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HEADER IMMUNE SYSTEM 16-SEP-02 1MQK TITLE CRYSTAL STRUCTURE OF THE UNLIGANDED FV-FRAGMENT OF THE ANTI- TITLE 2 CYTOCHROME C OXIDASE ANTIBODY 7E2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTIBODY 7E2 FV FRAGMENT, LIGHT CHAIN; COMPND 3 CHAIN: L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ANTIBODY 7E2 FV FRAGMENT, HEAVY CHAIN; COMPND 7 CHAIN: H; COMPND 8 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: JM83; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PASK68; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 11 ORGANISM_COMMON: MOUSE; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 13 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 14 EXPRESSION_SYSTEM_STRAIN: JM83; SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PASK68 KEYWDS ANTIBODY, MEMBRANE PROTEIN, CYTOCHROME C OXIDASE, HIGH- KEYWDS 2 RESOLUTION STRUCTURE EXPDTA X-RAY DIFFRACTION AUTHOR L.-O.ESSEN,A.HARRENGA,C.OSTERMEIER,H.MICHEL REVDAT 1 01-APR-03 1MQK 0 JRNL AUTH L.O.ESSEN,A.HARRENGA,C.OSTERMEIER,H.MICHEL JRNL TITL 1.3 A X-RAY STRUCTURE OF AN ANTIBODY FV FRAGMENT JRNL TITL 2 USED FOR INDUCED MEMBRANE-PROTEIN CRYSTALLIZATION. JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 59 677 2003 JRNL REFN ASTM ABCRE6 DK ISSN 0907-4449 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.OSTERMEIER,L.-O.ESSEN,H.MICHEL REMARK 1 TITL CRYSTALS OF AN ANTIBODY FV FRAGMENT AGAINST AN REMARK 1 TITL 2 INTEGRAL MEMBRANE PROTEIN DIFFRACTING TO 1.28 REMARK 1 TITL 3 RESOLUTION REMARK 1 REF PROTEINS: STRUCT., FUNCT., V. 21 74 1995 REMARK 1 REF 2 GENET. REMARK 1 REFN ASTM PSFGEY US ISSN 0887-3585 REMARK 1 REFERENCE 2 REMARK 1 AUTH C.OSTERMEIER,S.IWATA,B.LUDWIG,H.MICHEL REMARK 1 TITL FV FRAGMENT-MEDIATED CRYSTALLIZATION OF THE REMARK 1 TITL 2 MEMBRANE PROTEIN BACTERIAL CYTOCHROME C OXIDASE REMARK 1 REF NAT.STRUCT.BIOL. V. 2 842 1995 REMARK 1 REFN ASTM NSBIEW US ISSN 1072-8368 REMARK 1 REFERENCE 3 REMARK 1 AUTH S.IWATA,C.OSTERMEIER,B.LUDWIG,H.MICHEL REMARK 1 TITL STRUCTURE AT 2.8 RESOLUTION OF CYTOCHROME C REMARK 1 TITL 2 OXIDASE FROM PARACOCCUS DENITRIFICANS REMARK 1 REF NATURE V. 376 660 1995 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 REMARK 1 REFERENCE 4 REMARK 1 AUTH A.HARRENGA,H.MICHEL REMARK 1 TITL THE CYTOCHROME C OXIDASE FROM PARACOCCUS REMARK 1 TITL 2 DENITRIFICANS DOES NOT CHANGE THE METAL CENTER REMARK 1 TITL 3 UPON REDUCTION REMARK 1 REF J.BIOL.CHEM. V. 274 33296 1999 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 1 REFERENCE 5 REMARK 1 AUTH C.OSTERMEIER,A.HARRENGA,U.ERMLER,H.MICHEL REMARK 1 TITL STRUCTURE AT 2.7 RESOLUTION OF THE PARACOCCUS REMARK 1 TITL 2 DENITRIFICANS TWO-SUBUNIT CYTOCHROME C OXIDASE REMARK 1 TITL 3 COMPLEXED WITH AN ANTIBODY FV FRAGMENT REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 94 10547 1997 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 REMARK 2 REMARK 2 RESOLUTION. 1.28 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : SHELXL-93 REMARK 3 AUTHORS : G.M.SHELDRICK REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.28 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF). REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.136 REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.136 REMARK 3 FREE R VALUE (NO CUTOFF) : 0.196 REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 1922 REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 64005 REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F). REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1875 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 318 REMARK 3 REMARK 3 MODEL REFINEMENT. REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : NULL REMARK 3 NUMBER OF RESTRAINTS : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES. REMARK 3 BOND LENGTHS (A) : 0.021 REMARK 3 ANGLE DISTANCES (A) : 2.280 REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : NULL REMARK 3 ZERO CHIRAL VOLUMES (A**3) : NULL REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : NULL REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : NULL REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED: NULL REMARK 3 REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER REMARK 3 SPECIAL CASE: NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: USED WEIGHTED FULL MATRIX LEAST REMARK 3 SQUARES PROCEDURE OF SHELX-93 TO GENERATE MODEL. ONLY REMARK 3 ISOTROPIC MODEL PROVIDED REMARK 4 REMARK 4 1MQK 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 3.101 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB017105. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-JUN-1993 REMARK 200 TEMPERATURE (KELVIN) : 277.0 REMARK 200 PH : 6.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : MPG/DESY, HAMBURG REMARK 200 BEAMLINE : BW6 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000 REMARK 200 MONOCHROMATOR : MIRRORS REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : CCP4 (AGROVATA, ROTAVATA) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64251 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.280 REMARK 200 RESOLUTION RANGE LOW (A) : 22.500 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 85.1 REMARK 200 DATA REDUNDANCY : 2.800 REMARK 200 R MERGE (I) : 0.40000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 28.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.28 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.31 REMARK 200 COMPLETENESS FOR SHELL (%) : 63.4 REMARK 200 DATA REDUNDANCY IN SHELL : 1.90 REMARK 200 R MERGE FOR SHELL (I) : 0.21800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 5.200 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: X-PLOR REMARK 200 STARTING MODEL: PDB ENTRY 1QLE REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.83 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM PHOSPHATE, PH 6.0, REMARK 280 MICRODIALYSIS, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 1/2-X,-Y,1/2+Z REMARK 290 3555 -X,1/2+Y,1/2-Z REMARK 290 4555 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 25.71800 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.92300 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.02250 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.92300 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.71800 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.02250 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 2 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: L, 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLU L 110 REMARK 465 GLN L 111 REMARK 465 LYS L 112 REMARK 465 LEU L 113 REMARK 465 ILE L 114 REMARK 465 SER L 115 REMARK 465 GLU L 116 REMARK 465 GLU L 117 REMARK 465 ASP L 118 REMARK 465 LEU L 119 REMARK 465 MET L 120 REMARK 465 GLN H 124 REMARK 465 PHE H 125 REMARK 465 GLY H 126 REMARK 465 GLY H 127 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 ARG L 109 CA C O CB CG CD NE REMARK 470 ARG L 109 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 REMARK 500 OE1 GLU H 42 O HOH 124 1.20 REMARK 500 NZ LYS H 65 O HOH 198 1.44 REMARK 500 NZ LYS L 104 O HOH 289 1.59 REMARK 500 NE2 GLN H 110 O HOH 237 1.69 REMARK 500 CE LYS H 65 O HOH 198 1.78 REMARK 500 C PRO H 123 O HOH 195 1.96 REMARK 500 O PRO H 123 O HOH 195 2.01 REMARK 500 CE LYS H 65 O HOH 87 2.05 REMARK 500 NZ LYS H 65 O HOH 235 2.07 REMARK 500 CD GLN H 110 O HOH 237 2.08 REMARK 500 CD1 ILE L 21 O HOH 2 2.10 REMARK 500 CG2 ILE L 21 O HOH 2 2.12 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 ARG L 24 CD - NE - CZ ANGL. DEV. = 14.4 DEGREES REMARK 500 GLU L 81 CB - CG - CD ANGL. DEV. = 15.3 DEGREES REMARK 500 CYS H 96 CA - CB - SG ANGL. DEV. = 17.0 DEGREES 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 M RES CSSEQI PSI PHI REMARK 500 ALA L 51 -39.06 71.41 REMARK 500 TYR H 102 -102.44 76.48 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 246 DISTANCE = 5.53 ANGSTROMS REMARK 525 HOH 266 DISTANCE = 7.17 ANGSTROMS REMARK 525 HOH 316 DISTANCE = 5.20 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1AR1 RELATED DB: PDB REMARK 900 7E2 ANTIBODY COCRYSTALLIZED WITH THE PARACOCCUS REMARK 900 DENITRIFICANS TWO-SUBUNIT CYTOCHROME C OXIDASE REMARK 900 RELATED ID: 1QLE RELATED DB: PDB REMARK 900 7E2 ANTIBODY COCRYSTALLIZED WITH THE PARACOCCUS REMARK 900 DENITRIFICANS FOUR-SUBUNIT CYTOCHROME C OXIDASE REMARK 999 REMARK 999 SEQUENCE REMARK 999 ACCORDING TO THE AUTHOR, THE SEQUENCE FOR REMARK 999 THE HEAVY AND LIGHT CHAINS OF ANTIBODY 7E2 REMARK 999 HAS NOT BEEN DEPOSITED IN ANY SEQUENCE DATABASE. REMARK 999 SOME SEQUENCE INFORMATION IS PRESENT IN PDB REMARK 999 ENTRY 1QLE. DBREF 1MQK L 11 109 UNP P01636 KV5D_MOUSE 11 108 DBREF 1MQK H 1 98 UNP P18525 HV54_MOUSE 20 117 SEQRES 1 L 120 ASP ILE GLU LEU THR GLN THR PRO VAL SER LEU SER ALA SEQRES 2 L 120 SER VAL GLY GLU THR VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 120 GLU ASN ILE TYR SER TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 120 GLN GLY LYS SER PRO GLN PHE LEU VAL TYR ASN ALA LYS SEQRES 5 L 120 THR LEU GLY GLU GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 120 GLY SER GLY THR GLN PHE SER LEU LYS ILE ASN SER LEU SEQRES 7 L 120 LEU PRO GLU ASP PHE GLY SER TYR TYR CYS GLN HIS HIS SEQRES 8 L 120 TYR GLY THR PRO PRO LEU THR PHE GLY GLY GLY THR LYS SEQRES 9 L 120 LEU GLU ILE LYS ARG GLU GLN LYS LEU ILE SER GLU GLU SEQRES 10 L 120 ASP LEU MET SEQRES 1 H 127 GLU VAL LYS LEU GLN GLU SER GLY GLY ASP LEU VAL GLN SEQRES 2 H 127 PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 H 127 PHE THR PHE SER SER TYR THR MET SER TRP VAL ARG GLN SEQRES 4 H 127 THR PRO GLU LYS ARG LEU GLU TRP VAL ALA SER ILE ASN SEQRES 5 H 127 ASN GLY GLY GLY ARG THR TYR TYR PRO ASP THR VAL LYS SEQRES 6 H 127 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 H 127 LEU TYR LEU GLN MET SER SER LEU LYS SER GLU ASP THR SEQRES 8 H 127 ALA MET TYR TYR CYS VAL ARG HIS GLU TYR TYR TYR ALA SEQRES 9 H 127 MET ASP TYR TRP GLY GLN GLY THR THR VAL THR VAL SER SEQRES 10 H 127 SER ALA TRP ARG HIS PRO GLN PHE GLY GLY FORMUL 3 HOH *318(H2 O) HELIX 1 1 LEU L 79 PHE L 83 5 5 HELIX 2 2 THR H 28 TYR H 32 5 5 HELIX 3 3 ASN H 74 LYS H 76 5 3 HELIX 4 4 LYS H 87 THR H 91 5 5 SHEET 1 A 4 LEU L 4 THR L 7 0 SHEET 2 A 4 VAL L 19 ALA L 25 -1 O THR L 22 N THR L 7 SHEET 3 A 4 GLN L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 A 4 PHE L 62 SER L 67 -1 N SER L 63 O LYS L 74 SHEET 1 B 6 SER L 10 ALA L 13 0 SHEET 2 B 6 THR L 103 ILE L 107 1 O GLU L 106 N LEU L 11 SHEET 3 B 6 GLY L 84 HIS L 90 -1 N GLY L 84 O LEU L 105 SHEET 4 B 6 LEU L 33 GLN L 38 -1 N GLN L 38 O SER L 85 SHEET 5 B 6 GLN L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 B 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49 SHEET 1 C 4 LYS H 3 SER H 7 0 SHEET 2 C 4 LEU H 18 SER H 25 -1 O ALA H 23 N GLN H 5 SHEET 3 C 4 THR H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 C 4 PHE H 68 ASP H 73 -1 N THR H 69 O GLN H 82 SHEET 1 D 5 THR H 58 TYR H 59 0 SHEET 2 D 5 LEU H 45 ILE H 51 -1 N SER H 50 O TYR H 59 SHEET 3 D 5 MET H 34 GLN H 39 -1 N ARG H 38 O GLU H 46 SHEET 4 D 5 ALA H 92 GLU H 100 -1 O TYR H 95 N VAL H 37 SHEET 5 D 5 ALA H 104 TRP H 108 -1 O TYR H 107 N ARG H 98 SHEET 1 E 6 THR H 58 TYR H 59 0 SHEET 2 E 6 LEU H 45 ILE H 51 -1 N SER H 50 O TYR H 59 SHEET 3 E 6 MET H 34 GLN H 39 -1 N ARG H 38 O GLU H 46 SHEET 4 E 6 ALA H 92 GLU H 100 -1 O TYR H 95 N VAL H 37 SHEET 5 E 6 THR H 112 VAL H 116 -1 O THR H 112 N TYR H 94 SHEET 6 E 6 LEU H 11 VAL H 12 1 N VAL H 12 O THR H 115 SSBOND 1 CYS L 23 CYS L 88 SSBOND 2 CYS H 22 CYS H 96 CISPEP 1 THR L 7 PRO L 8 0 -8.53 CISPEP 2 PRO L 95 PRO L 96 0 1.88 CRYST1 51.436 56.045 99.846 90.00 90.00 90.00 P 21 21 21 4 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 0.019442 0.000000 0.000000 0.00000 SCALE2 0.000000 0.017843 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010015 0.00000