HEADER TRANSFERASE 09-JUL-10 3NW5
TITLE CRYSTAL STRUCTURE OF INSULIN-LIKE GROWTH FACTOR 1 RECEPTOR (IGF-1R-WT)
TITLE 2 COMPLEX WITH A CARBON-LINKED PROLINE ISOSTERE INHIBITOR (11B)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN-LIKE GROWTH FACTOR 1 RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN (RESIDUES 982-1286);
COMPND 5 SYNONYM: INSULIN-LIKE GROWTH FACTOR I RECEPTOR, IGF-I RECEPTOR;
COMPND 6 EC: 2.7.10.1;
COMPND 7 ENGINEERED: 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: UNIDENTIFIED BACULOVIRUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10469
KEYWDS HORMONE/GROWTH FACTOR, IGF-1R, KINASE DOMAIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.S.SACK
REVDAT 3 21-FEB-24 3NW5 1 REMARK SEQADV
REVDAT 2 08-SEP-10 3NW5 1 JRNL
REVDAT 1 28-JUL-10 3NW5 0
JRNL AUTH A.J.SAMPOGNARO,M.D.WITTMAN,J.M.CARBONI,C.CHANG,A.F.GREER,
JRNL AUTH 2 W.W.HURLBURT,J.S.SACK,D.M.VYAS
JRNL TITL PROLINE ISOSTERES IN A SERIES OF 2,4-DISUBSTITUTED
JRNL TITL 2 PYRROLO[1,2-F][1,2,4]TRIAZINE INHIBITORS OF IGF-1R KINASE
JRNL TITL 3 AND IR KINASE.
JRNL REF BIOORG.MED.CHEM.LETT. V. 20 5027 2010
JRNL REFN ISSN 0960-894X
JRNL PMID 20675137
JRNL DOI 10.1016/J.BMCL.2010.07.045
REMARK 2
REMARK 2 RESOLUTION. 2.14 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.9.3
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.14
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.91
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 16110
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
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 812
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 : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.14
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.29
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.54
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2722
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2115
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2581
REMARK 3 BIN R VALUE (WORKING SET) : 0.2076
REMARK 3 BIN FREE R VALUE : 0.2826
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.18
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 141
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 : 2408
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 205
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.94
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.29
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.90390
REMARK 3 B22 (A**2) : -4.12800
REMARK 3 B33 (A**2) : 5.03190
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.13410
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.258
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.287
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2497 ; 2.000 ; NULL
REMARK 3 BOND ANGLES : 3372 ; 2.000 ; NULL
REMARK 3 TORSION ANGLES : 880 ; 2.000 ; NULL
REMARK 3 TRIGONAL CARBON PLANES : 65 ; 2.000 ; NULL
REMARK 3 GENERAL PLANES : 357 ; 5.000 ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS : 2497 ; 20.000 ; NULL
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 302 ; 5.000 ; NULL
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 3193 ; 4.000 ; NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.13
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.38
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 19.40
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3NW5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1000060353.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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 FR-E DW
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MICROMAX CONFOCAL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 92
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 (DENZO)
REMARK 200 DATA SCALING SOFTWARE : HKL-2000 (SCALEPACK)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16126
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.140
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.14
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.47500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
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 53.32100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.64450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 53.32100
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 20.64450
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 950
REMARK 465 VAL A 951
REMARK 465 SER A 952
REMARK 465 ALA A 953
REMARK 465 ALA A 954
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 ASP A 955 CB CG OD1 OD2
REMARK 470 VAL A 956 CB CG1 CG2
REMARK 470 THR A1127 OG1 CG2
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 VAL A 956 110.84 73.50
REMARK 500 ASP A 960 -157.62 -136.62
REMARK 500 SER A 972 -97.73 -118.87
REMARK 500 LYS A 993 -126.37 53.46
REMARK 500 ASN A1028 88.28 -153.06
REMARK 500 MET A1068 83.11 64.18
REMARK 500 GLU A1069 22.26 -156.49
REMARK 500 ARG A1104 -10.43 77.70
REMARK 500 ASP A1105 43.56 -145.96
REMARK 500 PHE A1117 -2.68 84.29
REMARK 500 THR A1127 -146.77 75.09
REMARK 500 ARG A1128 149.38 -13.01
REMARK 500 ASP A1129 -5.70 72.88
REMARK 500 ILE A1130 -67.19 -94.89
REMARK 500 LYS A1141 -138.94 -100.54
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 LGX A 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3NW6 RELATED DB: PDB
REMARK 900 RELATED ID: 3NW7 RELATED DB: PDB
DBREF 3NW5 A 952 1256 UNP P08069 IGF1R_HUMAN 982 1286
SEQADV 3NW5 MET A 950 UNP P08069 EXPRESSION TAG
SEQADV 3NW5 VAL A 951 UNP P08069 EXPRESSION TAG
SEQRES 1 A 307 MET VAL SER ALA ALA ASP VAL TYR VAL PRO ASP GLU TRP
SEQRES 2 A 307 GLU VAL ALA ARG GLU LYS ILE THR MET SER ARG GLU LEU
SEQRES 3 A 307 GLY GLN GLY SER PHE GLY MET VAL TYR GLU GLY VAL ALA
SEQRES 4 A 307 LYS GLY VAL VAL LYS ASP GLU PRO GLU THR ARG VAL ALA
SEQRES 5 A 307 ILE LYS THR VAL ASN GLU ALA ALA SER MET ARG GLU ARG
SEQRES 6 A 307 ILE GLU PHE LEU ASN GLU ALA SER VAL MET LYS GLU PHE
SEQRES 7 A 307 ASN CYS HIS HIS VAL VAL ARG LEU LEU GLY VAL VAL SER
SEQRES 8 A 307 GLN GLY GLN PRO THR LEU VAL ILE MET GLU LEU MET THR
SEQRES 9 A 307 ARG GLY ASP LEU LYS SER TYR LEU ARG SER LEU ARG PRO
SEQRES 10 A 307 GLU MET GLU ASN ASN PRO VAL LEU ALA PRO PRO SER LEU
SEQRES 11 A 307 SER LYS MET ILE GLN MET ALA GLY GLU ILE ALA ASP GLY
SEQRES 12 A 307 MET ALA TYR LEU ASN ALA ASN LYS PHE VAL HIS ARG ASP
SEQRES 13 A 307 LEU ALA ALA ARG ASN CYS MET VAL ALA GLU ASP PHE THR
SEQRES 14 A 307 VAL LYS ILE GLY ASP PHE GLY MET THR ARG ASP ILE TYR
SEQRES 15 A 307 GLU THR ASP TYR TYR ARG LYS GLY GLY LYS GLY LEU LEU
SEQRES 16 A 307 PRO VAL ARG TRP MET SER PRO GLU SER LEU LYS ASP GLY
SEQRES 17 A 307 VAL PHE THR THR TYR SER ASP VAL TRP SER PHE GLY VAL
SEQRES 18 A 307 VAL LEU TRP GLU ILE ALA THR LEU ALA GLU GLN PRO TYR
SEQRES 19 A 307 GLN GLY LEU SER ASN GLU GLN VAL LEU ARG PHE VAL MET
SEQRES 20 A 307 GLU GLY GLY LEU LEU ASP LYS PRO ASP ASN CYS PRO ASP
SEQRES 21 A 307 MET LEU PHE GLU LEU MET ARG MET CYS TRP GLN TYR ASN
SEQRES 22 A 307 PRO LYS MET ARG PRO SER PHE LEU GLU ILE ILE SER SER
SEQRES 23 A 307 ILE LYS GLU GLU MET GLU PRO GLY PHE ARG GLU VAL SER
SEQRES 24 A 307 PHE TYR TYR SER GLU GLU ASN LYS
HET LGX A 1 32
HETNAM LGX N-(5-CYCLOPROPYL-1H-PYRAZOL-3-YL)-2-{(2R)-1-[(6-
HETNAM 2 LGX FLUOROPYRIDIN-3-YL)CARBONYL]PYRROLIDIN-2-YL}PYRROLO[2,
HETNAM 3 LGX 1-F][1,2,4]TRIAZIN-4-AMINE
FORMUL 2 LGX C22 H21 F N8 O
FORMUL 3 HOH *205(H2 O)
HELIX 1 1 ALA A 965 GLU A 967 5 3
HELIX 2 2 SER A 1010 SER A 1022 1 13
HELIX 3 3 VAL A 1023 PHE A 1027 5 5
HELIX 4 4 ASP A 1056 SER A 1063 1 8
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 TYR A 1131 TYR A 1135 5 5
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
SHEET 1 A 5 ILE A 969 GLN A 977 0
SHEET 2 A 5 MET A 982 ALA A 988 -1 O GLU A 985 N ARG A 973
SHEET 3 A 5 THR A 998 THR A1004 -1 O ILE A1002 N TYR A 984
SHEET 4 A 5 LEU A1046 GLU A1050 -1 O VAL A1047 N LYS A1003
SHEET 5 A 5 LEU A1035 VAL A1039 -1 N LEU A1036 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
CISPEP 1 GLN A 1043 PRO A 1044 0 -0.29
SITE 1 AC1 15 HOH A 11 HOH A 119 HOH A 172 LEU A 975
SITE 2 AC1 15 GLY A 976 GLN A 977 VAL A 983 ALA A1001
SITE 3 AC1 15 MET A1049 GLU A1050 MET A1052 THR A1053
SITE 4 AC1 15 GLY A1055 ASP A1056 ILE A1130
CRYST1 106.642 41.289 78.183 90.00 120.21 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 0.009377 0.000000 0.005460 0.00000
SCALE2 0.000000 0.024220 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014801 0.00000
(ATOM LINES ARE NOT SHOWN.)
END