HEADER IMMUNOGLOBULIN 06-FEB-96 1UCB
TITLE STRUCTURE OF UNCOMPLEXED FAB COMPARED TO COMPLEX (1CLY, 1CLZ)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHIMERIC HUMAN/MOUSE IGG FAB FRAGMENT BR96;
COMPND 3 CHAIN: L;
COMPND 4 FRAGMENT: MOUSE VH AND VL DOMAINS, HUMAN CL KAPPA AND CH1 IGG1
COMPND 5 DOMAINS;
COMPND 6 SYNONYM: CBR96 FAB, IMMUNOGLOBULIN;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CHIMERIC HUMAN/MOUSE IGG FAB FRAGMENT BR96;
COMPND 10 CHAIN: H;
COMPND 11 FRAGMENT: MOUSE VH AND VL DOMAINS, HUMAN CL KAPPA AND CH1 IGG1
COMPND 12 DOMAINS;
COMPND 13 SYNONYM: CBR96 FAB, IMMUNOGLOBULIN;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 FRAGMENT: CL AND CH1;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606;
SOURCE 6 ORGAN: SPLEEN;
SOURCE 7 EXPRESSION_SYSTEM: MUS MUSCULUS;
SOURCE 8 EXPRESSION_SYSTEM_COMMON: HOUSE MOUSE;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 10090;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BALB/C, 2X63-AG 8.653;
SOURCE 11 EXPRESSION_SYSTEM_CELL: SPLEEN, MYELOMA;
SOURCE 12 OTHER_DETAILS: MOUSE/HUMAN CHIMERA. MOUSE HYBRIDOMA PRODUCED BY
SOURCE 13 FUSIONING BALB/C SPLEEN CELLS WITH 2X63-AG 8.653 MOUSE MYELOMA
SOURCE 14 CELLS. HUMAN CONSTANT REGIONS INTRODUCED BY HOMOLOGOUS
SOURCE 15 RECOMBINATION. CL IS HUMAN KAPPA, CH1 IS HUMAN IGG1 DOMAIN.;
SOURCE 16 MOL_ID: 2;
SOURCE 17 FRAGMENT: CL AND CH1;
SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 19 ORGANISM_COMMON: HUMAN;
SOURCE 20 ORGANISM_TAXID: 9606;
SOURCE 21 ORGAN: SPLEEN;
SOURCE 22 EXPRESSION_SYSTEM: MUS MUSCULUS;
SOURCE 23 EXPRESSION_SYSTEM_COMMON: HOUSE MOUSE;
SOURCE 24 EXPRESSION_SYSTEM_TAXID: 10090;
SOURCE 25 EXPRESSION_SYSTEM_STRAIN: BALB/C, 2X63-AG 8.653;
SOURCE 26 EXPRESSION_SYSTEM_CELL: SPLEEN, MYELOMA;
SOURCE 27 OTHER_DETAILS: MOUSE/HUMAN CHIMERA. MOUSE HYBRIDOMA PRODUCED BY
SOURCE 28 FUSIONING BALB/C SPLEEN CELLS WITH 2X63-AG 8.653 MOUSE MYELOMA
SOURCE 29 CELLS. HUMAN CONSTANT REGIONS INTRODUCED BY HOMOLOGOUS
SOURCE 30 RECOMBINATION. CL IS HUMAN KAPPA, CH1 IS HUMAN IGG1 DOMAIN.
KEYWDS FAB, IMMUNOGLOBULIN, ANTIBODY, ANTI-TUMOR, CHIMERA
EXPDTA X-RAY DIFFRACTION
AUTHOR S.SHERIFF,J.BAJORATH
REVDAT 3 09-AUG-23 1UCB 1 REMARK
REVDAT 2 24-FEB-09 1UCB 1 VERSN
REVDAT 1 12-MAR-97 1UCB 0
JRNL AUTH S.SHERIFF,C.Y.CHANG,P.D.JEFFREY,J.BAJORATH
JRNL TITL X-RAY STRUCTURE OF THE UNCOMPLEXED ANTI-TUMOR ANTIBODY BR96
JRNL TITL 2 AND COMPARISON WITH ITS ANTIGEN-BOUND FORM.
JRNL REF J.MOL.BIOL. V. 259 938 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 8683596
JRNL DOI 10.1006/JMBI.1996.0371
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.Y.CHANG,P.D.JEFFREY,J.BAJORATH,I.HELLSTROM,K.E.HELLSTROM,
REMARK 1 AUTH 2 S.SHERIFF
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF THE
REMARK 1 TITL 2 MONOCLONAL ANTI-TUMOR ANTIBODY BR96 AND ITS COMPLEX WITH THE
REMARK 1 TITL 3 LEWIS Y DETERMINANT
REMARK 1 REF J.MOL.BIOL. V. 235 372 1994
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.0
REMARK 3 NUMBER OF REFLECTIONS : 13731
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : EX POST FACTO
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
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 : 3333
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 40
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.00
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) : 0.28
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) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 28.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.400
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 1UCB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176911.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : MAR-93
REMARK 200 TEMPERATURE (KELVIN) : 295
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS-NICOLET X100
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14826
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 36.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.0
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.04500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 65.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.50
REMARK 200 R MERGE FOR SHELL (I) : 0.10700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MERLOT, BRUTE
REMARK 200 STARTING MODEL: FV OF 1CLZ WITH CDRS REMOVED 1CLY (HUMAN IGG1,
REMARK 200 HUMAN KAPPA) AND OF 1CLZ (MOUSE IGG3, MOUSE KAPPA)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE (PH 4.6), 0.1 M
REMARK 280 AMMONIUM SULFATE, 15 % PEG 8000.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 30.55000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 87.15000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.55000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 87.15000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL
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 ASP L 1
REMARK 465 VAL L 2
REMARK 465 LEU L 3
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 L 104 CA - CB - CG ANGL. DEV. = 14.2 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 ASN L 28 -25.39 84.86
REMARK 500 ASN L 30 95.73 -163.85
REMARK 500 VAL L 51 -36.33 68.69
REMARK 500 ARG L 77 87.15 61.51
REMARK 500 ASN L 138 77.73 39.08
REMARK 500 ALA H 49 150.35 176.73
REMARK 500 PHE H 100B 70.37 -107.68
REMARK 500 ASP H 146 77.82 49.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 215
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE FAB LIGHT CHAIN (RESIDUES 1 - 214) HAS BEEN ASSIGNED
REMARK 999 CHAIN INDICATOR L. THE FAB HEAVY CHAIN (RESIDUES 1 -
REMARK 999 227) HAS BEEN ASSIGNED CHAIN INDICATOR H. THE FAB
REMARK 999 FRAGMENT IS NUMBERED BY THE CONVENTION OF E. KABAT
REMARK 999 (E.A. KABAT, T.T. WU, H.M. PERRY, K.S. GOTTESMAN, C.
REMARK 999 FOELLER SEQUENCES OF PROTEINS OF IMMUNOLOGICAL INTEREST,
REMARK 999 5TH ED.,. (1991), NATIONAL INSTITUTES OF HEALTH,
REMARK 999 BETHESDA, MD.).
DBREF 1UCB L 109 214 UNP P01834 KAC_HUMAN 1 106
DBREF 1UCB H 1 227 PDB 1UCB 1UCB 1 227
SEQRES 1 L 219 ASP VAL LEU MET THR GLN ILE PRO VAL SER LEU PRO VAL
SEQRES 2 L 219 SER LEU GLY ASP GLN ALA SER ILE SER CYS ARG SER SER
SEQRES 3 L 219 GLN ILE ILE VAL HIS ASN ASN GLY ASN THR TYR LEU GLU
SEQRES 4 L 219 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU
SEQRES 5 L 219 ILE TYR LYS VAL SER ASN ARG PHE SER GLY VAL PRO ASP
SEQRES 6 L 219 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU
SEQRES 7 L 219 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR
SEQRES 8 L 219 TYR CYS PHE GLN GLY SER HIS VAL PRO PHE THR PHE GLY
SEQRES 9 L 219 SER GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA
SEQRES 10 L 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU
SEQRES 11 L 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN
SEQRES 12 L 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP
SEQRES 13 L 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR
SEQRES 14 L 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER
SEQRES 15 L 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS
SEQRES 16 L 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER
SEQRES 17 L 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS
SEQRES 1 H 219 GLU VAL ASN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN
SEQRES 2 H 219 PRO GLY GLY SER LEU LYS VAL SER CYS VAL THR SER GLY
SEQRES 3 H 219 PHE THR PHE SER ASP TYR TYR MET TYR TRP VAL ARG GLN
SEQRES 4 H 219 THR PRO GLU LYS ARG LEU GLU TRP VAL ALA TYR ILE SER
SEQRES 5 H 219 GLN GLY GLY ASP ILE THR ASP TYR PRO ASP THR VAL LYS
SEQRES 6 H 219 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER
SEQRES 7 H 219 LEU TYR LEU GLN MET SER ARG LEU LYS SER GLU ASP THR
SEQRES 8 H 219 ALA MET TYR TYR CYS ALA ARG GLY LEU ASP ASP GLY ALA
SEQRES 9 H 219 TRP PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR VAL
SEQRES 10 H 219 SER VAL ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU
SEQRES 11 H 219 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA
SEQRES 12 H 219 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLN PRO VAL
SEQRES 13 H 219 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL
SEQRES 14 H 219 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR
SEQRES 15 H 219 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU
SEQRES 16 H 219 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO
SEQRES 17 H 219 SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO
HET SO4 L 215 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 O4 S 2-
FORMUL 4 HOH *40(H2 O)
HELIX 1 1 ALA L 80 ASP L 82 5 3
HELIX 2 2 ASP L 122 SER L 127 1 6
HELIX 3 3 LYS L 183 GLU L 187 1 5
HELIX 4 4 PHE H 29 ASP H 31 5 3
HELIX 5 5 SER H 84 ASP H 86 5 3
HELIX 6 6 SER H 128 SER H 130 5 3
HELIX 7 7 ASN H 162 GLY H 164 5 3
HELIX 8 8 SER H 195 SER H 197 5 3
HELIX 9 9 LYS H 213 SER H 215 5 3
SHEET 1 A 4 THR L 5 ILE L 7 0
SHEET 2 A 4 ALA L 19 ARG L 24 -1 N ARG L 24 O THR L 5
SHEET 3 A 4 ASP L 70 ILE L 75 -1 N ILE L 75 O ALA L 19
SHEET 4 A 4 PHE L 62 SER L 67 -1 N SER L 67 O ASP L 70
SHEET 1 B 5 SER L 10 VAL L 13 0
SHEET 2 B 5 THR L 102 ILE L 106 1 N LYS L 103 O LEU L 11
SHEET 3 B 5 GLY L 84 GLN L 90 -1 N TYR L 86 O THR L 102
SHEET 4 B 5 LEU L 33 GLN L 38 -1 N GLN L 38 O VAL L 85
SHEET 5 B 5 GLN L 45 ILE L 48 -1 N ILE L 48 O TRP L 35
SHEET 1 C 4 SER L 114 PHE L 118 0
SHEET 2 C 4 THR L 129 ASN L 137 -1 N ASN L 137 O SER L 114
SHEET 3 C 4 LEU L 175 SER L 182 -1 N LEU L 181 O ALA L 130
SHEET 4 C 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176
SHEET 1 D 3 ALA L 144 VAL L 150 0
SHEET 2 D 3 VAL L 191 HIS L 198 -1 N THR L 197 O LYS L 145
SHEET 3 D 3 VAL L 205 ASN L 210 -1 N PHE L 209 O TYR L 192
SHEET 1 E 4 ASN H 3 SER H 7 0
SHEET 2 E 4 LEU H 18 SER H 25 -1 N SER H 25 O ASN H 3
SHEET 3 E 4 SER H 77 MET H 82 -1 N MET H 82 O LEU H 18
SHEET 4 E 4 THR H 68 ASP H 72 -1 N ASP H 72 O SER H 77
SHEET 1 F 4 THR H 107 VAL H 109 0
SHEET 2 F 4 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 107
SHEET 3 F 4 MET H 34 THR H 40 -1 N GLN H 39 O MET H 89
SHEET 4 F 4 LEU H 45 ILE H 51 -1 N ILE H 51 O MET H 34
SHEET 1 G 4 SER H 120 LEU H 124 0
SHEET 2 G 4 THR H 137 LYS H 145 -1 N LYS H 145 O SER H 120
SHEET 3 G 4 LEU H 187 PRO H 194 -1 N VAL H 193 O ALA H 138
SHEET 4 G 4 VAL H 171 THR H 173 -1 N HIS H 172 O VAL H 190
SHEET 1 H 3 THR H 153 TRP H 157 0
SHEET 2 H 3 TYR H 206 HIS H 212 -1 N ASN H 211 O THR H 153
SHEET 3 H 3 THR H 217 VAL H 223 -1 N VAL H 223 O TYR H 206
SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.02
SSBOND 2 CYS L 134 CYS L 194 1555 1555 2.02
SSBOND 3 CYS H 22 CYS H 92 1555 1555 2.04
SSBOND 4 CYS H 142 CYS H 208 1555 1555 2.03
CISPEP 1 ILE L 7 PRO L 8 0 -0.14
CISPEP 2 VAL L 94 PRO L 95 0 0.07
CISPEP 3 TYR L 140 PRO L 141 0 -0.36
CISPEP 4 PHE H 148 PRO H 149 0 -0.31
CISPEP 5 GLN H 150 PRO H 151 0 0.00
SITE 1 AC1 5 THR H 200 GLN H 203 MET L 4 SER L 25
SITE 2 AC1 5 SER L 26
CRYST1 61.100 174.300 45.600 90.00 90.00 90.00 P 21 21 2 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 0.016367 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005737 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021930 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
