLU H 285
REMARK 465 ILE H 286
REMARK 465 HIS H 287
REMARK 465 SER H 288
REMARK 465 ASP H 289
REMARK 465 GLN H 290
REMARK 465 ILE H 291
REMARK 465 THR H 292
REMARK 465 ALA H 293
REMARK 465 SER H 294
REMARK 465 SER H 295
REMARK 465 GLN H 296
REMARK 465 TYR H 297
REMARK 465 GLY H 298
REMARK 465 THR H 299
REMARK 465 ASN H 300
REMARK 465 TRP H 301
REMARK 465 SER H 302
REMARK 465 VAL H 303
REMARK 465 GLU H 304
REMARK 465 ARG H 305
REMARK 465 SER H 306
REMARK 465 ARG H 307
REMARK 465 LEU H 308
REMARK 465 ASN H 309
REMARK 465 TYR H 310
REMARK 465 PRO H 311
REMARK 465 GLU H 312
REMARK 465 ASN H 313
REMARK 465 GLY H 314
REMARK 465 TRP H 315
REMARK 465 THR H 316
REMARK 465 PRO H 317
REMARK 465 GLY H 318
REMARK 465 GLU H 319
REMARK 465 ASP H 320
REMARK 465 SER H 321
REMARK 465 TYR H 322
REMARK 465 LYS H 323
REMARK 465 GLU H 324
REMARK 465 TRP H 325
REMARK 465 ILE H 326
REMARK 465 GLN H 327
REMARK 465 VAL H 328
REMARK 465 ASP H 329
REMARK 465 LEU H 330
REMARK 465 GLY H 331
REMARK 465 LEU H 332
REMARK 465 LEU H 333
REMARK 465 ARG H 334
REMARK 465 PHE H 335
REMARK 465 VAL H 336
REMARK 465 THR H 337
REMARK 465 ALA H 338
REMARK 465 VAL H 339
REMARK 465 GLY H 340
REMARK 465 THR H 341
REMARK 465 GLN H 342
REMARK 465 GLY H 343
REMARK 465 ALA H 344
REMARK 465 ILE H 345
REMARK 465 SER H 346
REMARK 465 LYS H 347
REMARK 465 GLU H 348
REMARK 465 THR H 349
REMARK 465 LYS H 350
REMARK 465 LYS H 351
REMARK 465 LYS H 352
REMARK 465 TYR H 353
REMARK 465 TYR H 354
REMARK 465 VAL H 355
REMARK 465 LYS H 356
REMARK 465 THR H 357
REMARK 465 TYR H 358
REMARK 465 ARG H 359
REMARK 465 VAL H 360
REMARK 465 ASP H 361
REMARK 465 ILE H 362
REMARK 465 SER H 363
REMARK 465 SER H 364
REMARK 465 ASN H 365
REMARK 465 GLY H 366
REMARK 465 GLU H 367
REMARK 465 ASP H 368
REMARK 465 TRP H 369
REMARK 465 ILE H 370
REMARK 465 SER H 371
REMARK 465 LEU H 372
REMARK 465 LYS H 373
REMARK 465 GLU H 374
REMARK 465 GLY H 375
REMARK 465 ASN H 376
REMARK 465 LYS H 377
REMARK 465 ALA H 378
REMARK 465 ILE H 379
REMARK 465 ILE H 380
REMARK 465 PHE H 381
REMARK 465 GLN H 382
REMARK 465 GLY H 383
REMARK 465 ASN H 384
REMARK 465 THR H 385
REMARK 465 ASN H 386
REMARK 465 PRO H 387
REMARK 465 THR H 388
REMARK 465 ASP H 389
REMARK 465 VAL H 390
REMARK 465 VAL H 391
REMARK 465 LEU H 392
REMARK 465 GLY H 393
REMARK 465 VAL H 394
REMARK 465 PHE H 395
REMARK 465 SER H 396
REMARK 465 LYS H 397
REMARK 465 PRO H 398
REMARK 465 LEU H 399
REMARK 465 ILE H 400
REMARK 465 THR H 401
REMARK 465 ARG H 402
REMARK 465 PHE H 403
REMARK 465 VAL H 404
REMARK 465 ARG H 405
REMARK 465 ILE H 406
REMARK 465 LYS H 407
REMARK 465 PRO H 408
REMARK 465 VAL H 409
REMARK 465 SER H 410
REMARK 465 TRP H 411
REMARK 465 GLU H 412
REMARK 465 THR H 413
REMARK 465 GLY H 414
REMARK 465 ILE H 415
REMARK 465 SER H 416
REMARK 465 MET H 417
REMARK 465 ARG H 418
REMARK 465 PHE H 419
REMARK 465 GLU H 420
REMARK 465 VAL H 421
REMARK 465 TYR H 422
REMARK 465 GLY H 423
REMARK 465 CYS H 424
REMARK 465 LYS H 425
REMARK 465 ILE H 426
REMARK 465 THR H 427
REMARK 465 ASP H 428
REMARK 465 TYR H 429
REMARK 465 PRO H 430
REMARK 465 CYS H 431
REMARK 465 SER H 432
REMARK 465 GLY H 433
REMARK 465 MET H 434
REMARK 465 LEU H 435
REMARK 465 GLY H 436
REMARK 465 MET H 437
REMARK 465 VAL H 438
REMARK 465 SER H 439
REMARK 465 GLY H 440
REMARK 465 LEU H 441
REMARK 465 ILE H 442
REMARK 465 SER H 443
REMARK 465 ASP H 444
REMARK 465 SER H 445
REMARK 465 GLN H 446
REMARK 465 ILE H 447
REMARK 465 THR H 448
REMARK 465 ALA H 449
REMARK 465 SER H 450
REMARK 465 ASN H 451
REMARK 465 GLN H 452
REMARK 465 ALA H 453
REMARK 465 ASP H 454
REMARK 465 ARG H 455
REMARK 465 ASN H 456
REMARK 465 TRP H 457
REMARK 465 MET H 458
REMARK 465 PRO H 459
REMARK 465 GLU H 460
REMARK 465 ASN H 461
REMARK 465 ILE H 462
REMARK 465 ARG H 463
REMARK 465 LEU H 464
REMARK 465 VAL H 465
REMARK 465 THR H 466
REMARK 465 SER H 467
REMARK 465 ARG H 468
REMARK 465 THR H 469
REMARK 465 GLY H 470
REMARK 465 TRP H 471
REMARK 465 ALA H 472
REMARK 465 LEU H 473
REMARK 465 PRO H 474
REMARK 465 PRO H 475
REMARK 465 SER H 476
REMARK 465 PRO H 477
REMARK 465 HIS H 478
REMARK 465 PRO H 479
REMARK 465 TYR H 480
REMARK 465 THR H 481
REMARK 465 ASN H 482
REMARK 465 GLU H 483
REMARK 465 TRP H 484
REMARK 465 LEU H 485
REMARK 465 GLN H 486
REMARK 465 VAL H 487
REMARK 465 ASP H 488
REMARK 465 LEU H 489
REMARK 465 GLY H 490
REMARK 465 ASP H 491
REMARK 465 GLU H 492
REMARK 465 LYS H 493
REMARK 465 ILE H 494
REMARK 465 VAL H 495
REMARK 465 ARG H 496
REMARK 465 GLY H 497
REMARK 465 VAL H 498
REMARK 465 ILE H 499
REMARK 465 ILE H 500
REMARK 465 GLN H 501
REMARK 465 GLY H 502
REMARK 465 GLY H 503
REMARK 465 LYS H 504
REMARK 465 HIS H 505
REMARK 465 ARG H 506
REMARK 465 GLU H 507
REMARK 465 ASN H 508
REMARK 465 LYS H 509
REMARK 465 VAL H 510
REMARK 465 PHE H 511
REMARK 465 MET H 512
REMARK 465 ARG H 513
REMARK 465 LYS H 514
REMARK 465 PHE H 515
REMARK 465 LYS H 516
REMARK 465 ILE H 517
REMARK 465 ALA H 518
REMARK 465 TYR H 519
REMARK 465 SER H 520
REMARK 465 ASN H 521
REMARK 465 ASN H 522
REMARK 465 GLY H 523
REMARK 465 SER H 524
REMARK 465 ASP H 525
REMARK 465 TRP H 526
REMARK 465 LYS H 527
REMARK 465 THR H 528
REMARK 465 ILE H 529
REMARK 465 MET H 530
REMARK 465 ASP H 531
REMARK 465 ASP H 532
REMARK 465 SER H 533
REMARK 465 LYS H 534
REMARK 465 ARG H 535
REMARK 465 LYS H 536
REMARK 465 ALA H 537
REMARK 465 LYS H 538
REMARK 465 SER H 539
REMARK 465 PHE H 540
REMARK 465 GLU H 541
REMARK 465 GLY H 542
REMARK 465 ASN H 543
REMARK 465 ASN H 544
REMARK 465 ASN H 545
REMARK 465 TYR H 546
REMARK 465 ASP H 547
REMARK 465 THR H 548
REMARK 465 PRO H 549
REMARK 465 GLU H 550
REMARK 465 LEU H 551
REMARK 465 ARG H 552
REMARK 465 THR H 553
REMARK 465 PHE H 554
REMARK 465 SER H 555
REMARK 465 PRO H 556
REMARK 465 LEU H 557
REMARK 465 SER H 558
REMARK 465 THR H 559
REMARK 465 ARG H 560
REMARK 465 PHE H 561
REMARK 465 ILE H 562
REMARK 465 ARG H 563
REMARK 465 ILE H 564
REMARK 465 TYR H 565
REMARK 465 PRO H 566
REMARK 465 GLU H 567
REMARK 465 ARG H 568
REMARK 465 ALA H 569
REMARK 465 THR H 570
REMARK 465 HIS H 571
REMARK 465 SER H 572
REMARK 465 GLY H 573
REMARK 465 LEU H 574
REMARK 465 GLY H 575
REMARK 465 LEU H 576
REMARK 465 ARG H 577
REMARK 465 MET H 578
REMARK 465 GLU H 579
REMARK 465 LEU H 580
REMARK 465 LEU H 581
REMARK 465 GLY H 582
REMARK 465 CYS H 583
REMARK 465 GLU H 584
REMARK 465 VAL H 585
REMARK 465 GLU H 586
REMARK 465 ARG H 587
REMARK 465 THR H 588
REMARK 465 LYS H 589
REMARK 465 HIS H 590
REMARK 465 HIS H 591
REMARK 465 HIS H 592
REMARK 465 HIS H 593
REMARK 465 HIS H 594
REMARK 465 HIS H 595
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 NE2 GLN A 345 OE1 GLU H 128 0.46
REMARK 500 CE2 PHE D 690 CB ARG E 540 0.52
REMARK 500 OE1 GLN D 610 CD1 LEU F 577 0.72
REMARK 500 CE2 PHE B 690 CG ARG D 540 0.80
REMARK 500 CD ARG A 540 CG PHE C 690 0.81
REMARK 500 CZ PHE D 690 CB ARG E 540 0.96
REMARK 500 CD1 TYR A 95 NH2 ARG G 277 0.96
REMARK 500 CE1 PHE B 690 CZ ARG D 540 1.01
REMARK 500 O SER C 523 CE1 HIS D 465 1.02
REMARK 500 CD2 PHE B 690 CD ARG D 540 1.04
REMARK 500 NE ARG C 540 CE1 PHE F 690 1.04
REMARK 500 OE2 GLU A 306 NZ LYS H 83 1.05
REMARK 500 O TYR C 654 N ASN C 655 1.06
REMARK 500 OE1 GLN B 660 CZ2 TRP G 105 1.09
REMARK 500 NH1 ARG A 540 CD1 PHE C 690 1.09
REMARK 500 O TYR D 654 N ASN D 655 1.10
REMARK 500 CD ARG A 540 CB PHE C 690 1.13
REMARK 500 CD1 PHE B 690 NE ARG D 540 1.13
REMARK 500 CZ ARG A 540 CD1 PHE C 690 1.17
REMARK 500 CE1 PHE B 690 NE ARG D 540 1.18
REMARK 500 CZ PHE A 275 CG ARG H 80 1.19
REMARK 500 CA ASN A 441 OE1 GLN C 691 1.22
REMARK 500 CE2 PHE B 690 CD ARG D 540 1.22
REMARK 500 CG ARG A 540 CD2 PHE C 690 1.33
REMARK 500 CA GLY C 518 NE2 GLN D 324 1.34
REMARK 500 CE1 HIS A 465 O SER B 523 1.38
REMARK 500 OD2 ASP A 408 CB PHE G 194 1.39
REMARK 500 O SER A 523 CE1 HIS B 465 1.40
REMARK 500 CE1 PHE B 690 NH2 ARG D 540 1.42
REMARK 500 CD ARG C 540 CZ PHE F 690 1.43
REMARK 500 CB ARG C 540 CZ PHE F 690 1.43
REMARK 500 CB ARG C 540 CE2 PHE F 690 1.44
REMARK 500 CA GLY A 518 NE2 GLN B 324 1.45
REMARK 500 CG PHE B 690 NE ARG D 540 1.46
REMARK 500 NE2 GLN A 324 CA GLY B 518 1.47
REMARK 500 CG ARG C 540 CZ PHE F 690 1.48
REMARK 500 CE2 PHE B 690 CB ARG D 540 1.48
REMARK 500 CD1 LEU E 626 CB PRO F 399 1.50
REMARK 500 CE2 PHE D 690 CG ARG E 540 1.50
REMARK 500 O TYR E 654 N ASN E 655 1.51
REMARK 500 CZ PHE B 690 NE ARG D 540 1.51
REMARK 500 OE1 GLN D 691 N GLY E 442 1.52
REMARK 500 NE2 GLN A 345 CD GLU H 128 1.53
REMARK 500 NE ARG A 540 CD1 PHE C 690 1.55
REMARK 500 CD GLN A 345 OE1 GLU H 128 1.55
REMARK 500 OD2 ASP A 408 CG PHE G 194 1.57
REMARK 500 N GLY C 518 NE2 GLN D 324 1.57
REMARK 500 N LEU A 274 NH2 ARG H 80 1.57
REMARK 500 CD GLN D 610 CD1 LEU F 577 1.59
REMARK 500 NE ARG A 540 CG PHE C 690 1.59
REMARK 500
REMARK 500 THIS ENTRY HAS 139 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 CE1 PHE A 690 NE ARG F 540 3455 0.68
REMARK 500 CE2 PHE A 690 CG ARG F 540 3455 0.78
REMARK 500 N ASP B 541 CE2 PHE E 690 3455 0.79
REMARK 500 CD1 LEU A 577 OE1 GLN E 610 3455 0.87
REMARK 500 C ARG B 540 CZ PHE E 690 3455 0.87
REMARK 500 CB ARG B 540 CE1 PHE E 690 3455 0.88
REMARK 500 CZ PHE G 386 ND2 ASN H 72 2554 0.89
REMARK 500 CE1 PHE A 690 CZ ARG F 540 3455 0.94
REMARK 500 CG LEU A 577 OE1 GLN E 610 3455 1.00
REMARK 500 CE2 PHE A 690 CD ARG F 540 3455 1.06
REMARK 500 N ASP B 541 CZ PHE E 690 3455 1.06
REMARK 500 NE2 GLN G 365 NE2 GLN G 365 2554 1.13
REMARK 500 CD1 PHE A 690 NE ARG F 540 3455 1.20
REMARK 500 CE1 PHE G 386 ND2 ASN H 72 2554 1.21
REMARK 500 CD2 PHE A 690 CD ARG F 540 3455 1.21
REMARK 500 CZ PHE A 690 NE ARG F 540 3455 1.22
REMARK 500 OE1 GLN A 610 CD1 LEU E 577 3455 1.30
REMARK 500 OE2 GLU A 692 N ASN F 441 3455 1.30
REMARK 500 CD1 LEU A 577 CD GLN E 610 3455 1.31
REMARK 500 CA ASP B 541 CE2 PHE E 690 3455 1.35
REMARK 500 OE1 GLN A 610 CG LEU E 577 3455 1.39
REMARK 500 CG2 THR G 385 NH1 ARG H 137 2554 1.43
REMARK 500 CA ARG B 540 CE1 PHE E 690 3455 1.45
REMARK 500 CE2 PHE A 690 CB ARG F 540 3455 1.47
REMARK 500 CZ PHE G 386 CG ASN H 72 2554 1.49
REMARK 500 N ASN B 441 OE1 GLN E 691 3455 1.50
REMARK 500 CA ARG B 540 CZ PHE E 690 3455 1.51
REMARK 500 CE LYS G 259 O ASN G 299 2554 1.58
REMARK 500 CZ PHE A 690 CD ARG F 540 3455 1.62
REMARK 500 CE1 PHE A 690 NH2 ARG F 540 3455 1.66
REMARK 500 CA GLN G 365 OE1 GLN G 365 2554 1.70
REMARK 500 CD ARG B 540 O SER E 689 3455 1.71
REMARK 500 CZ PHE A 690 CG ARG F 540 3455 1.72
REMARK 500 CB ARG B 540 CD1 PHE E 690 3455 1.81
REMARK 500 CZ PHE A 690 CZ ARG F 540 3455 1.81
REMARK 500 CG PHE A 690 CD ARG F 540 3455 1.82
REMARK 500 C ARG B 540 CE2 PHE E 690 3455 1.85
REMARK 500 CE2 PHE A 690 NE ARG F 540 3455 1.87
REMARK 500 OE1 GLN A 610 CB LEU E 577 3455 1.87
REMARK 500 CG PHE A 690 NE ARG F 540 3455 1.87
REMARK 500 OE2 GLU A 692 CA ASN F 441 3455 1.90
REMARK 500 CD GLN G 365 NE2 GLN G 365 2554 1.92
REMARK 500 CD LYS G 259 CA GLY G 300 2554 1.93
REMARK 500 CD1 PHE A 690 CZ ARG F 540 3455 1.94
REMARK 500 CD2 PHE A 690 CG ARG F 540 3455 1.98
REMARK 500 CB LEU A 577 NE2 GLN E 610 3455 2.00
REMARK 500 CG LEU A 577 CD GLN E 610 3455 2.01
REMARK 500 O ARG B 540 CZ PHE E 690 3455 2.02
REMARK 500 CD LYS G 259 C GLY G 300 2554 2.03
REMARK 500 CD GLN A 610 CD1 LEU E 577 3455 2.04
REMARK 500
REMARK 500 THIS ENTRY HAS 63 SYMMETRY CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TYR A 654 C ASN A 655 N 0.187
REMARK 500 VAL C 508 C GLU C 509 N -0.483
REMARK 500 VAL D 508 C GLU D 509 N -0.240
REMARK 500 TYR D 654 C ASN D 655 N -0.286
REMARK 500 CYS E 559 C MET E 560 N -0.150
REMARK 500 VAL F 508 C GLU F 509 N 0.298
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 TYR A 654 O - C - N ANGL. DEV. = -16.9 DEGREES
REMARK 500 VAL B 508 O - C - N ANGL. DEV. = -18.7 DEGREES
REMARK 500 TYR B 654 CA - C - N ANGL. DEV. = 19.3 DEGREES
REMARK 500 TYR B 654 O - C - N ANGL. DEV. = -20.5 DEGREES
REMARK 500 ASN B 655 C - N - CA ANGL. DEV. = 30.4 DEGREES
REMARK 500 VAL C 508 O - C - N ANGL. DEV. = -19.8 DEGREES
REMARK 500 TYR C 654 CA - C - N ANGL. DEV. = 25.1 DEGREES
REMARK 500 TYR C 654 O - C - N ANGL. DEV. = -71.3 DEGREES
REMARK 500 VAL D 508 CA - C - N ANGL. DEV. = -18.4 DEGREES
REMARK 500 GLU D 509 C - N - CA ANGL. DEV. = -20.8 DEGREES
REMARK 500 TYR D 654 CA - C - N ANGL. DEV. = 16.4 DEGREES
REMARK 500 TYR D 654 O - C - N ANGL. DEV. = -65.6 DEGREES
REMARK 500 CYS E 559 CA - C - N ANGL. DEV. = -19.1 DEGREES
REMARK 500 CYS E 559 O - C - N ANGL. DEV. = 17.3 DEGREES
REMARK 500 MET E 560 C - N - CA ANGL. DEV. = -20.6 DEGREES
REMARK 500 TYR E 654 CA - C - N ANGL. DEV. = 48.1 DEGREES
REMARK 500 TYR E 654 O - C - N ANGL. DEV. = -50.4 DEGREES
REMARK 500 ASN E 655 C - N - CA ANGL. DEV. = 52.4 DEGREES
REMARK 500 VAL F 508 O - C - N ANGL. DEV. = -14.4 DEGREES
REMARK 500 GLU F 509 C - N - CA ANGL. DEV. = 18.1 DEGREES
REMARK 500 CYS F 559 CA - C - N ANGL. DEV. = -25.4 DEGREES
REMARK 500 CYS F 559 O - C - N ANGL. DEV. = -12.4 DEGREES
REMARK 500 MET F 560 C - N - CA ANGL. DEV. = -23.9 DEGREES
REMARK 500 TYR F 654 CA - C - N ANGL. DEV. = -24.7 DEGREES
REMARK 500 ASN F 655 C - N - CA ANGL. DEV. = -20.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 51 -50.33 -122.34
REMARK 500 LEU A 77 42.42 70.08
REMARK 500 SER A 152 18.09 -160.00
REMARK 500 SER A 160 143.81 167.68
REMARK 500 SER A 175 -156.48 -68.16
REMARK 500 ASP A 287 71.49 -168.09
REMARK 500 PRO A 397 58.92 -68.38
REMARK 500 ARG A 429 -44.94 -133.01
REMARK 500 ASN A 550 19.54 59.08
REMARK 500 ASP A 700 43.33 -108.71
REMARK 500 ASN B 51 -50.39 -122.29
REMARK 500 LEU B 77 42.40 70.07
REMARK 500 SER B 152 18.10 -159.99
REMARK 500 SER B 160 143.76 167.88
REMARK 500 SER B 175 -156.61 -68.26
REMARK 500 ASP B 287 71.52 -168.15
REMARK 500 PRO B 397 58.91 -68.42
REMARK 500 ARG B 429 -44.85 -133.04
REMARK 500 VAL B 508 9.14 -55.47
REMARK 500 GLU B 509 143.16 174.68
REMARK 500 ASN B 550 19.54 59.16
REMARK 500 ASP B 700 43.29 -108.73
REMARK 500 ASN C 51 -50.31 -122.22
REMARK 500 LEU C 77 42.23 70.16
REMARK 500 SER C 152 17.99 -159.97
REMARK 500 SER C 160 143.79 167.77
REMARK 500 SER C 175 -156.54 -68.21
REMARK 500 ASP C 287 71.62 -168.16
REMARK 500 PRO C 397 58.90 -68.40
REMARK 500 ARG C 429 -44.91 -133.00
REMARK 500 VAL C 508 3.27 -55.48
REMARK 500 GLU C 509 143.03 175.48
REMARK 500 ASN C 550 19.42 59.21
REMARK 500 TYR C 654 -86.42 -127.22
REMARK 500 ASN C 655 95.23 102.43
REMARK 500 ASP C 700 43.42 -108.68
REMARK 500 ASN D 51 -50.40 -122.22
REMARK 500 LEU D 77 42.44 70.06
REMARK 500 SER D 152 18.04 -159.87
REMARK 500 SER D 160 143.70 167.81
REMARK 500 SER D 175 -156.47 -68.07
REMARK 500 ASP D 287 71.50 -168.09
REMARK 500 PRO D 397 59.02 -68.49
REMARK 500 ARG D 429 -44.91 -133.11
REMARK 500 VAL D 508 -0.31 -55.34
REMARK 500 GLU D 509 143.09 -170.55
REMARK 500 ASN D 550 19.33 59.28
REMARK 500 TYR D 654 -92.97 -127.21
REMARK 500 ASN D 655 95.21 111.83
REMARK 500 ASP D 700 43.43 -108.63
REMARK 500
REMARK 500 THIS ENTRY HAS 124 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 ARG H 80 ASP H 81 -149.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR G 57 0.08 SIDE CHAIN
REMARK 500 TYR G 429 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 TYR A 654 21.26
REMARK 500 VAL B 508 -22.78
REMARK 500 VAL C 508 -22.98
REMARK 500 TYR C 654 -77.72
REMARK 500 VAL D 508 -16.77
REMARK 500 TYR D 654 -68.34
REMARK 500 TYR E 654 17.62
REMARK 500 CYS F 559 -29.50
REMARK 500 TYR F 654 25.44
REMARK 500
REMARK 500 REMARK: NULL
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 CA H 601 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU H 78 OE1
REMARK 620 2 ASP H 85 OD2 85.3
REMARK 620 3 ASP H 126 OD1 97.5 102.0
REMARK 620 4 GLU H 128 O 111.7 147.8 102.6
REMARK 620 5 THR H 129 O 81.9 86.5 171.5 70.0
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA H 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4GZ8 RELATED DB: PDB
REMARK 900 RELATED ID: 4GZ9 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE OF CHAIN G IS BASED ON NCBI REFERENCE SEQUENCE: NP_
REMARK 999 033178.2. RESIDUE 475 IS A VAL IN THIS DATABASE SEQUENCE.
DBREF 4GZA A 33 703 UNP P70207 PLXA2_MOUSE 33 703
DBREF 4GZA B 33 703 UNP P70207 PLXA2_MOUSE 33 703
DBREF 4GZA C 33 703 UNP P70207 PLXA2_MOUSE 33 703
DBREF 4GZA D 33 703 UNP P70207 PLXA2_MOUSE 33 703
DBREF 4GZA E 33 703 UNP P70207 PLXA2_MOUSE 33 703
DBREF 4GZA F 33 703 UNP P70207 PLXA2_MOUSE 33 703
DBREF 4GZA G 21 555 UNP O08665 SEM3A_MOUSE 21 555
DBREF 4GZA H 22 586 UNP P97333 NRP1_MOUSE 22 586
SEQADV 4GZA GLU A 32 UNP P70207 EXPRESSION TAG
SEQADV 4GZA GLY A 704 UNP P70207 EXPRESSION TAG
SEQADV 4GZA THR A 705 UNP P70207 EXPRESSION TAG
SEQADV 4GZA LYS A 706 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS A 707 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS A 708 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS A 709 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS A 710 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS A 711 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS A 712 UNP P70207 EXPRESSION TAG
SEQADV 4GZA GLU B 32 UNP P70207 EXPRESSION TAG
SEQADV 4GZA GLY B 704 UNP P70207 EXPRESSION TAG
SEQADV 4GZA THR B 705 UNP P70207 EXPRESSION TAG
SEQADV 4GZA LYS B 706 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS B 707 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS B 708 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS B 709 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS B 710 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS B 711 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS B 712 UNP P70207 EXPRESSION TAG
SEQADV 4GZA GLU C 32 UNP P70207 EXPRESSION TAG
SEQADV 4GZA GLY C 704 UNP P70207 EXPRESSION TAG
SEQADV 4GZA THR C 705 UNP P70207 EXPRESSION TAG
SEQADV 4GZA LYS C 706 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS C 707 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS C 708 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS C 709 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS C 710 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS C 711 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS C 712 UNP P70207 EXPRESSION TAG
SEQADV 4GZA GLU D 32 UNP P70207 EXPRESSION TAG
SEQADV 4GZA GLY D 704 UNP P70207 EXPRESSION TAG
SEQADV 4GZA THR D 705 UNP P70207 EXPRESSION TAG
SEQADV 4GZA LYS D 706 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS D 707 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS D 708 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS D 709 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS D 710 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS D 711 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS D 712 UNP P70207 EXPRESSION TAG
SEQADV 4GZA GLU E 32 UNP P70207 EXPRESSION TAG
SEQADV 4GZA GLY E 704 UNP P70207 EXPRESSION TAG
SEQADV 4GZA THR E 705 UNP P70207 EXPRESSION TAG
SEQADV 4GZA LYS E 706 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS E 707 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS E 708 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS E 709 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS E 710 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS E 711 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS E 712 UNP P70207 EXPRESSION TAG
SEQADV 4GZA GLU F 32 UNP P70207 EXPRESSION TAG
SEQADV 4GZA GLY F 704 UNP P70207 EXPRESSION TAG
SEQADV 4GZA THR F 705 UNP P70207 EXPRESSION TAG
SEQADV 4GZA LYS F 706 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS F 707 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS F 708 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS F 709 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS F 710 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS F 711 UNP P70207 EXPRESSION TAG
SEQADV 4GZA HIS F 712 UNP P70207 EXPRESSION TAG
SEQADV 4GZA GLU G 18 UNP O08665 EXPRESSION TAG
SEQADV 4GZA THR G 19 UNP O08665 EXPRESSION TAG
SEQADV 4GZA GLY G 20 UNP O08665 EXPRESSION TAG
SEQADV 4GZA VAL G 475 UNP O08665 ILE 475 SEE REMARK 999
SEQADV 4GZA GLU H 19 UNP P97333 EXPRESSION TAG
SEQADV 4GZA THR H 20 UNP P97333 EXPRESSION TAG
SEQADV 4GZA GLY H 21 UNP P97333 EXPRESSION TAG
SEQADV 4GZA ARG H 587 UNP P97333 EXPRESSION TAG
SEQADV 4GZA THR H 588 UNP P97333 EXPRESSION TAG
SEQADV 4GZA LYS H 589 UNP P97333 EXPRESSION TAG
SEQADV 4GZA HIS H 590 UNP P97333 EXPRESSION TAG
SEQADV 4GZA HIS H 591 UNP P97333 EXPRESSION TAG
SEQADV 4GZA HIS H 592 UNP P97333 EXPRESSION TAG
SEQADV 4GZA HIS H 593 UNP P97333 EXPRESSION TAG
SEQADV 4GZA HIS H 594 UNP P97333 EXPRESSION TAG
SEQADV 4GZA HIS H 595 UNP P97333 EXPRESSION TAG
SEQRES 1 A 681 GLU THR GLY MET PRO GLN TYR SER THR PHE HIS SER GLU
SEQRES 2 A 681 ASN ARG ASP TRP THR PHE ASN HIS LEU THR VAL HIS ARG
SEQRES 3 A 681 ARG THR GLY ALA VAL TYR VAL GLY ALA ILE ASN ARG VAL
SEQRES 4 A 681 TYR LYS LEU THR GLY ASN LEU THR ILE GLN VAL ALA HIS
SEQRES 5 A 681 LYS THR GLY PRO GLU GLU ASP ASN LYS ALA CYS TYR PRO
SEQRES 6 A 681 PRO LEU ILE VAL GLN PRO CYS SER GLU VAL LEU THR LEU
SEQRES 7 A 681 THR ASN ASN VAL ASN LYS LEU LEU ILE ILE ASP TYR SER
SEQRES 8 A 681 GLU ASN ARG LEU LEU ALA CYS GLY SER LEU TYR GLN GLY
SEQRES 9 A 681 VAL CYS LYS LEU LEU ARG LEU ASP ASP LEU PHE ILE LEU
SEQRES 10 A 681 VAL GLU PRO SER HIS LYS LYS GLU HIS TYR LEU SER SER
SEQRES 11 A 681 VAL ASN LYS THR GLY THR MET TYR GLY VAL ILE VAL ARG
SEQRES 12 A 681 SER GLU GLY GLU ASP GLY LYS LEU PHE ILE GLY THR ALA
SEQRES 13 A 681 VAL ASP GLY LYS GLN ASP TYR PHE PRO THR LEU SER SER
SEQRES 14 A 681 ARG LYS LEU PRO ARG ASP PRO GLU SER SER ALA MET LEU
SEQRES 15 A 681 ASP TYR GLU LEU HIS SER ASP PHE VAL SER SER LEU ILE
SEQRES 16 A 681 LYS ILE PRO SER ASP THR LEU ALA LEU VAL SER HIS PHE
SEQRES 17 A 681 ASP ILE PHE TYR ILE TYR GLY PHE ALA SER GLY GLY PHE
SEQRES 18 A 681 VAL TYR PHE LEU THR VAL GLN PRO GLU THR PRO ASP GLY
SEQRES 19 A 681 MET ALA ILE ASN SER ALA GLY ASP LEU PHE TYR THR SER
SEQRES 20 A 681 ARG ILE VAL ARG LEU CYS LYS ASP ASP PRO LYS PHE HIS
SEQRES 21 A 681 SER TYR VAL SER LEU PRO PHE GLY CYS THR ARG ALA GLY
SEQRES 22 A 681 VAL GLU TYR ARG LEU LEU GLN ALA ALA TYR LEU ALA LYS
SEQRES 23 A 681 PRO GLY GLU ALA LEU ALA GLN ALA PHE ASN ILE SER SER
SEQRES 24 A 681 ASP GLU ASP VAL LEU PHE ALA ILE PHE SER LYS GLY GLN
SEQRES 25 A 681 LYS GLN TYR HIS HIS PRO PRO ASP ASP SER ALA LEU CYS
SEQRES 26 A 681 ALA PHE PRO ILE ARG ALA ILE ASN LEU GLN ILE LYS GLU
SEQRES 27 A 681 ARG LEU GLN SER CYS TYR HIS GLY GLU GLY ASN LEU GLU
SEQRES 28 A 681 LEU ASN TRP LEU LEU GLY LYS ASP VAL GLN CYS THR LYS
SEQRES 29 A 681 ALA PRO VAL PRO ILE ASP ASP ASN PHE CYS GLY LEU ASP
SEQRES 30 A 681 ILE ASN GLN PRO LEU GLY GLY SER THR PRO VAL GLU GLY
SEQRES 31 A 681 LEU THR LEU TYR THR THR SER ARG ASP ARG LEU THR SER
SEQRES 32 A 681 VAL ALA SER TYR VAL TYR ASN GLY TYR SER VAL VAL PHE
SEQRES 33 A 681 VAL GLY THR LYS SER GLY LYS LEU LYS LYS ILE ARG ALA
SEQRES 34 A 681 ASP GLY PRO PRO HIS GLY GLY VAL GLN TYR GLU MET VAL
SEQRES 35 A 681 SER VAL PHE LYS ASP GLY SER PRO ILE LEU ARG ASP MET
SEQRES 36 A 681 ALA PHE SER ILE ASN GLN LEU TYR LEU TYR VAL MET SER
SEQRES 37 A 681 GLU ARG GLN VAL THR ARG VAL PRO VAL GLU SER CYS GLU
SEQRES 38 A 681 GLN TYR THR THR CYS GLY GLU CYS LEU SER SER GLY ASP
SEQRES 39 A 681 PRO HIS CYS GLY TRP CYS ALA LEU HIS ASN MET CYS SER
SEQRES 40 A 681 ARG ARG ASP LYS CYS GLN ARG ALA TRP GLU ALA ASN ARG
SEQRES 41 A 681 PHE ALA ALA SER ILE SER GLN CYS MET SER LEU GLU VAL
SEQRES 42 A 681 HIS PRO ASN SER ILE SER VAL SER ASP HIS SER ARG LEU
SEQRES 43 A 681 LEU SER LEU VAL VAL ASN ASP ALA PRO ASN LEU SER GLU
SEQRES 44 A 681 GLY ILE ALA CYS ALA PHE GLY ASN LEU THR GLU VAL GLU
SEQRES 45 A 681 GLY GLN VAL SER GLY SER GLN VAL ILE CYS ILE SER PRO
SEQRES 46 A 681 GLY PRO LYS ASP VAL PRO VAL ILE PRO LEU ASP GLN ASP
SEQRES 47 A 681 TRP PHE GLY LEU GLU LEU GLN LEU ARG SER LYS GLU THR
SEQRES 48 A 681 GLY LYS ILE PHE VAL SER THR GLU PHE LYS PHE TYR ASN
SEQRES 49 A 681 CYS SER ALA HIS GLN LEU CYS LEU SER CYS VAL ASN SER
SEQRES 50 A 681 ALA PHE ARG CYS HIS TRP CYS LYS TYR ARG ASN LEU CYS
SEQRES 51 A 681 THR HIS ASP PRO THR THR CYS SER PHE GLN GLU GLY ARG
SEQRES 52 A 681 ILE ASN VAL SER GLU ASP CYS PRO GLN GLY THR LYS HIS
SEQRES 53 A 681 HIS HIS HIS HIS HIS
SEQRES 1 B 681 GLU THR GLY MET PRO GLN TYR SER THR PHE HIS SER GLU
SEQRES 2 B 681 ASN ARG ASP TRP THR PHE ASN HIS LEU THR VAL HIS ARG
SEQRES 3 B 681 ARG THR GLY ALA VAL TYR VAL GLY ALA ILE ASN ARG VAL
SEQRES 4 B 681 TYR LYS LEU THR GLY ASN LEU THR ILE GLN VAL ALA HIS
SEQRES 5 B 681 LYS THR GLY PRO GLU GLU ASP ASN LYS ALA CYS TYR PRO
SEQRES 6 B 681 PRO LEU ILE VAL GLN PRO CYS SER GLU VAL LEU THR LEU
SEQRES 7 B 681 THR ASN ASN VAL ASN LYS LEU LEU ILE ILE ASP TYR SER
SEQRES 8 B 681 GLU ASN ARG LEU LEU ALA CYS GLY SER LEU TYR GLN GLY
SEQRES 9 B 681 VAL CYS LYS LEU LEU ARG LEU ASP ASP LEU PHE ILE LEU
SEQRES 10 B 681 VAL GLU PRO SER HIS LYS LYS GLU HIS TYR LEU SER SER
SEQRES 11 B 681 VAL ASN LYS THR GLY THR MET TYR GLY VAL ILE VAL ARG
SEQRES 12 B 681 SER GLU GLY GLU ASP GLY LYS LEU PHE ILE GLY THR ALA
SEQRES 13 B 681 VAL ASP GLY LYS GLN ASP TYR PHE PRO THR LEU SER SER
SEQRES 14 B 681 ARG LYS LEU PRO ARG ASP PRO GLU SER SER ALA MET LEU
SEQRES 15 B 681 ASP TYR GLU LEU HIS SER ASP PHE VAL SER SER LEU ILE
SEQRES 16 B 681 LYS ILE PRO SER ASP THR LEU ALA LEU VAL SER HIS PHE
SEQRES 17 B 681 ASP ILE PHE TYR ILE TYR GLY PHE ALA SER GLY GLY PHE
SEQRES 18 B 681 VAL TYR PHE LEU THR VAL GLN PRO GLU THR PRO ASP GLY
SEQRES 19 B 681 MET ALA ILE ASN SER ALA GLY ASP LEU PHE TYR THR SER
SEQRES 20 B 681 ARG ILE VAL ARG LEU CYS LYS ASP ASP PRO LYS PHE HIS
SEQRES 21 B 681 SER TYR VAL SER LEU PRO PHE GLY CYS THR ARG ALA GLY
SEQRES 22 B 681 VAL GLU TYR ARG LEU LEU GLN ALA ALA TYR LEU ALA LYS
SEQRES 23 B 681 PRO GLY GLU ALA LEU ALA GLN ALA PHE ASN ILE SER SER
SEQRES 24 B 681 ASP GLU ASP VAL LEU PHE ALA ILE PHE SER LYS GLY GLN
SEQRES 25 B 681 LYS GLN TYR HIS HIS PRO PRO ASP ASP SER ALA LEU CYS
SEQRES 26 B 681 ALA PHE PRO ILE ARG ALA ILE ASN LEU GLN ILE LYS GLU
SEQRES 27 B 681 ARG LEU GLN SER CYS TYR HIS GLY GLU GLY ASN LEU GLU
SEQRES 28 B 681 LEU ASN TRP LEU LEU GLY LYS ASP VAL GLN CYS THR LYS
SEQRES 29 B 681 ALA PRO VAL PRO ILE ASP ASP ASN PHE CYS GLY LEU ASP
SEQRES 30 B 681 ILE ASN GLN PRO LEU GLY GLY SER THR PRO VAL GLU GLY
SEQRES 31 B 681 LEU THR LEU TYR THR THR SER ARG ASP ARG LEU THR SER
SEQRES 32 B 681 VAL ALA SER TYR VAL TYR ASN GLY TYR SER VAL VAL PHE
SEQRES 33 B 681 VAL GLY THR LYS SER GLY LYS LEU LYS LYS ILE ARG ALA
SEQRES 34 B 681 ASP GLY PRO PRO HIS GLY GLY VAL GLN TYR GLU MET VAL
SEQRES 35 B 681 SER VAL PHE LYS ASP GLY SER PRO ILE LEU ARG ASP MET
SEQRES 36 B 681 ALA PHE SER ILE ASN GLN LEU TYR LEU TYR VAL MET SER
SEQRES 37 B 681 GLU ARG GLN VAL THR ARG VAL PRO VAL GLU SER CYS GLU
SEQRES 38 B 681 GLN TYR THR THR CYS GLY GLU CYS LEU SER SER GLY ASP
SEQRES 39 B 681 PRO HIS CYS GLY TRP CYS ALA LEU HIS ASN MET CYS SER
SEQRES 40 B 681 ARG ARG ASP LYS CYS GLN ARG ALA TRP GLU ALA ASN ARG
SEQRES 41 B 681 PHE ALA ALA SER ILE SER GLN CYS MET SER LEU GLU VAL
SEQRES 42 B 681 HIS PRO ASN SER ILE SER VAL SER ASP HIS SER ARG LEU
SEQRES 43 B 681 LEU SER LEU VAL VAL ASN ASP ALA PRO ASN LEU SER GLU
SEQRES 44 B 681 GLY ILE ALA CYS ALA PHE GLY ASN LEU THR GLU VAL GLU
SEQRES 45 B 681 GLY GLN VAL SER GLY SER GLN VAL ILE CYS ILE SER PRO
SEQRES 46 B 681 GLY PRO LYS ASP VAL PRO VAL ILE PRO LEU ASP GLN ASP
SEQRES 47 B 681 TRP PHE GLY LEU GLU LEU GLN LEU ARG SER LYS GLU THR
SEQRES 48 B 681 GLY LYS ILE PHE VAL SER THR GLU PHE LYS PHE TYR ASN
SEQRES 49 B 681 CYS SER ALA HIS GLN LEU CYS LEU SER CYS VAL ASN SER
SEQRES 50 B 681 ALA PHE ARG CYS HIS TRP CYS LYS TYR ARG ASN LEU CYS
SEQRES 51 B 681 THR HIS ASP PRO THR THR CYS SER PHE GLN GLU GLY ARG
SEQRES 52 B 681 ILE ASN VAL SER GLU ASP CYS PRO GLN GLY THR LYS HIS
SEQRES 53 B 681 HIS HIS HIS HIS HIS
SEQRES 1 C 681 GLU THR GLY MET PRO GLN TYR SER THR PHE HIS SER GLU
SEQRES 2 C 681 ASN ARG ASP TRP THR PHE ASN HIS LEU THR VAL HIS ARG
SEQRES 3 C 681 ARG THR GLY ALA VAL TYR VAL GLY ALA ILE ASN ARG VAL
SEQRES 4 C 681 TYR LYS LEU THR GLY ASN LEU THR ILE GLN VAL ALA HIS
SEQRES 5 C 681 LYS THR GLY PRO GLU GLU ASP ASN LYS ALA CYS TYR PRO
SEQRES 6 C 681 PRO LEU ILE VAL GLN PRO CYS SER GLU VAL LEU THR LEU
SEQRES 7 C 681 THR ASN ASN VAL ASN LYS LEU LEU ILE ILE ASP TYR SER
SEQRES 8 C 681 GLU ASN ARG LEU LEU ALA CYS GLY SER LEU TYR GLN GLY
SEQRES 9 C 681 VAL CYS LYS LEU LEU ARG LEU ASP ASP LEU PHE ILE LEU
SEQRES 10 C 681 VAL GLU PRO SER HIS LYS LYS GLU HIS TYR LEU SER SER
SEQRES 11 C 681 VAL ASN LYS THR GLY THR MET TYR GLY VAL ILE VAL ARG
SEQRES 12 C 681 SER GLU GLY GLU ASP GLY LYS LEU PHE ILE GLY THR ALA
SEQRES 13 C 681 VAL ASP GLY LYS GLN ASP TYR PHE PRO THR LEU SER SER
SEQRES 14 C 681 ARG LYS LEU PRO ARG ASP PRO GLU SER SER ALA MET LEU
SEQRES 15 C 681 ASP TYR GLU LEU HIS SER ASP PHE VAL SER SER LEU ILE
SEQRES 16 C 681 LYS ILE PRO SER ASP THR LEU ALA LEU VAL SER HIS PHE
SEQRES 17 C 681 ASP ILE PHE TYR ILE TYR GLY PHE ALA SER GLY GLY PHE
SEQRES 18 C 681 VAL TYR PHE LEU THR VAL GLN PRO GLU THR PRO ASP GLY
SEQRES 19 C 681 MET ALA ILE ASN SER ALA GLY ASP LEU PHE TYR THR SER
SEQRES 20 C 681 ARG ILE VAL ARG LEU CYS LYS ASP ASP PRO LYS PHE HIS
SEQRES 21 C 681 SER TYR VAL SER LEU PRO PHE GLY CYS THR ARG ALA GLY
SEQRES 22 C 681 VAL GLU TYR ARG LEU LEU GLN ALA ALA TYR LEU ALA LYS
SEQRES 23 C 681 PRO GLY GLU ALA LEU ALA GLN ALA PHE ASN ILE SER SER
SEQRES 24 C 681 ASP GLU ASP VAL LEU PHE ALA ILE PHE SER LYS GLY GLN
SEQRES 25 C 681 LYS GLN TYR HIS HIS PRO PRO ASP ASP SER ALA LEU CYS
SEQRES 26 C 681 ALA PHE PRO ILE ARG ALA ILE ASN LEU GLN ILE LYS GLU
SEQRES 27 C 681 ARG LEU GLN SER CYS TYR HIS GLY GLU GLY ASN LEU GLU
SEQRES 28 C 681 LEU ASN TRP LEU LEU GLY LYS ASP VAL GLN CYS THR LYS
SEQRES 29 C 681 ALA PRO VAL PRO ILE ASP ASP ASN PHE CYS GLY LEU ASP
SEQRES 30 C 681 ILE ASN GLN PRO LEU GLY GLY SER THR PRO VAL GLU GLY
SEQRES 31 C 681 LEU THR LEU TYR THR THR SER ARG ASP ARG LEU THR SER
SEQRES 32 C 681 VAL ALA SER TYR VAL TYR ASN GLY TYR SER VAL VAL PHE
SEQRES 33 C 681 VAL GLY THR LYS SER GLY LYS LEU LYS LYS ILE ARG ALA
SEQRES 34 C 681 ASP GLY PRO PRO HIS GLY GLY VAL GLN TYR GLU MET VAL
SEQRES 35 C 681 SER VAL PHE LYS ASP GLY SER PRO ILE LEU ARG ASP MET
SEQRES 36 C 681 ALA PHE SER ILE ASN GLN LEU TYR LEU TYR VAL MET SER
SEQRES 37 C 681 GLU ARG GLN VAL THR ARG VAL PRO VAL GLU SER CYS GLU
SEQRES 38 C 681 GLN TYR THR THR CYS GLY GLU CYS LEU SER SER GLY ASP
SEQRES 39 C 681 PRO HIS CYS GLY TRP CYS ALA LEU HIS ASN MET CYS SER
SEQRES 40 C 681 ARG ARG ASP LYS CYS GLN ARG ALA TRP GLU ALA ASN ARG
SEQRES 41 C 681 PHE ALA ALA SER ILE SER GLN CYS MET SER LEU GLU VAL
SEQRES 42 C 681 HIS PRO ASN SER ILE SER VAL SER ASP HIS SER ARG LEU
SEQRES 43 C 681 LEU SER LEU VAL VAL ASN ASP ALA PRO ASN LEU SER GLU
SEQRES 44 C 681 GLY ILE ALA CYS ALA PHE GLY ASN LEU THR GLU VAL GLU
SEQRES 45 C 681 GLY GLN VAL SER GLY SER GLN VAL ILE CYS ILE SER PRO
SEQRES 46 C 681 GLY PRO LYS ASP VAL PRO VAL ILE PRO LEU ASP GLN ASP
SEQRES 47 C 681 TRP PHE GLY LEU GLU LEU GLN LEU ARG SER LYS GLU THR
SEQRES 48 C 681 GLY LYS ILE PHE VAL SER THR GLU PHE LYS PHE TYR ASN
SEQRES 49 C 681 CYS SER ALA HIS GLN LEU CYS LEU SER CYS VAL ASN SER
SEQRES 50 C 681 ALA PHE ARG CYS HIS TRP CYS LYS TYR ARG ASN LEU CYS
SEQRES 51 C 681 THR HIS ASP PRO THR THR CYS SER PHE GLN GLU GLY ARG
SEQRES 52 C 681 ILE ASN VAL SER GLU ASP CYS PRO GLN GLY THR LYS HIS
SEQRES 53 C 681 HIS HIS HIS HIS HIS
SEQRES 1 D 681 GLU THR GLY MET PRO GLN TYR SER THR PHE HIS SER GLU
SEQRES 2 D 681 ASN ARG ASP TRP THR PHE ASN HIS LEU THR VAL HIS ARG
SEQRES 3 D 681 ARG THR GLY ALA VAL TYR VAL GLY ALA ILE ASN ARG VAL
SEQRES 4 D 681 TYR LYS LEU THR GLY ASN LEU THR ILE GLN VAL ALA HIS
SEQRES 5 D 681 LYS THR GLY PRO GLU GLU ASP ASN LYS ALA CYS TYR PRO
SEQRES 6 D 681 PRO LEU ILE VAL GLN PRO CYS SER GLU VAL LEU THR LEU
SEQRES 7 D 681 THR ASN ASN VAL ASN LYS LEU LEU ILE ILE ASP TYR SER
SEQRES 8 D 681 GLU ASN ARG LEU LEU ALA CYS GLY SER LEU TYR GLN GLY
SEQRES 9 D 681 VAL CYS LYS LEU LEU ARG LEU ASP ASP LEU PHE ILE LEU
SEQRES 10 D 681 VAL GLU PRO SER HIS LYS LYS GLU HIS TYR LEU SER SER
SEQRES 11 D 681 VAL ASN LYS THR GLY THR MET TYR GLY VAL ILE VAL ARG
SEQRES 12 D 681 SER GLU GLY GLU ASP GLY LYS LEU PHE ILE GLY THR ALA
SEQRES 13 D 681 VAL ASP GLY LYS GLN ASP TYR PHE PRO THR LEU SER SER
SEQRES 14 D 681 ARG LYS LEU PRO ARG ASP PRO GLU SER SER ALA MET LEU
SEQRES 15 D 681 ASP TYR GLU LEU HIS SER ASP PHE VAL SER SER LEU ILE
SEQRES 16 D 681 LYS ILE PRO SER ASP THR LEU ALA LEU VAL SER HIS PHE
SEQRES 17 D 681 ASP ILE PHE TYR ILE TYR GLY PHE ALA SER GLY GLY PHE
SEQRES 18 D 681 VAL TYR PHE LEU THR VAL GLN PRO GLU THR PRO ASP GLY
SEQRES 19 D 681 MET ALA ILE ASN SER ALA GLY ASP LEU PHE TYR THR SER
SEQRES 20 D 681 ARG ILE VAL ARG LEU CYS LYS ASP ASP PRO LYS PHE HIS
SEQRES 21 D 681 SER TYR VAL SER LEU PRO PHE GLY CYS THR ARG ALA GLY
SEQRES 22 D 681 VAL GLU TYR ARG LEU LEU GLN ALA ALA TYR LEU ALA LYS
SEQRES 23 D 681 PRO GLY GLU ALA LEU ALA GLN ALA PHE ASN ILE SER SER
SEQRES 24 D 681 ASP GLU ASP VAL LEU PHE ALA ILE PHE SER LYS GLY GLN
SEQRES 25 D 681 LYS GLN TYR HIS HIS PRO PRO ASP ASP SER ALA LEU CYS
SEQRES 26 D 681 ALA PHE PRO ILE ARG ALA ILE ASN LEU GLN ILE LYS GLU
SEQRES 27 D 681 ARG LEU GLN SER CYS TYR HIS GLY GLU GLY ASN LEU GLU
SEQRES 28 D 681 LEU ASN TRP LEU LEU GLY LYS ASP VAL GLN CYS THR LYS
SEQRES 29 D 681 ALA PRO VAL PRO ILE ASP ASP ASN PHE CYS GLY LEU ASP
SEQRES 30 D 681 ILE ASN GLN PRO LEU GLY GLY SER THR PRO VAL GLU GLY
SEQRES 31 D 681 LEU THR LEU TYR THR THR SER ARG ASP ARG LEU THR SER
SEQRES 32 D 681 VAL ALA SER TYR VAL TYR ASN GLY TYR SER VAL VAL PHE
SEQRES 33 D 681 VAL GLY THR LYS SER GLY LYS LEU LYS LYS ILE ARG ALA
SEQRES 34 D 681 ASP GLY PRO PRO HIS GLY GLY VAL GLN TYR GLU MET VAL
SEQRES 35 D 681 SER VAL PHE LYS ASP GLY SER PRO ILE LEU ARG ASP MET
SEQRES 36 D 681 ALA PHE SER ILE ASN GLN LEU TYR LEU TYR VAL MET SER
SEQRES 37 D 681 GLU ARG GLN VAL THR ARG VAL PRO VAL GLU SER CYS GLU
SEQRES 38 D 681 GLN TYR THR THR CYS GLY GLU CYS LEU SER SER GLY ASP
SEQRES 39 D 681 PRO HIS CYS GLY TRP CYS ALA LEU HIS ASN MET CYS SER
SEQRES 40 D 681 ARG ARG ASP LYS CYS GLN ARG ALA TRP GLU ALA ASN ARG
SEQRES 41 D 681 PHE ALA ALA SER ILE SER GLN CYS MET SER LEU GLU VAL
SEQRES 42 D 681 HIS PRO ASN SER ILE SER VAL SER ASP HIS SER ARG LEU
SEQRES 43 D 681 LEU SER LEU VAL VAL ASN ASP ALA PRO ASN LEU SER GLU
SEQRES 44 D 681 GLY ILE ALA CYS ALA PHE GLY ASN LEU THR GLU VAL GLU
SEQRES 45 D 681 GLY GLN VAL SER GLY SER GLN VAL ILE CYS ILE SER PRO
SEQRES 46 D 681 GLY PRO LYS ASP VAL PRO VAL ILE PRO LEU ASP GLN ASP
SEQRES 47 D 681 TRP PHE GLY LEU GLU LEU GLN LEU ARG SER LYS GLU THR
SEQRES 48 D 681 GLY LYS ILE PHE VAL SER THR GLU PHE LYS PHE TYR ASN
SEQRES 49 D 681 CYS SER ALA HIS GLN LEU CYS LEU SER CYS VAL ASN SER
SEQRES 50 D 681 ALA PHE ARG CYS HIS TRP CYS LYS TYR ARG ASN LEU CYS
SEQRES 51 D 681 THR HIS ASP PRO THR THR CYS SER PHE GLN GLU GLY ARG
SEQRES 52 D 681 ILE ASN VAL SER GLU ASP CYS PRO GLN GLY THR LYS HIS
SEQRES 53 D 681 HIS HIS HIS HIS HIS
SEQRES 1 E 681 GLU THR GLY MET PRO GLN TYR SER THR PHE HIS SER GLU
SEQRES 2 E 681 ASN ARG ASP TRP THR PHE ASN HIS LEU THR VAL HIS ARG
SEQRES 3 E 681 ARG THR GLY ALA VAL TYR VAL GLY ALA ILE ASN ARG VAL
SEQRES 4 E 681 TYR LYS LEU THR GLY ASN LEU THR ILE GLN VAL ALA HIS
SEQRES 5 E 681 LYS THR GLY PRO GLU GLU ASP ASN LYS ALA CYS TYR PRO
SEQRES 6 E 681 PRO LEU ILE VAL GLN PRO CYS SER GLU VAL LEU THR LEU
SEQRES 7 E 681 THR ASN ASN VAL ASN LYS LEU LEU ILE ILE ASP TYR SER
SEQRES 8 E 681 GLU ASN ARG LEU LEU ALA CYS GLY SER LEU TYR GLN GLY
SEQRES 9 E 681 VAL CYS LYS LEU LEU ARG LEU ASP ASP LEU PHE ILE LEU
SEQRES 10 E 681 VAL GLU PRO SER HIS LYS LYS GLU HIS TYR LEU SER SER
SEQRES 11 E 681 VAL ASN LYS THR GLY THR MET TYR GLY VAL ILE VAL ARG
SEQRES 12 E 681 SER GLU GLY GLU ASP GLY LYS LEU PHE ILE GLY THR ALA
SEQRES 13 E 681 VAL ASP GLY LYS GLN ASP TYR PHE PRO THR LEU SER SER
SEQRES 14 E 681 ARG LYS LEU PRO ARG ASP PRO GLU SER SER ALA MET LEU
SEQRES 15 E 681 ASP TYR GLU LEU HIS SER ASP PHE VAL SER SER LEU ILE
SEQRES 16 E 681 LYS ILE PRO SER ASP THR LEU ALA LEU VAL SER HIS PHE
SEQRES 17 E 681 ASP ILE PHE TYR ILE TYR GLY PHE ALA SER GLY GLY PHE
SEQRES 18 E 681 VAL TYR PHE LEU THR VAL GLN PRO GLU THR PRO ASP GLY
SEQRES 19 E 681 MET ALA ILE ASN SER ALA GLY ASP LEU PHE TYR THR SER
SEQRES 20 E 681 ARG ILE VAL ARG LEU CYS LYS ASP ASP PRO LYS PHE HIS
SEQRES 21 E 681 SER TYR VAL SER LEU PRO PHE GLY CYS THR ARG ALA GLY
SEQRES 22 E 681 VAL GLU TYR ARG LEU LEU GLN ALA ALA TYR LEU ALA LYS
SEQRES 23 E 681 PRO GLY GLU ALA LEU ALA GLN ALA PHE ASN ILE SER SER
SEQRES 24 E 681 ASP GLU ASP VAL LEU PHE ALA ILE PHE SER LYS GLY GLN
SEQRES 25 E 681 LYS GLN TYR HIS HIS PRO PRO ASP ASP SER ALA LEU CYS
SEQRES 26 E 681 ALA PHE PRO ILE ARG ALA ILE ASN LEU GLN ILE LYS GLU
SEQRES 27 E 681 ARG LEU GLN SER CYS TYR HIS GLY GLU GLY ASN LEU GLU
SEQRES 28 E 681 LEU ASN TRP LEU LEU GLY LYS ASP VAL GLN CYS THR LYS
SEQRES 29 E 681 ALA PRO VAL PRO ILE ASP ASP ASN PHE CYS GLY LEU ASP
SEQRES 30 E 681 ILE ASN GLN PRO LEU GLY GLY SER THR PRO VAL GLU GLY
SEQRES 31 E 681 LEU THR LEU TYR THR THR SER ARG ASP ARG LEU THR SER
SEQRES 32 E 681 VAL ALA SER TYR VAL TYR ASN GLY TYR SER VAL VAL PHE
SEQRES 33 E 681 VAL GLY THR LYS SER GLY LYS LEU LYS LYS ILE ARG ALA
SEQRES 34 E 681 ASP GLY PRO PRO HIS GLY GLY VAL GLN TYR GLU MET VAL
SEQRES 35 E 681 SER VAL PHE LYS ASP GLY SER PRO ILE LEU ARG ASP MET
SEQRES 36 E 681 ALA PHE SER ILE ASN GLN LEU TYR LEU TYR VAL MET SER
SEQRES 37 E 681 GLU ARG GLN VAL THR ARG VAL PRO VAL GLU SER CYS GLU
SEQRES 38 E 681 GLN TYR THR THR CYS GLY GLU CYS LEU SER SER GLY ASP
SEQRES 39 E 681 PRO HIS CYS GLY TRP CYS ALA LEU HIS ASN MET CYS SER
SEQRES 40 E 681 ARG ARG ASP LYS CYS GLN ARG ALA TRP GLU ALA ASN ARG
SEQRES 41 E 681 PHE ALA ALA SER ILE SER GLN CYS MET SER LEU GLU VAL
SEQRES 42 E 681 HIS PRO ASN SER ILE SER VAL SER ASP HIS SER ARG LEU
SEQRES 43 E 681 LEU SER LEU VAL VAL ASN ASP ALA PRO ASN LEU SER GLU
SEQRES 44 E 681 GLY ILE ALA CYS ALA PHE GLY ASN LEU THR GLU VAL GLU
SEQRES 45 E 681 GLY GLN VAL SER GLY SER GLN VAL ILE CYS ILE SER PRO
SEQRES 46 E 681 GLY PRO LYS ASP VAL PRO VAL ILE PRO LEU ASP GLN ASP
SEQRES 47 E 681 TRP PHE GLY LEU GLU LEU GLN LEU ARG SER LYS GLU THR
SEQRES 48 E 681 GLY LYS ILE PHE VAL SER THR GLU PHE LYS PHE TYR ASN
SEQRES 49 E 681 CYS SER ALA HIS GLN LEU CYS LEU SER CYS VAL ASN SER
SEQRES 50 E 681 ALA PHE ARG CYS HIS TRP CYS LYS TYR ARG ASN LEU CYS
SEQRES 51 E 681 THR HIS ASP PRO THR THR CYS SER PHE GLN GLU GLY ARG
SEQRES 52 E 681 ILE ASN VAL SER GLU ASP CYS PRO GLN GLY THR LYS HIS
SEQRES 53 E 681 HIS HIS HIS HIS HIS
SEQRES 1 F 681 GLU THR GLY MET PRO GLN TYR SER THR PHE HIS SER GLU
SEQRES 2 F 681 ASN ARG ASP TRP THR PHE ASN HIS LEU THR VAL HIS ARG
SEQRES 3 F 681 ARG THR GLY ALA VAL TYR VAL GLY ALA ILE ASN ARG VAL
SEQRES 4 F 681 TYR LYS LEU THR GLY ASN LEU THR ILE GLN VAL ALA HIS
SEQRES 5 F 681 LYS THR GLY PRO GLU GLU ASP ASN LYS ALA CYS TYR PRO
SEQRES 6 F 681 PRO LEU ILE VAL GLN PRO CYS SER GLU VAL LEU THR LEU
SEQRES 7 F 681 THR ASN ASN VAL ASN LYS LEU LEU ILE ILE ASP TYR SER
SEQRES 8 F 681 GLU ASN ARG LEU LEU ALA CYS GLY SER LEU TYR GLN GLY
SEQRES 9 F 681 VAL CYS LYS LEU LEU ARG LEU ASP ASP LEU PHE ILE LEU
SEQRES 10 F 681 VAL GLU PRO SER HIS LYS LYS GLU HIS TYR LEU SER SER
SEQRES 11 F 681 VAL ASN LYS THR GLY THR MET TYR GLY VAL ILE VAL ARG
SEQRES 12 F 681 SER GLU GLY GLU ASP GLY LYS LEU PHE ILE GLY THR ALA
SEQRES 13 F 681 VAL ASP GLY LYS GLN ASP TYR PHE PRO THR LEU SER SER
SEQRES 14 F 681 ARG LYS LEU PRO ARG ASP PRO GLU SER SER ALA MET LEU
SEQRES 15 F 681 ASP TYR GLU LEU HIS SER ASP PHE VAL SER SER LEU ILE
SEQRES 16 F 681 LYS ILE PRO SER ASP THR LEU ALA LEU VAL SER HIS PHE
SEQRES 17 F 681 ASP ILE PHE TYR ILE TYR GLY PHE ALA SER GLY GLY PHE
SEQRES 18 F 681 VAL TYR PHE LEU THR VAL GLN PRO GLU THR PRO ASP GLY
SEQRES 19 F 681 MET ALA ILE ASN SER ALA GLY ASP LEU PHE TYR THR SER
SEQRES 20 F 681 ARG ILE VAL ARG LEU CYS LYS ASP ASP PRO LYS PHE HIS
SEQRES 21 F 681 SER TYR VAL SER LEU PRO PHE GLY CYS THR ARG ALA GLY
SEQRES 22 F 681 VAL GLU TYR ARG LEU LEU GLN ALA ALA TYR LEU ALA LYS
SEQRES 23 F 681 PRO GLY GLU ALA LEU ALA GLN ALA PHE ASN ILE SER SER
SEQRES 24 F 681 ASP GLU ASP VAL LEU PHE ALA ILE PHE SER LYS GLY GLN
SEQRES 25 F 681 LYS GLN TYR HIS HIS PRO PRO ASP ASP SER ALA LEU CYS
SEQRES 26 F 681 ALA PHE PRO ILE ARG ALA ILE ASN LEU GLN ILE LYS GLU
SEQRES 27 F 681 ARG LEU GLN SER CYS TYR HIS GLY GLU GLY ASN LEU GLU
SEQRES 28 F 681 LEU ASN TRP LEU LEU GLY LYS ASP VAL GLN CYS THR LYS
SEQRES 29 F 681 ALA PRO VAL PRO ILE ASP ASP ASN PHE CYS GLY LEU ASP
SEQRES 30 F 681 ILE ASN GLN PRO LEU GLY GLY SER THR PRO VAL GLU GLY
SEQRES 31 F 681 LEU THR LEU TYR THR THR SER ARG ASP ARG LEU THR SER
SEQRES 32 F 681 VAL ALA SER TYR VAL TYR ASN GLY TYR SER VAL VAL PHE
SEQRES 33 F 681 VAL GLY THR LYS SER GLY LYS LEU LYS LYS ILE ARG ALA
SEQRES 34 F 681 ASP GLY PRO PRO HIS GLY GLY VAL GLN TYR GLU MET VAL
SEQRES 35 F 681 SER VAL PHE LYS ASP GLY SER PRO ILE LEU ARG ASP MET
SEQRES 36 F 681 ALA PHE SER ILE ASN GLN LEU TYR LEU TYR VAL MET SER
SEQRES 37 F 681 GLU ARG GLN VAL THR ARG VAL PRO VAL GLU SER CYS GLU
SEQRES 38 F 681 GLN TYR THR THR CYS GLY GLU CYS LEU SER SER GLY ASP
SEQRES 39 F 681 PRO HIS CYS GLY TRP CYS ALA LEU HIS ASN MET CYS SER
SEQRES 40 F 681 ARG ARG ASP LYS CYS GLN ARG ALA TRP GLU ALA ASN ARG
SEQRES 41 F 681 PHE ALA ALA SER ILE SER GLN CYS MET SER LEU GLU VAL
SEQRES 42 F 681 HIS PRO ASN SER ILE SER VAL SER ASP HIS SER ARG LEU
SEQRES 43 F 681 LEU SER LEU VAL VAL ASN ASP ALA PRO ASN LEU SER GLU
SEQRES 44 F 681 GLY ILE ALA CYS ALA PHE GLY ASN LEU THR GLU VAL GLU
SEQRES 45 F 681 GLY GLN VAL SER GLY SER GLN VAL ILE CYS ILE SER PRO
SEQRES 46 F 681 GLY PRO LYS ASP VAL PRO VAL ILE PRO LEU ASP GLN ASP
SEQRES 47 F 681 TRP PHE GLY LEU GLU LEU GLN LEU ARG SER LYS GLU THR
SEQRES 48 F 681 GLY LYS ILE PHE VAL SER THR GLU PHE LYS PHE TYR ASN
SEQRES 49 F 681 CYS SER ALA HIS GLN LEU CYS LEU SER CYS VAL ASN SER
SEQRES 50 F 681 ALA PHE ARG CYS HIS TRP CYS LYS TYR ARG ASN LEU CYS
SEQRES 51 F 681 THR HIS ASP PRO THR THR CYS SER PHE GLN GLU GLY ARG
SEQRES 52 F 681 ILE ASN VAL SER GLU ASP CYS PRO GLN GLY THR LYS HIS
SEQRES 53 F 681 HIS HIS HIS HIS HIS
SEQRES 1 G 538 GLU THR GLY ASN TYR ALA ASN GLY LYS ASN ASN VAL PRO
SEQRES 2 G 538 ARG LEU LYS LEU SER TYR LYS GLU MET LEU GLU SER ASN
SEQRES 3 G 538 ASN VAL ILE THR PHE ASN GLY LEU ALA ASN SER SER SER
SEQRES 4 G 538 TYR HIS THR PHE LEU LEU ASP GLU GLU ARG SER ARG LEU
SEQRES 5 G 538 TYR VAL GLY ALA LYS ASP HIS ILE PHE SER PHE ASN LEU
SEQRES 6 G 538 VAL ASN ILE LYS ASP PHE GLN LYS ILE VAL TRP PRO VAL
SEQRES 7 G 538 SER TYR THR ARG ARG ASP GLU CYS LYS TRP ALA GLY LYS
SEQRES 8 G 538 ASP ILE LEU LYS GLU CYS ALA ASN PHE ILE LYS VAL LEU
SEQRES 9 G 538 GLU ALA TYR ASN GLN THR HIS LEU TYR ALA CYS GLY THR
SEQRES 10 G 538 GLY ALA PHE HIS PRO ILE CYS THR TYR ILE GLU VAL GLY
SEQRES 11 G 538 HIS HIS PRO GLU ASP ASN ILE PHE LYS LEU GLN ASP SER
SEQRES 12 G 538 HIS PHE GLU ASN GLY ARG GLY LYS SER PRO TYR ASP PRO
SEQRES 13 G 538 LYS LEU LEU THR ALA SER LEU LEU ILE ASP GLY GLU LEU
SEQRES 14 G 538 TYR SER GLY THR ALA ALA ASP PHE MET GLY ARG ASP PHE
SEQRES 15 G 538 ALA ILE PHE ARG THR LEU GLY HIS HIS HIS PRO ILE ARG
SEQRES 16 G 538 THR GLU GLN HIS ASP SER ARG TRP LEU ASN ASP PRO ARG
SEQRES 17 G 538 PHE ILE SER ALA HIS LEU ILE PRO GLU SER ASP ASN PRO
SEQRES 18 G 538 GLU ASP ASP LYS VAL TYR PHE PHE PHE ARG GLU ASN ALA
SEQRES 19 G 538 ILE ASP GLY GLU HIS SER GLY LYS ALA THR HIS ALA ARG
SEQRES 20 G 538 ILE GLY GLN ILE CYS LYS ASN ASP PHE GLY GLY HIS ARG
SEQRES 21 G 538 SER LEU VAL ASN LYS TRP THR THR PHE LEU LYS ALA ARG
SEQRES 22 G 538 LEU ILE CYS SER VAL PRO GLY PRO ASN GLY ILE ASP THR
SEQRES 23 G 538 HIS PHE ASP GLU LEU GLN ASP VAL PHE LEU MET ASN SER
SEQRES 24 G 538 LYS ASP PRO LYS ASN PRO ILE VAL TYR GLY VAL PHE THR
SEQRES 25 G 538 THR SER SER ASN ILE PHE LYS GLY SER ALA VAL CYS MET
SEQRES 26 G 538 TYR SER MET SER ASP VAL ARG ARG VAL PHE LEU GLY PRO
SEQRES 27 G 538 TYR ALA HIS ARG ASP GLY PRO ASN TYR GLN TRP VAL PRO
SEQRES 28 G 538 TYR GLN GLY ARG VAL PRO TYR PRO ARG PRO GLY THR CYS
SEQRES 29 G 538 PRO SER LYS THR PHE GLY GLY PHE ASP SER THR LYS ASP
SEQRES 30 G 538 LEU PRO ASP ASP VAL ILE THR PHE ALA ARG SER HIS PRO
SEQRES 31 G 538 ALA MET TYR ASN PRO VAL PHE PRO ILE ASN ASN ARG PRO
SEQRES 32 G 538 ILE MET ILE LYS THR ASP VAL ASN TYR GLN PHE THR GLN
SEQRES 33 G 538 ILE VAL VAL ASP ARG VAL ASP ALA GLU ASP GLY GLN TYR
SEQRES 34 G 538 ASP VAL MET PHE ILE GLY THR ASP VAL GLY THR VAL LEU
SEQRES 35 G 538 LYS VAL VAL SER VAL PRO LYS GLU THR TRP HIS ASP LEU
SEQRES 36 G 538 GLU GLU VAL LEU LEU GLU GLU MET THR VAL PHE ARG GLU
SEQRES 37 G 538 PRO THR THR ILE SER ALA MET GLU LEU SER THR LYS GLN
SEQRES 38 G 538 GLN GLN LEU TYR ILE GLY SER THR ALA GLY VAL ALA GLN
SEQRES 39 G 538 LEU PRO LEU HIS ARG CYS ASP ILE TYR GLY LYS ALA CYS
SEQRES 40 G 538 ALA GLU CYS CYS LEU ALA ARG ASP PRO TYR CYS ALA TRP
SEQRES 41 G 538 ASP GLY SER SER CYS SER ARG TYR PHE PRO THR ALA LYS
SEQRES 42 G 538 ARG ARG THR ARG ARG
SEQRES 1 H 577 GLU THR GLY PHE ARG SER ASP LYS CYS GLY GLY THR ILE
SEQRES 2 H 577 LYS ILE GLU ASN PRO GLY TYR LEU THR SER PRO GLY TYR
SEQRES 3 H 577 PRO HIS SER TYR HIS PRO SER GLU LYS CYS GLU TRP LEU
SEQRES 4 H 577 ILE GLN ALA PRO GLU PRO TYR GLN ARG ILE MET ILE ASN
SEQRES 5 H 577 PHE ASN PRO HIS PHE ASP LEU GLU ASP ARG ASP CYS LYS
SEQRES 6 H 577 TYR ASP TYR VAL GLU VAL ILE ASP GLY GLU ASN GLU GLY
SEQRES 7 H 577 GLY ARG LEU TRP GLY LYS PHE CYS GLY LYS ILE ALA PRO
SEQRES 8 H 577 SER PRO VAL VAL SER SER GLY PRO PHE LEU PHE ILE LYS
SEQRES 9 H 577 PHE VAL SER ASP TYR GLU THR HIS GLY ALA GLY PHE SER
SEQRES 10 H 577 ILE ARG TYR GLU ILE PHE LYS ARG GLY PRO GLU CYS SER
SEQRES 11 H 577 GLN ASN TYR THR ALA PRO THR GLY VAL ILE LYS SER PRO
SEQRES 12 H 577 GLY PHE PRO GLU LYS TYR PRO ASN SER LEU GLU CYS THR
SEQRES 13 H 577 TYR ILE ILE PHE ALA PRO LYS MET SER GLU ILE ILE LEU
SEQRES 14 H 577 GLU PHE GLU SER PHE ASP LEU GLU GLN ASP SER ASN PRO
SEQRES 15 H 577 PRO GLY GLY MET PHE CYS ARG TYR ASP ARG LEU GLU ILE
SEQRES 16 H 577 TRP ASP GLY PHE PRO GLU VAL GLY PRO HIS ILE GLY ARG
SEQRES 17 H 577 TYR CYS GLY GLN LYS THR PRO GLY ARG ILE ARG SER SER
SEQRES 18 H 577 SER GLY VAL LEU SER MET VAL PHE TYR THR ASP SER ALA
SEQRES 19 H 577 ILE ALA LYS GLU GLY PHE SER ALA ASN TYR SER VAL LEU
SEQRES 20 H 577 GLN SER SER ILE SER GLU ASP PHE LYS CYS MET GLU ALA
SEQRES 21 H 577 LEU GLY MET GLU SER GLY GLU ILE HIS SER ASP GLN ILE
SEQRES 22 H 577 THR ALA SER SER GLN TYR GLY THR ASN TRP SER VAL GLU
SEQRES 23 H 577 ARG SER ARG LEU ASN TYR PRO GLU ASN GLY TRP THR PRO
SEQRES 24 H 577 GLY GLU ASP SER TYR LYS GLU TRP ILE GLN VAL ASP LEU
SEQRES 25 H 577 GLY LEU LEU ARG PHE VAL THR ALA VAL GLY THR GLN GLY
SEQRES 26 H 577 ALA ILE SER LYS GLU THR LYS LYS LYS TYR TYR VAL LYS
SEQRES 27 H 577 THR TYR ARG VAL ASP ILE SER SER ASN GLY GLU ASP TRP
SEQRES 28 H 577 ILE SER LEU LYS GLU GLY ASN LYS ALA ILE ILE PHE GLN
SEQRES 29 H 577 GLY ASN THR ASN PRO THR ASP VAL VAL LEU GLY VAL PHE
SEQRES 30 H 577 SER LYS PRO LEU ILE THR ARG PHE VAL ARG ILE LYS PRO
SEQRES 31 H 577 VAL SER TRP GLU THR GLY ILE SER MET ARG PHE GLU VAL
SEQRES 32 H 577 TYR GLY CYS LYS ILE THR ASP TYR PRO CYS SER GLY MET
SEQRES 33 H 577 LEU GLY MET VAL SER GLY LEU ILE SER ASP SER GLN ILE
SEQRES 34 H 577 THR ALA SER ASN GLN ALA ASP ARG ASN TRP MET PRO GLU
SEQRES 35 H 577 ASN ILE ARG LEU VAL THR SER ARG THR GLY TRP ALA LEU
SEQRES 36 H 577 PRO PRO SER PRO HIS PRO TYR THR ASN GLU TRP LEU GLN
SEQRES 37 H 577 VAL ASP LEU GLY ASP GLU LYS ILE VAL ARG GLY VAL ILE
SEQRES 38 H 577 ILE GLN GLY GLY LYS HIS ARG GLU ASN LYS VAL PHE MET
SEQRES 39 H 577 ARG LYS PHE LYS ILE ALA TYR SER ASN ASN GLY SER ASP
SEQRES 40 H 577 TRP LYS THR ILE MET ASP ASP SER LYS ARG LYS ALA LYS
SEQRES 41 H 577 SER PHE GLU GLY ASN ASN ASN TYR ASP THR PRO GLU LEU
SEQRES 42 H 577 ARG THR PHE SER PRO LEU SER THR ARG PHE ILE ARG ILE
SEQRES 43 H 577 TYR PRO GLU ARG ALA THR HIS SER GLY LEU GLY LEU ARG
SEQRES 44 H 577 MET GLU LEU LEU GLY CYS GLU VAL GLU ARG THR LYS HIS
SEQRES 45 H 577 HIS HIS HIS HIS HIS
HET CA H 601 1
HETNAM CA CALCIUM ION
FORMUL 9 CA CA 2+
HELIX 1 1 TYR A 121 GLU A 123 5 3
HELIX 2 2 LEU A 132 GLY A 135 5 4
HELIX 3 3 LYS A 154 TYR A 158 5 5
HELIX 4 4 PRO A 229 VAL A 236 1 8
HELIX 5 5 GLY A 319 ASN A 327 1 9
HELIX 6 6 ILE A 360 TYR A 375 1 16
HELIX 7 7 LEU A 383 GLY A 388 1 6
HELIX 8 8 SER A 510 TYR A 514 5 5
HELIX 9 9 THR A 516 LEU A 521 1 6
HELIX 10 10 ARG A 539 CYS A 543 5 5
HELIX 11 11 SER A 555 CYS A 559 5 5
HELIX 12 12 CYS A 656 HIS A 659 5 4
HELIX 13 13 LEU A 661 ASN A 667 1 7
HELIX 14 14 ASP A 684 CYS A 688 5 5
HELIX 15 15 PHE A 690 GLU A 692 5 3
HELIX 16 16 VAL A 697 CYS A 701 5 5
HELIX 17 17 TYR B 121 GLU B 123 5 3
HELIX 18 18 LEU B 132 GLY B 135 5 4
HELIX 19 19 LYS B 154 TYR B 158 5 5
HELIX 20 20 PRO B 229 VAL B 236 1 8
HELIX 21 21 GLY B 319 ASN B 327 1 9
HELIX 22 22 ILE B 360 TYR B 375 1 16
HELIX 23 23 LEU B 383 GLY B 388 1 6
HELIX 24 24 SER B 510 TYR B 514 5 5
HELIX 25 25 THR B 516 LEU B 521 1 6
HELIX 26 26 ARG B 539 CYS B 543 5 5
HELIX 27 27 SER B 555 CYS B 559 5 5
HELIX 28 28 CYS B 656 HIS B 659 5 4
HELIX 29 29 LEU B 661 ASN B 667 1 7
HELIX 30 30 ASP B 684 CYS B 688 5 5
HELIX 31 31 PHE B 690 GLU B 692 5 3
HELIX 32 32 VAL B 697 CYS B 701 5 5
HELIX 33 33 TYR C 121 GLU C 123 5 3
HELIX 34 34 LEU C 132 GLY C 135 5 4
HELIX 35 35 LYS C 154 TYR C 158 5 5
HELIX 36 36 PRO C 229 VAL C 236 1 8
HELIX 37 37 GLY C 319 ASN C 327 1 9
HELIX 38 38 ILE C 360 TYR C 375 1 16
HELIX 39 39 LEU C 383 GLY C 388 1 6
HELIX 40 40 SER C 510 TYR C 514 5 5
HELIX 41 41 THR C 516 LEU C 521 1 6
HELIX 42 42 ARG C 539 CYS C 543 5 5
HELIX 43 43 SER C 555 CYS C 559 5 5
HELIX 44 44 CYS C 656 HIS C 659 5 4
HELIX 45 45 LEU C 661 ASN C 667 1 7
HELIX 46 46 ASP C 684 CYS C 688 5 5
HELIX 47 47 PHE C 690 GLU C 692 5 3
HELIX 48 48 VAL C 697 CYS C 701 5 5
HELIX 49 49 TYR D 121 GLU D 123 5 3
HELIX 50 50 LEU D 132 GLY D 135 5 4
HELIX 51 51 LYS D 154 TYR D 158 5 5
HELIX 52 52 PRO D 229 VAL D 236 1 8
HELIX 53 53 GLY D 319 ASN D 327 1 9
HELIX 54 54 ILE D 360 TYR D 375 1 16
HELIX 55 55 LEU D 383 GLY D 388 1 6
HELIX 56 56 SER D 510 TYR D 514 5 5
HELIX 57 57 THR D 516 LEU D 521 1 6
HELIX 58 58 ARG D 539 CYS D 543 5 5
HELIX 59 59 SER D 555 CYS D 559 5 5
HELIX 60 60 CYS D 656 HIS D 659 5 4
HELIX 61 61 LEU D 661 ASN D 667 1 7
HELIX 62 62 ASP D 684 CYS D 688 5 5
HELIX 63 63 PHE D 690 GLU D 692 5 3
HELIX 64 64 VAL D 697 CYS D 701 5 5
HELIX 65 65 TYR E 121 GLU E 123 5 3
HELIX 66 66 LEU E 132 GLY E 135 5 4
HELIX 67 67 LYS E 154 TYR E 158 5 5
HELIX 68 68 PRO E 229 VAL E 236 1 8
HELIX 69 69 GLY E 319 ASN E 327 1 9
HELIX 70 70 ILE E 360 TYR E 375 1 16
HELIX 71 71 LEU E 383 GLY E 388 1 6
HELIX 72 72 SER E 510 TYR E 514 5 5
HELIX 73 73 THR E 516 LEU E 521 1 6
HELIX 74 74 ARG E 539 CYS E 543 5 5
HELIX 75 75 SER E 555 CYS E 559 5 5
HELIX 76 76 CYS E 656 HIS E 659 5 4
HELIX 77 77 LEU E 661 ASN E 667 1 7
HELIX 78 78 ASP E 684 CYS E 688 5 5
HELIX 79 79 PHE E 690 GLU E 692 5 3
HELIX 80 80 VAL E 697 CYS E 701 5 5
HELIX 81 81 TYR F 121 GLU F 123 5 3
HELIX 82 82 LEU F 132 GLY F 135 5 4
HELIX 83 83 LYS F 154 TYR F 158 5 5
HELIX 84 84 PRO F 229 VAL F 236 1 8
HELIX 85 85 GLY F 319 ASN F 327 1 9
HELIX 86 86 ILE F 360 TYR F 375 1 16
HELIX 87 87 LEU F 383 GLY F 388 1 6
HELIX 88 88 SER F 510 TYR F 514 5 5
HELIX 89 89 THR F 516 LEU F 521 1 6
HELIX 90 90 ARG F 539 CYS F 543 5 5
HELIX 91 91 SER F 555 CYS F 559 5 5
HELIX 92 92 CYS F 656 HIS F 659 5 4
HELIX 93 93 LEU F 661 ASN F 667 1 7
HELIX 94 94 ASP F 684 CYS F 688 5 5
HELIX 95 95 PHE F 690 GLU F 692 5 3
HELIX 96 96 VAL F 697 CYS F 701 5 5
HELIX 97 97 SER G 35 GLU G 41 1 7
HELIX 98 98 SER G 96 ALA G 106 1 11
HELIX 99 99 ASN G 237 ASP G 240 5 4
HELIX 100 100 SER G 344 LEU G 353 1 10
HELIX 101 101 SER G 391 LEU G 395 5 5
HELIX 102 102 PRO G 396 SER G 405 1 10
HELIX 103 103 PRO G 415 ARG G 419 5 5
HELIX 104 104 ASP H 79 LYS H 83 5 5
SHEET 1 A 4 THR A 40 HIS A 42 0
SHEET 2 A 4 GLN A 502 PRO A 507 -1 O VAL A 503 N PHE A 41
SHEET 3 A 4 TYR A 494 MET A 498 -1 N VAL A 497 O THR A 504
SHEET 4 A 4 ALA A 487 PHE A 488 -1 N ALA A 487 O TYR A 496
SHEET 1 B 4 PHE A 50 VAL A 55 0
SHEET 2 B 4 VAL A 62 ALA A 66 -1 O TYR A 63 N THR A 54
SHEET 3 B 4 ARG A 69 LEU A 73 -1 O LEU A 73 N VAL A 62
SHEET 4 B 4 ILE A 79 LYS A 84 -1 O GLN A 80 N LYS A 72
SHEET 1 C 2 GLU A 88 ASP A 90 0
SHEET 2 C 2 THR A 108 THR A 110 -1 O THR A 108 N ASP A 90
SHEET 1 D 4 ASN A 114 ASP A 120 0
SHEET 2 D 4 ARG A 125 GLY A 130 -1 O LEU A 127 N ILE A 118
SHEET 3 D 4 CYS A 137 ARG A 141 -1 O LEU A 140 N LEU A 126
SHEET 4 D 4 ILE A 147 VAL A 149 -1 O LEU A 148 N LEU A 139
SHEET 1 E 4 MET A 168 VAL A 173 0
SHEET 2 E 4 LYS A 181 THR A 186 -1 O PHE A 183 N VAL A 171
SHEET 3 E 4 LEU A 198 LYS A 202 -1 O ARG A 201 N LEU A 182
SHEET 4 E 4 LEU A 225 ILE A 226 -1 O ILE A 226 N LEU A 198
SHEET 1 F 5 PHE A 242 SER A 249 0
SHEET 2 F 5 PHE A 252 PRO A 260 -1 O VAL A 258 N PHE A 242
SHEET 3 F 5 TYR A 276 CYS A 284 -1 O THR A 277 N GLN A 259
SHEET 4 F 5 VAL A 294 ARG A 302 -1 O LEU A 296 N ILE A 280
SHEET 5 F 5 VAL A 419 GLU A 420 1 O VAL A 419 N PRO A 297
SHEET 1 G 8 PHE A 242 SER A 249 0
SHEET 2 G 8 PHE A 252 PRO A 260 -1 O VAL A 258 N PHE A 242
SHEET 3 G 8 TYR A 276 CYS A 284 -1 O THR A 277 N GLN A 259
SHEET 4 G 8 VAL A 294 ARG A 302 -1 O LEU A 296 N ILE A 280
SHEET 5 G 8 VAL A 305 ALA A 316 -1 O TYR A 307 N CYS A 300
SHEET 6 G 8 VAL A 334 LYS A 341 -1 O VAL A 334 N ALA A 316
SHEET 7 G 8 SER A 353 PRO A 359 -1 O PHE A 358 N LEU A 335
SHEET 8 G 8 LEU A 422 THR A 427 -1 O LEU A 424 N LEU A 355
SHEET 1 H 4 LEU A 432 TYR A 440 0
SHEET 2 H 4 TYR A 443 THR A 450 -1 O PHE A 447 N ALA A 436
SHEET 3 H 4 LYS A 454 ALA A 460 -1 O ILE A 458 N VAL A 446
SHEET 4 H 4 GLY A 467 SER A 474 -1 O VAL A 468 N ARG A 459
SHEET 1 I 3 MET A 536 SER A 538 0
SHEET 2 I 3 GLY A 529 CYS A 531 -1 N CYS A 531 O MET A 536
SHEET 3 I 3 PHE A 552 ALA A 553 -1 O ALA A 553 N TRP A 530
SHEET 1 J 4 SER A 561 HIS A 565 0
SHEET 2 J 4 LEU A 577 ASN A 583 -1 O VAL A 581 N GLU A 563
SHEET 3 J 4 GLN A 610 ILE A 614 -1 O VAL A 611 N LEU A 580
SHEET 4 J 4 GLN A 605 SER A 607 -1 N SER A 607 O GLN A 610
SHEET 1 K 5 SER A 568 SER A 570 0
SHEET 2 K 5 ILE A 645 TYR A 654 1 O TYR A 654 N ILE A 569
SHEET 3 K 5 TRP A 630 SER A 639 -1 N LEU A 633 O PHE A 651
SHEET 4 K 5 ILE A 592 PHE A 596 -1 N ALA A 595 O GLN A 636
SHEET 5 K 5 THR A 600 GLU A 603 -1 O VAL A 602 N CYS A 594
SHEET 1 L 3 LEU A 680 THR A 682 0
SHEET 2 L 3 HIS A 673 CYS A 675 -1 N HIS A 673 O THR A 682
SHEET 3 L 3 ARG A 694 ILE A 695 -1 O ILE A 695 N TRP A 674
SHEET 1 M 4 THR B 40 HIS B 42 0
SHEET 2 M 4 GLN B 502 PRO B 507 -1 O VAL B 503 N PHE B 41
SHEET 3 M 4 TYR B 494 MET B 498 -1 N VAL B 497 O THR B 504
SHEET 4 M 4 ALA B 487 PHE B 488 -1 N ALA B 487 O TYR B 496
SHEET 1 N 4 PHE B 50 VAL B 55 0
SHEET 2 N 4 VAL B 62 ALA B 66 -1 O TYR B 63 N THR B 54
SHEET 3 N 4 ARG B 69 LEU B 73 -1 O LEU B 73 N VAL B 62
SHEET 4 N 4 ILE B 79 LYS B 84 -1 O GLN B 80 N LYS B 72
SHEET 1 O 2 GLU B 88 ASP B 90 0
SHEET 2 O 2 THR B 108 THR B 110 -1 O THR B 108 N ASP B 90
SHEET 1 P 4 ASN B 114 ASP B 120 0
SHEET 2 P 4 ARG B 125 GLY B 130 -1 O LEU B 127 N ILE B 118
SHEET 3 P 4 CYS B 137 ARG B 141 -1 O LEU B 140 N LEU B 126
SHEET 4 P 4 ILE B 147 VAL B 149 -1 O LEU B 148 N LEU B 139
SHEET 1 Q 4 MET B 168 VAL B 173 0
SHEET 2 Q 4 LYS B 181 THR B 186 -1 O PHE B 183 N VAL B 171
SHEET 3 Q 4 LEU B 198 LYS B 202 -1 O ARG B 201 N LEU B 182
SHEET 4 Q 4 LEU B 225 ILE B 226 -1 O ILE B 226 N LEU B 198
SHEET 1 R 5 PHE B 242 SER B 249 0
SHEET 2 R 5 PHE B 252 PRO B 260 -1 O VAL B 258 N PHE B 242
SHEET 3 R 5 TYR B 276 CYS B 284 -1 O THR B 277 N GLN B 259
SHEET 4 R 5 VAL B 294 ARG B 302 -1 O LEU B 296 N ILE B 280
SHEET 5 R 5 VAL B 419 GLU B 420 1 O VAL B 419 N PRO B 297
SHEET 1 S 8 PHE B 242 SER B 249 0
SHEET 2 S 8 PHE B 252 PRO B 260 -1 O VAL B 258 N PHE B 242
SHEET 3 S 8 TYR B 276 CYS B 284 -1 O THR B 277 N GLN B 259
SHEET 4 S 8 VAL B 294 ARG B 302 -1 O LEU B 296 N ILE B 280
SHEET 5 S 8 VAL B 305 ALA B 316 -1 O TYR B 307 N CYS B 300
SHEET 6 S 8 VAL B 334 LYS B 341 -1 O VAL B 334 N ALA B 316
SHEET 7 S 8 SER B 353 PRO B 359 -1 O PHE B 358 N LEU B 335
SHEET 8 S 8 LEU B 422 THR B 427 -1 O LEU B 424 N LEU B 355
SHEET 1 T 4 LEU B 432 TYR B 440 0
SHEET 2 T 4 TYR B 443 THR B 450 -1 O PHE B 447 N ALA B 436
SHEET 3 T 4 LYS B 454 ALA B 460 -1 O ILE B 458 N VAL B 446
SHEET 4 T 4 GLY B 467 SER B 474 -1 O VAL B 468 N ARG B 459
SHEET 1 U 3 MET B 536 SER B 538 0
SHEET 2 U 3 GLY B 529 CYS B 531 -1 N CYS B 531 O MET B 536
SHEET 3 U 3 PHE B 552 ALA B 553 -1 O ALA B 553 N TRP B 530
SHEET 1 V 4 SER B 561 HIS B 565 0
SHEET 2 V 4 LEU B 577 ASN B 583 -1 O VAL B 581 N GLU B 563
SHEET 3 V 4 GLN B 610 ILE B 614 -1 O VAL B 611 N LEU B 580
SHEET 4 V 4 GLN B 605 SER B 607 -1 N SER B 607 O GLN B 610
SHEET 1 W 5 SER B 568 SER B 570 0
SHEET 2 W 5 ILE B 645 TYR B 654 1 O TYR B 654 N ILE B 569
SHEET 3 W 5 TRP B 630 SER B 639 -1 N LEU B 633 O PHE B 651
SHEET 4 W 5 ILE B 592 PHE B 596 -1 N ALA B 595 O GLN B 636
SHEET 5 W 5 THR B 600 GLU B 603 -1 O VAL B 602 N CYS B 594
SHEET 1 X 3 LEU B 680 THR B 682 0
SHEET 2 X 3 HIS B 673 CYS B 675 -1 N HIS B 673 O THR B 682
SHEET 3 X 3 ARG B 694 ILE B 695 -1 O ILE B 695 N TRP B 674
SHEET 1 Y 4 THR C 40 HIS C 42 0
SHEET 2 Y 4 GLN C 502 PRO C 507 -1 O VAL C 503 N PHE C 41
SHEET 3 Y 4 TYR C 494 MET C 498 -1 N VAL C 497 O THR C 504
SHEET 4 Y 4 ALA C 487 PHE C 488 -1 N ALA C 487 O TYR C 496
SHEET 1 Z 4 PHE C 50 VAL C 55 0
SHEET 2 Z 4 VAL C 62 ALA C 66 -1 O TYR C 63 N THR C 54
SHEET 3 Z 4 ARG C 69 LEU C 73 -1 O LEU C 73 N VAL C 62
SHEET 4 Z 4 ILE C 79 LYS C 84 -1 O GLN C 80 N LYS C 72
SHEET 1 AA 2 GLU C 88 ASP C 90 0
SHEET 2 AA 2 THR C 108 THR C 110 -1 O THR C 108 N ASP C 90
SHEET 1 AB 4 ASN C 114 ASP C 120 0
SHEET 2 AB 4 ARG C 125 GLY C 130 -1 O LEU C 127 N ILE C 118
SHEET 3 AB 4 CYS C 137 ARG C 141 -1 O LEU C 140 N LEU C 126
SHEET 4 AB 4 ILE C 147 VAL C 149 -1 O LEU C 148 N LEU C 139
SHEET 1 AC 4 MET C 168 VAL C 173 0
SHEET 2 AC 4 LYS C 181 THR C 186 -1 O PHE C 183 N VAL C 171
SHEET 3 AC 4 LEU C 198 LYS C 202 -1 O ARG C 201 N LEU C 182
SHEET 4 AC 4 LEU C 225 ILE C 226 -1 O ILE C 226 N LEU C 198
SHEET 1 AD 5 PHE C 242 SER C 249 0
SHEET 2 AD 5 PHE C 252 PRO C 260 -1 O VAL C 258 N PHE C 242
SHEET 3 AD 5 TYR C 276 CYS C 284 -1 O THR C 277 N GLN C 259
SHEET 4 AD 5 VAL C 294 ARG C 302 -1 O LEU C 296 N ILE C 280
SHEET 5 AD 5 VAL C 419 GLU C 420 1 O VAL C 419 N PRO C 297
SHEET 1 AE 8 PHE C 242 SER C 249 0
SHEET 2 AE 8 PHE C 252 PRO C 260 -1 O VAL C 258 N PHE C 242
SHEET 3 AE 8 TYR C 276 CYS C 284 -1 O THR C 277 N GLN C 259
SHEET 4 AE 8 VAL C 294 ARG C 302 -1 O LEU C 296 N ILE C 280
SHEET 5 AE 8 VAL C 305 ALA C 316 -1 O TYR C 307 N CYS C 300
SHEET 6 AE 8 VAL C 334 LYS C 341 -1 O VAL C 334 N ALA C 316
SHEET 7 AE 8 SER C 353 PRO C 359 -1 O PHE C 358 N LEU C 335
SHEET 8 AE 8 LEU C 422 THR C 427 -1 O LEU C 424 N LEU C 355
SHEET 1 AF 4 LEU C 432 TYR C 440 0
SHEET 2 AF 4 TYR C 443 THR C 450 -1 O PHE C 447 N ALA C 436
SHEET 3 AF 4 LYS C 454 ALA C 460 -1 O ILE C 458 N VAL C 446
SHEET 4 AF 4 GLY C 467 SER C 474 -1 O VAL C 468 N ARG C 459
SHEET 1 AG 3 MET C 536 SER C 538 0
SHEET 2 AG 3 GLY C 529 CYS C 531 -1 N CYS C 531 O MET C 536
SHEET 3 AG 3 PHE C 552 ALA C 553 -1 O ALA C 553 N TRP C 530
SHEET 1 AH 4 SER C 561 HIS C 565 0
SHEET 2 AH 4 LEU C 577 ASN C 583 -1 O VAL C 581 N GLU C 563
SHEET 3 AH 4 GLN C 610 ILE C 614 -1 O VAL C 611 N LEU C 580
SHEET 4 AH 4 GLN C 605 SER C 607 -1 N SER C 607 O GLN C 610
SHEET 1 AI 5 SER C 568 SER C 570 0
SHEET 2 AI 5 ILE C 645 TYR C 654 1 O TYR C 654 N ILE C 569
SHEET 3 AI 5 TRP C 630 SER C 639 -1 N LEU C 633 O PHE C 651
SHEET 4 AI 5 ILE C 592 PHE C 596 -1 N ALA C 595 O GLN C 636
SHEET 5 AI 5 THR C 600 GLU C 603 -1 O VAL C 602 N CYS C 594
SHEET 1 AJ 3 LEU C 680 THR C 682 0
SHEET 2 AJ 3 HIS C 673 CYS C 675 -1 N HIS C 673 O THR C 682
SHEET 3 AJ 3 ARG C 694 ILE C 695 -1 O ILE C 695 N TRP C 674
SHEET 1 AK 4 THR D 40 HIS D 42 0
SHEET 2 AK 4 GLN D 502 PRO D 507 -1 O VAL D 503 N PHE D 41
SHEET 3 AK 4 TYR D 494 MET D 498 -1 N VAL D 497 O THR D 504
SHEET 4 AK 4 ALA D 487 PHE D 488 -1 N ALA D 487 O TYR D 496
SHEET 1 AL 4 PHE D 50 VAL D 55 0
SHEET 2 AL 4 VAL D 62 ALA D 66 -1 O TYR D 63 N THR D 54
SHEET 3 AL 4 ARG D 69 LEU D 73 -1 O LEU D 73 N VAL D 62
SHEET 4 AL 4 ILE D 79 LYS D 84 -1 O GLN D 80 N LYS D 72
SHEET 1 AM 2 GLU D 88 ASP D 90 0
SHEET 2 AM 2 THR D 108 THR D 110 -1 O THR D 108 N ASP D 90
SHEET 1 AN 4 ASN D 114 ASP D 120 0
SHEET 2 AN 4 ARG D 125 GLY D 130 -1 O LEU D 127 N ILE D 118
SHEET 3 AN 4 CYS D 137 ARG D 141 -1 O LEU D 140 N LEU D 126
SHEET 4 AN 4 ILE D 147 VAL D 149 -1 O LEU D 148 N LEU D 139
SHEET 1 AO 4 MET D 168 VAL D 173 0
SHEET 2 AO 4 LYS D 181 THR D 186 -1 O PHE D 183 N VAL D 171
SHEET 3 AO 4 LEU D 198 LYS D 202 -1 O ARG D 201 N LEU D 182
SHEET 4 AO 4 LEU D 225 ILE D 226 -1 O ILE D 226 N LEU D 198
SHEET 1 AP 5 PHE D 242 SER D 249 0
SHEET 2 AP 5 PHE D 252 PRO D 260 -1 O VAL D 258 N PHE D 242
SHEET 3 AP 5 TYR D 276 CYS D 284 -1 O THR D 277 N GLN D 259
SHEET 4 AP 5 VAL D 294 ARG D 302 -1 O LEU D 296 N ILE D 280
SHEET 5 AP 5 VAL D 419 GLU D 420 1 O VAL D 419 N PRO D 297
SHEET 1 AQ 8 PHE D 242 SER D 249 0
SHEET 2 AQ 8 PHE D 252 PRO D 260 -1 O VAL D 258 N PHE D 242
SHEET 3 AQ 8 TYR D 276 CYS D 284 -1 O THR D 277 N GLN D 259
SHEET 4 AQ 8 VAL D 294 ARG D 302 -1 O LEU D 296 N ILE D 280
SHEET 5 AQ 8 VAL D 305 ALA D 316 -1 O TYR D 307 N CYS D 300
SHEET 6 AQ 8 VAL D 334 LYS D 341 -1 O VAL D 334 N ALA D 316
SHEET 7 AQ 8 SER D 353 PRO D 359 -1 O PHE D 358 N LEU D 335
SHEET 8 AQ 8 LEU D 422 THR D 427 -1 O LEU D 424 N LEU D 355
SHEET 1 AR 4 LEU D 432 TYR D 440 0
SHEET 2 AR 4 TYR D 443 THR D 450 -1 O PHE D 447 N ALA D 436
SHEET 3 AR 4 LYS D 454 ALA D 460 -1 O ILE D 458 N VAL D 446
SHEET 4 AR 4 GLY D 467 SER D 474 -1 O VAL D 468 N ARG D 459
SHEET 1 AS 3 MET D 536 SER D 538 0
SHEET 2 AS 3 GLY D 529 CYS D 531 -1 N CYS D 531 O MET D 536
SHEET 3 AS 3 PHE D 552 ALA D 553 -1 O ALA D 553 N TRP D 530
SHEET 1 AT 4 SER D 561 HIS D 565 0
SHEET 2 AT 4 LEU D 577 ASN D 583 -1 O VAL D 581 N GLU D 563
SHEET 3 AT 4 GLN D 610 ILE D 614 -1 O VAL D 611 N LEU D 580
SHEET 4 AT 4 GLN D 605 SER D 607 -1 N SER D 607 O GLN D 610
SHEET 1 AU 5 SER D 568 SER D 570 0
SHEET 2 AU 5 ILE D 645 TYR D 654 1 O TYR D 654 N ILE D 569
SHEET 3 AU 5 TRP D 630 SER D 639 -1 N LEU D 633 O PHE D 651
SHEET 4 AU 5 ILE D 592 PHE D 596 -1 N ALA D 595 O GLN D 636
SHEET 5 AU 5 THR D 600 GLU D 603 -1 O VAL D 602 N CYS D 594
SHEET 1 AV 3 LEU D 680 THR D 682 0
SHEET 2 AV 3 HIS D 673 CYS D 675 -1 N HIS D 673 O THR D 682
SHEET 3 AV 3 ARG D 694 ILE D 695 -1 O ILE D 695 N TRP D 674
SHEET 1 AW 4 THR E 40 HIS E 42 0
SHEET 2 AW 4 GLN E 502 PRO E 507 -1 O VAL E 503 N PHE E 41
SHEET 3 AW 4 TYR E 494 MET E 498 -1 N VAL E 497 O THR E 504
SHEET 4 AW 4 ALA E 487 PHE E 488 -1 N ALA E 487 O TYR E 496
SHEET 1 AX 4 PHE E 50 VAL E 55 0
SHEET 2 AX 4 VAL E 62 ALA E 66 -1 O TYR E 63 N THR E 54
SHEET 3 AX 4 ARG E 69 LEU E 73 -1 O LEU E 73 N VAL E 62
SHEET 4 AX 4 ILE E 79 LYS E 84 -1 O GLN E 80 N LYS E 72
SHEET 1 AY 2 GLU E 88 ASP E 90 0
SHEET 2 AY 2 THR E 108 THR E 110 -1 O THR E 108 N ASP E 90
SHEET 1 AZ 4 ASN E 114 ASP E 120 0
SHEET 2 AZ 4 ARG E 125 GLY E 130 -1 O LEU E 127 N ILE E 118
SHEET 3 AZ 4 CYS E 137 ARG E 141 -1 O LEU E 140 N LEU E 126
SHEET 4 AZ 4 ILE E 147 VAL E 149 -1 O LEU E 148 N LEU E 139
SHEET 1 BA 4 MET E 168 VAL E 173 0
SHEET 2 BA 4 LYS E 181 THR E 186 -1 O PHE E 183 N VAL E 171
SHEET 3 BA 4 LEU E 198 LYS E 202 -1 O ARG E 201 N LEU E 182
SHEET 4 BA 4 LEU E 225 ILE E 226 -1 O ILE E 226 N LEU E 198
SHEET 1 BB 5 PHE E 242 SER E 249 0
SHEET 2 BB 5 PHE E 252 PRO E 260 -1 O VAL E 258 N PHE E 242
SHEET 3 BB 5 TYR E 276 CYS E 284 -1 O THR E 277 N GLN E 259
SHEET 4 BB 5 VAL E 294 ARG E 302 -1 O LEU E 296 N ILE E 280
SHEET 5 BB 5 VAL E 419 GLU E 420 1 O VAL E 419 N PRO E 297
SHEET 1 BC 8 PHE E 242 SER E 249 0
SHEET 2 BC 8 PHE E 252 PRO E 260 -1 O VAL E 258 N PHE E 242
SHEET 3 BC 8 TYR E 276 CYS E 284 -1 O THR E 277 N GLN E 259
SHEET 4 BC 8 VAL E 294 ARG E 302 -1 O LEU E 296 N ILE E 280
SHEET 5 BC 8 VAL E 305 ALA E 316 -1 O TYR E 307 N CYS E 300
SHEET 6 BC 8 VAL E 334 LYS E 341 -1 O VAL E 334 N ALA E 316
SHEET 7 BC 8 SER E 353 PRO E 359 -1 O PHE E 358 N LEU E 335
SHEET 8 BC 8 LEU E 422 THR E 427 -1 O LEU E 424 N LEU E 355
SHEET 1 BD 4 LEU E 432 TYR E 440 0
SHEET 2 BD 4 TYR E 443 THR E 450 -1 O PHE E 447 N ALA E 436
SHEET 3 BD 4 LYS E 454 ALA E 460 -1 O ILE E 458 N VAL E 446
SHEET 4 BD 4 GLY E 467 SER E 474 -1 O VAL E 468 N ARG E 459
SHEET 1 BE 3 MET E 536 SER E 538 0
SHEET 2 BE 3 GLY E 529 CYS E 531 -1 N CYS E 531 O MET E 536
SHEET 3 BE 3 PHE E 552 ALA E 553 -1 O ALA E 553 N TRP E 530
SHEET 1 BF 4 SER E 561 HIS E 565 0
SHEET 2 BF 4 LEU E 577 ASN E 583 -1 O VAL E 581 N GLU E 563
SHEET 3 BF 4 GLN E 610 ILE E 614 -1 O VAL E 611 N LEU E 580
SHEET 4 BF 4 GLN E 605 SER E 607 -1 N SER E 607 O GLN E 610
SHEET 1 BG 5 SER E 568 SER E 570 0
SHEET 2 BG 5 ILE E 645 TYR E 654 1 O TYR E 654 N ILE E 569
SHEET 3 BG 5 TRP E 630 SER E 639 -1 N LEU E 633 O PHE E 651
SHEET 4 BG 5 ILE E 592 PHE E 596 -1 N ALA E 595 O GLN E 636
SHEET 5 BG 5 THR E 600 GLU E 603 -1 O VAL E 602 N CYS E 594
SHEET 1 BH 3 LEU E 680 THR E 682 0
SHEET 2 BH 3 HIS E 673 CYS E 675 -1 N HIS E 673 O THR E 682
SHEET 3 BH 3 ARG E 694 ILE E 695 -1 O ILE E 695 N TRP E 674
SHEET 1 BI 4 THR F 40 HIS F 42 0
SHEET 2 BI 4 GLN F 502 PRO F 507 -1 O VAL F 503 N PHE F 41
SHEET 3 BI 4 TYR F 494 MET F 498 -1 N VAL F 497 O THR F 504
SHEET 4 BI 4 ALA F 487 PHE F 488 -1 N ALA F 487 O TYR F 496
SHEET 1 BJ 4 PHE F 50 VAL F 55 0
SHEET 2 BJ 4 VAL F 62 ALA F 66 -1 O TYR F 63 N THR F 54
SHEET 3 BJ 4 ARG F 69 LEU F 73 -1 O LEU F 73 N VAL F 62
SHEET 4 BJ 4 ILE F 79 LYS F 84 -1 O GLN F 80 N LYS F 72
SHEET 1 BK 2 GLU F 88 ASP F 90 0
SHEET 2 BK 2 THR F 108 THR F 110 -1 O THR F 108 N ASP F 90
SHEET 1 BL 4 ASN F 114 ASP F 120 0
SHEET 2 BL 4 ARG F 125 GLY F 130 -1 O LEU F 127 N ILE F 118
SHEET 3 BL 4 CYS F 137 ARG F 141 -1 O LEU F 140 N LEU F 126
SHEET 4 BL 4 ILE F 147 VAL F 149 -1 O LEU F 148 N LEU F 139
SHEET 1 BM 4 MET F 168 VAL F 173 0
SHEET 2 BM 4 LYS F 181 THR F 186 -1 O PHE F 183 N VAL F 171
SHEET 3 BM 4 LEU F 198 LYS F 202 -1 O ARG F 201 N LEU F 182
SHEET 4 BM 4 LEU F 225 ILE F 226 -1 O ILE F 226 N LEU F 198
SHEET 1 BN 5 PHE F 242 SER F 249 0
SHEET 2 BN 5 PHE F 252 PRO F 260 -1 O VAL F 258 N PHE F 242
SHEET 3 BN 5 TYR F 276 CYS F 284 -1 O THR F 277 N GLN F 259
SHEET 4 BN 5 VAL F 294 ARG F 302 -1 O LEU F 296 N ILE F 280
SHEET 5 BN 5 VAL F 419 GLU F 420 1 O VAL F 419 N PRO F 297
SHEET 1 BO 8 PHE F 242 SER F 249 0
SHEET 2 BO 8 PHE F 252 PRO F 260 -1 O VAL F 258 N PHE F 242
SHEET 3 BO 8 TYR F 276 CYS F 284 -1 O THR F 277 N GLN F 259
SHEET 4 BO 8 VAL F 294 ARG F 302 -1 O LEU F 296 N ILE F 280
SHEET 5 BO 8 VAL F 305 ALA F 316 -1 O TYR F 307 N CYS F 300
SHEET 6 BO 8 VAL F 334 LYS F 341 -1 O VAL F 334 N ALA F 316
SHEET 7 BO 8 SER F 353 PRO F 359 -1 O PHE F 358 N LEU F 335
SHEET 8 BO 8 LEU F 422 THR F 427 -1 O LEU F 424 N LEU F 355
SHEET 1 BP 4 LEU F 432 TYR F 440 0
SHEET 2 BP 4 TYR F 443 THR F 450 -1 O PHE F 447 N ALA F 436
SHEET 3 BP 4 LYS F 454 ALA F 460 -1 O ILE F 458 N VAL F 446
SHEET 4 BP 4 GLY F 467 SER F 474 -1 O VAL F 468 N ARG F 459
SHEET 1 BQ 3 MET F 536 SER F 538 0
SHEET 2 BQ 3 GLY F 529 CYS F 531 -1 N CYS F 531 O MET F 536
SHEET 3 BQ 3 PHE F 552 ALA F 553 -1 O ALA F 553 N TRP F 530
SHEET 1 BR 4 SER F 561 HIS F 565 0
SHEET 2 BR 4 LEU F 577 ASN F 583 -1 O VAL F 581 N GLU F 563
SHEET 3 BR 4 GLN F 610 ILE F 614 -1 O VAL F 611 N LEU F 580
SHEET 4 BR 4 GLN F 605 SER F 607 -1 N SER F 607 O GLN F 610
SHEET 1 BS 5 SER F 568 SER F 570 0
SHEET 2 BS 5 ILE F 645 TYR F 654 1 O TYR F 654 N ILE F 569
SHEET 3 BS 5 TRP F 630 SER F 639 -1 N LEU F 633 O PHE F 651
SHEET 4 BS 5 ILE F 592 PHE F 596 -1 N ALA F 595 O GLN F 636
SHEET 5 BS 5 THR F 600 GLU F 603 -1 O VAL F 602 N CYS F 594
SHEET 1 BT 3 LEU F 680 THR F 682 0
SHEET 2 BT 3 HIS F 673 CYS F 675 -1 N HIS F 673 O THR F 682
SHEET 3 BT 3 ARG F 694 ILE F 695 -1 O ILE F 695 N TRP F 674
SHEET 1 BU 4 ILE G 46 PHE G 48 0
SHEET 2 BU 4 VAL G 509 PRO G 513 -1 O GLN G 511 N ILE G 46
SHEET 3 BU 4 GLN G 500 GLY G 504 -1 N LEU G 501 O LEU G 512
SHEET 4 BU 4 ALA G 491 SER G 495 -1 N ALA G 491 O GLY G 504
SHEET 1 BV 4 THR G 59 ASP G 63 0
SHEET 2 BV 4 ARG G 68 ALA G 73 -1 O TYR G 70 N LEU G 61
SHEET 3 BV 4 HIS G 76 ASN G 81 -1 O PHE G 80 N LEU G 69
SHEET 4 BV 4 PHE G 88 VAL G 92 -1 O GLN G 89 N SER G 79
SHEET 1 BW 4 ILE G 118 ALA G 123 0
SHEET 2 BW 4 HIS G 128 GLY G 133 -1 O TYR G 130 N GLU G 122
SHEET 3 BW 4 ILE G 140 GLU G 145 -1 O ILE G 144 N LEU G 129
SHEET 4 BW 4 LYS G 156 ASN G 164 -1 O GLU G 163 N CYS G 141
SHEET 1 BX 4 ALA G 178 ILE G 182 0
SHEET 2 BX 4 GLU G 185 ALA G 191 -1 O TYR G 187 N LEU G 180
SHEET 3 BX 4 PHE G 199 LEU G 205 -1 O PHE G 202 N SER G 188
SHEET 4 BX 4 ILE G 211 ARG G 212 -1 O ILE G 211 N ARG G 203
SHEET 1 BY 4 ARG G 225 ILE G 232 0
SHEET 2 BY 4 LYS G 242 ASN G 250 -1 O TYR G 244 N HIS G 230
SHEET 3 BY 4 THR G 261 CYS G 269 -1 O ILE G 268 N VAL G 243
SHEET 4 BY 4 LEU G 287 ARG G 290 -1 O ALA G 289 N ILE G 265
SHEET 1 BZ 2 SER G 294 VAL G 295 0
SHEET 2 BZ 2 THR G 303 HIS G 304 -1 O THR G 303 N VAL G 295
SHEET 1 CA 4 GLU G 307 MET G 314 0
SHEET 2 CA 4 ILE G 323 THR G 329 -1 O ILE G 323 N MET G 314
SHEET 3 CA 4 SER G 338 TYR G 343 -1 O ALA G 339 N PHE G 328
SHEET 4 CA 4 MET G 422 LYS G 424 -1 O LYS G 424 N SER G 338
SHEET 1 CB 2 ALA G 357 HIS G 358 0
SHEET 2 CB 2 VAL G 367 PRO G 368 -1 O VAL G 367 N HIS G 358
SHEET 1 CC 4 PHE G 431 ASP G 440 0
SHEET 2 CC 4 GLN G 445 THR G 453 -1 O GLY G 452 N GLN G 433
SHEET 3 CC 4 VAL G 458 VAL G 462 -1 O VAL G 461 N MET G 449
SHEET 4 CC 4 GLU G 478 MET G 480 -1 O GLU G 478 N LYS G 460
SHEET 1 CD 5 GLY H 29 LYS H 32 0
SHEET 2 CD 5 LYS H 53 GLN H 59 1 O LEU H 57 N GLY H 29
SHEET 3 CD 5 PHE H 118 VAL H 124 -1 O ILE H 121 N TRP H 56
SHEET 4 CD 5 TYR H 86 ASP H 91 -1 N GLU H 88 O LYS H 122
SHEET 5 CD 5 ARG H 98 PHE H 103 -1 O ARG H 98 N ASP H 91
SHEET 1 CE 4 GLY H 37 THR H 40 0
SHEET 2 CE 4 SER H 135 ILE H 140 -1 O ILE H 136 N LEU H 39
SHEET 3 CE 4 ILE H 67 PHE H 71 -1 N MET H 68 O GLU H 139
SHEET 4 CE 4 VAL H 112 VAL H 113 -1 O VAL H 112 N ILE H 69
SSBOND 1 CYS A 94 CYS A 103 1555 1555 2.04
SSBOND 2 CYS A 129 CYS A 137 1555 1555 2.03
SSBOND 3 CYS A 284 CYS A 405 1555 1555 2.04
SSBOND 4 CYS A 300 CYS A 356 1555 1555 2.02
SSBOND 5 CYS A 374 CYS A 393 1555 1555 2.04
SSBOND 6 CYS A 511 CYS A 528 1555 1555 2.03
SSBOND 7 CYS A 517 CYS A 559 1555 1555 2.03
SSBOND 8 CYS A 520 CYS A 537 1555 1555 2.04
SSBOND 9 CYS A 531 CYS A 543 1555 1555 2.04
SSBOND 10 CYS A 594 CYS A 613 1555 1555 2.02
SSBOND 11 CYS A 656 CYS A 672 1555 1555 2.04
SSBOND 12 CYS A 662 CYS A 701 1555 1555 2.03
SSBOND 13 CYS A 665 CYS A 681 1555 1555 2.04
SSBOND 14 CYS A 675 CYS A 688 1555 1555 2.03
SSBOND 15 CYS B 94 CYS B 103 1555 1555 2.04
SSBOND 16 CYS B 129 CYS B 137 1555 1555 2.03
SSBOND 17 CYS B 284 CYS B 405 1555 1555 2.04
SSBOND 18 CYS B 300 CYS B 356 1555 1555 2.02
SSBOND 19 CYS B 374 CYS B 393 1555 1555 2.04
SSBOND 20 CYS B 511 CYS B 528 1555 1555 2.03
SSBOND 21 CYS B 517 CYS B 559 1555 1555 2.03
SSBOND 22 CYS B 520 CYS B 537 1555 1555 2.04
SSBOND 23 CYS B 531 CYS B 543 1555 1555 2.04
SSBOND 24 CYS B 594 CYS B 613 1555 1555 2.02
SSBOND 25 CYS B 656 CYS B 672 1555 1555 2.04
SSBOND 26 CYS B 662 CYS B 701 1555 1555 2.03
SSBOND 27 CYS B 665 CYS B 681 1555 1555 2.04
SSBOND 28 CYS B 675 CYS B 688 1555 1555 2.03
SSBOND 29 CYS C 94 CYS C 103 1555 1555 2.04
SSBOND 30 CYS C 129 CYS C 137 1555 1555 2.04
SSBOND 31 CYS C 284 CYS C 405 1555 1555 2.04
SSBOND 32 CYS C 300 CYS C 356 1555 1555 2.02
SSBOND 33 CYS C 374 CYS C 393 1555 1555 2.04
SSBOND 34 CYS C 511 CYS C 528 1555 1555 2.03
SSBOND 35 CYS C 517 CYS C 559 1555 1555 2.03
SSBOND 36 CYS C 520 CYS C 537 1555 1555 2.04
SSBOND 37 CYS C 531 CYS C 543 1555 1555 2.04
SSBOND 38 CYS C 594 CYS C 613 1555 1555 2.02
SSBOND 39 CYS C 656 CYS C 672 1555 1555 2.04
SSBOND 40 CYS C 662 CYS C 701 1555 1555 2.03
SSBOND 41 CYS C 665 CYS C 681 1555 1555 2.04
SSBOND 42 CYS C 675 CYS C 688 1555 1555 2.03
SSBOND 43 CYS D 94 CYS D 103 1555 1555 2.04
SSBOND 44 CYS D 129 CYS D 137 1555 1555 2.03
SSBOND 45 CYS D 284 CYS D 405 1555 1555 2.04
SSBOND 46 CYS D 300 CYS D 356 1555 1555 2.02
SSBOND 47 CYS D 374 CYS D 393 1555 1555 2.04
SSBOND 48 CYS D 511 CYS D 528 1555 1555 2.03
SSBOND 49 CYS D 517 CYS D 559 1555 1555 2.03
SSBOND 50 CYS D 520 CYS D 537 1555 1555 2.04
SSBOND 51 CYS D 531 CYS D 543 1555 1555 2.04
SSBOND 52 CYS D 594 CYS D 613 1555 1555 2.02
SSBOND 53 CYS D 656 CYS D 672 1555 1555 2.04
SSBOND 54 CYS D 662 CYS D 701 1555 1555 2.03
SSBOND 55 CYS D 665 CYS D 681 1555 1555 2.04
SSBOND 56 CYS D 675 CYS D 688 1555 1555 2.03
SSBOND 57 CYS E 94 CYS E 103 1555 1555 2.04
SSBOND 58 CYS E 129 CYS E 137 1555 1555 2.03
SSBOND 59 CYS E 284 CYS E 405 1555 1555 2.04
SSBOND 60 CYS E 300 CYS E 356 1555 1555 2.02
SSBOND 61 CYS E 374 CYS E 393 1555 1555 2.04
SSBOND 62 CYS E 511 CYS E 528 1555 1555 2.03
SSBOND 63 CYS E 517 CYS E 559 1555 1555 2.03
SSBOND 64 CYS E 520 CYS E 537 1555 1555 2.05
SSBOND 65 CYS E 531 CYS E 543 1555 1555 2.04
SSBOND 66 CYS E 594 CYS E 613 1555 1555 2.02
SSBOND 67 CYS E 656 CYS E 672 1555 1555 2.04
SSBOND 68 CYS E 662 CYS E 701 1555 1555 2.03
SSBOND 69 CYS E 665 CYS E 681 1555 1555 2.04
SSBOND 70 CYS E 675 CYS E 688 1555 1555 2.03
SSBOND 71 CYS F 94 CYS F 103 1555 1555 2.04
SSBOND 72 CYS F 129 CYS F 137 1555 1555 2.04
SSBOND 73 CYS F 284 CYS F 405 1555 1555 2.04
SSBOND 74 CYS F 300 CYS F 356 1555 1555 2.02
SSBOND 75 CYS F 374 CYS F 393 1555 1555 2.04
SSBOND 76 CYS F 511 CYS F 528 1555 1555 2.03
SSBOND 77 CYS F 517 CYS F 559 1555 1555 2.03
SSBOND 78 CYS F 520 CYS F 537 1555 1555 2.04
SSBOND 79 CYS F 531 CYS F 543 1555 1555 2.04
SSBOND 80 CYS F 594 CYS F 613 1555 1555 2.02
SSBOND 81 CYS F 656 CYS F 672 1555 1555 2.04
SSBOND 82 CYS F 662 CYS F 701 1555 1555 2.03
SSBOND 83 CYS F 665 CYS F 681 1555 1555 2.04
SSBOND 84 CYS F 675 CYS F 688 1555 1555 2.03
SSBOND 85 CYS G 103 CYS G 114 1555 1555 2.05
SSBOND 86 CYS G 132 CYS G 141 1555 1555 2.07
SSBOND 87 CYS G 269 CYS G 381 1555 1555 2.05
SSBOND 88 CYS G 293 CYS G 341 1555 1555 2.06
SSBOND 89 CYS H 27 CYS H 54 1555 1555 2.06
SSBOND 90 CYS H 82 CYS H 104 1555 1555 2.06
LINK OE1 GLU H 78 CA CA H 601 1555 1555 2.44
LINK OD2 ASP H 85 CA CA H 601 1555 1555 2.32
LINK OD1 ASP H 126 CA CA H 601 1555 1555 2.37
LINK O GLU H 128 CA CA H 601 1555 1555 2.42
LINK O THR H 129 CA CA H 601 1555 1555 2.30
CISPEP 1 GLY A 86 PRO A 87 0 -1.42
CISPEP 2 TYR A 95 PRO A 96 0 -3.29
CISPEP 3 SER A 237 HIS A 238 0 7.75
CISPEP 4 GLN A 411 PRO A 412 0 -2.50
CISPEP 5 PRO A 463 PRO A 464 0 -0.23
CISPEP 6 HIS A 565 PRO A 566 0 -1.53
CISPEP 7 GLY B 86 PRO B 87 0 -1.64
CISPEP 8 TYR B 95 PRO B 96 0 -3.34
CISPEP 9 SER B 237 HIS B 238 0 7.91
CISPEP 10 GLN B 411 PRO B 412 0 -2.57
CISPEP 11 PRO B 463 PRO B 464 0 -0.36
CISPEP 12 HIS B 565 PRO B 566 0 -1.54
CISPEP 13 GLY C 86 PRO C 87 0 -1.48
CISPEP 14 TYR C 95 PRO C 96 0 -3.37
CISPEP 15 SER C 237 HIS C 238 0 7.84
CISPEP 16 GLN C 411 PRO C 412 0 -2.54
CISPEP 17 PRO C 463 PRO C 464 0 -0.21
CISPEP 18 HIS C 565 PRO C 566 0 -1.58
CISPEP 19 GLY D 86 PRO D 87 0 -1.52
CISPEP 20 TYR D 95 PRO D 96 0 -3.33
CISPEP 21 SER D 237 HIS D 238 0 7.66
CISPEP 22 GLN D 411 PRO D 412 0 -2.65
CISPEP 23 PRO D 463 PRO D 464 0 -0.26
CISPEP 24 HIS D 565 PRO D 566 0 -1.55
CISPEP 25 GLY E 86 PRO E 87 0 -1.50
CISPEP 26 TYR E 95 PRO E 96 0 -3.33
CISPEP 27 SER E 237 HIS E 238 0 7.73
CISPEP 28 GLN E 411 PRO E 412 0 -2.55
CISPEP 29 PRO E 463 PRO E 464 0 -0.09
CISPEP 30 HIS E 565 PRO E 566 0 -1.51
CISPEP 31 TYR E 654 ASN E 655 0 -27.71
CISPEP 32 GLY F 86 PRO F 87 0 -1.50
CISPEP 33 TYR F 95 PRO F 96 0 -3.29
CISPEP 34 SER F 237 HIS F 238 0 7.78
CISPEP 35 GLN F 411 PRO F 412 0 -2.70
CISPEP 36 PRO F 463 PRO F 464 0 -0.16
CISPEP 37 HIS F 565 PRO F 566 0 -1.43
CISPEP 38 TYR G 375 PRO G 376 0 -0.46
CISPEP 39 TYR H 44 PRO H 45 0 7.24
SITE 1 AC1 5 GLU H 78 ASP H 85 ASP H 126 GLU H 128
SITE 2 AC1 5 THR H 129
CRYST1 191.632 293.604 252.176 90.00 106.38 90.00 C 1 2 1 24
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 0.005218 0.000000 0.001533 0.00000
SCALE2 0.000000 0.003406 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004133 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
