HEADER TRANSFERASE 12-JAN-07 2OJ9
TITLE STRUCTURE OF IGF-1R KINASE DOMAIN COMPLEXED WITH A BENZIMIDAZOLE
TITLE 2 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN-LIKE GROWTH FACTOR 1 RECEPTOR PRECURSOR (EC
COMPND 3 2.7.10.1) (INSULIN-LIKE GROWTH FACTOR I RECEPTOR) (IGF-I RECEPTOR)
COMPND 4 (CD221 ANTIGEN);
COMPND 5 CHAIN: A;
COMPND 6 FRAGMENT: KINASE DOMAIN, RESIDUES 982-1286;
COMPND 7 SYNONYM: CD221 ANTIGEN, IGF1R;
COMPND 8 EC: 2.7.1.112;
COMPND 9 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;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS HORMONE/GROWTH FACTOR, IGF-1R, KINASE DOMAIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.S.SACK,B.L.JACOBSON
REVDAT 3 27-DEC-23 2OJ9 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2OJ9 1 VERSN
REVDAT 1 01-MAY-07 2OJ9 0
JRNL AUTH U.VELAPARTHI,M.WITTMAN,P.LIU,K.STOFFAN,K.ZIMMERMANN,X.SANG,
JRNL AUTH 2 J.CARBONI,A.LI,R.ATTAR,M.GOTTARDIS,A.GREER,C.Y.CHANG,
JRNL AUTH 3 B.L.JACOBSEN,J.S.SACK,Y.SUN,D.R.LANGLEY,B.BALASUBRAMANIAN,
JRNL AUTH 4 D.VYAS
JRNL TITL DISCOVERY AND INITIAL SAR OF
JRNL TITL 2 3-(1H-BENZO[D]IMIDAZOL-2-YL)PYRIDIN-2(1H)-ONES AS INHIBITORS
JRNL TITL 3 OF INSULIN-LIKE GROWTH FACTOR 1-RECEPTOR (IGF-1R).
JRNL REF BIOORG.MED.CHEM.LETT. V. 17 2317 2007
JRNL REFN ISSN 0960-894X
JRNL PMID 17317169
JRNL DOI 10.1016/J.BMCL.2007.01.102
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT 1.9.3
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 13.21
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 21499
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1096
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 : 9
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.12
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.70
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3019
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 20.350
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2862
REMARK 3 BIN R VALUE (WORKING SET) : 0.1998
REMARK 3 BIN FREE R VALUE : 0.2726
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 157
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 : 2358
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 204
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.06
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.72593
REMARK 3 B22 (A**2) : -0.98521
REMARK 3 B33 (A**2) : -0.74072
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -5.69129
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
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) : NULL
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 : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2441 ; 2.000 ; NULL
REMARK 3 BOND ANGLES : 3280 ; 2.000 ; NULL
REMARK 3 TORSION ANGLES : 547 ; 0.000 ; NULL
REMARK 3 TRIGONAL CARBON PLANES : 72 ; 2.000 ; NULL
REMARK 3 GENERAL PLANES : 351 ; 5.000 ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS : 2437 ; 20.000 ; NULL
REMARK 3 BAD NON-BONDED CONTACTS : 97 ; 5.000 ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : NULL ; NULL ; 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 : NULL ; NULL ; NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.02
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL
REMARK 3 OTHER TORSION ANGLES (DEGREES) : NULL
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 2OJ9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JAN-07.
REMARK 100 THE DEPOSITION ID IS D_1000041204.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUN-99
REMARK 200 TEMPERATURE (KELVIN) : 100.0
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54180
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21556
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
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 (%) : 96.5
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.24000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
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 (%): 48.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP,
REMARK 280 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 22.14450
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). AUTHORS STATE THAT A MONOMER
REMARK 300 IS THE BIOLOGICAL UNIT OF THIS POLYPEPTIDE. SEE REMARK 350
REMARK 300 FOR INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
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 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 MET A 1068
REMARK 465 GLU A 1069
REMARK 465 ASN A 1070
REMARK 465 ASN A 1071
REMARK 465 PRO A 1072
REMARK 465 VAL A 1073
REMARK 465 LEU A 1074
REMARK 465 ALA A 1075
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 GLU A1067 CG CD OE1 OE2
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 PRO A 959 C - N - CA ANGL. DEV. = 18.1 DEGREES
REMARK 500 PRO A 959 C - N - CD ANGL. DEV. = -20.3 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 ASP A 955 36.45 -73.60
REMARK 500 VAL A 956 106.23 -35.12
REMARK 500 TYR A 957 -135.98 -112.79
REMARK 500 VAL A 958 74.92 -112.16
REMARK 500 PRO A 959 -47.79 -13.76
REMARK 500 ASP A 960 178.23 39.30
REMARK 500 LYS A 993 -63.44 -28.59
REMARK 500 ALA A1009 134.92 -178.48
REMARK 500 ARG A1104 -12.60 78.05
REMARK 500 ASP A1105 41.94 -143.01
REMARK 500 MET A1126 -33.39 70.41
REMARK 500 TYR A1131 61.88 -118.16
REMARK 500 LYS A1141 54.24 37.48
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 BMI A 301
DBREF 2OJ9 A 952 1256 UNP P08069 IGF1R_HUMAN 982 1286
SEQADV 2OJ9 MET A 950 UNP P08069 CLONING ARTIFACT
SEQADV 2OJ9 VAL A 951 UNP P08069 CLONING ARTIFACT
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 BMI A 301 30
HETNAM BMI 3-[5-(1H-IMIDAZOL-1-YL)-7-METHYL-1H-BENZIMIDAZOL-2-YL]-
HETNAM 2 BMI 4-[(PYRIDIN-2-YLMETHYL)AMINO]PYRIDIN-2(1H)-ONE
FORMUL 2 BMI C22 H19 N7 O
FORMUL 3 HOH *204(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 PRO A 1145 MET A 1149 5 5
HELIX 9 9 SER A 1150 GLY A 1157 1 8
HELIX 10 10 THR A 1160 THR A 1177 1 18
HELIX 11 11 SER A 1187 GLU A 1197 1 11
HELIX 12 12 PRO A 1208 TRP A 1219 1 12
HELIX 13 13 ASN A 1222 ARG A 1226 5 5
HELIX 14 14 SER A 1228 LYS A 1237 1 10
HELIX 15 15 GLU A 1238 MET A 1240 5 3
HELIX 16 16 GLU A 1241 PRO A 1242 5 2
HELIX 17 17 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 VAL A 992 -1 O VAL A 983 N LEU A 975
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 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 LYS A1138 0
SHEET 2 C 2 GLY A1142 LEU A1144 -1 O LEU A1144 N TYR A1136
CISPEP 1 GLN A 1043 PRO A 1044 0 -0.32
SITE 1 AC1 11 HOH A 112 LEU A 975 ALA A1001 MET A1049
SITE 2 AC1 11 GLU A1050 LEU A1051 MET A1052 THR A1053
SITE 3 AC1 11 GLY A1055 MET A1112 THR A1127
CRYST1 57.271 44.289 65.744 90.00 99.05 90.00 P 1 21 1 2
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 0.017461 0.000000 0.002781 0.00000
SCALE2 0.000000 0.022579 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015402 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
