HEADER ANTITOXIN 24-SEP-20 7K7Y TITLE CRYSTAL STRUCTURE OF BONT/E LC-HN DOMAIN IN COMPLEX WITH VHH JLE-E9 COMPND MOL_ID: 1; COMPND 2 MOLECULE: BOTULINUM NEUROTOXIN TYPE E; COMPND 3 CHAIN: A, E, G, B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: JLE-E9; COMPND 7 CHAIN: D, C, F, H; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM BOTULINUM; SOURCE 3 ORGANISM_TAXID: 1491; SOURCE 4 GENE: BONT, FDB75_10755; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 9 ORGANISM_TAXID: 30538; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS BOTULINUM NEUROTOXIN (BONT), VHH, RECEPTOR-BINDING DOMAIN, TOXIN, KEYWDS 2 ANTITOXIN EXPDTA X-RAY DIFFRACTION AUTHOR K.LAM,R.JIN REVDAT 1 14-OCT-20 7K7Y 0 JRNL AUTH K.H.LAM,K.PERRY,C.B.SHOEMAKER,R.JIN JRNL TITL TWO VHH ANTIBODIES NEUTRALIZE BOTULINUM NEUROTOXIN E1 BY JRNL TITL 2 BLOCKING ITS MEMBRANE TRANSLOCATION IN HOST CELLS. JRNL REF TOXINS V. 12 2020 JRNL REFN ESSN 2072-6651 JRNL PMID 32992561 JRNL DOI 10.3390/TOXINS12100616 REMARK 2 REMARK 2 RESOLUTION. 3.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC V5.7 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 74.09 REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 94.6 REMARK 3 NUMBER OF REFLECTIONS : 55219 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : 0.263 REMARK 3 R VALUE (WORKING SET) : 0.261 REMARK 3 FREE R VALUE : 0.288 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910 REMARK 3 FREE R VALUE TEST SET COUNT : 4992 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 28699 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 125.4 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 123.8 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): NULL REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.625 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : NULL ; NULL REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : NULL ; NULL REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : NULL ; NULL REMARK 3 STAGGERED (DEGREES) : NULL ; NULL REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 7K7Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-SEP-20. REMARK 100 THE DEPOSITION ID IS D_1000252027. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-NOV-17 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 24-ID-E REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97919 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55326 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.600 REMARK 200 RESOLUTION RANGE LOW (A) : 148.190 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4 REMARK 200 DATA REDUNDANCY : 3.800 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.70 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 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 3FFZ REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.46 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 12 % PEG 20K, 0.1 M SODIUM CITRATE PH REMARK 280 5.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 54.51750 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 105.25250 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 104.32500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 105.25250 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 54.51750 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 104.32500 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 REMARK 350 BIOMOLECULE: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A -4 REMARK 465 PRO A -3 REMARK 465 LEU A -2 REMARK 465 GLY A -1 REMARK 465 SER A 0 REMARK 465 THR A 459 REMARK 465 SER A 460 REMARK 465 ASN A 461 REMARK 465 ASN A 462 REMARK 465 ASN A 463 REMARK 465 TYR A 464 REMARK 465 GLU A 465 REMARK 465 ASN A 466 REMARK 465 ASP A 467 REMARK 465 LEU A 468 REMARK 465 ASP A 469 REMARK 465 GLN A 470 REMARK 465 VAL A 471 REMARK 465 ILE A 472 REMARK 465 LEU A 473 REMARK 465 ASN A 474 REMARK 465 PHE A 475 REMARK 465 ASN A 476 REMARK 465 SER A 477 REMARK 465 GLU A 478 REMARK 465 SER A 479 REMARK 465 ALA A 480 REMARK 465 PRO A 481 REMARK 465 GLY A 482 REMARK 465 LEU A 483 REMARK 465 SER A 484 REMARK 465 ASP A 485 REMARK 465 GLU A 486 REMARK 465 LYS A 487 REMARK 465 LEU A 488 REMARK 465 ASN A 489 REMARK 465 LEU A 490 REMARK 465 THR A 491 REMARK 465 ILE A 492 REMARK 465 GLN A 493 REMARK 465 ASN A 494 REMARK 465 ASP A 495 REMARK 465 ALA A 496 REMARK 465 TYR A 497 REMARK 465 ILE A 498 REMARK 465 PRO A 499 REMARK 465 LYS A 500 REMARK 465 ASP A 832 REMARK 465 ASP A 833 REMARK 465 LYS A 834 REMARK 465 ILE A 835 REMARK 465 LEU A 836 REMARK 465 ILE A 837 REMARK 465 SER A 838 REMARK 465 TYR A 839 REMARK 465 PHE A 840 REMARK 465 ASN A 841 REMARK 465 LYS A 842 REMARK 465 PHE A 843 REMARK 465 PHE A 844 REMARK 465 LYS A 845 REMARK 465 GLY D -4 REMARK 465 PRO D -3 REMARK 465 LEU D -2 REMARK 465 SER D 124 REMARK 465 GLY E -4 REMARK 465 PRO E -3 REMARK 465 LEU E -2 REMARK 465 GLY E -1 REMARK 465 SER E 0 REMARK 465 THR E 459 REMARK 465 SER E 460 REMARK 465 ASN E 461 REMARK 465 ASN E 462 REMARK 465 ASN E 463 REMARK 465 TYR E 464 REMARK 465 GLU E 465 REMARK 465 ASN E 466 REMARK 465 ASP E 467 REMARK 465 LEU E 468 REMARK 465 ASP E 469 REMARK 465 GLN E 470 REMARK 465 VAL E 471 REMARK 465 ILE E 472 REMARK 465 LEU E 473 REMARK 465 ASN E 474 REMARK 465 PHE E 475 REMARK 465 ASN E 476 REMARK 465 SER E 477 REMARK 465 GLU E 478 REMARK 465 SER E 479 REMARK 465 ALA E 480 REMARK 465 PRO E 481 REMARK 465 GLY E 482 REMARK 465 LEU E 483 REMARK 465 SER E 484 REMARK 465 ASP E 485 REMARK 465 GLU E 486 REMARK 465 LYS E 487 REMARK 465 LEU E 488 REMARK 465 ASN E 489 REMARK 465 LEU E 490 REMARK 465 THR E 491 REMARK 465 ILE E 492 REMARK 465 GLN E 493 REMARK 465 ASN E 494 REMARK 465 ASP E 495 REMARK 465 ALA E 496 REMARK 465 TYR E 497 REMARK 465 ILE E 498 REMARK 465 PRO E 499 REMARK 465 LYS E 500 REMARK 465 SER E 652 REMARK 465 PHE E 653 REMARK 465 LEU E 654 REMARK 465 GLY E 655 REMARK 465 SER E 656 REMARK 465 SER E 657 REMARK 465 ASP E 658 REMARK 465 ASN E 659 REMARK 465 GLY E 801 REMARK 465 SER E 802 REMARK 465 ILE E 803 REMARK 465 LEU E 804 REMARK 465 GLY E 805 REMARK 465 GLU E 806 REMARK 465 ASP E 832 REMARK 465 ASP E 833 REMARK 465 LYS E 834 REMARK 465 ILE E 835 REMARK 465 LEU E 836 REMARK 465 ILE E 837 REMARK 465 SER E 838 REMARK 465 TYR E 839 REMARK 465 PHE E 840 REMARK 465 ASN E 841 REMARK 465 LYS E 842 REMARK 465 PHE E 843 REMARK 465 PHE E 844 REMARK 465 LYS E 845 REMARK 465 GLY G -4 REMARK 465 PRO G -3 REMARK 465 LEU G -2 REMARK 465 GLY G -1 REMARK 465 SER G 0 REMARK 465 MET G 1 REMARK 465 THR G 459 REMARK 465 SER G 460 REMARK 465 ASN G 461 REMARK 465 ASN G 462 REMARK 465 ASN G 463 REMARK 465 TYR G 464 REMARK 465 GLU G 465 REMARK 465 ASN G 466 REMARK 465 ASP G 467 REMARK 465 LEU G 468 REMARK 465 ASP G 469 REMARK 465 GLN G 470 REMARK 465 VAL G 471 REMARK 465 ILE G 472 REMARK 465 LEU G 473 REMARK 465 ASN G 474 REMARK 465 PHE G 475 REMARK 465 ASN G 476 REMARK 465 SER G 477 REMARK 465 GLU G 478 REMARK 465 SER G 479 REMARK 465 ALA G 480 REMARK 465 PRO G 481 REMARK 465 GLY G 482 REMARK 465 LEU G 483 REMARK 465 SER G 484 REMARK 465 ASP G 485 REMARK 465 GLU G 486 REMARK 465 LYS G 487 REMARK 465 LEU G 488 REMARK 465 ASN G 489 REMARK 465 LEU G 490 REMARK 465 THR G 491 REMARK 465 ILE G 492 REMARK 465 GLN G 493 REMARK 465 ASN G 494 REMARK 465 GLY G 505 REMARK 465 GLY G 655 REMARK 465 SER G 656 REMARK 465 SER G 657 REMARK 465 ASP G 658 REMARK 465 ASP G 832 REMARK 465 ASP G 833 REMARK 465 LYS G 834 REMARK 465 ILE G 835 REMARK 465 LEU G 836 REMARK 465 ILE G 837 REMARK 465 SER G 838 REMARK 465 TYR G 839 REMARK 465 PHE G 840 REMARK 465 ASN G 841 REMARK 465 LYS G 842 REMARK 465 PHE G 843 REMARK 465 PHE G 844 REMARK 465 LYS G 845 REMARK 465 GLY B -4 REMARK 465 PRO B -3 REMARK 465 LEU B -2 REMARK 465 GLY B -1 REMARK 465 SER B 0 REMARK 465 MET B 1 REMARK 465 VAL B 458 REMARK 465 THR B 459 REMARK 465 SER B 460 REMARK 465 ASN B 461 REMARK 465 ASN B 462 REMARK 465 ASN B 463 REMARK 465 TYR B 464 REMARK 465 GLU B 465 REMARK 465 ASN B 466 REMARK 465 ASP B 467 REMARK 465 LEU B 468 REMARK 465 ASP B 469 REMARK 465 GLN B 470 REMARK 465 VAL B 471 REMARK 465 ILE B 472 REMARK 465 LEU B 473 REMARK 465 ASN B 474 REMARK 465 PHE B 475 REMARK 465 ASN B 476 REMARK 465 SER B 477 REMARK 465 GLU B 478 REMARK 465 SER B 479 REMARK 465 ALA B 480 REMARK 465 PRO B 481 REMARK 465 GLY B 482 REMARK 465 LEU B 483 REMARK 465 SER B 484 REMARK 465 ASP B 485 REMARK 465 GLU B 486 REMARK 465 LYS B 487 REMARK 465 LEU B 488 REMARK 465 ASN B 489 REMARK 465 LEU B 490 REMARK 465 THR B 491 REMARK 465 ILE B 492 REMARK 465 GLN B 493 REMARK 465 ASN B 494 REMARK 465 ASP B 495 REMARK 465 ALA B 496 REMARK 465 TYR B 497 REMARK 465 ILE B 498 REMARK 465 PRO B 499 REMARK 465 LYS B 500 REMARK 465 GLY B 655 REMARK 465 SER B 656 REMARK 465 SER B 657 REMARK 465 ASP B 658 REMARK 465 ASP B 832 REMARK 465 ASP B 833 REMARK 465 LYS B 834 REMARK 465 ILE B 835 REMARK 465 LEU B 836 REMARK 465 ILE B 837 REMARK 465 SER B 838 REMARK 465 TYR B 839 REMARK 465 PHE B 840 REMARK 465 ASN B 841 REMARK 465 LYS B 842 REMARK 465 PHE B 843 REMARK 465 PHE B 844 REMARK 465 LYS B 845 REMARK 465 GLY C -4 REMARK 465 PRO C -3 REMARK 465 LEU C -2 REMARK 465 GLY C -1 REMARK 465 SER C 0 REMARK 465 SER C 124 REMARK 465 GLY F -4 REMARK 465 PRO F -3 REMARK 465 LEU F -2 REMARK 465 GLY F -1 REMARK 465 SER F 0 REMARK 465 GLY F 10 REMARK 465 LEU F 11 REMARK 465 THR F 121 REMARK 465 VAL F 122 REMARK 465 SER F 123 REMARK 465 SER F 124 REMARK 465 GLY H -4 REMARK 465 PRO H -3 REMARK 465 LEU H -2 REMARK 465 GLY H -1 REMARK 465 SER H 0 REMARK 465 SER H 124 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 MET A 1 CG SD CE REMARK 470 LEU A 295 CG CD1 CD2 REMARK 470 TYR A 501 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS A 660 CG CD CE NZ REMARK 470 LYS A 722 CB CG CD CE NZ REMARK 470 LYS A 737 CG CD CE NZ REMARK 470 ARG D 27 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 43 CG CD CE NZ REMARK 470 ARG D 45 CG CD NE CZ NH1 NH2 REMARK 470 MET E 1 CG SD CE REMARK 470 ARG E 16 CG CD NE CZ NH1 NH2 REMARK 470 MET E 199 CG SD CE REMARK 470 GLN E 237 CG CD OE1 NE2 REMARK 470 ARG E 245 CG CD NE CZ NH1 NH2 REMARK 470 GLN E 354 CG CD OE1 NE2 REMARK 470 TYR E 355 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS E 356 CD CE NZ REMARK 470 LEU E 641 CG CD1 CD2 REMARK 470 VAL E 647 CG1 CG2 REMARK 470 ILE E 650 CG1 CG2 CD1 REMARK 470 LYS E 651 CG CD CE NZ REMARK 470 ILE E 715 CG2 REMARK 470 LYS E 737 CG CD CE NZ REMARK 470 LYS E 781 CG CD CE NZ REMARK 470 ILE E 798 CG1 CG2 CD1 REMARK 470 GLN E 799 CG CD OE1 NE2 REMARK 470 HIS E 800 CG ND1 CD2 CE1 NE2 REMARK 470 LEU E 827 CG CD1 CD2 REMARK 470 TYR E 830 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 THR E 831 OG1 CG2 REMARK 470 LYS G 135 CG CD CE NZ REMARK 470 ARG G 245 CG CD NE CZ NH1 NH2 REMARK 470 LEU G 295 CG CD1 CD2 REMARK 470 TYR G 357 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG G 402 CG CD NE CZ NH1 NH2 REMARK 470 TYR G 497 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ILE G 498 CG1 CG2 CD1 REMARK 470 LYS G 500 CG CD CE NZ REMARK 470 ASP G 502 CG OD1 OD2 REMARK 470 THR G 506 OG1 CG2 REMARK 470 LEU G 646 CG CD1 CD2 REMARK 470 LEU G 654 CG CD1 CD2 REMARK 470 LYS G 722 CB CG CD CE NZ REMARK 470 ASN G 732 CG OD1 ND2 REMARK 470 GLU G 806 CG CD OE1 OE2 REMARK 470 LEU B 295 CG CD1 CD2 REMARK 470 ASP B 502 CG OD1 OD2 REMARK 470 LYS B 565 CG CD CE NZ REMARK 470 LEU B 654 CG CD1 CD2 REMARK 470 LYS B 660 CG CD CE NZ REMARK 470 LYS B 662 CB CG CD CE NZ REMARK 470 LYS B 722 CB CG CD CE NZ REMARK 470 LYS B 737 CG CD CE NZ REMARK 470 LYS B 826 CG CD CE NZ REMARK 470 GLN C 1 CG CD OE1 NE2 REMARK 470 ARG C 27 CG CD NE CZ NH1 NH2 REMARK 470 PRO C 41 CG CD REMARK 470 LYS C 43 CG CD CE NZ REMARK 470 GLU C 44 CG CD OE1 OE2 REMARK 470 GLN F 1 CG CD OE1 NE2 REMARK 470 VAL F 12 CG1 CG2 REMARK 470 GLN F 13 CG CD OE1 NE2 REMARK 470 ARG F 19 CG CD NE CZ NH1 NH2 REMARK 470 ARG F 27 CG CD NE CZ NH1 NH2 REMARK 470 GLN F 39 CG CD OE1 NE2 REMARK 470 PRO F 41 CG CD REMARK 470 LYS F 43 CG CD CE NZ REMARK 470 GLU F 44 CG CD OE1 OE2 REMARK 470 ARG F 45 CG CD NE CZ NH1 NH2 REMARK 470 PHE F 68 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG F 72 CG CD NE CZ NH1 NH2 REMARK 470 PRO F 88 CG CD REMARK 470 GLN H 1 CG CD OE1 NE2 REMARK 470 ARG H 27 CG CD NE CZ NH1 NH2 REMARK 470 LYS H 43 CG CD CE NZ REMARK 470 GLU H 44 CG CD OE1 OE2 REMARK 470 ARG H 45 CG CD NE CZ NH1 NH2 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 OD1 ASN A 164 NZ LYS A 225 2.15 REMARK 500 OD1 ASN E 164 NZ LYS E 225 2.18 REMARK 500 O SER G 652 NE2 HIS G 800 2.19 REMARK 500 OD1 ASN G 164 NZ LYS G 225 2.19 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 OG1 THR E 17 O ALA G 313 2354 2.18 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 46 93.53 -69.90 REMARK 500 SER A 174 2.74 -67.64 REMARK 500 VAL A 291 -157.56 -126.17 REMARK 500 LEU A 296 10.80 -141.96 REMARK 500 ASN A 378 -112.22 52.08 REMARK 500 ASP A 445 -45.46 78.24 REMARK 500 ASP A 455 -145.12 -147.32 REMARK 500 PHE A 636 -53.58 -125.00 REMARK 500 GLU A 637 78.91 58.64 REMARK 500 LEU A 734 47.24 -89.02 REMARK 500 ASN A 780 -73.74 -92.58 REMARK 500 ALA D 14 -5.69 68.93 REMARK 500 ARG D 27 41.54 -82.21 REMARK 500 PHE D 29 -38.55 -136.83 REMARK 500 GLU D 44 142.92 -171.71 REMARK 500 VAL D 48 -76.83 -120.74 REMARK 500 ARG D 67 50.08 -118.70 REMARK 500 MET D 83 79.32 -107.27 REMARK 500 ARG D 102 -163.75 56.87 REMARK 500 TYR D 103 -42.78 69.58 REMARK 500 THR D 104 77.19 53.60 REMARK 500 SER E 174 1.90 -67.58 REMARK 500 SER E 292 1.46 -62.96 REMARK 500 ASN E 293 76.87 -172.81 REMARK 500 ASN E 378 -111.70 51.66 REMARK 500 PRO E 398 -178.80 -62.79 REMARK 500 ASP E 445 -45.21 78.05 REMARK 500 ASP E 455 -145.15 -148.76 REMARK 500 PHE E 636 -53.68 -124.07 REMARK 500 GLU E 637 78.56 58.16 REMARK 500 LEU E 734 47.15 -89.20 REMARK 500 ASN E 780 -69.78 -96.29 REMARK 500 ASN G 46 93.98 -69.99 REMARK 500 SER G 174 4.36 -68.50 REMARK 500 VAL G 291 -156.54 -128.15 REMARK 500 SER G 292 84.70 -60.77 REMARK 500 LEU G 296 10.75 -142.70 REMARK 500 ASN G 378 -112.56 51.60 REMARK 500 PRO G 398 -179.85 -62.77 REMARK 500 ASP G 445 -44.97 78.28 REMARK 500 ASP G 455 -145.31 -146.39 REMARK 500 ASN G 518 -169.41 -129.81 REMARK 500 PHE G 636 -54.32 -124.80 REMARK 500 GLU G 637 78.93 58.46 REMARK 500 LEU G 734 46.06 -89.27 REMARK 500 ASN G 780 -70.18 -95.35 REMARK 500 SER B 174 1.34 -67.22 REMARK 500 VAL B 291 -161.66 -129.20 REMARK 500 LEU B 296 10.87 -141.65 REMARK 500 ASN B 378 -112.59 52.00 REMARK 500 REMARK 500 THIS ENTRY HAS 84 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF1 7K7Y A 1 845 UNP A0A6B4PXW0_CLOBO DBREF2 7K7Y A A0A6B4PXW0 1 845 DBREF 7K7Y D -4 124 PDB 7K7Y 7K7Y -4 124 DBREF1 7K7Y E 1 845 UNP A0A6B4PXW0_CLOBO DBREF2 7K7Y E A0A6B4PXW0 1 845 DBREF1 7K7Y G 1 845 UNP A0A6B4PXW0_CLOBO DBREF2 7K7Y G A0A6B4PXW0 1 845 DBREF1 7K7Y B 1 845 UNP A0A6B4PXW0_CLOBO DBREF2 7K7Y B A0A6B4PXW0 1 845 DBREF 7K7Y C -4 124 PDB 7K7Y 7K7Y -4 124 DBREF 7K7Y F -4 124 PDB 7K7Y 7K7Y -4 124 DBREF 7K7Y H -4 124 PDB 7K7Y 7K7Y -4 124 SEQADV 7K7Y GLY A -4 UNP A0A6B4PXW EXPRESSION TAG SEQADV 7K7Y PRO A -3 UNP A0A6B4PXW EXPRESSION TAG SEQADV 7K7Y LEU A -2 UNP A0A6B4PXW EXPRESSION TAG SEQADV 7K7Y GLY A -1 UNP A0A6B4PXW EXPRESSION TAG SEQADV 7K7Y SER A 0 UNP A0A6B4PXW EXPRESSION TAG SEQADV 7K7Y GLY E -4 UNP A0A6B4PXW EXPRESSION TAG SEQADV 7K7Y PRO E -3 UNP A0A6B4PXW EXPRESSION TAG SEQADV 7K7Y LEU E -2 UNP A0A6B4PXW EXPRESSION TAG SEQADV 7K7Y GLY E -1 UNP A0A6B4PXW EXPRESSION TAG SEQADV 7K7Y SER E 0 UNP A0A6B4PXW EXPRESSION TAG SEQADV 7K7Y GLY G -4 UNP A0A6B4PXW EXPRESSION TAG SEQADV 7K7Y PRO G -3 UNP A0A6B4PXW EXPRESSION TAG SEQADV 7K7Y LEU G -2 UNP A0A6B4PXW EXPRESSION TAG SEQADV 7K7Y GLY G -1 UNP A0A6B4PXW EXPRESSION TAG SEQADV 7K7Y SER G 0 UNP A0A6B4PXW EXPRESSION TAG SEQADV 7K7Y GLY B -4 UNP A0A6B4PXW EXPRESSION TAG SEQADV 7K7Y PRO B -3 UNP A0A6B4PXW EXPRESSION TAG SEQADV 7K7Y LEU B -2 UNP A0A6B4PXW EXPRESSION TAG SEQADV 7K7Y GLY B -1 UNP A0A6B4PXW EXPRESSION TAG SEQADV 7K7Y SER B 0 UNP A0A6B4PXW EXPRESSION TAG SEQRES 1 A 850 GLY PRO LEU GLY SER MET PRO LYS ILE ASN SER PHE ASN SEQRES 2 A 850 TYR ASN ASP PRO VAL ASN ASP ARG THR ILE LEU TYR ILE SEQRES 3 A 850 LYS PRO GLY GLY CYS GLN GLU PHE TYR LYS SER PHE ASN SEQRES 4 A 850 ILE MET LYS ASN ILE TRP ILE ILE PRO GLU ARG ASN VAL SEQRES 5 A 850 ILE GLY THR THR PRO GLN ASP PHE HIS PRO PRO THR SER SEQRES 6 A 850 LEU LYS ASN GLY ASP SER SER TYR TYR ASP PRO ASN TYR SEQRES 7 A 850 LEU GLN SER ASP GLU GLU LYS ASP ARG PHE LEU LYS ILE SEQRES 8 A 850 VAL THR LYS ILE PHE ASN ARG ILE ASN ASN ASN LEU SER SEQRES 9 A 850 GLY GLY ILE LEU LEU GLU GLU LEU SER LYS ALA ASN PRO SEQRES 10 A 850 TYR LEU GLY ASN ASP ASN THR PRO ASP ASN GLN PHE HIS SEQRES 11 A 850 ILE GLY ASP ALA SER ALA VAL GLU ILE LYS PHE SER ASN SEQRES 12 A 850 GLY SER GLN ASP ILE LEU LEU PRO ASN VAL ILE ILE MET SEQRES 13 A 850 GLY ALA GLU PRO ASP LEU PHE GLU THR ASN SER SER ASN SEQRES 14 A 850 ILE SER LEU ARG ASN ASN TYR MET PRO SER ASN HIS GLY SEQRES 15 A 850 PHE GLY SER ILE ALA ILE VAL THR PHE SER PRO GLU TYR SEQRES 16 A 850 SER PHE ARG PHE ASN ASP ASN SER MET ASN GLU PHE ILE SEQRES 17 A 850 GLN ASP PRO ALA LEU THR LEU MET HIS GLU LEU ILE HIS SEQRES 18 A 850 SER LEU HIS GLY LEU TYR GLY ALA LYS GLY ILE THR THR SEQRES 19 A 850 LYS TYR THR ILE THR GLN LYS GLN ASN PRO LEU ILE THR SEQRES 20 A 850 ASN ILE ARG GLY THR ASN ILE GLU GLU PHE LEU THR PHE SEQRES 21 A 850 GLY GLY THR ASP LEU ASN ILE ILE THR SER ALA GLN SER SEQRES 22 A 850 ASN ASP ILE TYR THR ASN LEU LEU ALA ASP TYR LYS LYS SEQRES 23 A 850 ILE ALA SER LYS LEU SER LYS VAL GLN VAL SER ASN PRO SEQRES 24 A 850 LEU LEU ASN PRO TYR LYS ASP VAL PHE GLU ALA LYS TYR SEQRES 25 A 850 GLY LEU ASP LYS ASP ALA SER GLY ILE TYR SER VAL ASN SEQRES 26 A 850 ILE ASN LYS PHE ASN ASP ILE PHE LYS LYS LEU TYR SER SEQRES 27 A 850 PHE THR GLU PHE ASP LEU ALA THR LYS PHE GLN VAL LYS SEQRES 28 A 850 CYS ARG GLN THR TYR ILE GLY GLN TYR LYS TYR PHE LYS SEQRES 29 A 850 LEU SER ASN LEU LEU ASN ASP SER ILE TYR ASN ILE SER SEQRES 30 A 850 GLU GLY TYR ASN ILE ASN ASN LEU LYS VAL ASN PHE ARG SEQRES 31 A 850 GLY GLN ASN ALA ASN LEU ASN PRO ARG ILE ILE THR PRO SEQRES 32 A 850 ILE THR GLY ARG GLY LEU VAL LYS LYS ILE ILE ARG PHE SEQRES 33 A 850 CYS LYS ASN ILE VAL SER VAL LYS GLY ILE ARG LYS SER SEQRES 34 A 850 ILE CYS ILE GLU ILE ASN ASN GLY GLU LEU PHE PHE VAL SEQRES 35 A 850 ALA SER GLU ASN SER TYR ASN ASP ASP ASN ILE ASN THR SEQRES 36 A 850 PRO LYS GLU ILE ASP ASP THR VAL THR SER ASN ASN ASN SEQRES 37 A 850 TYR GLU ASN ASP LEU ASP GLN VAL ILE LEU ASN PHE ASN SEQRES 38 A 850 SER GLU SER ALA PRO GLY LEU SER ASP GLU LYS LEU ASN SEQRES 39 A 850 LEU THR ILE GLN ASN ASP ALA TYR ILE PRO LYS TYR ASP SEQRES 40 A 850 SER ASN GLY THR SER ASP ILE GLU GLN HIS ASP VAL ASN SEQRES 41 A 850 GLU LEU ASN VAL PHE PHE TYR LEU ASP ALA GLN LYS VAL SEQRES 42 A 850 PRO GLU GLY GLU ASN ASN VAL ASN LEU THR SER SER ILE SEQRES 43 A 850 ASP THR ALA LEU LEU GLU GLN PRO LYS ILE TYR THR PHE SEQRES 44 A 850 PHE SER SER GLU PHE ILE ASN ASN VAL ASN LYS PRO VAL SEQRES 45 A 850 GLN ALA ALA LEU PHE VAL SER TRP ILE GLN GLN VAL LEU SEQRES 46 A 850 VAL ASP PHE THR THR GLU ALA ASN GLN LYS SER THR VAL SEQRES 47 A 850 ASP LYS ILE ALA ASP ILE SER ILE VAL VAL PRO TYR ILE SEQRES 48 A 850 GLY LEU ALA LEU ASN ILE GLY ASN GLU ALA GLN LYS GLY SEQRES 49 A 850 ASN PHE LYS ASP ALA LEU GLU LEU LEU GLY ALA GLY ILE SEQRES 50 A 850 LEU LEU GLU PHE GLU PRO GLU LEU LEU ILE PRO THR ILE SEQRES 51 A 850 LEU VAL PHE THR ILE LYS SER PHE LEU GLY SER SER ASP SEQRES 52 A 850 ASN LYS ASN LYS VAL ILE LYS ALA ILE ASN ASN ALA LEU SEQRES 53 A 850 LYS GLU ARG ASP GLU LYS TRP LYS GLU VAL TYR SER PHE SEQRES 54 A 850 ILE VAL SER ASN TRP MET THR LYS ILE ASN THR GLN PHE SEQRES 55 A 850 ASN LYS ARG LYS GLU GLN MET TYR GLN ALA LEU GLN ASN SEQRES 56 A 850 GLN VAL ASN ALA ILE LYS THR ILE ILE GLU SER LYS TYR SEQRES 57 A 850 ASN SER TYR THR LEU GLU GLU LYS ASN GLU LEU THR ASN SEQRES 58 A 850 LYS TYR ASP ILE LYS GLN ILE GLU ASN GLU LEU ASN GLN SEQRES 59 A 850 LYS VAL SER ILE ALA MET ASN ASN ILE ASP ARG PHE LEU SEQRES 60 A 850 THR GLU SER SER ILE SER TYR LEU MET LYS LEU ILE ASN SEQRES 61 A 850 GLU VAL LYS ILE ASN LYS LEU ARG GLU TYR ASP GLU ASN SEQRES 62 A 850 VAL LYS THR TYR LEU LEU ASN TYR ILE ILE GLN HIS GLY SEQRES 63 A 850 SER ILE LEU GLY GLU SER GLN GLN GLU LEU ASN SER MET SEQRES 64 A 850 VAL THR ASP THR LEU ASN ASN SER ILE PRO PHE LYS LEU SEQRES 65 A 850 SER SER TYR THR ASP ASP LYS ILE LEU ILE SER TYR PHE SEQRES 66 A 850 ASN LYS PHE PHE LYS SEQRES 1 D 129 GLY PRO LEU GLY SER GLN LEU GLN LEU VAL GLU THR GLY SEQRES 2 D 129 GLY GLY LEU VAL GLN ALA GLY GLY SER LEU ARG LEU SER SEQRES 3 D 129 CYS ALA ALA SER GLY ARG THR PHE SER SER TYR SER MET SEQRES 4 D 129 GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU TYR SEQRES 5 D 129 VAL ALA ALA VAL ASN SER ASN GLY ASP SER THR PHE TYR SEQRES 6 D 129 ALA ASP SER ILE LYS GLY ARG PHE THR VAL SER ARG ASP SEQRES 7 D 129 ALA ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER LEU SEQRES 8 D 129 LYS PRO GLU ASP THR ALA LEU TYR TYR CYS ALA ALA VAL SEQRES 9 D 129 TYR GLY ARG TYR THR TYR GLN SER PRO LYS SER TYR GLU SEQRES 10 D 129 TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 1 E 850 GLY PRO LEU GLY SER MET PRO LYS ILE ASN SER PHE ASN SEQRES 2 E 850 TYR ASN ASP PRO VAL ASN ASP ARG THR ILE LEU TYR ILE SEQRES 3 E 850 LYS PRO GLY GLY CYS GLN GLU PHE TYR LYS SER PHE ASN SEQRES 4 E 850 ILE MET LYS ASN ILE TRP ILE ILE PRO GLU ARG ASN VAL SEQRES 5 E 850 ILE GLY THR THR PRO GLN ASP PHE HIS PRO PRO THR SER SEQRES 6 E 850 LEU LYS ASN GLY ASP SER SER TYR TYR ASP PRO ASN TYR SEQRES 7 E 850 LEU GLN SER ASP GLU GLU LYS ASP ARG PHE LEU LYS ILE SEQRES 8 E 850 VAL THR LYS ILE PHE ASN ARG ILE ASN ASN ASN LEU SER SEQRES 9 E 850 GLY GLY ILE LEU LEU GLU GLU LEU SER LYS ALA ASN PRO SEQRES 10 E 850 TYR LEU GLY ASN ASP ASN THR PRO ASP ASN GLN PHE HIS SEQRES 11 E 850 ILE GLY ASP ALA SER ALA VAL GLU ILE LYS PHE SER ASN SEQRES 12 E 850 GLY SER GLN ASP ILE LEU LEU PRO ASN VAL ILE ILE MET SEQRES 13 E 850 GLY ALA GLU PRO ASP LEU PHE GLU THR ASN SER SER ASN SEQRES 14 E 850 ILE SER LEU ARG ASN ASN TYR MET PRO SER ASN HIS GLY SEQRES 15 E 850 PHE GLY SER ILE ALA ILE VAL THR PHE SER PRO GLU TYR SEQRES 16 E 850 SER PHE ARG PHE ASN ASP ASN SER MET ASN GLU PHE ILE SEQRES 17 E 850 GLN ASP PRO ALA LEU THR LEU MET HIS GLU LEU ILE HIS SEQRES 18 E 850 SER LEU HIS GLY LEU TYR GLY ALA LYS GLY ILE THR THR SEQRES 19 E 850 LYS TYR THR ILE THR GLN LYS GLN ASN PRO LEU ILE THR SEQRES 20 E 850 ASN ILE ARG GLY THR ASN ILE GLU GLU PHE LEU THR PHE SEQRES 21 E 850 GLY GLY THR ASP LEU ASN ILE ILE THR SER ALA GLN SER SEQRES 22 E 850 ASN ASP ILE TYR THR ASN LEU LEU ALA ASP TYR LYS LYS SEQRES 23 E 850 ILE ALA SER LYS LEU SER LYS VAL GLN VAL SER ASN PRO SEQRES 24 E 850 LEU LEU ASN PRO TYR LYS ASP VAL PHE GLU ALA LYS TYR SEQRES 25 E 850 GLY LEU ASP LYS ASP ALA SER GLY ILE TYR SER VAL ASN SEQRES 26 E 850 ILE ASN LYS PHE ASN ASP ILE PHE LYS LYS LEU TYR SER SEQRES 27 E 850 PHE THR GLU PHE ASP LEU ALA THR LYS PHE GLN VAL LYS SEQRES 28 E 850 CYS ARG GLN THR TYR ILE GLY GLN TYR LYS TYR PHE LYS SEQRES 29 E 850 LEU SER ASN LEU LEU ASN ASP SER ILE TYR ASN ILE SER SEQRES 30 E 850 GLU GLY TYR ASN ILE ASN ASN LEU LYS VAL ASN PHE ARG SEQRES 31 E 850 GLY GLN ASN ALA ASN LEU ASN PRO ARG ILE ILE THR PRO SEQRES 32 E 850 ILE THR GLY ARG GLY LEU VAL LYS LYS ILE ILE ARG PHE SEQRES 33 E 850 CYS LYS ASN ILE VAL SER VAL LYS GLY ILE ARG LYS SER SEQRES 34 E 850 ILE CYS ILE GLU ILE ASN ASN GLY GLU LEU PHE PHE VAL SEQRES 35 E 850 ALA SER GLU ASN SER TYR ASN ASP ASP ASN ILE ASN THR SEQRES 36 E 850 PRO LYS GLU ILE ASP ASP THR VAL THR SER ASN ASN ASN SEQRES 37 E 850 TYR GLU ASN ASP LEU ASP GLN VAL ILE LEU ASN PHE ASN SEQRES 38 E 850 SER GLU SER ALA PRO GLY LEU SER ASP GLU LYS LEU ASN SEQRES 39 E 850 LEU THR ILE GLN ASN ASP ALA TYR ILE PRO LYS TYR ASP SEQRES 40 E 850 SER ASN GLY THR SER ASP ILE GLU GLN HIS ASP VAL ASN SEQRES 41 E 850 GLU LEU ASN VAL PHE PHE TYR LEU ASP ALA GLN LYS VAL SEQRES 42 E 850 PRO GLU GLY GLU ASN ASN VAL ASN LEU THR SER SER ILE SEQRES 43 E 850 ASP THR ALA LEU LEU GLU GLN PRO LYS ILE TYR THR PHE SEQRES 44 E 850 PHE SER SER GLU PHE ILE ASN ASN VAL ASN LYS PRO VAL SEQRES 45 E 850 GLN ALA ALA LEU PHE VAL SER TRP ILE GLN GLN VAL LEU SEQRES 46 E 850 VAL ASP PHE THR THR GLU ALA ASN GLN LYS SER THR VAL SEQRES 47 E 850 ASP LYS ILE ALA ASP ILE SER ILE VAL VAL PRO TYR ILE SEQRES 48 E 850 GLY LEU ALA LEU ASN ILE GLY ASN GLU ALA GLN LYS GLY SEQRES 49 E 850 ASN PHE LYS ASP ALA LEU GLU LEU LEU GLY ALA GLY ILE SEQRES 50 E 850 LEU LEU GLU PHE GLU PRO GLU LEU LEU ILE PRO THR ILE SEQRES 51 E 850 LEU VAL PHE THR ILE LYS SER PHE LEU GLY SER SER ASP SEQRES 52 E 850 ASN LYS ASN LYS VAL ILE LYS ALA ILE ASN ASN ALA LEU SEQRES 53 E 850 LYS GLU ARG ASP GLU LYS TRP LYS GLU VAL TYR SER PHE SEQRES 54 E 850 ILE VAL SER ASN TRP MET THR LYS ILE ASN THR GLN PHE SEQRES 55 E 850 ASN LYS ARG LYS GLU GLN MET TYR GLN ALA LEU GLN ASN SEQRES 56 E 850 GLN VAL ASN ALA ILE LYS THR ILE ILE GLU SER LYS TYR SEQRES 57 E 850 ASN SER TYR THR LEU GLU GLU LYS ASN GLU LEU THR ASN SEQRES 58 E 850 LYS TYR ASP ILE LYS GLN ILE GLU ASN GLU LEU ASN GLN SEQRES 59 E 850 LYS VAL SER ILE ALA MET ASN ASN ILE ASP ARG PHE LEU SEQRES 60 E 850 THR GLU SER SER ILE SER TYR LEU MET LYS LEU ILE ASN SEQRES 61 E 850 GLU VAL LYS ILE ASN LYS LEU ARG GLU TYR ASP GLU ASN SEQRES 62 E 850 VAL LYS THR TYR LEU LEU ASN TYR ILE ILE GLN HIS GLY SEQRES 63 E 850 SER ILE LEU GLY GLU SER GLN GLN GLU LEU ASN SER MET SEQRES 64 E 850 VAL THR ASP THR LEU ASN ASN SER ILE PRO PHE LYS LEU SEQRES 65 E 850 SER SER TYR THR ASP ASP LYS ILE LEU ILE SER TYR PHE SEQRES 66 E 850 ASN LYS PHE PHE LYS SEQRES 1 G 850 GLY PRO LEU GLY SER MET PRO LYS ILE ASN SER PHE ASN SEQRES 2 G 850 TYR ASN ASP PRO VAL ASN ASP ARG THR ILE LEU TYR ILE SEQRES 3 G 850 LYS PRO GLY GLY CYS GLN GLU PHE TYR LYS SER PHE ASN SEQRES 4 G 850 ILE MET LYS ASN ILE TRP ILE ILE PRO GLU ARG ASN VAL SEQRES 5 G 850 ILE GLY THR THR PRO GLN ASP PHE HIS PRO PRO THR SER SEQRES 6 G 850 LEU LYS ASN GLY ASP SER SER TYR TYR ASP PRO ASN TYR SEQRES 7 G 850 LEU GLN SER ASP GLU GLU LYS ASP ARG PHE LEU LYS ILE SEQRES 8 G 850 VAL THR LYS ILE PHE ASN ARG ILE ASN ASN ASN LEU SER SEQRES 9 G 850 GLY GLY ILE LEU LEU GLU GLU LEU SER LYS ALA ASN PRO SEQRES 10 G 850 TYR LEU GLY ASN ASP ASN THR PRO ASP ASN GLN PHE HIS SEQRES 11 G 850 ILE GLY ASP ALA SER ALA VAL GLU ILE LYS PHE SER ASN SEQRES 12 G 850 GLY SER GLN ASP ILE LEU LEU PRO ASN VAL ILE ILE MET SEQRES 13 G 850 GLY ALA GLU PRO ASP LEU PHE GLU THR ASN SER SER ASN SEQRES 14 G 850 ILE SER LEU ARG ASN ASN TYR MET PRO SER ASN HIS GLY SEQRES 15 G 850 PHE GLY SER ILE ALA ILE VAL THR PHE SER PRO GLU TYR SEQRES 16 G 850 SER PHE ARG PHE ASN ASP ASN SER MET ASN GLU PHE ILE SEQRES 17 G 850 GLN ASP PRO ALA LEU THR LEU MET HIS GLU LEU ILE HIS SEQRES 18 G 850 SER LEU HIS GLY LEU TYR GLY ALA LYS GLY ILE THR THR SEQRES 19 G 850 LYS TYR THR ILE THR GLN LYS GLN ASN PRO LEU ILE THR SEQRES 20 G 850 ASN ILE ARG GLY THR ASN ILE GLU GLU PHE LEU THR PHE SEQRES 21 G 850 GLY GLY THR ASP LEU ASN ILE ILE THR SER ALA GLN SER SEQRES 22 G 850 ASN ASP ILE TYR THR ASN LEU LEU ALA ASP TYR LYS LYS SEQRES 23 G 850 ILE ALA SER LYS LEU SER LYS VAL GLN VAL SER ASN PRO SEQRES 24 G 850 LEU LEU ASN PRO TYR LYS ASP VAL PHE GLU ALA LYS TYR SEQRES 25 G 850 GLY LEU ASP LYS ASP ALA SER GLY ILE TYR SER VAL ASN SEQRES 26 G 850 ILE ASN LYS PHE ASN ASP ILE PHE LYS LYS LEU TYR SER SEQRES 27 G 850 PHE THR GLU PHE ASP LEU ALA THR LYS PHE GLN VAL LYS SEQRES 28 G 850 CYS ARG GLN THR TYR ILE GLY GLN TYR LYS TYR PHE LYS SEQRES 29 G 850 LEU SER ASN LEU LEU ASN ASP SER ILE TYR ASN ILE SER SEQRES 30 G 850 GLU GLY TYR ASN ILE ASN ASN LEU LYS VAL ASN PHE ARG SEQRES 31 G 850 GLY GLN ASN ALA ASN LEU ASN PRO ARG ILE ILE THR PRO SEQRES 32 G 850 ILE THR GLY ARG GLY LEU VAL LYS LYS ILE ILE ARG PHE SEQRES 33 G 850 CYS LYS ASN ILE VAL SER VAL LYS GLY ILE ARG LYS SER SEQRES 34 G 850 ILE CYS ILE GLU ILE ASN ASN GLY GLU LEU PHE PHE VAL SEQRES 35 G 850 ALA SER GLU ASN SER TYR ASN ASP ASP ASN ILE ASN THR SEQRES 36 G 850 PRO LYS GLU ILE ASP ASP THR VAL THR SER ASN ASN ASN SEQRES 37 G 850 TYR GLU ASN ASP LEU ASP GLN VAL ILE LEU ASN PHE ASN SEQRES 38 G 850 SER GLU SER ALA PRO GLY LEU SER ASP GLU LYS LEU ASN SEQRES 39 G 850 LEU THR ILE GLN ASN ASP ALA TYR ILE PRO LYS TYR ASP SEQRES 40 G 850 SER ASN GLY THR SER ASP ILE GLU GLN HIS ASP VAL ASN SEQRES 41 G 850 GLU LEU ASN VAL PHE PHE TYR LEU ASP ALA GLN LYS VAL SEQRES 42 G 850 PRO GLU GLY GLU ASN ASN VAL ASN LEU THR SER SER ILE SEQRES 43 G 850 ASP THR ALA LEU LEU GLU GLN PRO LYS ILE TYR THR PHE SEQRES 44 G 850 PHE SER SER GLU PHE ILE ASN ASN VAL ASN LYS PRO VAL SEQRES 45 G 850 GLN ALA ALA LEU PHE VAL SER TRP ILE GLN GLN VAL LEU SEQRES 46 G 850 VAL ASP PHE THR THR GLU ALA ASN GLN LYS SER THR VAL SEQRES 47 G 850 ASP LYS ILE ALA ASP ILE SER ILE VAL VAL PRO TYR ILE SEQRES 48 G 850 GLY LEU ALA LEU ASN ILE GLY ASN GLU ALA GLN LYS GLY SEQRES 49 G 850 ASN PHE LYS ASP ALA LEU GLU LEU LEU GLY ALA GLY ILE SEQRES 50 G 850 LEU LEU GLU PHE GLU PRO GLU LEU LEU ILE PRO THR ILE SEQRES 51 G 850 LEU VAL PHE THR ILE LYS SER PHE LEU GLY SER SER ASP SEQRES 52 G 850 ASN LYS ASN LYS VAL ILE LYS ALA ILE ASN ASN ALA LEU SEQRES 53 G 850 LYS GLU ARG ASP GLU LYS TRP LYS GLU VAL TYR SER PHE SEQRES 54 G 850 ILE VAL SER ASN TRP MET THR LYS ILE ASN THR GLN PHE SEQRES 55 G 850 ASN LYS ARG LYS GLU GLN MET TYR GLN ALA LEU GLN ASN SEQRES 56 G 850 GLN VAL ASN ALA ILE LYS THR ILE ILE GLU SER LYS TYR SEQRES 57 G 850 ASN SER TYR THR LEU GLU GLU LYS ASN GLU LEU THR ASN SEQRES 58 G 850 LYS TYR ASP ILE LYS GLN ILE GLU ASN GLU LEU ASN GLN SEQRES 59 G 850 LYS VAL SER ILE ALA MET ASN ASN ILE ASP ARG PHE LEU SEQRES 60 G 850 THR GLU SER SER ILE SER TYR LEU MET LYS LEU ILE ASN SEQRES 61 G 850 GLU VAL LYS ILE ASN LYS LEU ARG GLU TYR ASP GLU ASN SEQRES 62 G 850 VAL LYS THR TYR LEU LEU ASN TYR ILE ILE GLN HIS GLY SEQRES 63 G 850 SER ILE LEU GLY GLU SER GLN GLN GLU LEU ASN SER MET SEQRES 64 G 850 VAL THR ASP THR LEU ASN ASN SER ILE PRO PHE LYS LEU SEQRES 65 G 850 SER SER TYR THR ASP ASP LYS ILE LEU ILE SER TYR PHE SEQRES 66 G 850 ASN LYS PHE PHE LYS SEQRES 1 B 850 GLY PRO LEU GLY SER MET PRO LYS ILE ASN SER PHE ASN SEQRES 2 B 850 TYR ASN ASP PRO VAL ASN ASP ARG THR ILE LEU TYR ILE SEQRES 3 B 850 LYS PRO GLY GLY CYS GLN GLU PHE TYR LYS SER PHE ASN SEQRES 4 B 850 ILE MET LYS ASN ILE TRP ILE ILE PRO GLU ARG ASN VAL SEQRES 5 B 850 ILE GLY THR THR PRO GLN ASP PHE HIS PRO PRO THR SER SEQRES 6 B 850 LEU LYS ASN GLY ASP SER SER TYR TYR ASP PRO ASN TYR SEQRES 7 B 850 LEU GLN SER ASP GLU GLU LYS ASP ARG PHE LEU LYS ILE SEQRES 8 B 850 VAL THR LYS ILE PHE ASN ARG ILE ASN ASN ASN LEU SER SEQRES 9 B 850 GLY GLY ILE LEU LEU GLU GLU LEU SER LYS ALA ASN PRO SEQRES 10 B 850 TYR LEU GLY ASN ASP ASN THR PRO ASP ASN GLN PHE HIS SEQRES 11 B 850 ILE GLY ASP ALA SER ALA VAL GLU ILE LYS PHE SER ASN SEQRES 12 B 850 GLY SER GLN ASP ILE LEU LEU PRO ASN VAL ILE ILE MET SEQRES 13 B 850 GLY ALA GLU PRO ASP LEU PHE GLU THR ASN SER SER ASN SEQRES 14 B 850 ILE SER LEU ARG ASN ASN TYR MET PRO SER ASN HIS GLY SEQRES 15 B 850 PHE GLY SER ILE ALA ILE VAL THR PHE SER PRO GLU TYR SEQRES 16 B 850 SER PHE ARG PHE ASN ASP ASN SER MET ASN GLU PHE ILE SEQRES 17 B 850 GLN ASP PRO ALA LEU THR LEU MET HIS GLU LEU ILE HIS SEQRES 18 B 850 SER LEU HIS GLY LEU TYR GLY ALA LYS GLY ILE THR THR SEQRES 19 B 850 LYS TYR THR ILE THR GLN LYS GLN ASN PRO LEU ILE THR SEQRES 20 B 850 ASN ILE ARG GLY THR ASN ILE GLU GLU PHE LEU THR PHE SEQRES 21 B 850 GLY GLY THR ASP LEU ASN ILE ILE THR SER ALA GLN SER SEQRES 22 B 850 ASN ASP ILE TYR THR ASN LEU LEU ALA ASP TYR LYS LYS SEQRES 23 B 850 ILE ALA SER LYS LEU SER LYS VAL GLN VAL SER ASN PRO SEQRES 24 B 850 LEU LEU ASN PRO TYR LYS ASP VAL PHE GLU ALA LYS TYR SEQRES 25 B 850 GLY LEU ASP LYS ASP ALA SER GLY ILE TYR SER VAL ASN SEQRES 26 B 850 ILE ASN LYS PHE ASN ASP ILE PHE LYS LYS LEU TYR SER SEQRES 27 B 850 PHE THR GLU PHE ASP LEU ALA THR LYS PHE GLN VAL LYS SEQRES 28 B 850 CYS ARG GLN THR TYR ILE GLY GLN TYR LYS TYR PHE LYS SEQRES 29 B 850 LEU SER ASN LEU LEU ASN ASP SER ILE TYR ASN ILE SER SEQRES 30 B 850 GLU GLY TYR ASN ILE ASN ASN LEU LYS VAL ASN PHE ARG SEQRES 31 B 850 GLY GLN ASN ALA ASN LEU ASN PRO ARG ILE ILE THR PRO SEQRES 32 B 850 ILE THR GLY ARG GLY LEU VAL LYS LYS ILE ILE ARG PHE SEQRES 33 B 850 CYS LYS ASN ILE VAL SER VAL LYS GLY ILE ARG LYS SER SEQRES 34 B 850 ILE CYS ILE GLU ILE ASN ASN GLY GLU LEU PHE PHE VAL SEQRES 35 B 850 ALA SER GLU ASN SER TYR ASN ASP ASP ASN ILE ASN THR SEQRES 36 B 850 PRO LYS GLU ILE ASP ASP THR VAL THR SER ASN ASN ASN SEQRES 37 B 850 TYR GLU ASN ASP LEU ASP GLN VAL ILE LEU ASN PHE ASN SEQRES 38 B 850 SER GLU SER ALA PRO GLY LEU SER ASP GLU LYS LEU ASN SEQRES 39 B 850 LEU THR ILE GLN ASN ASP ALA TYR ILE PRO LYS TYR ASP SEQRES 40 B 850 SER ASN GLY THR SER ASP ILE GLU GLN HIS ASP VAL ASN SEQRES 41 B 850 GLU LEU ASN VAL PHE PHE TYR LEU ASP ALA GLN LYS VAL SEQRES 42 B 850 PRO GLU GLY GLU ASN ASN VAL ASN LEU THR SER SER ILE SEQRES 43 B 850 ASP THR ALA LEU LEU GLU GLN PRO LYS ILE TYR THR PHE SEQRES 44 B 850 PHE SER SER GLU PHE ILE ASN ASN VAL ASN LYS PRO VAL SEQRES 45 B 850 GLN ALA ALA LEU PHE VAL SER TRP ILE GLN GLN VAL LEU SEQRES 46 B 850 VAL ASP PHE THR THR GLU ALA ASN GLN LYS SER THR VAL SEQRES 47 B 850 ASP LYS ILE ALA ASP ILE SER ILE VAL VAL PRO TYR ILE SEQRES 48 B 850 GLY LEU ALA LEU ASN ILE GLY ASN GLU ALA GLN LYS GLY SEQRES 49 B 850 ASN PHE LYS ASP ALA LEU GLU LEU LEU GLY ALA GLY ILE SEQRES 50 B 850 LEU LEU GLU PHE GLU PRO GLU LEU LEU ILE PRO THR ILE SEQRES 51 B 850 LEU VAL PHE THR ILE LYS SER PHE LEU GLY SER SER ASP SEQRES 52 B 850 ASN LYS ASN LYS VAL ILE LYS ALA ILE ASN ASN ALA LEU SEQRES 53 B 850 LYS GLU ARG ASP GLU LYS TRP LYS GLU VAL TYR SER PHE SEQRES 54 B 850 ILE VAL SER ASN TRP MET THR LYS ILE ASN THR GLN PHE SEQRES 55 B 850 ASN LYS ARG LYS GLU GLN MET TYR GLN ALA LEU GLN ASN SEQRES 56 B 850 GLN VAL ASN ALA ILE LYS THR ILE ILE GLU SER LYS TYR SEQRES 57 B 850 ASN SER TYR THR LEU GLU GLU LYS ASN GLU LEU THR ASN SEQRES 58 B 850 LYS TYR ASP ILE LYS GLN ILE GLU ASN GLU LEU ASN GLN SEQRES 59 B 850 LYS VAL SER ILE ALA MET ASN ASN ILE ASP ARG PHE LEU SEQRES 60 B 850 THR GLU SER SER ILE SER TYR LEU MET LYS LEU ILE ASN SEQRES 61 B 850 GLU VAL LYS ILE ASN LYS LEU ARG GLU TYR ASP GLU ASN SEQRES 62 B 850 VAL LYS THR TYR LEU LEU ASN TYR ILE ILE GLN HIS GLY SEQRES 63 B 850 SER ILE LEU GLY GLU SER GLN GLN GLU LEU ASN SER MET SEQRES 64 B 850 VAL THR ASP THR LEU ASN ASN SER ILE PRO PHE LYS LEU SEQRES 65 B 850 SER SER TYR THR ASP ASP LYS ILE LEU ILE SER TYR PHE SEQRES 66 B 850 ASN LYS PHE PHE LYS SEQRES 1 C 129 GLY PRO LEU GLY SER GLN LEU GLN LEU VAL GLU THR GLY SEQRES 2 C 129 GLY GLY LEU VAL GLN ALA GLY GLY SER LEU ARG LEU SER SEQRES 3 C 129 CYS ALA ALA SER GLY ARG THR PHE SER SER TYR SER MET SEQRES 4 C 129 GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU TYR SEQRES 5 C 129 VAL ALA ALA VAL ASN SER ASN GLY ASP SER THR PHE TYR SEQRES 6 C 129 ALA ASP SER ILE LYS GLY ARG PHE THR VAL SER ARG ASP SEQRES 7 C 129 ALA ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER LEU SEQRES 8 C 129 LYS PRO GLU ASP THR ALA LEU TYR TYR CYS ALA ALA VAL SEQRES 9 C 129 TYR GLY ARG TYR THR TYR GLN SER PRO LYS SER TYR GLU SEQRES 10 C 129 TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 1 F 129 GLY PRO LEU GLY SER GLN LEU GLN LEU VAL GLU THR GLY SEQRES 2 F 129 GLY GLY LEU VAL GLN ALA GLY GLY SER LEU ARG LEU SER SEQRES 3 F 129 CYS ALA ALA SER GLY ARG THR PHE SER SER TYR SER MET SEQRES 4 F 129 GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU TYR SEQRES 5 F 129 VAL ALA ALA VAL ASN SER ASN GLY ASP SER THR PHE TYR SEQRES 6 F 129 ALA ASP SER ILE LYS GLY ARG PHE THR VAL SER ARG ASP SEQRES 7 F 129 ALA ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER LEU SEQRES 8 F 129 LYS PRO GLU ASP THR ALA LEU TYR TYR CYS ALA ALA VAL SEQRES 9 F 129 TYR GLY ARG TYR THR TYR GLN SER PRO LYS SER TYR GLU SEQRES 10 F 129 TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 1 H 129 GLY PRO LEU GLY SER GLN LEU GLN LEU VAL GLU THR GLY SEQRES 2 H 129 GLY GLY LEU VAL GLN ALA GLY GLY SER LEU ARG LEU SER SEQRES 3 H 129 CYS ALA ALA SER GLY ARG THR PHE SER SER TYR SER MET SEQRES 4 H 129 GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU TYR SEQRES 5 H 129 VAL ALA ALA VAL ASN SER ASN GLY ASP SER THR PHE TYR SEQRES 6 H 129 ALA ASP SER ILE LYS GLY ARG PHE THR VAL SER ARG ASP SEQRES 7 H 129 ALA ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER LEU SEQRES 8 H 129 LYS PRO GLU ASP THR ALA LEU TYR TYR CYS ALA ALA VAL SEQRES 9 H 129 TYR GLY ARG TYR THR TYR GLN SER PRO LYS SER TYR GLU SEQRES 10 H 129 TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER HELIX 1 AA1 THR A 51 HIS A 56 5 6 HELIX 2 AA2 SER A 76 ASN A 96 1 21 HELIX 3 AA3 ASN A 97 ALA A 110 1 14 HELIX 4 AA4 MET A 172 HIS A 176 5 5 HELIX 5 AA5 ASP A 205 TYR A 222 1 18 HELIX 6 AA6 ILE A 249 GLY A 256 1 8 HELIX 7 AA7 GLY A 257 ILE A 263 5 7 HELIX 8 AA8 THR A 264 SER A 287 1 24 HELIX 9 AA9 LEU A 296 TYR A 307 1 12 HELIX 10 AB1 ASN A 320 PHE A 334 1 15 HELIX 11 AB2 THR A 335 PHE A 343 1 9 HELIX 12 AB3 ILE A 377 ASN A 388 5 12 HELIX 13 AB4 ASN A 392 ARG A 394 5 3 HELIX 14 AB5 GLY A 432 LEU A 434 5 3 HELIX 15 AB6 SER A 439 TYR A 443 5 5 HELIX 16 AB7 ASP A 445 THR A 450 5 6 HELIX 17 AB8 ASN A 518 ALA A 525 1 8 HELIX 18 AB9 SER A 540 GLU A 547 1 8 HELIX 19 AC1 SER A 556 ASN A 564 1 9 HELIX 20 AC2 LEU A 571 ASN A 588 1 18 HELIX 21 AC3 TYR A 605 ASN A 611 1 7 HELIX 22 AC4 ASN A 614 ASN A 620 1 7 HELIX 23 AC5 ASN A 620 GLY A 629 1 10 HELIX 24 AC6 ALA A 630 LEU A 633 5 4 HELIX 25 AC7 ASN A 659 ILE A 693 1 35 HELIX 26 AC8 ILE A 693 LYS A 722 1 30 HELIX 27 AC9 THR A 727 LEU A 734 1 8 HELIX 28 AD1 ASP A 739 HIS A 800 1 62 HELIX 29 AD2 HIS A 800 GLY A 805 1 6 HELIX 30 AD3 GLU A 806 ASN A 820 1 15 HELIX 31 AD4 LYS A 826 THR A 831 1 6 HELIX 32 AD5 LYS D 87 THR D 91 5 5 HELIX 33 AD6 THR E 51 HIS E 56 5 6 HELIX 34 AD7 SER E 76 ASN E 96 1 21 HELIX 35 AD8 ASN E 97 ALA E 110 1 14 HELIX 36 AD9 MET E 172 HIS E 176 5 5 HELIX 37 AE1 ASP E 205 TYR E 222 1 18 HELIX 38 AE2 ILE E 249 GLY E 256 1 8 HELIX 39 AE3 GLY E 257 ILE E 263 5 7 HELIX 40 AE4 THR E 264 SER E 287 1 24 HELIX 41 AE5 LEU E 296 TYR E 307 1 12 HELIX 42 AE6 ASN E 320 PHE E 334 1 15 HELIX 43 AE7 THR E 335 PHE E 343 1 9 HELIX 44 AE8 ILE E 377 ASN E 388 5 12 HELIX 45 AE9 ASN E 392 ARG E 394 5 3 HELIX 46 AF1 GLY E 432 LEU E 434 5 3 HELIX 47 AF2 SER E 439 TYR E 443 5 5 HELIX 48 AF3 ASP E 445 THR E 450 5 6 HELIX 49 AF4 ASN E 518 GLN E 526 1 9 HELIX 50 AF5 SER E 540 GLU E 547 1 8 HELIX 51 AF6 SER E 556 ASN E 564 1 9 HELIX 52 AF7 LEU E 571 ASN E 588 1 18 HELIX 53 AF8 TYR E 605 ASN E 611 1 7 HELIX 54 AF9 ASN E 614 ASN E 620 1 7 HELIX 55 AG1 ASN E 620 GLY E 629 1 10 HELIX 56 AG2 ALA E 630 LEU E 633 5 4 HELIX 57 AG3 ASN E 661 ILE E 693 1 33 HELIX 58 AG4 ILE E 693 LYS E 722 1 30 HELIX 59 AG5 THR E 727 LEU E 734 1 8 HELIX 60 AG6 ASP E 739 HIS E 800 1 62 HELIX 61 AG7 GLN E 808 ASN E 820 1 13 HELIX 62 AG8 LYS E 826 THR E 831 1 6 HELIX 63 AG9 SER G 76 ASN G 96 1 21 HELIX 64 AH1 ASN G 97 ALA G 110 1 14 HELIX 65 AH2 MET G 172 HIS G 176 5 5 HELIX 66 AH3 ASP G 205 TYR G 222 1 18 HELIX 67 AH4 ILE G 249 GLY G 256 1 8 HELIX 68 AH5 GLY G 257 ILE G 263 5 7 HELIX 69 AH6 THR G 264 SER G 287 1 24 HELIX 70 AH7 SER G 292 TYR G 307 1 16 HELIX 71 AH8 ASN G 320 PHE G 334 1 15 HELIX 72 AH9 THR G 335 PHE G 343 1 9 HELIX 73 AI1 ILE G 377 ASN G 388 5 12 HELIX 74 AI2 ASN G 392 ARG G 394 5 3 HELIX 75 AI3 GLY G 432 LEU G 434 5 3 HELIX 76 AI4 SER G 439 TYR G 443 5 5 HELIX 77 AI5 ASP G 445 THR G 450 5 6 HELIX 78 AI6 ASN G 518 GLN G 526 1 9 HELIX 79 AI7 SER G 540 GLU G 547 1 8 HELIX 80 AI8 SER G 556 ASN G 564 1 9 HELIX 81 AI9 LEU G 571 ASN G 588 1 18 HELIX 82 AJ1 TYR G 605 ASN G 611 1 7 HELIX 83 AJ2 ASN G 614 ASN G 620 1 7 HELIX 84 AJ3 ASN G 620 GLY G 629 1 10 HELIX 85 AJ4 ALA G 630 LEU G 634 5 5 HELIX 86 AJ5 LYS G 660 ILE G 693 1 34 HELIX 87 AJ6 ILE G 693 LYS G 722 1 30 HELIX 88 AJ7 THR G 727 LEU G 734 1 8 HELIX 89 AJ8 ASP G 739 HIS G 800 1 62 HELIX 90 AJ9 LEU G 804 GLU G 806 5 3 HELIX 91 AK1 SER G 807 LEU G 819 1 13 HELIX 92 AK2 LYS G 826 THR G 831 1 6 HELIX 93 AK3 THR B 51 HIS B 56 5 6 HELIX 94 AK4 SER B 76 ASN B 96 1 21 HELIX 95 AK5 ASN B 97 ALA B 110 1 14 HELIX 96 AK6 MET B 172 HIS B 176 5 5 HELIX 97 AK7 ASP B 205 TYR B 222 1 18 HELIX 98 AK8 ILE B 249 GLY B 256 1 8 HELIX 99 AK9 GLY B 257 ILE B 263 5 7 HELIX 100 AL1 THR B 264 SER B 287 1 24 HELIX 101 AL2 SER B 292 TYR B 307 1 16 HELIX 102 AL3 ASN B 320 PHE B 334 1 15 HELIX 103 AL4 THR B 335 PHE B 343 1 9 HELIX 104 AL5 ILE B 377 ASN B 388 5 12 HELIX 105 AL6 ASN B 392 ARG B 394 5 3 HELIX 106 AL7 GLY B 432 LEU B 434 5 3 HELIX 107 AL8 SER B 439 TYR B 443 5 5 HELIX 108 AL9 ASP B 445 THR B 450 5 6 HELIX 109 AM1 ASN B 518 GLN B 526 1 9 HELIX 110 AM2 SER B 540 GLU B 547 1 8 HELIX 111 AM3 SER B 556 ASN B 564 1 9 HELIX 112 AM4 LEU B 571 ASN B 588 1 18 HELIX 113 AM5 TYR B 605 ASN B 611 1 7 HELIX 114 AM6 ASN B 614 ASN B 620 1 7 HELIX 115 AM7 ASN B 620 GLY B 629 1 10 HELIX 116 AM8 ALA B 630 LEU B 633 5 4 HELIX 117 AM9 LYS B 660 ILE B 693 1 34 HELIX 118 AN1 ILE B 693 LYS B 722 1 30 HELIX 119 AN2 THR B 727 LEU B 734 1 8 HELIX 120 AN3 ASP B 739 HIS B 800 1 62 HELIX 121 AN4 SER B 807 LEU B 819 1 13 HELIX 122 AN5 LYS B 826 THR B 831 1 6 HELIX 123 AN6 LYS C 87 THR C 91 5 5 HELIX 124 AN7 LYS F 87 THR F 91 5 5 HELIX 125 AN8 LYS H 87 THR H 91 5 5 SHEET 1 AA1 8 GLN A 141 LEU A 144 0 SHEET 2 AA1 8 VAL A 132 LYS A 135 -1 N ILE A 134 O ASP A 142 SHEET 3 AA1 8 ILE A 18 LYS A 22 -1 N LYS A 22 O GLU A 133 SHEET 4 AA1 8 TYR A 30 MET A 36 -1 O SER A 32 N LEU A 19 SHEET 5 AA1 8 ILE A 39 ILE A 42 -1 O ILE A 41 N PHE A 33 SHEET 6 AA1 8 VAL A 148 MET A 151 1 O ILE A 150 N ILE A 42 SHEET 7 AA1 8 ALA A 182 THR A 185 1 O VAL A 184 N ILE A 149 SHEET 8 AA1 8 ASN A 161 ASN A 164 -1 N SER A 163 O ILE A 183 SHEET 1 AA2 2 SER A 60 LEU A 61 0 SHEET 2 AA2 2 GLY A 505 THR A 506 -1 O THR A 506 N SER A 60 SHEET 1 AA3 2 SER A 66 TYR A 68 0 SHEET 2 AA3 2 LEU A 404 LYS A 406 -1 O VAL A 405 N SER A 67 SHEET 1 AA4 4 GLU A 201 ILE A 203 0 SHEET 2 AA4 4 TYR A 190 ASN A 195 -1 N PHE A 194 O PHE A 202 SHEET 3 AA4 4 LYS A 356 LEU A 360 -1 O PHE A 358 N SER A 191 SHEET 4 AA4 4 ILE A 396 THR A 397 -1 O THR A 397 N LYS A 359 SHEET 1 AA5 2 THR A 232 ILE A 233 0 SHEET 2 AA5 2 THR A 247 ASN A 248 -1 O THR A 247 N ILE A 233 SHEET 1 AA6 2 LEU A 309 LYS A 311 0 SHEET 2 AA6 2 TYR A 317 VAL A 319 -1 O SER A 318 N ASP A 310 SHEET 1 AA7 3 ARG A 422 ASN A 430 0 SHEET 2 AA7 3 ILE A 408 VAL A 416 -1 N LYS A 413 O ILE A 425 SHEET 3 AA7 3 GLU A 510 ASP A 513 1 O HIS A 512 N ARG A 410 SHEET 1 AA8 2 GLU A 453 ILE A 454 0 SHEET 2 AA8 2 THR A 649 ILE A 650 1 O THR A 649 N ILE A 454 SHEET 1 AA9 2 ASN A 536 THR A 538 0 SHEET 2 AA9 2 LYS A 550 TYR A 552 1 O ILE A 551 N ASN A 536 SHEET 1 AB1 4 VAL D 5 THR D 7 0 SHEET 2 AB1 4 LEU D 18 ALA D 23 -1 O ALA D 23 N VAL D 5 SHEET 3 AB1 4 THR D 78 MET D 83 -1 O MET D 83 N LEU D 18 SHEET 4 AB1 4 PHE D 68 ASP D 73 -1 N THR D 69 O GLN D 82 SHEET 1 AB2 5 THR D 58 TYR D 60 0 SHEET 2 AB2 5 ARG D 45 VAL D 51 -1 N ALA D 50 O PHE D 59 SHEET 3 AB2 5 TYR D 32 GLN D 39 -1 N TRP D 36 O ALA D 49 SHEET 4 AB2 5 LEU D 93 TYR D 100 -1 O LEU D 93 N GLN D 39 SHEET 5 AB2 5 TYR D 113 TRP D 114 -1 O TYR D 113 N ALA D 98 SHEET 1 AB3 5 THR D 58 TYR D 60 0 SHEET 2 AB3 5 ARG D 45 VAL D 51 -1 N ALA D 50 O PHE D 59 SHEET 3 AB3 5 TYR D 32 GLN D 39 -1 N TRP D 36 O ALA D 49 SHEET 4 AB3 5 LEU D 93 TYR D 100 -1 O LEU D 93 N GLN D 39 SHEET 5 AB3 5 THR D 118 GLN D 119 -1 O THR D 118 N TYR D 94 SHEET 1 AB4 8 GLN E 141 LEU E 144 0 SHEET 2 AB4 8 VAL E 132 LYS E 135 -1 N ILE E 134 O ASP E 142 SHEET 3 AB4 8 ILE E 18 LYS E 22 -1 N LYS E 22 O GLU E 133 SHEET 4 AB4 8 TYR E 30 MET E 36 -1 O SER E 32 N LEU E 19 SHEET 5 AB4 8 ILE E 39 ILE E 41 -1 O ILE E 41 N PHE E 33 SHEET 6 AB4 8 VAL E 148 MET E 151 1 O ILE E 150 N TRP E 40 SHEET 7 AB4 8 ALA E 182 THR E 185 1 O VAL E 184 N ILE E 149 SHEET 8 AB4 8 ASN E 161 ASN E 164 -1 N ASN E 161 O THR E 185 SHEET 1 AB5 2 SER E 60 LEU E 61 0 SHEET 2 AB5 2 GLY E 505 THR E 506 -1 O THR E 506 N SER E 60 SHEET 1 AB6 2 SER E 66 TYR E 68 0 SHEET 2 AB6 2 LEU E 404 LYS E 406 -1 O VAL E 405 N SER E 67 SHEET 1 AB7 4 GLU E 201 ILE E 203 0 SHEET 2 AB7 4 TYR E 190 ASN E 195 -1 N PHE E 194 O PHE E 202 SHEET 3 AB7 4 LYS E 356 LEU E 360 -1 O PHE E 358 N SER E 191 SHEET 4 AB7 4 ILE E 396 THR E 397 -1 O THR E 397 N LYS E 359 SHEET 1 AB8 2 THR E 232 ILE E 233 0 SHEET 2 AB8 2 THR E 247 ASN E 248 -1 O THR E 247 N ILE E 233 SHEET 1 AB9 2 LEU E 309 LYS E 311 0 SHEET 2 AB9 2 TYR E 317 VAL E 319 -1 O SER E 318 N ASP E 310 SHEET 1 AC1 3 ARG E 422 ASN E 430 0 SHEET 2 AC1 3 ILE E 408 VAL E 416 -1 N ILE E 415 O LYS E 423 SHEET 3 AC1 3 GLU E 510 ASP E 513 1 O HIS E 512 N ARG E 410 SHEET 1 AC2 2 GLU E 453 ILE E 454 0 SHEET 2 AC2 2 THR E 649 ILE E 650 1 O THR E 649 N ILE E 454 SHEET 1 AC3 2 ASN E 536 THR E 538 0 SHEET 2 AC3 2 LYS E 550 TYR E 552 1 O ILE E 551 N ASN E 536 SHEET 1 AC4 8 GLN G 141 LEU G 144 0 SHEET 2 AC4 8 VAL G 132 LYS G 135 -1 N VAL G 132 O LEU G 144 SHEET 3 AC4 8 ILE G 18 LYS G 22 -1 N LYS G 22 O GLU G 133 SHEET 4 AC4 8 TYR G 30 MET G 36 -1 O SER G 32 N LEU G 19 SHEET 5 AC4 8 ILE G 39 ILE G 41 -1 O ILE G 41 N PHE G 33 SHEET 6 AC4 8 VAL G 148 MET G 151 1 O ILE G 150 N TRP G 40 SHEET 7 AC4 8 ALA G 182 THR G 185 1 O VAL G 184 N ILE G 149 SHEET 8 AC4 8 ASN G 161 ASN G 164 -1 N SER G 163 O ILE G 183 SHEET 1 AC5 2 SER G 66 TYR G 68 0 SHEET 2 AC5 2 LEU G 404 LYS G 406 -1 O VAL G 405 N SER G 67 SHEET 1 AC6 4 GLU G 201 ILE G 203 0 SHEET 2 AC6 4 TYR G 190 ASN G 195 -1 N PHE G 194 O PHE G 202 SHEET 3 AC6 4 LYS G 356 LEU G 360 -1 O PHE G 358 N SER G 191 SHEET 4 AC6 4 ILE G 396 THR G 397 -1 O THR G 397 N LYS G 359 SHEET 1 AC7 2 THR G 232 ILE G 233 0 SHEET 2 AC7 2 THR G 247 ASN G 248 -1 O THR G 247 N ILE G 233 SHEET 1 AC8 2 LEU G 309 LYS G 311 0 SHEET 2 AC8 2 TYR G 317 VAL G 319 -1 O SER G 318 N ASP G 310 SHEET 1 AC9 3 ARG G 422 ASN G 430 0 SHEET 2 AC9 3 ILE G 408 VAL G 416 -1 N LYS G 413 O ILE G 425 SHEET 3 AC9 3 GLU G 510 ASP G 513 1 O HIS G 512 N ARG G 410 SHEET 1 AD1 2 GLU G 453 ILE G 454 0 SHEET 2 AD1 2 THR G 649 ILE G 650 1 O THR G 649 N ILE G 454 SHEET 1 AD2 2 ASN G 536 THR G 538 0 SHEET 2 AD2 2 LYS G 550 TYR G 552 1 O ILE G 551 N ASN G 536 SHEET 1 AD3 8 GLN B 141 LEU B 144 0 SHEET 2 AD3 8 VAL B 132 LYS B 135 -1 N ILE B 134 O ASP B 142 SHEET 3 AD3 8 ILE B 18 LYS B 22 -1 N LYS B 22 O GLU B 133 SHEET 4 AD3 8 TYR B 30 MET B 36 -1 O SER B 32 N LEU B 19 SHEET 5 AD3 8 ILE B 39 ILE B 42 -1 O ILE B 41 N PHE B 33 SHEET 6 AD3 8 VAL B 148 MET B 151 1 O ILE B 150 N ILE B 42 SHEET 7 AD3 8 ALA B 182 THR B 185 1 O VAL B 184 N ILE B 149 SHEET 8 AD3 8 ASN B 161 ASN B 164 -1 N SER B 163 O ILE B 183 SHEET 1 AD4 2 SER B 60 LEU B 61 0 SHEET 2 AD4 2 GLY B 505 THR B 506 -1 O THR B 506 N SER B 60 SHEET 1 AD5 2 SER B 66 TYR B 68 0 SHEET 2 AD5 2 LEU B 404 LYS B 406 -1 O VAL B 405 N SER B 67 SHEET 1 AD6 4 GLU B 201 ILE B 203 0 SHEET 2 AD6 4 TYR B 190 ASN B 195 -1 N PHE B 194 O PHE B 202 SHEET 3 AD6 4 LYS B 356 LEU B 360 -1 O PHE B 358 N SER B 191 SHEET 4 AD6 4 ILE B 396 THR B 397 -1 O THR B 397 N LYS B 359 SHEET 1 AD7 2 THR B 232 ILE B 233 0 SHEET 2 AD7 2 THR B 247 ASN B 248 -1 O THR B 247 N ILE B 233 SHEET 1 AD8 2 LEU B 309 LYS B 311 0 SHEET 2 AD8 2 TYR B 317 VAL B 319 -1 O SER B 318 N ASP B 310 SHEET 1 AD9 3 ARG B 422 ASN B 430 0 SHEET 2 AD9 3 ILE B 408 VAL B 416 -1 N LYS B 413 O ILE B 425 SHEET 3 AD9 3 GLU B 510 ASP B 513 1 O HIS B 512 N ARG B 410 SHEET 1 AE1 2 GLU B 453 ILE B 454 0 SHEET 2 AE1 2 THR B 649 ILE B 650 1 O THR B 649 N ILE B 454 SHEET 1 AE2 2 ASN B 536 THR B 538 0 SHEET 2 AE2 2 LYS B 550 TYR B 552 1 O ILE B 551 N ASN B 536 SHEET 1 AE3 4 VAL C 5 THR C 7 0 SHEET 2 AE3 4 LEU C 18 ALA C 23 -1 O ALA C 23 N VAL C 5 SHEET 3 AE3 4 THR C 78 MET C 83 -1 O MET C 83 N LEU C 18 SHEET 4 AE3 4 PHE C 68 ASP C 73 -1 N THR C 69 O GLN C 82 SHEET 1 AE4 5 THR C 58 TYR C 60 0 SHEET 2 AE4 5 ARG C 45 VAL C 51 -1 N ALA C 50 O PHE C 59 SHEET 3 AE4 5 TYR C 32 GLN C 39 -1 N TRP C 36 O ALA C 49 SHEET 4 AE4 5 LEU C 93 TYR C 100 -1 O LEU C 93 N GLN C 39 SHEET 5 AE4 5 TYR C 113 TRP C 114 -1 O TYR C 113 N ALA C 98 SHEET 1 AE5 5 THR C 58 TYR C 60 0 SHEET 2 AE5 5 ARG C 45 VAL C 51 -1 N ALA C 50 O PHE C 59 SHEET 3 AE5 5 TYR C 32 GLN C 39 -1 N TRP C 36 O ALA C 49 SHEET 4 AE5 5 LEU C 93 TYR C 100 -1 O LEU C 93 N GLN C 39 SHEET 5 AE5 5 THR C 118 GLN C 119 -1 O THR C 118 N TYR C 94 SHEET 1 AE6 4 VAL F 5 THR F 7 0 SHEET 2 AE6 4 LEU F 18 ALA F 23 -1 O ALA F 23 N VAL F 5 SHEET 3 AE6 4 THR F 78 MET F 83 -1 O LEU F 81 N LEU F 20 SHEET 4 AE6 4 THR F 69 ASP F 73 -1 N THR F 69 O GLN F 82 SHEET 1 AE7 5 THR F 58 TYR F 60 0 SHEET 2 AE7 5 GLU F 46 VAL F 51 -1 N ALA F 50 O PHE F 59 SHEET 3 AE7 5 TYR F 32 GLN F 39 -1 N TRP F 36 O ALA F 49 SHEET 4 AE7 5 LEU F 93 TYR F 100 -1 O LEU F 93 N GLN F 39 SHEET 5 AE7 5 TYR F 113 TRP F 114 -1 O TYR F 113 N ALA F 98 SHEET 1 AE8 5 THR F 58 TYR F 60 0 SHEET 2 AE8 5 GLU F 46 VAL F 51 -1 N ALA F 50 O PHE F 59 SHEET 3 AE8 5 TYR F 32 GLN F 39 -1 N TRP F 36 O ALA F 49 SHEET 4 AE8 5 LEU F 93 TYR F 100 -1 O LEU F 93 N GLN F 39 SHEET 5 AE8 5 THR F 118 GLN F 119 -1 O THR F 118 N TYR F 94 SHEET 1 AE9 4 VAL H 5 THR H 7 0 SHEET 2 AE9 4 LEU H 18 ALA H 23 -1 O ALA H 23 N VAL H 5 SHEET 3 AE9 4 THR H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AE9 4 THR H 69 ASP H 73 -1 N ASP H 73 O THR H 78 SHEET 1 AF1 5 THR H 58 TYR H 60 0 SHEET 2 AF1 5 ARG H 45 VAL H 51 -1 N ALA H 50 O PHE H 59 SHEET 3 AF1 5 TYR H 32 GLN H 39 -1 N TRP H 36 O ALA H 49 SHEET 4 AF1 5 ALA H 92 TYR H 100 -1 O LEU H 93 N GLN H 39 SHEET 5 AF1 5 TYR H 113 TRP H 114 -1 O TYR H 113 N ALA H 98 SHEET 1 AF2 5 THR H 58 TYR H 60 0 SHEET 2 AF2 5 ARG H 45 VAL H 51 -1 N ALA H 50 O PHE H 59 SHEET 3 AF2 5 TYR H 32 GLN H 39 -1 N TRP H 36 O ALA H 49 SHEET 4 AF2 5 ALA H 92 TYR H 100 -1 O LEU H 93 N GLN H 39 SHEET 5 AF2 5 THR H 118 VAL H 120 -1 O THR H 118 N TYR H 94 SSBOND 1 CYS A 412 CYS A 426 1555 1555 2.03 SSBOND 2 CYS D 22 CYS D 96 1555 1555 2.04 SSBOND 3 CYS E 412 CYS E 426 1555 1555 2.03 SSBOND 4 CYS G 412 CYS G 426 1555 1555 2.03 SSBOND 5 CYS B 412 CYS B 426 1555 1555 2.03 SSBOND 6 CYS C 22 CYS C 96 1555 1555 2.04 SSBOND 7 CYS F 22 CYS F 96 1555 1555 2.04 SSBOND 8 CYS H 22 CYS H 96 1555 1555 2.04 CRYST1 109.035 208.650 210.505 90.00 90.00 90.00 P 21 21 21 16 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.009171 0.000000 0.000000 0.00000 SCALE2 0.000000 0.004793 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004750 0.00000