HEADER HYDROLASE/HYDROLASE INHIBITOR 07-NOV-04 1XXM
TITLE THE MODULAR ARCHITECTURE OF PROTEIN-PROTEIN BINDING SITE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-LACTAMASE TEM;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TEM-1; TEM-2; TEM-3; TEM-4; TEM-5; TEM-6; TEM-8/CAZ-2; TEM-
COMPND 5 16/CAZ-7; TEM-24/CAZ-6; IRT-4; PENICILLINASE;
COMPND 6 EC: 3.5.2.6;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: BETA-LACTAMASE INHIBITORY PROTEIN;
COMPND 11 CHAIN: C, D;
COMPND 12 SYNONYM: BLIP;
COMPND 13 ENGINEERED: YES;
COMPND 14 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: BLA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: STREPTOMYCES CLAVULIGERUS;
SOURCE 10 ORGANISM_TAXID: 1901;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS PROTEIN-PROTEIN COMPLEX; TEM-1 BETA-LACTAMASE; BETA-2 LACTAMASE
KEYWDS 2 INHIBITOR PROTEIN; BLIP, ISRAEL STRUCTURAL PROTEOMICS CENTER, ISPC,
KEYWDS 3 STRUCTURAL GENOMICS, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.REICHMANN,O.RAHAT,S.ALBECK,R.MEGED,O.DYM,G.SCHREIBER,ISRAEL
AUTHOR 2 STRUCTURAL PROTEOMICS CENTER (ISPC)
REVDAT 4 23-AUG-23 1XXM 1 REMARK
REVDAT 3 20-OCT-21 1XXM 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1XXM 1 VERSN
REVDAT 1 18-JAN-05 1XXM 0
JRNL AUTH D.REICHMANN,O.RAHAT,S.ALBECK,R.MEGED,O.DYM,G.SCHREIBER
JRNL TITL THE MODULAR ARCHITECTURE OF PROTEIN-PROTEIN BINDING
JRNL TITL 2 INTERFACES
JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 57 2005
JRNL REFN ISSN 0027-8424
JRNL PMID 15618400
JRNL DOI 10.1073/PNAS.0407280102
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 1.90
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) (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 71472
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM 10%
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7231
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 : 6468
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 417
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.01400
REMARK 3 B22 (A**2) : -3.03700
REMARK 3 B33 (A**2) : 1.02300
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.12
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.18
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 1XXM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-NOV-04.
REMARK 100 THE DEPOSITION ID IS D_1000030883.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-AUG-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : YALE MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 71746
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : 0.04500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 7.70
REMARK 200 R MERGE FOR SHELL (I) : 0.31100
REMARK 200 R SYM FOR SHELL (I) : 0.04700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 28.90
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1S0W
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: LICL; SODIUM ACETATE; PEG 6000, PH 5.,
REMARK 280 MICROBATCH, TEMPERATURE 298K
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 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 22.85300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 78.47550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 62.23650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 78.47550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.85300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 62.23650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
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: 2150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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: 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 MET A 69 -148.73 60.00
REMARK 500 LEU A 220 -126.40 -104.89
REMARK 500 TYR C1050 -127.00 -137.18
REMARK 500 ALA C1080 79.99 -156.30
REMARK 500 GLU B 58 142.87 -176.84
REMARK 500 MET B 69 -148.31 59.00
REMARK 500 ASN B 175 -13.00 74.19
REMARK 500 LEU B 220 -128.14 -103.30
REMARK 500 HIS B 287 33.37 -85.25
REMARK 500 TYR D1050 -123.94 -147.38
REMARK 500 ALA D1080 75.84 -153.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C2002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C1133 OD2
REMARK 620 2 ASP C1163 O 91.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D2001 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D1133 OD2
REMARK 620 2 ARG D1144 O 73.3
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1S0W RELATED DB: PDB
REMARK 900 1B LACTAMSE/B LACTAMASE INHIBITOR
REMARK 900 RELATED ID: W00178 RELATED DB: TARGETDB
DBREF 1XXM A 26 288 UNP P62593 BLAT_ECOLI 24 286
DBREF 1XXM B 26 288 UNP P62593 BLAT_ECOLI 24 286
DBREF 1XXM C 1001 1165 UNP P35804 BLIP_STRCL 37 201
DBREF 1XXM D 1001 1165 UNP P35804 BLIP_STRCL 37 201
SEQADV 1XXM ILE A 84 UNP P62593 VAL 82 ENGINEERED MUTATION
SEQADV 1XXM ALA A 104 UNP P62593 GLU 102 ENGINEERED MUTATION
SEQADV 1XXM ALA A 105 UNP P62593 TYR 103 ENGINEERED MUTATION
SEQADV 1XXM ILE B 84 UNP P62593 VAL 82 ENGINEERED MUTATION
SEQADV 1XXM ALA B 104 UNP P62593 GLU 102 ENGINEERED MUTATION
SEQADV 1XXM ALA B 105 UNP P62593 TYR 103 ENGINEERED MUTATION
SEQADV 1XXM ALA C 1074 UNP P35804 LYS 110 ENGINEERED MUTATION
SEQADV 1XXM ALA C 1142 UNP P35804 PHE 178 ENGINEERED MUTATION
SEQADV 1XXM ALA C 1143 UNP P35804 TYR 179 ENGINEERED MUTATION
SEQADV 1XXM ALA D 1074 UNP P35804 LYS 110 ENGINEERED MUTATION
SEQADV 1XXM ALA D 1142 UNP P35804 PHE 178 ENGINEERED MUTATION
SEQADV 1XXM ALA D 1143 UNP P35804 TYR 179 ENGINEERED MUTATION
SEQRES 1 A 263 HIS PRO GLU THR LEU VAL LYS VAL LYS ASP ALA GLU ASP
SEQRES 2 A 263 GLN LEU GLY ALA ARG VAL GLY TYR ILE GLU LEU ASP LEU
SEQRES 3 A 263 ASN SER GLY LYS ILE LEU GLU SER PHE ARG PRO GLU GLU
SEQRES 4 A 263 ARG PHE PRO MET MET SER THR PHE LYS VAL LEU LEU CYS
SEQRES 5 A 263 GLY ALA VAL LEU SER ARG ILE ASP ALA GLY GLN GLU GLN
SEQRES 6 A 263 LEU GLY ARG ARG ILE HIS TYR SER GLN ASN ASP LEU VAL
SEQRES 7 A 263 ALA ALA SER PRO VAL THR GLU LYS HIS LEU THR ASP GLY
SEQRES 8 A 263 MET THR VAL ARG GLU LEU CYS SER ALA ALA ILE THR MET
SEQRES 9 A 263 SER ASP ASN THR ALA ALA ASN LEU LEU LEU THR THR ILE
SEQRES 10 A 263 GLY GLY PRO LYS GLU LEU THR ALA PHE LEU HIS ASN MET
SEQRES 11 A 263 GLY ASP HIS VAL THR ARG LEU ASP ARG TRP GLU PRO GLU
SEQRES 12 A 263 LEU ASN GLU ALA ILE PRO ASN ASP GLU ARG ASP THR THR
SEQRES 13 A 263 MET PRO ALA ALA MET ALA THR THR LEU ARG LYS LEU LEU
SEQRES 14 A 263 THR GLY GLU LEU LEU THR LEU ALA SER ARG GLN GLN LEU
SEQRES 15 A 263 ILE ASP TRP MET GLU ALA ASP LYS VAL ALA GLY PRO LEU
SEQRES 16 A 263 LEU ARG SER ALA LEU PRO ALA GLY TRP PHE ILE ALA ASP
SEQRES 17 A 263 LYS SER GLY ALA GLY GLU ARG GLY SER ARG GLY ILE ILE
SEQRES 18 A 263 ALA ALA LEU GLY PRO ASP GLY LYS PRO SER ARG ILE VAL
SEQRES 19 A 263 VAL ILE TYR THR THR GLY SER GLN ALA THR MET ASP GLU
SEQRES 20 A 263 ARG ASN ARG GLN ILE ALA GLU ILE GLY ALA SER LEU ILE
SEQRES 21 A 263 LYS HIS TRP
SEQRES 1 C 165 ALA GLY VAL MET THR GLY ALA LYS PHE THR GLN ILE GLN
SEQRES 2 C 165 PHE GLY MET THR ARG GLN GLN VAL LEU ASP ILE ALA GLY
SEQRES 3 C 165 ALA GLU ASN CYS GLU THR GLY GLY SER PHE GLY ASP SER
SEQRES 4 C 165 ILE HIS CYS ARG GLY HIS ALA ALA GLY ASP TYR TYR ALA
SEQRES 5 C 165 TYR ALA THR PHE GLY PHE THR SER ALA ALA ALA ASP ALA
SEQRES 6 C 165 LYS VAL ASP SER LYS SER GLN GLU ALA LEU LEU ALA PRO
SEQRES 7 C 165 SER ALA PRO THR LEU THR LEU ALA LYS PHE ASN GLN VAL
SEQRES 8 C 165 THR VAL GLY MET THR ARG ALA GLN VAL LEU ALA THR VAL
SEQRES 9 C 165 GLY GLN GLY SER CYS THR THR TRP SER GLU TYR TYR PRO
SEQRES 10 C 165 ALA TYR PRO SER THR ALA GLY VAL THR LEU SER LEU SER
SEQRES 11 C 165 CYS PHE ASP VAL ASP GLY TYR SER SER THR GLY ALA ALA
SEQRES 12 C 165 ARG GLY SER ALA HIS LEU TRP PHE THR ASP GLY VAL LEU
SEQRES 13 C 165 GLN GLY LYS ARG GLN TRP ASP LEU VAL
SEQRES 1 B 263 HIS PRO GLU THR LEU VAL LYS VAL LYS ASP ALA GLU ASP
SEQRES 2 B 263 GLN LEU GLY ALA ARG VAL GLY TYR ILE GLU LEU ASP LEU
SEQRES 3 B 263 ASN SER GLY LYS ILE LEU GLU SER PHE ARG PRO GLU GLU
SEQRES 4 B 263 ARG PHE PRO MET MET SER THR PHE LYS VAL LEU LEU CYS
SEQRES 5 B 263 GLY ALA VAL LEU SER ARG ILE ASP ALA GLY GLN GLU GLN
SEQRES 6 B 263 LEU GLY ARG ARG ILE HIS TYR SER GLN ASN ASP LEU VAL
SEQRES 7 B 263 ALA ALA SER PRO VAL THR GLU LYS HIS LEU THR ASP GLY
SEQRES 8 B 263 MET THR VAL ARG GLU LEU CYS SER ALA ALA ILE THR MET
SEQRES 9 B 263 SER ASP ASN THR ALA ALA ASN LEU LEU LEU THR THR ILE
SEQRES 10 B 263 GLY GLY PRO LYS GLU LEU THR ALA PHE LEU HIS ASN MET
SEQRES 11 B 263 GLY ASP HIS VAL THR ARG LEU ASP ARG TRP GLU PRO GLU
SEQRES 12 B 263 LEU ASN GLU ALA ILE PRO ASN ASP GLU ARG ASP THR THR
SEQRES 13 B 263 MET PRO ALA ALA MET ALA THR THR LEU ARG LYS LEU LEU
SEQRES 14 B 263 THR GLY GLU LEU LEU THR LEU ALA SER ARG GLN GLN LEU
SEQRES 15 B 263 ILE ASP TRP MET GLU ALA ASP LYS VAL ALA GLY PRO LEU
SEQRES 16 B 263 LEU ARG SER ALA LEU PRO ALA GLY TRP PHE ILE ALA ASP
SEQRES 17 B 263 LYS SER GLY ALA GLY GLU ARG GLY SER ARG GLY ILE ILE
SEQRES 18 B 263 ALA ALA LEU GLY PRO ASP GLY LYS PRO SER ARG ILE VAL
SEQRES 19 B 263 VAL ILE TYR THR THR GLY SER GLN ALA THR MET ASP GLU
SEQRES 20 B 263 ARG ASN ARG GLN ILE ALA GLU ILE GLY ALA SER LEU ILE
SEQRES 21 B 263 LYS HIS TRP
SEQRES 1 D 165 ALA GLY VAL MET THR GLY ALA LYS PHE THR GLN ILE GLN
SEQRES 2 D 165 PHE GLY MET THR ARG GLN GLN VAL LEU ASP ILE ALA GLY
SEQRES 3 D 165 ALA GLU ASN CYS GLU THR GLY GLY SER PHE GLY ASP SER
SEQRES 4 D 165 ILE HIS CYS ARG GLY HIS ALA ALA GLY ASP TYR TYR ALA
SEQRES 5 D 165 TYR ALA THR PHE GLY PHE THR SER ALA ALA ALA ASP ALA
SEQRES 6 D 165 LYS VAL ASP SER LYS SER GLN GLU ALA LEU LEU ALA PRO
SEQRES 7 D 165 SER ALA PRO THR LEU THR LEU ALA LYS PHE ASN GLN VAL
SEQRES 8 D 165 THR VAL GLY MET THR ARG ALA GLN VAL LEU ALA THR VAL
SEQRES 9 D 165 GLY GLN GLY SER CYS THR THR TRP SER GLU TYR TYR PRO
SEQRES 10 D 165 ALA TYR PRO SER THR ALA GLY VAL THR LEU SER LEU SER
SEQRES 11 D 165 CYS PHE ASP VAL ASP GLY TYR SER SER THR GLY ALA ALA
SEQRES 12 D 165 ARG GLY SER ALA HIS LEU TRP PHE THR ASP GLY VAL LEU
SEQRES 13 D 165 GLN GLY LYS ARG GLN TRP ASP LEU VAL
HET CA C2002 1
HET CA D2001 1
HETNAM CA CALCIUM ION
FORMUL 5 CA 2(CA 2+)
FORMUL 7 HOH *417(H2 O)
HELIX 1 1 HIS A 26 GLY A 41 1 16
HELIX 2 2 THR A 71 ALA A 86 1 16
HELIX 3 3 SER A 98 LEU A 102 5 5
HELIX 4 4 SER A 106 HIS A 112 1 7
HELIX 5 5 VAL A 119 SER A 130 1 12
HELIX 6 6 ASP A 131 ILE A 142 1 12
HELIX 7 7 GLY A 144 ASN A 154 1 11
HELIX 8 8 PRO A 167 GLU A 171 5 5
HELIX 9 9 MET A 182 GLY A 196 1 15
HELIX 10 10 THR A 200 ALA A 213 1 14
HELIX 11 11 LEU A 220 LEU A 225 5 6
HELIX 12 12 THR A 269 HIS A 287 1 19
HELIX 13 13 THR C 1005 ILE C 1012 1 8
HELIX 14 14 THR C 1017 GLY C 1026 1 10
HELIX 15 15 GLY C 1033 GLY C 1037 5 5
HELIX 16 16 THR C 1084 VAL C 1091 1 8
HELIX 17 17 THR C 1096 GLY C 1105 1 10
HELIX 18 18 HIS B 26 GLY B 41 1 16
HELIX 19 19 THR B 71 ALA B 86 1 16
HELIX 20 20 SER B 98 LEU B 102 5 5
HELIX 21 21 SER B 106 HIS B 112 1 7
HELIX 22 22 VAL B 119 SER B 130 1 12
HELIX 23 23 ASP B 131 GLY B 143 1 13
HELIX 24 24 GLY B 144 MET B 155 1 12
HELIX 25 25 PRO B 167 GLU B 171 5 5
HELIX 26 26 MET B 182 GLY B 196 1 15
HELIX 27 27 THR B 200 ALA B 213 1 14
HELIX 28 28 LEU B 220 LEU B 225 5 6
HELIX 29 29 THR B 269 HIS B 287 1 19
HELIX 30 30 THR D 1005 ILE D 1012 1 8
HELIX 31 31 THR D 1017 GLY D 1026 1 10
HELIX 32 32 GLY D 1034 GLY D 1037 5 4
HELIX 33 33 THR D 1084 VAL D 1091 1 8
HELIX 34 34 THR D 1096 GLY D 1105 1 10
SHEET 1 A 5 ILE A 56 PHE A 60 0
SHEET 2 A 5 VAL A 44 ASP A 50 -1 N GLU A 48 O LEU A 57
SHEET 3 A 5 ARG A 257 THR A 263 -1 O TYR A 262 N GLY A 45
SHEET 4 A 5 ARG A 243 GLY A 250 -1 N ALA A 247 O VAL A 259
SHEET 5 A 5 PHE A 230 ALA A 237 -1 N PHE A 230 O GLY A 250
SHEET 1 B 2 PHE A 66 PRO A 67 0
SHEET 2 B 2 THR A 180 THR A 181 -1 O THR A 181 N PHE A 66
SHEET 1 C 2 ARG A 94 ILE A 95 0
SHEET 2 C 2 MET A 117 THR A 118 -1 O MET A 117 N ILE A 95
SHEET 1 D 8 CYS C1030 GLU C1031 0
SHEET 2 D 8 ILE C1040 ALA C1047 -1 O HIS C1041 N GLU C1031
SHEET 3 D 8 TYR C1050 PHE C1058 -1 O ALA C1052 N GLY C1044
SHEET 4 D 8 VAL C1067 GLU C1073 -1 O SER C1071 N THR C1055
SHEET 5 D 8 CYS C1109 TYR C1115 -1 O TRP C1112 N GLN C1072
SHEET 6 D 8 THR C1126 PHE C1132 -1 O SER C1130 N THR C1110
SHEET 7 D 8 SER C1146 THR C1152 -1 O LEU C1149 N LEU C1129
SHEET 8 D 8 VAL C1155 TRP C1162 -1 O GLN C1157 N TRP C1150
SHEET 1 E 5 ILE B 56 PHE B 60 0
SHEET 2 E 5 ARG B 43 ASP B 50 -1 N GLU B 48 O LEU B 57
SHEET 3 E 5 ARG B 257 THR B 264 -1 O TYR B 262 N GLY B 45
SHEET 4 E 5 ARG B 243 GLY B 250 -1 N ILE B 245 O ILE B 261
SHEET 5 E 5 PHE B 230 ALA B 237 -1 N PHE B 230 O GLY B 250
SHEET 1 F 2 PHE B 66 PRO B 67 0
SHEET 2 F 2 THR B 180 THR B 181 -1 O THR B 181 N PHE B 66
SHEET 1 G 2 ARG B 94 ILE B 95 0
SHEET 2 G 2 MET B 117 THR B 118 -1 O MET B 117 N ILE B 95
SHEET 1 H 8 CYS D1030 THR D1032 0
SHEET 2 H 8 ILE D1040 ALA D1047 -1 O HIS D1041 N GLU D1031
SHEET 3 H 8 TYR D1050 PHE D1058 -1 O ALA D1052 N GLY D1044
SHEET 4 H 8 VAL D1067 GLU D1073 -1 O SER D1071 N THR D1055
SHEET 5 H 8 CYS D1109 TYR D1115 -1 O GLU D1114 N LYS D1070
SHEET 6 H 8 THR D1126 PHE D1132 -1 O SER D1128 N SER D1113
SHEET 7 H 8 SER D1146 THR D1152 -1 O PHE D1151 N LEU D1127
SHEET 8 H 8 VAL D1155 TRP D1162 -1 O GLN D1157 N TRP D1150
SSBOND 1 CYS A 77 CYS A 123 1555 1555 2.04
SSBOND 2 CYS C 1030 CYS C 1042 1555 1555 2.71
SSBOND 3 CYS C 1109 CYS C 1131 1555 1555 2.04
SSBOND 4 CYS B 77 CYS B 123 1555 1555 2.04
SSBOND 5 CYS D 1030 CYS D 1042 1555 1555 2.04
SSBOND 6 CYS D 1109 CYS D 1131 1555 1555 2.03
LINK OD2 ASP C1133 CA CA C2002 1555 1555 3.04
LINK O ASP C1163 CA CA C2002 1555 1555 3.03
LINK OD2 ASP D1133 CA CA D2001 1555 1555 3.07
LINK O ARG D1144 CA CA D2001 1555 1555 3.36
CISPEP 1 GLU A 166 PRO A 167 0 0.11
CISPEP 2 TYR C 1119 PRO C 1120 0 0.68
CISPEP 3 GLU B 166 PRO B 167 0 0.28
CISPEP 4 TYR D 1119 PRO D 1120 0 0.49
SITE 1 AC1 2 ASP D1133 ARG D1144
SITE 1 AC2 3 ASP C1133 ARG C1144 ASP C1163
CRYST1 45.706 124.473 156.951 90.00 90.00 90.00 P 21 21 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 0.021879 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008034 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006371 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
