HEADER COMPLEX (IMMUNOGLOBULIN/HYDROLASE) 23-OCT-96 1KIQ
TITLE FV MUTANT Y(B 101)F (VH DOMAIN) OF MOUSE MONOCLONAL
TITLE 2 ANTIBODY D1.3 COMPLEXED WITH HEN EGG WHITE LYSOZYME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONOCLONAL ANTIBODY D1.3;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: MONOCLONAL ANTIBODY D1.3;
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: LYSOZYME;
COMPND 13 CHAIN: C;
COMPND 14 EC: 3.2.1.17;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 ORGAN: EGG;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 10 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 11 ORGANISM_TAXID: 10090;
SOURCE 12 ORGAN: EGG;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 17 ORGANISM_COMMON: CHICKEN;
SOURCE 18 ORGANISM_TAXID: 9031;
SOURCE 19 ORGAN: EGG;
SOURCE 20 CELL: EGG;
SOURCE 21 CELLULAR_LOCATION: EGG WHITE;
SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 23 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS IMMUNOGLOBULIN V REGION, SIGNAL, HYDROLASE, GLYCOSIDASE,
KEYWDS 2 BACTERIOLYTIC ENZYME, EGG WHITE, COMPLEX
KEYWDS 3 (IMMUNOGLOBULIN/HYDROLASE)
EXPDTA X-RAY DIFFRACTION
AUTHOR B.A.FIELDS,R.J.POLJAK,R.A.MARIUZZA
REVDAT 3 24-FEB-09 1KIQ 1 VERSN
REVDAT 2 01-APR-03 1KIQ 1 JRNL
REVDAT 1 23-DEC-96 1KIQ 0
JRNL AUTH B.A.FIELDS,F.A.GOLDBAUM,W.DALL'ACQUA,E.L.MALCHIODI,
JRNL AUTH 2 A.CAUERHFF,F.P.SCHWARZ,X.YSERN,R.J.POLJAK,
JRNL AUTH 3 R.A.MARIUZZA
JRNL TITL HYDROGEN BONDING AND SOLVENT STRUCTURE IN AN
JRNL TITL 2 ANTIGEN-ANTIBODY INTERFACE. CRYSTAL STRUCTURES AND
JRNL TITL 3 THERMODYNAMIC CHARACTERIZATION OF THREE FV MUTANTS
JRNL TITL 4 COMPLEXED WITH LYSOZYME.
JRNL REF BIOCHEMISTRY V. 35 15494 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8952503
JRNL DOI 10.1021/BI961709E
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.N.BHAT,G.A.BENTLEY,G.BOULOT,M.I.GREENE,D.TELLO,
REMARK 1 AUTH 2 W.DALL'ACQUA,H.SOUCHON,F.P.SCHWARZ,R.A.MARIUZZA,
REMARK 1 AUTH 3 R.J.POLJAK
REMARK 1 TITL BOUND WATER MOLECULES AND CONFORMATIONAL
REMARK 1 TITL 2 STABILIZATION HELP MEDIATE AN ANTIGEN-ANTIBODY
REMARK 1 TITL 3 ASSOCIATION
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 91 1089 1994
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 2
REMARK 1 AUTH X.YSERN,B.A.FIELDS,T.N.BHAT,F.A.GOLDBAUM,
REMARK 1 AUTH 2 W.DALL'ACQUA,F.P.SCHWARZ,R.J.POLJAK,R.A.MARIUZZA
REMARK 1 TITL SOLVENT REARRANGEMENT IN AN ANTIGEN-ANTIBODY
REMARK 1 TITL 2 INTERFACE INTRODUCED BY SITE-DIRECTED MUTAGENESIS
REMARK 1 TITL 3 OF THE ANTIBODY COMBINING SITE
REMARK 1 REF J.MOL.BIOL. V. 238 496 1994
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 73.9
REMARK 3 NUMBER OF REFLECTIONS : 23568
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : 2730
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 166
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) : 0.22
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) : 0.016
REMARK 3 BOND ANGLES (DEGREES) : 1.90
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 1KIQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-MAR-93
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XENGEN
REMARK 200 DATA SCALING SOFTWARE : XENGEN
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33574
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.3
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.1
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: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 64.89000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.18000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 64.89000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.18000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU C 129 CA - CB - CG ANGL. DEV. = 15.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 51 -52.58 64.52
REMARK 500 SER A 77 70.48 47.60
REMARK 500 SER A 93 -155.73 59.89
REMARK 500 PHE B 101 41.19 70.11
REMARK 500 SER B 115 -164.25 -73.49
REMARK 500 ASN C 44 109.65 -165.83
REMARK 500 ARG C 68 17.68 -141.05
REMARK 500 LEU C 84 77.45 -102.00
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1KIQ A 1 107 GB 545862 AAB30177 1 108
DBREF 1KIQ B 1 116 GB 896294 AAA69766 133 248
DBREF 1KIQ C 1 129 UNP P00698 LYSC_CHICK 19 147
SEQADV 1KIQ VAL A 3 GB 545862 GLU 3 CONFLICT
SEQADV 1KIQ TYR A 50 GB 545862 LYS 50 CONFLICT
SEQADV 1KIQ THR A 51 GB 545862 ALA 51 CONFLICT
SEQADV 1KIQ THR A 52 GB 545862 GLN 52 CONFLICT
SEQADV 1KIQ A GB 545862 PRO 95 DELETION
SEQADV 1KIQ ARG A 96 GB 545862 TRP 97 CONFLICT
SEQADV 1KIQ PHE B 101 GB 896294 TYR 233 CONFLICT
SEQADV 1KIQ LEU B 112 GB 896294 VAL 244 CONFLICT
SEQRES 1 A 107 ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU SER ALA
SEQRES 2 A 107 SER VAL GLY GLU THR VAL THR ILE THR CYS ARG ALA SER
SEQRES 3 A 107 GLY ASN ILE HIS ASN TYR LEU ALA TRP TYR GLN GLN LYS
SEQRES 4 A 107 GLN GLY LYS SER PRO GLN LEU LEU VAL TYR TYR THR THR
SEQRES 5 A 107 THR LEU ALA ASP GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 A 107 GLY SER GLY THR GLN TYR SER LEU LYS ILE ASN SER LEU
SEQRES 7 A 107 GLN PRO GLU ASP PHE GLY SER TYR TYR CYS GLN HIS PHE
SEQRES 8 A 107 TRP SER THR PRO ARG THR PHE GLY GLY GLY THR LYS LEU
SEQRES 9 A 107 GLU ILE LYS
SEQRES 1 B 116 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL ALA
SEQRES 2 B 116 PRO SER GLN SER LEU SER ILE THR CYS THR VAL SER GLY
SEQRES 3 B 116 PHE SER LEU THR GLY TYR GLY VAL ASN TRP VAL ARG GLN
SEQRES 4 B 116 PRO PRO GLY LYS GLY LEU GLU TRP LEU GLY MET ILE TRP
SEQRES 5 B 116 GLY ASP GLY ASN THR ASP TYR ASN SER ALA LEU LYS SER
SEQRES 6 B 116 ARG LEU SER ILE SER LYS ASP ASN SER LYS SER GLN VAL
SEQRES 7 B 116 PHE LEU LYS MET ASN SER LEU HIS THR ASP ASP THR ALA
SEQRES 8 B 116 ARG TYR TYR CYS ALA ARG GLU ARG ASP PHE ARG LEU ASP
SEQRES 9 B 116 TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SER
SEQRES 1 C 129 LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS
SEQRES 2 C 129 ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY
SEQRES 3 C 129 ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN
SEQRES 4 C 129 THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP
SEQRES 5 C 129 TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN
SEQRES 6 C 129 ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE
SEQRES 7 C 129 PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER
SEQRES 8 C 129 VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY
SEQRES 9 C 129 MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY
SEQRES 10 C 129 THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU
FORMUL 4 HOH *166(H2 O)
HELIX 1 1 PRO A 80 ASP A 82 5 3
HELIX 2 2 LYS B 64 ARG B 66 5 3
HELIX 3 3 THR B 87 ASP B 89 5 3
HELIX 4 4 ARG C 5 ARG C 14 1 10
HELIX 5 5 TYR C 20 GLY C 22 5 3
HELIX 6 6 LEU C 25 SER C 36 1 12
HELIX 7 7 THR C 89 ILE C 98 1 10
HELIX 8 8 GLY C 104 ALA C 107 5 4
HELIX 9 9 VAL C 109 ARG C 114 1 6
HELIX 10 10 VAL C 120 TRP C 123 5 4
SHEET 1 A 4 LEU A 4 SER A 7 0
SHEET 2 A 4 VAL A 19 ALA A 25 -1 N ARG A 24 O THR A 5
SHEET 3 A 4 GLN A 70 ILE A 75 -1 N ILE A 75 O VAL A 19
SHEET 4 A 4 PHE A 62 SER A 67 -1 N SER A 67 O GLN A 70
SHEET 1 B 5 SER A 10 ALA A 13 0
SHEET 2 B 5 THR A 102 ILE A 106 1 N LYS A 103 O LEU A 11
SHEET 3 B 5 GLY A 84 HIS A 90 -1 N TYR A 86 O THR A 102
SHEET 4 B 5 LEU A 33 GLN A 38 -1 N GLN A 38 O SER A 85
SHEET 5 B 5 GLN A 45 VAL A 48 -1 N VAL A 48 O TRP A 35
SHEET 1 C 4 GLN B 3 SER B 7 0
SHEET 2 C 4 LEU B 18 SER B 25 -1 N SER B 25 O GLN B 3
SHEET 3 C 4 GLN B 77 MET B 82 -1 N MET B 82 O LEU B 18
SHEET 4 C 4 LEU B 67 ASP B 72 -1 N ASP B 72 O GLN B 77
SHEET 1 D 5 THR B 110 LEU B 112 0
SHEET 2 D 5 ALA B 91 GLU B 98 -1 N TYR B 93 O THR B 110
SHEET 3 D 5 GLY B 33 GLN B 39 -1 N GLN B 39 O ARG B 92
SHEET 4 D 5 LEU B 45 ILE B 51 -1 N ILE B 51 O VAL B 34
SHEET 5 D 5 THR B 57 TYR B 59 -1 N ASP B 58 O MET B 50
SHEET 1 E 2 THR C 43 ARG C 45 0
SHEET 2 E 2 THR C 51 TYR C 53 -1 N ASP C 52 O ASN C 44
SHEET 1 F 2 ALA B 96 GLU B 98 0
SHEET 2 F 2 LEU B 103 TRP B 106 -1 N TYR B 105 O ARG B 97
SSBOND 1 CYS A 23 CYS A 88 1555 1555 2.01
SSBOND 2 CYS B 22 CYS B 95 1555 1555 2.06
SSBOND 3 CYS C 6 CYS C 127 1555 1555 2.04
SSBOND 4 CYS C 30 CYS C 115 1555 1555 2.02
SSBOND 5 CYS C 64 CYS C 80 1555 1555 2.03
SSBOND 6 CYS C 76 CYS C 94 1555 1555 2.03
CISPEP 1 SER A 7 PRO A 8 0 -0.17
CISPEP 2 THR A 94 PRO A 95 0 -0.36
CRYST1 129.780 60.360 56.830 90.00 119.14 90.00 C 1 2 1 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 0.007705 0.000000 0.004296 0.00000
SCALE2 0.000000 0.016567 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020146 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
