HEADER HORMONE/GROWTH FACTOR 23-APR-03 1P4O
TITLE STRUCTURE OF APO UNACTIVATED IGF-1R KINASE DOMAIN AT 1.5A RESOLUTION.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN-LIKE GROWTH FACTOR I RECEPTOR PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: KINASE DOMAIN;
COMPND 5 SYNONYM: CD221 ANTIGEN, IGF1R;
COMPND 6 EC: 2.7.1.112;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: IGF1R;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS IGF-1R, KINASE DOMAIN, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MUNSHI,M.KORNIENKO,D.L.HALL,P.L.DARKE,L.WAXMAN,L.C.KUO
REVDAT 6 14-FEB-24 1P4O 1 REMARK
REVDAT 5 27-OCT-21 1P4O 1 SEQADV
REVDAT 4 13-JUL-11 1P4O 1 VERSN
REVDAT 3 24-FEB-09 1P4O 1 VERSN
REVDAT 2 05-APR-05 1P4O 1 JRNL
REVDAT 1 29-APR-03 1P4O 0
JRNL AUTH S.MUNSHI,D.L.HALL,M.KORNIENKO,P.L.DARKE,L.C.KUO
JRNL TITL STRUCTURE OF APO, UNACTIVATED INSULIN-LIKE GROWTH FACTOR-1
JRNL TITL 2 RECEPTOR KINASE AT 1.5 A RESOLUTION.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 59 1725 2003
JRNL REFN ISSN 0907-4449
JRNL PMID 14501110
JRNL DOI 10.1107/S0907444903015415
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
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) (%) : 80.3
REMARK 3 NUMBER OF REFLECTIONS : 89007
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : 9.8% OF THE TOTAL REFLECTIONS
REMARK 3 USED
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 10812
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 : 4958
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 635
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) : 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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
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 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 1P4O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-APR-03.
REMARK 100 THE DEPOSITION ID IS D_1000019002.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 98666
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 53.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 8K, 0.1M LICL, 10% ETHYLENE
REMARK 280 GLYCOL, 10% GLYCEROL AND 0.1M TRIS-HCL BUFFER, PH 8.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
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
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 42.78000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 MET A 943
REMARK 465 ALA A 944
REMARK 465 SER A 945
REMARK 465 VAL A 946
REMARK 465 ASN A 947
REMARK 465 LYS A 1256
REMARK 465 LEU A 1257
REMARK 465 PRO A 1258
REMARK 465 GLU A 1259
REMARK 465 PRO A 1260
REMARK 465 GLU A 1261
REMARK 465 GLU A 1262
REMARK 465 LEU A 1263
REMARK 465 ASP A 1264
REMARK 465 MET B 943
REMARK 465 ALA B 944
REMARK 465 SER B 945
REMARK 465 VAL B 946
REMARK 465 GLU B 1261
REMARK 465 GLU B 1262
REMARK 465 LEU B 1263
REMARK 465 ASP B 1264
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 GLU A 949 -49.73 -131.98
REMARK 500 ASP A 960 -156.68 -135.06
REMARK 500 ARG A1104 -18.95 81.10
REMARK 500 LYS A1141 -140.76 -100.42
REMARK 500 PRO B 948 31.32 -59.75
REMARK 500 GLU B 949 -125.50 -163.10
REMARK 500 ASP B 960 -156.66 -137.21
REMARK 500 ASN B1028 73.43 -153.51
REMARK 500 ARG B1104 -17.46 81.68
REMARK 500 ASP B1105 42.09 -140.93
REMARK 500 LYS B1141 -136.53 -105.14
REMARK 500 GLU B1259 96.50 171.41
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1P4O A 944 1264 UNP P08069 IGF1R_HUMAN 974 1294
DBREF 1P4O B 944 1264 UNP P08069 IGF1R_HUMAN 974 1294
SEQADV 1P4O MET A 943 UNP P08069 INITIATING METHIONINE
SEQADV 1P4O ALA A 1067 UNP P08069 GLU 1097 ENGINEERED MUTATION
SEQADV 1P4O ALA A 1069 UNP P08069 GLU 1099 ENGINEERED MUTATION
SEQADV 1P4O MET B 943 UNP P08069 INITIATING METHIONINE
SEQADV 1P4O ALA B 1067 UNP P08069 GLU 1097 ENGINEERED MUTATION
SEQADV 1P4O ALA B 1069 UNP P08069 GLU 1099 ENGINEERED MUTATION
SEQRES 1 A 322 MET ALA SER VAL ASN PRO GLU TYR PHE SER ALA ALA ASP
SEQRES 2 A 322 VAL TYR VAL PRO ASP GLU TRP GLU VAL ALA ARG GLU LYS
SEQRES 3 A 322 ILE THR MET SER ARG GLU LEU GLY GLN GLY SER PHE GLY
SEQRES 4 A 322 MET VAL TYR GLU GLY VAL ALA LYS GLY VAL VAL LYS ASP
SEQRES 5 A 322 GLU PRO GLU THR ARG VAL ALA ILE LYS THR VAL ASN GLU
SEQRES 6 A 322 ALA ALA SER MET ARG GLU ARG ILE GLU PHE LEU ASN GLU
SEQRES 7 A 322 ALA SER VAL MET LYS GLU PHE ASN CYS HIS HIS VAL VAL
SEQRES 8 A 322 ARG LEU LEU GLY VAL VAL SER GLN GLY GLN PRO THR LEU
SEQRES 9 A 322 VAL ILE MET GLU LEU MET THR ARG GLY ASP LEU LYS SER
SEQRES 10 A 322 TYR LEU ARG SER LEU ARG PRO ALA MET ALA ASN ASN PRO
SEQRES 11 A 322 VAL LEU ALA PRO PRO SER LEU SER LYS MET ILE GLN MET
SEQRES 12 A 322 ALA GLY GLU ILE ALA ASP GLY MET ALA TYR LEU ASN ALA
SEQRES 13 A 322 ASN LYS PHE VAL HIS ARG ASP LEU ALA ALA ARG ASN CYS
SEQRES 14 A 322 MET VAL ALA GLU ASP PHE THR VAL LYS ILE GLY ASP PHE
SEQRES 15 A 322 GLY MET THR ARG ASP ILE TYR GLU THR ASP TYR TYR ARG
SEQRES 16 A 322 LYS GLY GLY LYS GLY LEU LEU PRO VAL ARG TRP MET SER
SEQRES 17 A 322 PRO GLU SER LEU LYS ASP GLY VAL PHE THR THR TYR SER
SEQRES 18 A 322 ASP VAL TRP SER PHE GLY VAL VAL LEU TRP GLU ILE ALA
SEQRES 19 A 322 THR LEU ALA GLU GLN PRO TYR GLN GLY LEU SER ASN GLU
SEQRES 20 A 322 GLN VAL LEU ARG PHE VAL MET GLU GLY GLY LEU LEU ASP
SEQRES 21 A 322 LYS PRO ASP ASN CYS PRO ASP MET LEU PHE GLU LEU MET
SEQRES 22 A 322 ARG MET CYS TRP GLN TYR ASN PRO LYS MET ARG PRO SER
SEQRES 23 A 322 PHE LEU GLU ILE ILE SER SER ILE LYS GLU GLU MET GLU
SEQRES 24 A 322 PRO GLY PHE ARG GLU VAL SER PHE TYR TYR SER GLU GLU
SEQRES 25 A 322 ASN LYS LEU PRO GLU PRO GLU GLU LEU ASP
SEQRES 1 B 322 MET ALA SER VAL ASN PRO GLU TYR PHE SER ALA ALA ASP
SEQRES 2 B 322 VAL TYR VAL PRO ASP GLU TRP GLU VAL ALA ARG GLU LYS
SEQRES 3 B 322 ILE THR MET SER ARG GLU LEU GLY GLN GLY SER PHE GLY
SEQRES 4 B 322 MET VAL TYR GLU GLY VAL ALA LYS GLY VAL VAL LYS ASP
SEQRES 5 B 322 GLU PRO GLU THR ARG VAL ALA ILE LYS THR VAL ASN GLU
SEQRES 6 B 322 ALA ALA SER MET ARG GLU ARG ILE GLU PHE LEU ASN GLU
SEQRES 7 B 322 ALA SER VAL MET LYS GLU PHE ASN CYS HIS HIS VAL VAL
SEQRES 8 B 322 ARG LEU LEU GLY VAL VAL SER GLN GLY GLN PRO THR LEU
SEQRES 9 B 322 VAL ILE MET GLU LEU MET THR ARG GLY ASP LEU LYS SER
SEQRES 10 B 322 TYR LEU ARG SER LEU ARG PRO ALA MET ALA ASN ASN PRO
SEQRES 11 B 322 VAL LEU ALA PRO PRO SER LEU SER LYS MET ILE GLN MET
SEQRES 12 B 322 ALA GLY GLU ILE ALA ASP GLY MET ALA TYR LEU ASN ALA
SEQRES 13 B 322 ASN LYS PHE VAL HIS ARG ASP LEU ALA ALA ARG ASN CYS
SEQRES 14 B 322 MET VAL ALA GLU ASP PHE THR VAL LYS ILE GLY ASP PHE
SEQRES 15 B 322 GLY MET THR ARG ASP ILE TYR GLU THR ASP TYR TYR ARG
SEQRES 16 B 322 LYS GLY GLY LYS GLY LEU LEU PRO VAL ARG TRP MET SER
SEQRES 17 B 322 PRO GLU SER LEU LYS ASP GLY VAL PHE THR THR TYR SER
SEQRES 18 B 322 ASP VAL TRP SER PHE GLY VAL VAL LEU TRP GLU ILE ALA
SEQRES 19 B 322 THR LEU ALA GLU GLN PRO TYR GLN GLY LEU SER ASN GLU
SEQRES 20 B 322 GLN VAL LEU ARG PHE VAL MET GLU GLY GLY LEU LEU ASP
SEQRES 21 B 322 LYS PRO ASP ASN CYS PRO ASP MET LEU PHE GLU LEU MET
SEQRES 22 B 322 ARG MET CYS TRP GLN TYR ASN PRO LYS MET ARG PRO SER
SEQRES 23 B 322 PHE LEU GLU ILE ILE SER SER ILE LYS GLU GLU MET GLU
SEQRES 24 B 322 PRO GLY PHE ARG GLU VAL SER PHE TYR TYR SER GLU GLU
SEQRES 25 B 322 ASN LYS LEU PRO GLU PRO GLU GLU LEU ASP
FORMUL 3 HOH *635(H2 O)
HELIX 1 1 ALA A 965 GLU A 967 5 3
HELIX 2 2 SER A 1010 MET A 1024 1 15
HELIX 3 3 LYS A 1025 PHE A 1027 5 3
HELIX 4 4 ASP A 1056 ASN A 1071 1 16
HELIX 5 5 SER A 1078 ASN A 1099 1 22
HELIX 6 6 ALA A 1107 ARG A 1109 5 3
HELIX 7 7 ARG A 1128 TYR A 1135 5 8
HELIX 8 8 GLY A 1139 LYS A 1141 5 3
HELIX 9 9 PRO A 1145 MET A 1149 5 5
HELIX 10 10 SER A 1150 GLY A 1157 1 8
HELIX 11 11 THR A 1160 LEU A 1178 1 19
HELIX 12 12 SER A 1187 GLU A 1197 1 11
HELIX 13 13 PRO A 1208 TRP A 1219 1 12
HELIX 14 14 ASN A 1222 ARG A 1226 5 5
HELIX 15 15 SER A 1228 LYS A 1237 1 10
HELIX 16 16 GLU A 1238 MET A 1240 5 3
HELIX 17 17 GLU A 1241 PRO A 1242 5 2
HELIX 18 18 GLY A 1243 SER A 1248 1 6
HELIX 19 19 ALA B 965 GLU B 967 5 3
HELIX 20 20 SER B 1010 MET B 1024 1 15
HELIX 21 21 LYS B 1025 PHE B 1027 5 3
HELIX 22 22 ASP B 1056 ASN B 1071 1 16
HELIX 23 23 SER B 1078 ASN B 1099 1 22
HELIX 24 24 ALA B 1107 ARG B 1109 5 3
HELIX 25 25 ARG B 1128 TYR B 1135 5 8
HELIX 26 26 GLY B 1139 LYS B 1141 5 3
HELIX 27 27 PRO B 1145 MET B 1149 5 5
HELIX 28 28 SER B 1150 GLY B 1157 1 8
HELIX 29 29 THR B 1160 LEU B 1178 1 19
HELIX 30 30 SER B 1187 GLU B 1197 1 11
HELIX 31 31 PRO B 1208 TRP B 1219 1 12
HELIX 32 32 ASN B 1222 ARG B 1226 5 5
HELIX 33 33 SER B 1228 LYS B 1237 1 10
HELIX 34 34 GLU B 1238 MET B 1240 5 3
HELIX 35 35 GLU B 1241 PRO B 1242 5 2
HELIX 36 36 GLY B 1243 SER B 1248 1 6
HELIX 37 37 SER B 1252 LYS B 1256 5 5
SHEET 1 A 5 ILE A 969 GLN A 977 0
SHEET 2 A 5 MET A 982 VAL A 992 -1 O GLU A 985 N ARG A 973
SHEET 3 A 5 GLU A 995 THR A1004 -1 O ILE A1002 N TYR A 984
SHEET 4 A 5 LEU A1046 GLU A1050 -1 O MET A1049 N ALA A1001
SHEET 5 A 5 LEU A1035 VAL A1039 -1 N GLY A1037 O ILE A1048
SHEET 1 B 2 CYS A1111 VAL A1113 0
SHEET 2 B 2 VAL A1119 ILE A1121 -1 O LYS A1120 N MET A1112
SHEET 1 C 2 TYR A1136 ARG A1137 0
SHEET 2 C 2 LEU A1143 LEU A1144 -1 O LEU A1144 N TYR A1136
SHEET 1 D 5 ILE B 969 GLN B 977 0
SHEET 2 D 5 MET B 982 VAL B 992 -1 O GLU B 985 N ARG B 973
SHEET 3 D 5 GLU B 995 THR B1004 -1 O ILE B1002 N TYR B 984
SHEET 4 D 5 LEU B1046 GLU B1050 -1 O MET B1049 N ALA B1001
SHEET 5 D 5 LEU B1035 VAL B1039 -1 N GLY B1037 O ILE B1048
SHEET 1 E 2 CYS B1111 VAL B1113 0
SHEET 2 E 2 VAL B1119 ILE B1121 -1 O LYS B1120 N MET B1112
SHEET 1 F 2 TYR B1136 ARG B1137 0
SHEET 2 F 2 LEU B1143 LEU B1144 -1 O LEU B1144 N TYR B1136
CISPEP 1 GLN A 1043 PRO A 1044 0 -0.06
CISPEP 2 GLN B 1043 PRO B 1044 0 -0.11
CRYST1 52.950 85.560 78.880 90.00 99.10 90.00 P 1 21 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 0.018886 0.000000 0.003025 0.00000
SCALE2 0.000000 0.011688 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012839 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
