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HEADER APOPTOSIS 01-JUL-05 2A5Y TITLE STRUCTURE OF A CED-4/CED-9 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: APOPTOSIS REGULATOR CED-9; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 48-251; COMPND 5 SYNONYM: CELL DEATH PROTEIN 9; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: CED-4; COMPND 10 CHAIN: B, C; COMPND 11 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS; SOURCE 3 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 4 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 5 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PBB75, PET-21B; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 EXPRESSION_SYSTEM_COMMON: BACTERIA KEYWDS CED-4, CED-9, CED-3 ACTIVATION, APOPTOSIS EXPDTA X-RAY DIFFRACTION AUTHOR N.YAN,Q.LIU,Q.HAO,L.GU,Y.SHI REVDAT 2 21-MAR-06 2A5Y 1 JRNL REVDAT 1 11-OCT-05 2A5Y 0 JRNL AUTH N.YAN,J.CHAI,E.S.LEE,L.GU,Q.LIU,J.HE,J.W.WU, JRNL AUTH 2 D.KOKEL,H.LI,Q.HAO,D.XUE,Y.SHI JRNL TITL STRUCTURE OF THE CED-4-CED-9 COMPLEX PROVIDES JRNL TITL 2 INSIGHTS INTO PROGRAMMED CELL DEATH IN JRNL TITL 3 CAENORHABDITIS ELEGANS. JRNL REF NATURE V. 437 831 2005 JRNL REFN ASTM NATUAS UK ISSN 0028-0836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 52166 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.249 REMARK 3 FREE R VALUE : 0.277 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 2433 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 8406 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 64 REMARK 3 SOLVENT ATOMS : 260 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 1.49 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : 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 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : NULL REMARK 3 BSOL : NULL REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2A5Y COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-17) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB033528. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-JUL-2004; 30-SEP-2004 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y REMARK 200 RADIATION SOURCE : NSLS; NSLS REMARK 200 BEAMLINE : X25; X25 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9645; 0.9791, 0.9794, 0.9600 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD; CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54599 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 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; MAD REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD REMARK 200 SOFTWARE USED: SOLVE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, HEPES, AMMONIUM SULFATE, REMARK 280 PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,1/2+Z REMARK 290 3555 1/2-Y,1/2+X,1/4+Z REMARK 290 4555 1/2+Y,1/2-X,3/4+Z REMARK 290 5555 1/2-X,1/2+Y,1/4-Z REMARK 290 6555 1/2+X,1/2-Y,3/4-Z REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,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 104.96400 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 64.44900 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 64.44900 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 52.48200 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 64.44900 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 64.44900 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 157.44600 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 64.44900 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 64.44900 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 52.48200 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 64.44900 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 64.44900 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 157.44600 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 104.96400 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 3 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 APPLY THE FOLLOWING TO CHAINS: A, 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 LEU A 48 REMARK 465 PRO A 49 REMARK 465 SER A 50 REMARK 465 PRO A 51 REMARK 465 SER A 52 REMARK 465 ARG A 53 REMARK 465 GLN A 54 REMARK 465 ALA A 55 REMARK 465 SER A 56 REMARK 465 THR A 57 REMARK 465 ARG A 58 REMARK 465 ARG A 59 REMARK 465 MET A 60 REMARK 465 SER A 61 REMARK 465 ILE A 62 REMARK 465 GLY A 63 REMARK 465 GLU A 64 REMARK 465 SER A 65 REMARK 465 ILE A 66 REMARK 465 THR A 161 REMARK 465 ASP A 162 REMARK 465 LYS A 242 REMARK 465 VAL A 243 REMARK 465 GLY A 244 REMARK 465 ARG A 245 REMARK 465 ARG A 246 REMARK 465 LYS A 247 REMARK 465 GLN A 248 REMARK 465 ASN A 249 REMARK 465 ARG A 250 REMARK 465 ARG A 251 REMARK 465 VAL B 311 REMARK 465 GLY B 312 REMARK 465 ASP B 417 REMARK 465 ILE B 418 REMARK 465 CYS B 419 REMARK 465 SER B 420 REMARK 465 ASN B 421 REMARK 465 GLU B 422 REMARK 465 GLU B 423 REMARK 465 GLY B 488 REMARK 465 ASN B 489 REMARK 465 ASN B 490 REMARK 465 ASN B 491 REMARK 465 VAL B 492 REMARK 465 SER B 493 REMARK 465 VAL B 494 REMARK 465 PRO B 495 REMARK 465 GLU B 496 REMARK 465 ARG B 497 REMARK 465 HIS B 498 REMARK 465 ILE B 499 REMARK 465 PRO B 500 REMARK 465 SER B 501 REMARK 465 HIS B 502 REMARK 465 PHE B 503 REMARK 465 GLN B 504 REMARK 465 LYS B 505 REMARK 465 PHE B 506 REMARK 465 ARG B 507 REMARK 465 ARG B 508 REMARK 465 SER B 509 REMARK 465 SER B 510 REMARK 465 ALA B 511 REMARK 465 SER B 512 REMARK 465 GLU B 513 REMARK 465 MET B 514 REMARK 465 TYR B 515 REMARK 465 PRO B 516 REMARK 465 LYS B 517 REMARK 465 THR B 518 REMARK 465 THR B 519 REMARK 465 GLU B 520 REMARK 465 LYS B 544 REMARK 465 ASN B 545 REMARK 465 PHE B 546 REMARK 465 ALA B 547 REMARK 465 CYS B 548 REMARK 465 CYS B 549 REMARK 465 MET C 1 REMARK 465 LEU C 2 REMARK 465 CYS C 3 REMARK 465 GLU C 4 REMARK 465 ILE C 5 REMARK 465 GLU C 6 REMARK 465 CYS C 7 REMARK 465 ARG C 8 REMARK 465 ALA C 9 REMARK 465 LEU C 10 REMARK 465 SER C 11 REMARK 465 THR C 12 REMARK 465 ALA C 13 REMARK 465 HIS C 14 REMARK 465 THR C 15 REMARK 465 ARG C 16 REMARK 465 LEU C 17 REMARK 465 ILE C 18 REMARK 465 HIS C 19 REMARK 465 ASP C 20 REMARK 465 PHE C 21 REMARK 465 GLU C 22 REMARK 465 PRO C 23 REMARK 465 ARG C 24 REMARK 465 ASP C 25 REMARK 465 ALA C 26 REMARK 465 LEU C 27 REMARK 465 THR C 28 REMARK 465 TYR C 29 REMARK 465 LEU C 30 REMARK 465 GLU C 31 REMARK 465 GLY C 32 REMARK 465 LYS C 33 REMARK 465 ASN C 34 REMARK 465 ILE C 35 REMARK 465 PHE C 36 REMARK 465 THR C 37 REMARK 465 GLU C 38 REMARK 465 ASP C 39 REMARK 465 HIS C 40 REMARK 465 SER C 41 REMARK 465 GLU C 42 REMARK 465 LEU C 43 REMARK 465 ILE C 44 REMARK 465 SER C 45 REMARK 465 LYS C 46 REMARK 465 MET C 47 REMARK 465 SER C 48 REMARK 465 THR C 49 REMARK 465 ARG C 50 REMARK 465 LEU C 51 REMARK 465 GLU C 52 REMARK 465 ARG C 53 REMARK 465 ILE C 54 REMARK 465 ALA C 55 REMARK 465 ASN C 56 REMARK 465 PHE C 57 REMARK 465 LEU C 58 REMARK 465 ARG C 59 REMARK 465 ILE C 60 REMARK 465 TYR C 61 REMARK 465 ARG C 62 REMARK 465 ARG C 63 REMARK 465 GLN C 64 REMARK 465 ALA C 65 REMARK 465 SER C 66 REMARK 465 GLU C 67 REMARK 465 LEU C 68 REMARK 465 GLY C 69 REMARK 465 PRO C 70 REMARK 465 LEU C 71 REMARK 465 ILE C 72 REMARK 465 ASP C 73 REMARK 465 PHE C 74 REMARK 465 PHE C 75 REMARK 465 ASN C 76 REMARK 465 TYR C 77 REMARK 465 ASN C 78 REMARK 465 ASN C 79 REMARK 465 GLN C 80 REMARK 465 SER C 81 REMARK 465 HIS C 82 REMARK 465 LEU C 83 REMARK 465 ALA C 84 REMARK 465 ASP C 85 REMARK 465 PHE C 86 REMARK 465 LEU C 87 REMARK 465 GLU C 88 REMARK 465 ASP C 89 REMARK 465 TYR C 90 REMARK 465 ILE C 91 REMARK 465 ASP C 92 REMARK 465 PHE C 93 REMARK 465 ALA C 94 REMARK 465 ILE C 95 REMARK 465 ASN C 96 REMARK 465 GLU C 97 REMARK 465 PRO C 98 REMARK 465 ASP C 99 REMARK 465 LEU C 100 REMARK 465 LEU C 101 REMARK 465 ARG C 102 REMARK 465 PRO C 103 REMARK 465 VAL C 104 REMARK 465 VAL C 105 REMARK 465 ILE C 106 REMARK 465 ALA C 107 REMARK 465 PRO C 108 REMARK 465 PRO C 415 REMARK 465 VAL C 416 REMARK 465 ASP C 417 REMARK 465 ILE C 418 REMARK 465 CYS C 419 REMARK 465 SER C 420 REMARK 465 ASN C 421 REMARK 465 GLU C 422 REMARK 465 GLU C 423 REMARK 465 GLU C 424 REMARK 465 GLN C 425 REMARK 465 LEU C 426 REMARK 465 ARG C 483 REMARK 465 LEU C 484 REMARK 465 LEU C 485 REMARK 465 GLU C 486 REMARK 465 ILE C 487 REMARK 465 GLY C 488 REMARK 465 ASN C 489 REMARK 465 ASN C 490 REMARK 465 ASN C 491 REMARK 465 VAL C 492 REMARK 465 SER C 493 REMARK 465 VAL C 494 REMARK 465 PRO C 495 REMARK 465 GLU C 496 REMARK 465 ARG C 497 REMARK 465 HIS C 498 REMARK 465 ILE C 499 REMARK 465 PRO C 500 REMARK 465 SER C 501 REMARK 465 HIS C 502 REMARK 465 PHE C 503 REMARK 465 GLN C 504 REMARK 465 LYS C 505 REMARK 465 PHE C 506 REMARK 465 ARG C 507 REMARK 465 ARG C 508 REMARK 465 SER C 509 REMARK 465 SER C 510 REMARK 465 ALA C 511 REMARK 465 SER C 512 REMARK 465 GLU C 513 REMARK 465 MET C 514 REMARK 465 TYR C 515 REMARK 465 PRO C 516 REMARK 465 LYS C 517 REMARK 465 THR C 518 REMARK 465 THR C 519 REMARK 465 GLU C 520 REMARK 465 GLU C 521 REMARK 465 THR C 522 REMARK 465 VAL C 523 REMARK 465 ILE C 524 REMARK 465 ARG C 525 REMARK 465 PRO C 526 REMARK 465 GLU C 527 REMARK 465 ASP C 528 REMARK 465 PHE C 529 REMARK 465 PRO C 530 REMARK 465 LYS C 531 REMARK 465 PHE C 532 REMARK 465 LYS C 544 REMARK 465 ASN C 545 REMARK 465 PHE C 546 REMARK 465 ALA C 547 REMARK 465 CYS C 548 REMARK 465 CYS C 549 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 REMARK 500 O ASP B 469 N GLN B 471 2.15 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),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 ASP A 67 C ASP A 67 O -0.054 REMARK 500 LYS A 69 CB LYS A 69 CG 0.060 REMARK 500 MET A 116 SD MET A 116 CE -0.077 REMARK 500 GLN A 163 CD GLN A 163 OE1 0.067 REMARK 500 GLN A 163 CD GLN A 163 NE2 0.065 REMARK 500 MET A 166 SD MET A 166 CE -0.101 REMARK 500 MET A 185 SD MET A 185 CE -0.078 REMARK 500 MET A 186 SD MET A 186 CE -0.046 REMARK 500 MET A 225 SD MET A 225 CE -0.097 REMARK 500 MET B 1 SD MET B 1 CE 0.069 REMARK 500 MET B 47 CG MET B 47 SD 0.048 REMARK 500 MET B 234 SD MET B 234 CE -0.051 REMARK 500 GLU C 134 C GLU C 134 O 0.053 REMARK 500 MET C 210 SD MET C 210 CE -0.044 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: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 GLY A 68 N - CA - C ANGL. DEV. = 29.1 DEGREES REMARK 500 LYS A 69 N - CA - C ANGL. DEV. = 17.5 DEGREES REMARK 500 GLY A 68 CA - C - N ANGL. DEV. =-11.0 DEGREES REMARK 500 LYS A 69 C - N - CA ANGL. DEV. = 9.7 DEGREES REMARK 500 ILE A 70 N - CA - C ANGL. DEV. = 13.0 DEGREES REMARK 500 VAL A 153 N - CA - C ANGL. DEV. = 10.7 DEGREES REMARK 500 GLU A 190 N - CA - C ANGL. DEV. =-11.1 DEGREES REMARK 500 THR B 37 N - CA - C ANGL. DEV. = -8.7 DEGREES REMARK 500 VAL B 105 N - CA - C ANGL. DEV. = 9.2 DEGREES REMARK 500 LEU B 155 N - CA - C ANGL. DEV. = -8.8 DEGREES REMARK 500 LEU B 157 N - CA - C ANGL. DEV. = -8.9 DEGREES REMARK 500 SER B 222 N - CA - C ANGL. DEV. =-11.7 DEGREES REMARK 500 ARG B 267 N - CA - C ANGL. DEV. =-11.1 DEGREES REMARK 500 CYS B 268 N - CA - C ANGL. DEV. = 10.4 DEGREES REMARK 500 LEU B 269 N - CA - C ANGL. DEV. =-11.9 DEGREES REMARK 500 THR B 271 N - CA - C ANGL. DEV. = -8.7 DEGREES REMARK 500 GLY B 359 N - CA - C ANGL. DEV. = -8.7 DEGREES REMARK 500 ASP B 428 N - CA - C ANGL. DEV. = -9.1 DEGREES REMARK 500 ILE B 479 N - CA - C ANGL. DEV. = -8.8 DEGREES REMARK 500 LEU B 480 N - CA - C ANGL. DEV. =-10.3 DEGREES REMARK 500 LEU C 120 CA - CB - CG ANGL. DEV. = 9.0 DEGREES REMARK 500 GLU C 134 CB - CA - C ANGL. DEV. = 10.9 DEGREES REMARK 500 ARG C 267 N - CA - C ANGL. DEV. = -8.9 DEGREES REMARK 500 LEU C 269 N - CA - C ANGL. DEV. =-13.6 DEGREES REMARK 500 PRO C 308 N - CA - C ANGL. DEV. = 9.2 DEGREES REMARK 500 GLU C 341 N - CA - C ANGL. DEV. =-10.6 DEGREES REMARK 500 PRO C 342 N - CA - C ANGL. DEV. = 10.0 DEGREES REMARK 500 PRO C 342 C - N - CA ANGL. DEV. = 16.4 DEGREES REMARK 500 PRO C 342 C - N - CD ANGL. DEV. =-13.6 DEGREES REMARK 500 LEU C 535 N - CA - C ANGL. DEV. =-12.8 DEGREES DBREF 2A5Y A 48 251 UNP P41958 CED9_CAEEL 48 251 DBREF 2A5Y B 1 549 UNP P30429 CED4_CAEEL 1 549 DBREF 2A5Y C 1 549 UNP P30429 CED4_CAEEL 1 549 SEQADV 2A5Y SER A 107 UNP P41958 CYS 107 ENGINEERED SEQADV 2A5Y SER A 135 UNP P41958 CYS 135 ENGINEERED SEQADV 2A5Y SER A 164 UNP P41958 CYS 164 ENGINEERED SEQRES 1 A 204 LEU PRO SER PRO SER ARG GLN ALA SER THR ARG ARG MET SEQRES 2 A 204 SER ILE GLY GLU SER ILE ASP GLY LYS ILE ASN ASP TRP SEQRES 3 A 204 GLU GLU PRO ARG LEU ASP ILE GLU GLY PHE VAL VAL ASP SEQRES 4 A 204 TYR PHE THR HIS ARG ILE ARG GLN ASN GLY MET GLU TRP SEQRES 5 A 204 PHE GLY ALA PRO GLY LEU PRO SER GLY VAL GLN PRO GLU SEQRES 6 A 204 HIS GLU MET MET ARG VAL MET GLY THR ILE PHE GLU LYS SEQRES 7 A 204 LYS HIS ALA GLU ASN PHE GLU THR PHE SER GLU GLN LEU SEQRES 8 A 204 LEU ALA VAL PRO ARG ILE SER PHE SER LEU TYR GLN ASP SEQRES 9 A 204 VAL VAL ARG THR VAL GLY ASN ALA GLN THR ASP GLN SER SEQRES 10 A 204 PRO MET SER TYR GLY ARG LEU ILE GLY LEU ILE SER PHE SEQRES 11 A 204 GLY GLY PHE VAL ALA ALA LYS MET MET GLU SER VAL GLU SEQRES 12 A 204 LEU GLN GLY GLN VAL ARG ASN LEU PHE VAL TYR THR SER SEQRES 13 A 204 LEU PHE ILE LYS THR ARG ILE ARG ASN ASN TRP LYS GLU SEQRES 14 A 204 HIS ASN ARG SER TRP ASP ASP PHE MET THR LEU GLY LYS SEQRES 15 A 204 GLN MET LYS GLU ASP TYR GLU ARG ALA GLU ALA GLU LYS SEQRES 16 A 204 VAL GLY ARG ARG LYS GLN ASN ARG ARG SEQRES 1 B 549 MET LEU CYS GLU ILE GLU CYS ARG ALA LEU SER THR ALA SEQRES 2 B 549 HIS THR ARG LEU ILE HIS ASP PHE GLU PRO ARG ASP ALA SEQRES 3 B 549 LEU THR TYR LEU GLU GLY LYS ASN ILE PHE THR GLU ASP SEQRES 4 B 549 HIS SER GLU LEU ILE SER LYS MET SER THR ARG LEU GLU SEQRES 5 B 549 ARG ILE ALA ASN PHE LEU ARG ILE TYR ARG ARG GLN ALA SEQRES 6 B 549 SER GLU LEU GLY PRO LEU ILE ASP PHE PHE ASN TYR ASN SEQRES 7 B 549 ASN GLN SER HIS LEU ALA ASP PHE LEU GLU ASP TYR ILE SEQRES 8 B 549 ASP PHE ALA ILE ASN GLU PRO ASP LEU LEU ARG PRO VAL SEQRES 9 B 549 VAL ILE ALA PRO GLN PHE SER ARG GLN MET LEU ASP ARG SEQRES 10 B 549 LYS LEU LEU LEU GLY ASN VAL PRO LYS GLN MET THR CYS SEQRES 11 B 549 TYR ILE ARG GLU TYR HIS VAL ASP ARG VAL ILE LYS LYS SEQRES 12 B 549 LEU ASP GLU MET CYS ASP LEU ASP SER PHE PHE LEU PHE SEQRES 13 B 549 LEU HIS GLY ARG ALA GLY SER GLY LYS SER VAL ILE ALA SEQRES 14 B 549 SER GLN ALA LEU SER LYS SER ASP GLN LEU ILE GLY ILE SEQRES 15 B 549 ASN TYR ASP SER ILE VAL TRP LEU LYS ASP SER GLY THR SEQRES 16 B 549 ALA PRO LYS SER THR PHE ASP LEU PHE THR ASP ILE LEU SEQRES 17 B 549 LEU MET LEU LYS SER GLU ASP ASP LEU LEU ASN PHE PRO SEQRES 18 B 549 SER VAL GLU HIS VAL THR SER VAL VAL LEU LYS ARG MET SEQRES 19 B 549 ILE CYS ASN ALA LEU ILE ASP ARG PRO ASN THR LEU PHE SEQRES 20 B 549 VAL PHE ASP ASP VAL VAL GLN GLU GLU THR ILE ARG TRP SEQRES 21 B 549 ALA GLN GLU LEU ARG LEU ARG CYS LEU VAL THR THR ARG SEQRES 22 B 549 ASP VAL GLU ILE SER ASN ALA ALA SER GLN THR CYS GLU SEQRES 23 B 549 PHE ILE GLU VAL THR SER LEU GLU ILE ASP GLU CYS TYR SEQRES 24 B 549 ASP PHE LEU GLU ALA TYR GLY MET PRO MET PRO VAL GLY SEQRES 25 B 549 GLU LYS GLU GLU ASP VAL LEU ASN LYS THR ILE GLU LEU SEQRES 26 B 549 SER SER GLY ASN PRO ALA THR LEU MET MET PHE PHE LYS SEQRES 27 B 549 SER CYS GLU PRO LYS THR PHE GLU LYS MET ALA GLN LEU SEQRES 28 B 549 ASN ASN LYS LEU GLU SER ARG GLY LEU VAL GLY VAL GLU SEQRES 29 B 549 CYS ILE THR PRO TYR SER TYR LYS SER LEU ALA MET ALA SEQRES 30 B 549 LEU GLN ARG CYS VAL GLU VAL LEU SER ASP GLU ASP ARG SEQRES 31 B 549 SER ALA LEU ALA PHE ALA VAL VAL MET PRO PRO GLY VAL SEQRES 32 B 549 ASP ILE PRO VAL LYS LEU TRP SER CYS VAL ILE PRO VAL SEQRES 33 B 549 ASP ILE CYS SER ASN GLU GLU GLU GLN LEU ASP ASP GLU SEQRES 34 B 549 VAL ALA ASP ARG LEU LYS ARG LEU SER LYS ARG GLY ALA SEQRES 35 B 549 LEU LEU SER GLY LYS ARG MET PRO VAL LEU THR PHE LYS SEQRES 36 B 549 ILE ASP HIS ILE ILE HIS MET PHE LEU LYS HIS VAL VAL SEQRES 37 B 549 ASP ALA GLN THR ILE ALA ASN GLY ILE SER ILE LEU GLU SEQRES 38 B 549 GLN ARG LEU LEU GLU ILE GLY ASN ASN ASN VAL SER VAL SEQRES 39 B 549 PRO GLU ARG HIS ILE PRO SER HIS PHE GLN LYS PHE ARG SEQRES 40 B 549 ARG SER SER ALA SER GLU MET TYR PRO LYS THR THR GLU SEQRES 41 B 549 GLU THR VAL ILE ARG PRO GLU ASP PHE PRO LYS PHE MET SEQRES 42 B 549 GLN LEU HIS GLN LYS PHE TYR ASP SER LEU LYS ASN PHE SEQRES 43 B 549 ALA CYS CYS SEQRES 1 C 549 MET LEU CYS GLU ILE GLU CYS ARG ALA LEU SER THR ALA SEQRES 2 C 549 HIS THR ARG LEU ILE HIS ASP PHE GLU PRO ARG ASP ALA SEQRES 3 C 549 LEU THR TYR LEU GLU GLY LYS ASN ILE PHE THR GLU ASP SEQRES 4 C 549 HIS SER GLU LEU ILE SER LYS MET SER THR ARG LEU GLU SEQRES 5 C 549 ARG ILE ALA ASN PHE LEU ARG ILE TYR ARG ARG GLN ALA SEQRES 6 C 549 SER GLU LEU GLY PRO LEU ILE ASP PHE PHE ASN TYR ASN SEQRES 7 C 549 ASN GLN SER HIS LEU ALA ASP PHE LEU GLU ASP TYR ILE SEQRES 8 C 549 ASP PHE ALA ILE ASN GLU PRO ASP LEU LEU ARG PRO VAL SEQRES 9 C 549 VAL ILE ALA PRO GLN PHE SER ARG GLN MET LEU ASP ARG SEQRES 10 C 549 LYS LEU LEU LEU GLY ASN VAL PRO LYS GLN MET THR CYS SEQRES 11 C 549 TYR ILE ARG GLU TYR HIS VAL ASP ARG VAL ILE LYS LYS SEQRES 12 C 549 LEU ASP GLU MET CYS ASP LEU ASP SER PHE PHE LEU PHE SEQRES 13 C 549 LEU HIS GLY ARG ALA GLY SER GLY LYS SER VAL ILE ALA SEQRES 14 C 549 SER GLN ALA LEU SER LYS SER ASP GLN LEU ILE GLY ILE SEQRES 15 C 549 ASN TYR ASP SER ILE VAL TRP LEU LYS ASP SER GLY THR SEQRES 16 C 549 ALA PRO LYS SER THR PHE ASP LEU PHE THR ASP ILE LEU SEQRES 17 C 549 LEU MET LEU LYS SER GLU ASP ASP LEU LEU ASN PHE PRO SEQRES 18 C 549 SER VAL GLU HIS VAL THR SER VAL VAL LEU LYS ARG MET SEQRES 19 C 549 ILE CYS ASN ALA LEU ILE ASP ARG PRO ASN THR LEU PHE SEQRES 20 C 549 VAL PHE ASP ASP VAL VAL GLN GLU GLU THR ILE ARG TRP SEQRES 21 C 549 ALA GLN GLU LEU ARG LEU ARG CYS LEU VAL THR THR ARG SEQRES 22 C 549 ASP VAL GLU ILE SER ASN ALA ALA SER GLN THR CYS GLU SEQRES 23 C 549 PHE ILE GLU VAL THR SER LEU GLU ILE ASP GLU CYS TYR SEQRES 24 C 549 ASP PHE LEU GLU ALA TYR GLY MET PRO MET PRO VAL GLY SEQRES 25 C 549 GLU LYS GLU GLU ASP VAL LEU ASN LYS THR ILE GLU LEU SEQRES 26 C 549 SER SER GLY ASN PRO ALA THR LEU MET MET PHE PHE LYS SEQRES 27 C 549 SER CYS GLU PRO LYS THR PHE GLU LYS MET ALA GLN LEU SEQRES 28 C 549 ASN ASN LYS LEU GLU SER ARG GLY LEU VAL GLY VAL GLU SEQRES 29 C 549 CYS ILE THR PRO TYR SER TYR LYS SER LEU ALA MET ALA SEQRES 30 C 549 LEU GLN ARG CYS VAL GLU VAL LEU SER ASP GLU ASP ARG SEQRES 31 C 549 SER ALA LEU ALA PHE ALA VAL VAL MET PRO PRO GLY VAL SEQRES 32 C 549 ASP ILE PRO VAL LYS LEU TRP SER CYS VAL ILE PRO VAL SEQRES 33 C 549 ASP ILE CYS SER ASN GLU GLU GLU GLN LEU ASP ASP GLU SEQRES 34 C 549 VAL ALA ASP ARG LEU LYS ARG LEU SER LYS ARG GLY ALA SEQRES 35 C 549 LEU LEU SER GLY LYS ARG MET PRO VAL LEU THR PHE LYS SEQRES 36 C 549 ILE ASP HIS ILE ILE HIS MET PHE LEU LYS HIS VAL VAL SEQRES 37 C 549 ASP ALA GLN THR ILE ALA ASN GLY ILE SER ILE LEU GLU SEQRES 38 C 549 GLN ARG LEU LEU GLU ILE GLY ASN ASN ASN VAL SER VAL SEQRES 39 C 549 PRO GLU ARG HIS ILE PRO SER HIS PHE GLN LYS PHE ARG SEQRES 40 C 549 ARG SER SER ALA SER GLU MET TYR PRO LYS THR THR GLU SEQRES 41 C 549 GLU THR VAL ILE ARG PRO GLU ASP PHE PRO LYS PHE MET SEQRES 42 C 549 GLN LEU HIS GLN LYS PHE TYR ASP SER LEU LYS ASN PHE SEQRES 43 C 549 ALA CYS CYS HET MG 501 1 HET MG 502 1 HET ATP 301 31 HET ATP 401 31 HETNAM MG MAGNESIUM ION HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE FORMUL 4 MG 2(MG 2+) FORMUL 6 ATP 2(C10 H16 N5 O13 P3) FORMUL 8 HOH *260(H2 O) HELIX 1 1 ASN A 71 LEU A 78 5 8 HELIX 2 2 ASP A 79 GLN A 94 1 16 HELIX 3 3 GLN A 110 HIS A 127 1 18 HELIX 4 4 ASN A 130 ALA A 140 1 11 HELIX 5 5 SER A 145 ARG A 154 1 10 HELIX 6 6 SER A 167 GLU A 187 1 21 HELIX 7 7 GLN A 194 ARG A 211 1 18 HELIX 8 8 SER A 220 GLU A 239 1 20 HELIX 9 9 CYS B 3 PHE B 21 1 19 HELIX 10 10 GLU B 22 ASP B 25 5 4 HELIX 11 11 ALA B 26 LYS B 33 1 8 HELIX 12 12 THR B 37 LYS B 46 1 10 HELIX 13 13 THR B 49 ALA B 65 1 17 HELIX 14 14 LEU B 68 ASN B 78 1 11 HELIX 15 15 GLN B 80 GLU B 97 1 18 HELIX 16 16 LEU B 100 VAL B 105 1 6 HELIX 17 17 SER B 111 GLY B 122 1 12 HELIX 18 18 ARG B 133 CYS B 148 1 16 HELIX 19 19 GLY B 164 SER B 176 1 13 HELIX 20 20 LYS B 198 LYS B 212 1 15 HELIX 21 21 THR B 227 ILE B 240 1 14 HELIX 22 22 GLN B 254 LEU B 264 1 11 HELIX 23 23 ASP B 274 ALA B 281 5 8 HELIX 24 24 GLU B 294 TYR B 305 1 12 HELIX 25 25 GLU B 313 SER B 327 1 15 HELIX 26 26 ASN B 329 LYS B 338 1 10 HELIX 27 27 THR B 344 GLY B 359 1 16 HELIX 28 28 SER B 373 VAL B 384 1 12 HELIX 29 29 SER B 386 LEU B 393 1 8 HELIX 30 30 ALA B 394 VAL B 398 5 5 HELIX 31 31 VAL B 407 ILE B 414 1 8 HELIX 32 32 ASP B 427 LEU B 437 1 11 HELIX 33 33 ASP B 457 HIS B 466 1 10 HELIX 34 34 ALA B 470 SER B 478 1 9 HELIX 35 35 HIS B 536 ASP B 541 1 6 HELIX 36 36 GLN C 109 GLY C 122 1 14 HELIX 37 37 ARG C 133 CYS C 148 1 16 HELIX 38 38 GLY C 164 LYS C 175 1 12 HELIX 39 39 LYS C 198 LYS C 212 1 15 HELIX 40 40 SER C 213 PHE C 220 1 8 HELIX 41 41 THR C 227 LEU C 239 1 13 HELIX 42 42 GLN C 254 LEU C 264 1 11 HELIX 43 43 ASP C 274 ASN C 279 5 6 HELIX 44 44 GLU C 294 TYR C 305 1 12 HELIX 45 45 GLY C 312 SER C 326 1 15 HELIX 46 46 ASN C 329 CYS C 340 1 12 HELIX 47 47 THR C 344 GLY C 359 1 16 HELIX 48 48 LEU C 360 GLU C 364 5 5 HELIX 49 49 SER C 373 GLU C 383 1 11 HELIX 50 50 GLU C 388 LEU C 393 1 6 HELIX 51 51 VAL C 407 CYS C 412 1 6 HELIX 52 52 LYS C 435 ARG C 440 1 6 HELIX 53 53 ASP C 457 HIS C 466 1 10 HELIX 54 54 GLN C 471 ILE C 479 1 9 HELIX 55 55 MET C 533 LEU C 535 5 3 HELIX 56 56 HIS C 536 LEU C 543 1 8 SHEET 1 A 5 SER B 186 LYS B 191 0 SHEET 2 A 5 THR B 245 VAL B 252 1 O VAL B 248 N VAL B 188 SHEET 3 A 5 ARG B 267 THR B 272 1 O ARG B 267 N PHE B 247 SHEET 4 A 5 PHE B 153 HIS B 158 1 N LEU B 157 O VAL B 270 SHEET 5 A 5 CYS B 285 GLU B 289 1 O GLU B 286 N PHE B 156 SHEET 1 B 3 ILE B 405 PRO B 406 0 SHEET 2 B 3 THR B 453 LYS B 455 -1 O PHE B 454 N ILE B 405 SHEET 3 B 3 SER B 445 LYS B 447 -1 N SER B 445 O LYS B 455 SHEET 1 C 5 SER C 186 LYS C 191 0 SHEET 2 C 5 THR C 245 ASP C 250 1 O VAL C 248 N VAL C 188 SHEET 3 C 5 ARG C 267 THR C 272 1 O ARG C 267 N PHE C 247 SHEET 4 C 5 PHE C 154 GLY C 159 1 N LEU C 157 O VAL C 270 SHEET 5 C 5 GLU C 286 VAL C 290 1 O VAL C 290 N HIS C 158 SHEET 1 D 3 ASP C 404 PRO C 406 0 SHEET 2 D 3 THR C 453 LYS C 455 -1 O PHE C 454 N ILE C 405 SHEET 3 D 3 SER C 445 LYS C 447 -1 N LYS C 447 O THR C 453 CISPEP 1 MET B 449 PRO B 450 0 -0.01 CISPEP 2 GLU C 341 PRO C 342 0 2.61 CISPEP 3 MET C 449 PRO C 450 0 0.22 CRYST1 128.898 128.898 209.928 90.00 90.00 90.00 P 41 21 2 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 0.007758 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007758 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004764 0.00000