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HEADER IMMUNE SYSTEM 14-MAR-01 1I8K TITLE CRYSTAL STRUCTURE OF DSFV MR1 IN COMPLEX WITH THE PEPTIDE TITLE 2 ANTIGEN OF THE MUTANT EPIDERMAL GROWTH FACTOR RECEPTOR, TITLE 3 EGFRVIII, AT LIQUID NITROGEN TEMPERATURE COMPND MOL_ID: 1; COMPND 2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR ANTIBODY COMPND 3 MR1SCFV LIGHT CHAIN; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: DSFV MR1 VARIABLE DOMAIN LIGHT CHAIN; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR ANTIBODY COMPND 10 MR1SCFV HEAVY CHAIN; COMPND 11 CHAIN: B; COMPND 12 SYNONYM: DSFV MR1 VARIABLE DOMAIN HEAVY CHAIN; COMPND 13 ENGINEERED: YES; COMPND 14 MUTATION: YES; COMPND 15 MOL_ID: 3; COMPND 16 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR, EGFRVIII COMPND 17 PEPTIDE ANTIGEN; COMPND 18 CHAIN: C; COMPND 19 FRAGMENT: N-TERMINAL FRAGMENT; COMPND 20 SYNONYM: EPIDERMAL GROWTH FACTOR RECEPTOR, EGFRVIII COMPND 21 PEPTIDE ANTIGEN; COMPND 22 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: TG1; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: M13KO7 HELPER PHAGE; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 10 ORGANISM_COMMON: MOUSE; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 13 EXPRESSION_SYSTEM_STRAIN: TG1; SOURCE 14 EXPRESSION_SYSTEM_VECTOR_TYPE: M13KO7 HELPER PHAGE; SOURCE 15 MOL_ID: 3; SOURCE 16 SYNTHETIC: YES; SOURCE 17 OTHER_DETAILS: THE PEPTIDE SEQUENCE IS FROM THE N-TERMINAL SOURCE 18 OF THE MUTANT EPIDERMAL GROWTH FACTOR RECEPTOR, EGFRVIII KEYWDS ANTIBODY-PEPTIDE COMPLEX, IMMUNOGLOBULIN FOLD, PEPTIDE KEYWDS 2 ANTIGEN, TYPE II' BETA TURN. EXPDTA X-RAY DIFFRACTION AUTHOR R.C.LANDRY,A.C.KLIMOWICZ,S.J.LAVICTOIRE,S.BORISOVA, AUTHOR 2 D.T.KOTTACHCHI,I.A.LORIMER,S.V.EVANS REVDAT 2 02-AUG-05 1I8K 1 DBREF SEQADV REVDAT 1 14-MAR-02 1I8K 0 JRNL AUTH R.C.LANDRY,A.C.KLIMOWICZ,S.J.LAVICTOIRE,S.BORISOVA, JRNL AUTH 2 D.T.KOTTACHCHI,I.A.LORIMER,S.V.EVANS JRNL TITL ANTIBODY RECOGNITION OF A CONFORMATIONAL EPITOPE JRNL TITL 2 IN A PEPTIDE ANTIGEN: FV-PEPTIDE COMPLEX OF AN JRNL TITL 3 ANTIBODY FRAGMENT SPECIFIC FOR THE MUTANT EGF JRNL TITL 4 RECEPTOR, EGFRVIII. JRNL REF J.MOL.BIOL. V. 308 883 2001 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000 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 : 24309 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) : 0.172 REMARK 3 FREE R VALUE : 0.224 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 2406 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) : 1.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.88 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.37 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2160 REMARK 3 BIN FREE R VALUE : 0.2760 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 310 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 : 1820 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 260 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 13.94 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.00 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) : 0.014 REMARK 3 BOND ANGLES (DEGREES) : 2.60 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 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 1I8K 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 RCSB013039. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 28-JUN-1999 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS REMARK 200 BEAMLINE : X8C REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9789 REMARK 200 MONOCHROMATOR : COLLIMATING MIRROR OPTICS REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24309 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 6.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 7.260 REMARK 200 R MERGE (I) : 0.05200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 18.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4 REMARK 200 DATA REDUNDANCY IN SHELL : 6.94 REMARK 200 R MERGE FOR SHELL (I) : 0.14300 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: MERLOT REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.80 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CHLORIDE, MPD, PEG 10K, PH REMARK 280 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 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 -X,Y,1/2-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 1/2+X,1/2+Y,Z REMARK 290 6555 1/2-X,1/2-Y,1/2+Z REMARK 290 7555 1/2-X,1/2+Y,1/2-Z REMARK 290 8555 1/2+X,1/2-Y,-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 54.30000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.30000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 55.25000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 22.40000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 55.25000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 22.40000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 54.30000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 55.25000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 22.40000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 54.30000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 55.25000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 22.40000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 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 LYS A 107 REMARK 465 GLY B 420 REMARK 465 ILE B 421 REMARK 465 GLU B 422 REMARK 465 GLY B 423 REMARK 465 ARG B 424 REMARK 465 GLU C 499 REMARK 465 GLU C 500 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 VAL B 337 CA VAL B 337 CB 0.128 REMARK 500 VAL C 507 CA VAL C 507 CB 0.108 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 THR B 397 N - CA - CB ANGL. DEV. =-16.0 DEGREES REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH 611 DISTANCE = 6.34 ANGSTROMS REMARK 525 HOH 665 DISTANCE = 7.24 ANGSTROMS REMARK 525 HOH 721 DISTANCE = 8.68 ANGSTROMS REMARK 525 HOH 722 DISTANCE = 9.52 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1I8I RELATED DB: PDB REMARK 900 SAME PROTEIN, AT ROOM TEMPERATURE REMARK 999 REMARK 999 SEQUENCE REMARK 999 RESIDUES 100 OF CHAIN A AND 344 OF CHAIN B HAVE REMARK 999 BEEN MUTATED TO CYS RESIDUES TO INTRODUCE A REMARK 999 DISULFIDE BRIDGE BETWEEN CHAINS A AND B. REMARK 999 REMARK 999 THERE IS NO SEQUENCE DATABASE MATCH FOR CHAIN C REMARK 999 BECAUSE THE SEQUENCE OF EGFRVIII HAS NOT YET REMARK 999 BEEN DEPOSITED IN ANY DATABASE. THE DNA REMARK 999 SEQUENCE OF THE NORMAL EGF RECEPTOR HAS BEEN REMARK 999 DEPOSITED (NM_005228). DBREF 1I8K A 1 107 UNP Q8R028 Q8R028 136 242 DBREF 1I8K B 301 424 UNP P18529 HV58_MOUSE 1 124 SEQADV 1I8K CYS A 100 UNP Q8R028 ASP 235 ENGINEERED SEQADV 1I8K CYS B 344 UNP P18529 ARG 44 ENGINEERED SEQADV 1I8K GLY B 420 UNP P18529 SER 120 CONFLICT SEQADV 1I8K ILE B 421 UNP P18529 SER 121 CONFLICT SEQADV 1I8K GLU B 422 UNP P18529 GLY 122 CONFLICT SEQADV 1I8K ARG B 424 UNP P18529 GLY 124 CONFLICT SEQRES 1 A 107 ASP ILE GLU LEU THR GLN SER PRO ALA SER LEU SER VAL SEQRES 2 A 107 ALA THR GLY GLU LYS VAL THR ILE ARG CYS MET THR SER SEQRES 3 A 107 THR ASP ILE ASP ASP ASP MET ASN TRP TYR GLN GLN LYS SEQRES 4 A 107 PRO GLY GLU PRO PRO LYS PHE LEU ILE SER GLU GLY ASN SEQRES 5 A 107 THR LEU ARG PRO GLY VAL PRO SER ARG PHE SER SER SER SEQRES 6 A 107 GLY THR GLY THR ASP PHE VAL PHE THR ILE GLU ASN THR SEQRES 7 A 107 LEU SER GLU ASP VAL GLY ASP TYR TYR CYS LEU GLN SER SEQRES 8 A 107 PHE ASN VAL PRO LEU THR PHE GLY CYS GLY THR LYS LEU SEQRES 9 A 107 GLU ILE LYS SEQRES 1 B 124 GLN VAL LYS LEU GLN GLN SER GLY GLY GLY LEU VAL LYS SEQRES 2 B 124 PRO GLY ALA SER LEU LYS LEU SER CYS VAL THR SER GLY SEQRES 3 B 124 PHE THR PHE ARG LYS PHE GLY MET SER TRP VAL ARG GLN SEQRES 4 B 124 THR SER ASP LYS CYS LEU GLU TRP VAL ALA SER ILE SER SEQRES 5 B 124 THR GLY GLY TYR ASN THR TYR TYR SER ASP ASN VAL LYS SEQRES 6 B 124 GLY ARG PHE THR ILE SER ARG GLU ASN ALA LYS ASN THR SEQRES 7 B 124 LEU TYR LEU GLN MET SER SER LEU LYS SER GLU ASP THR SEQRES 8 B 124 ALA LEU TYR TYR CYS THR ARG GLY TYR SER SER THR SER SEQRES 9 B 124 TYR ALA MET ASP TYR TRP GLY GLN GLY THR THR VAL THR SEQRES 10 B 124 VAL SER GLY ILE GLU GLY ARG SEQRES 1 C 12 GLU GLU LYS LYS GLY ASN TYR VAL VAL THR ASP HIS FORMUL 4 HOH *260(H2 O) HELIX 1 1 LEU A 79 VAL A 83 5 5 HELIX 2 2 THR B 328 PHE B 332 5 5 HELIX 3 3 ASN B 374 LYS B 376 5 3 HELIX 4 4 LYS B 387 THR B 391 5 5 SHEET 1 A 4 LEU A 4 SER A 7 0 SHEET 2 A 4 VAL A 19 THR A 25 -1 N ARG A 22 O SER A 7 SHEET 3 A 4 ASP A 70 ILE A 75 -1 O PHE A 71 N CYS A 23 SHEET 4 A 4 PHE A 62 THR A 67 -1 N SER A 63 O THR A 74 SHEET 1 B 5 THR A 53 LEU A 54 0 SHEET 2 B 5 LYS A 45 SER A 49 -1 N SER A 49 O THR A 53 SHEET 3 B 5 MET A 33 GLN A 38 -1 O TRP A 35 N LEU A 47 SHEET 4 B 5 GLY A 84 GLN A 90 -1 O ASP A 85 N GLN A 38 SHEET 5 B 5 THR A 97 PHE A 98 -1 O THR A 97 N GLN A 90 SHEET 1 C 6 THR A 53 LEU A 54 0 SHEET 2 C 6 LYS A 45 SER A 49 -1 N SER A 49 O THR A 53 SHEET 3 C 6 MET A 33 GLN A 38 -1 O TRP A 35 N LEU A 47 SHEET 4 C 6 GLY A 84 GLN A 90 -1 O ASP A 85 N GLN A 38 SHEET 5 C 6 THR A 102 GLU A 105 -1 O THR A 102 N TYR A 86 SHEET 6 C 6 SER A 10 SER A 12 1 N LEU A 11 O LYS A 103 SHEET 1 D 4 LYS B 303 SER B 307 0 SHEET 2 D 4 LEU B 318 SER B 325 -1 N SER B 321 O SER B 307 SHEET 3 D 4 THR B 378 MET B 383 -1 N LEU B 379 O CYS B 322 SHEET 4 D 4 PHE B 368 GLU B 373 -1 O THR B 369 N GLN B 382 SHEET 1 E 5 SER B 404 TRP B 410 0 SHEET 2 E 5 ALA B 392 SER B 401 -1 N ARG B 398 O TYR B 409 SHEET 3 E 5 MET B 334 GLN B 339 -1 N SER B 335 O THR B 397 SHEET 4 E 5 LEU B 345 ILE B 351 -1 O GLU B 346 N ARG B 338 SHEET 5 E 5 THR B 358 TYR B 360 -1 N TYR B 359 O SER B 350 SHEET 1 F 4 SER B 404 TRP B 410 0 SHEET 2 F 4 ALA B 392 SER B 401 -1 N ARG B 398 O TYR B 409 SHEET 3 F 4 THR B 414 VAL B 418 -1 O THR B 414 N TYR B 394 SHEET 4 F 4 GLY B 310 VAL B 312 1 O GLY B 310 N THR B 417 SSBOND 1 CYS A 23 CYS A 88 SSBOND 2 CYS A 100 CYS B 344 SSBOND 3 CYS B 322 CYS B 396 CISPEP 1 SER A 7 PRO A 8 0 -14.53 CISPEP 2 VAL A 94 PRO A 95 0 -1.50 CRYST1 110.500 44.800 108.600 90.00 90.00 90.00 C 2 2 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.009050 0.000000 0.000000 0.00000 SCALE2 0.000000 0.022321 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009208 0.00000