HEADER TRANSFERASE/SIGNALING PROTEIN 27-AUG-05 2AUH
TITLE CRYSTAL STRUCTURE OF THE GRB14 BPS REGION IN COMPLEX WITH
TITLE 2 THE INSULIN RECEPTOR TYROSINE KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TYROSINE KINASE DOMAIN;
COMPND 5 SYNONYM: IR, CD220 ANTIGEN;
COMPND 6 EC: 2.7.1.112;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: GROWTH FACTOR RECEPTOR-BOUND PROTEIN 14;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: BPS REGION;
COMPND 12 SYNONYM: GRB14 ADAPTOR PROTEIN;
COMPND 13 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: INSR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: GRB14;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TYROSINE KINASE, BPS REGION, TRANSFERASE/SIGNALING PROTEIN
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.S.DEPETRIS,J.HU,I.GIMPELEVICH,L.J.HOLT,R.J.DALY,
AUTHOR 2 S.R.HUBBARD
REVDAT 3 24-FEB-09 2AUH 1 VERSN
REVDAT 2 02-SEP-08 2AUH 1 KEYWDS
REVDAT 1 01-NOV-05 2AUH 0
JRNL AUTH R.S.DEPETRIS,J.HU,I.GIMPELEVICH,L.J.HOLT,R.J.DALY,
JRNL AUTH 2 S.R.HUBBARD
JRNL TITL STRUCTURAL BASIS FOR INHIBITION OF THE INSULIN
JRNL TITL 2 RECEPTOR BY THE ADAPTOR PROTEIN GRB14.
JRNL REF MOL.CELL V. 20 325 2005
JRNL REFN ISSN 1097-2765
JRNL PMID 16246733
JRNL DOI 10.1016/J.MOLCEL.2005.09.001
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 3.20 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.27
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 211618.380
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 9903
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 SET) : 0.223
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT : 526
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.011
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.40
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1480
REMARK 3 BIN R VALUE (WORKING SET) : 0.2950
REMARK 3 BIN FREE R VALUE : 0.3390
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 77
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.039
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2637
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.53000
REMARK 3 B22 (A**2) : -8.53000
REMARK 3 B33 (A**2) : 17.07000
REMARK 3 B12 (A**2) : 8.18000
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) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.47
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) : 0.44
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.57
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.50
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.84
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.240 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.240 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.470 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.460 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.23
REMARK 3 BSOL : 10.00
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : TOPPAR:PARAMCSDX.MISC
REMARK 3 PARAMETER FILE 5 : DNA-RNA.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2AUH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-SEP-05.
REMARK 100 THE RCSB ID CODE IS RCSB034326.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-APR-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9903
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 29.270
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.37700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: 1IR3
REMARK 200
REMARK 200 REMARK: BECAUSE OF THE MODEST RESOLUTION, THE ASSIGNMENT AND
REMARK 200 POSITIONS OF THE TWO CALCIUM IONS SHOULD BE CONSIDERED
REMARK 200 TENTATIVE.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.95000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 21.97500
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 43.95000
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 21.97500
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: 2580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 VAL A 978
REMARK 465 PHE A 979
REMARK 465 PRO A 980
REMARK 465 SER A 981
REMARK 465 SER A 982
REMARK 465 VAL A 983
REMARK 465 SER B 361
REMARK 465 SER B 362
REMARK 465 GLN B 363
REMARK 465 SER B 364
REMARK 465 ILE B 365
REMARK 465 SER B 366
REMARK 465 PRO B 367
REMARK 465 MET B 368
REMARK 465 ARG B 369
REMARK 465 SER B 370
REMARK 465 ILE B 371
REMARK 465 SER B 372
REMARK 465 GLY B 410
REMARK 465 SER B 411
REMARK 465 LEU B 412
REMARK 465 ARG B 413
REMARK 465 LEU B 414
REMARK 465 GLY B 415
REMARK 465 THR B 416
REMARK 465 HIS B 417
REMARK 465 GLY B 418
REMARK 465 SER B 419
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 A 988 CG CD OE1 OE2
REMARK 470 ASN A1014 CG OD1 ND2
REMARK 470 ARG A1016 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1024 CG CD OE1 OE2
REMARK 470 GLU A1034 CG CD OE1 OE2
REMARK 470 LYS A1068 CG CD CE NZ
REMARK 470 GLU A1096 CG CD OE1 OE2
REMARK 470 ARG A1243 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1280 CG CD OE1 OE2
REMARK 470 LYS A1283 CG CD CE NZ
REMARK 470 GLN B 384 CG CD OE1 NE2
REMARK 470 LYS B 385 CG CD CE NZ
REMARK 470 LYS B 409 CG CD CE NZ
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 PRO A 986 160.50 -41.89
REMARK 500 ASP A 987 -165.51 -170.00
REMARK 500 GLU A 988 2.38 -47.99
REMARK 500 TRP A 989 -71.78 -115.11
REMARK 500 GLU A 990 87.27 -1.74
REMARK 500 LEU A 999 -75.85 -79.14
REMARK 500 LYS A1020 96.52 -47.50
REMARK 500 ALA A1023 -79.31 -61.10
REMARK 500 ALA A1036 -156.29 -95.35
REMARK 500 VAL A1060 119.52 -16.06
REMARK 500 ASN A1097 36.70 -99.26
REMARK 500 LYS A1126 25.80 -74.37
REMARK 500 LYS A1127 78.53 48.62
REMARK 500 ARG A1131 -21.21 72.15
REMARK 500 PHE A1144 13.00 81.30
REMARK 500 PRO A1250 -33.91 -32.17
REMARK 500 LYS A1264 -38.37 -23.24
REMARK 500 ASP A1266 49.01 -102.16
REMARK 500 SER A1270 15.82 -68.21
REMARK 500 ASN B 374 163.16 -39.84
REMARK 500 SER B 375 -54.29 -129.08
REMARK 500 SER B 386 -178.41 -64.54
REMARK 500 ARG B 387 120.74 176.81
REMARK 500 ALA B 399 -76.32 -39.57
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 A 1 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A1150 OD1
REMARK 620 2 CA A 2 CA 77.9
REMARK 620 3 ASP A1150 OD2 51.0 79.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 2 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A1150 OD2
REMARK 620 2 GLU A1047 OE1 70.5
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 A 1
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2
DBREF 2AUH A 978 1283 UNP P06213 INSR_HUMAN 1005 1310
DBREF 2AUH B 373 419 UNP Q14449 GRB14_HUMAN 361 419
SEQADV 2AUH PTR A 1158 UNP P06213 TYR 1185 MODIFIED RESIDUE
SEQADV 2AUH PTR A 1162 UNP P06213 TYR 1189 MODIFIED RESIDUE
SEQADV 2AUH PTR A 1163 UNP P06213 TYR 1190 MODIFIED RESIDUE
SEQADV 2AUH ASN A 1251 UNP P06213 LYS 1278 VARIANT
SEQADV 2AUH SER A 981 UNP P06213 CYS 1008 ENGINEERED
SEQADV 2AUH SER B 411 UNP Q14449 CYS 411 ENGINEERED
SEQRES 1 A 306 VAL PHE PRO SER SER VAL TYR VAL PRO ASP GLU TRP GLU
SEQRES 2 A 306 VAL SER ARG GLU LYS ILE THR LEU LEU ARG GLU LEU GLY
SEQRES 3 A 306 GLN GLY SER PHE GLY MET VAL TYR GLU GLY ASN ALA ARG
SEQRES 4 A 306 ASP ILE ILE LYS GLY GLU ALA GLU THR ARG VAL ALA VAL
SEQRES 5 A 306 LYS THR VAL ASN GLU SER ALA SER LEU ARG GLU ARG ILE
SEQRES 6 A 306 GLU PHE LEU ASN GLU ALA SER VAL MET LYS GLY PHE THR
SEQRES 7 A 306 CYS HIS HIS VAL VAL ARG LEU LEU GLY VAL VAL SER LYS
SEQRES 8 A 306 GLY GLN PRO THR LEU VAL VAL MET GLU LEU MET ALA HIS
SEQRES 9 A 306 GLY ASP LEU LYS SER TYR LEU ARG SER LEU ARG PRO GLU
SEQRES 10 A 306 ALA GLU ASN ASN PRO GLY ARG PRO PRO PRO THR LEU GLN
SEQRES 11 A 306 GLU MET ILE GLN MET ALA ALA GLU ILE ALA ASP GLY MET
SEQRES 12 A 306 ALA TYR LEU ASN ALA LYS LYS PHE VAL HIS ARG ASP LEU
SEQRES 13 A 306 ALA ALA ARG ASN CYS MET VAL ALA HIS ASP PHE THR VAL
SEQRES 14 A 306 LYS ILE GLY ASP PHE GLY MET THR ARG ASP ILE PTR GLU
SEQRES 15 A 306 THR ASP PTR PTR ARG LYS GLY GLY LYS GLY LEU LEU PRO
SEQRES 16 A 306 VAL ARG TRP MET ALA PRO GLU SER LEU LYS ASP GLY VAL
SEQRES 17 A 306 PHE THR THR SER SER ASP MET TRP SER PHE GLY VAL VAL
SEQRES 18 A 306 LEU TRP GLU ILE THR SER LEU ALA GLU GLN PRO TYR GLN
SEQRES 19 A 306 GLY LEU SER ASN GLU GLN VAL LEU LYS PHE VAL MET ASP
SEQRES 20 A 306 GLY GLY TYR LEU ASP GLN PRO ASP ASN CYS PRO GLU ARG
SEQRES 21 A 306 VAL THR ASP LEU MET ARG MET CYS TRP GLN PHE ASN PRO
SEQRES 22 A 306 ASN MET ARG PRO THR PHE LEU GLU ILE VAL ASN LEU LEU
SEQRES 23 A 306 LYS ASP ASP LEU HIS PRO SER PHE PRO GLU VAL SER PHE
SEQRES 24 A 306 PHE HIS SER GLU GLU ASN LYS
SEQRES 1 B 59 SER SER GLN SER ILE SER PRO MET ARG SER ILE SER GLU
SEQRES 2 B 59 ASN SER LEU VAL ALA MET ASP PHE SER GLY GLN LYS SER
SEQRES 3 B 59 ARG VAL ILE GLU ASN PRO THR GLU ALA LEU SER VAL ALA
SEQRES 4 B 59 VAL GLU GLU GLY LEU ALA TRP ARG LYS LYS GLY SER LEU
SEQRES 5 B 59 ARG LEU GLY THR HIS GLY SER
MODRES 2AUH PTR A 1158 TYR O-PHOSPHOTYROSINE
MODRES 2AUH PTR A 1162 TYR O-PHOSPHOTYROSINE
MODRES 2AUH PTR A 1163 TYR O-PHOSPHOTYROSINE
HET PTR A1158 16
HET PTR A1162 16
HET PTR A1163 16
HET CA A 1 1
HET CA A 2 1
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM CA CALCIUM ION
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 1 PTR 3(C9 H12 N O6 P)
FORMUL 3 CA 2(CA 2+)
HELIX 1 1 SER A 992 GLU A 994 5 3
HELIX 2 2 SER A 1037 GLY A 1053 1 17
HELIX 3 3 ASP A 1083 SER A 1090 1 8
HELIX 4 4 THR A 1105 LYS A 1126 1 22
HELIX 5 5 ALA A 1134 ARG A 1136 5 3
HELIX 6 6 PRO A 1172 MET A 1176 5 5
HELIX 7 7 ALA A 1177 GLY A 1184 1 8
HELIX 8 8 THR A 1187 THR A 1203 1 17
HELIX 9 9 SER A 1214 ASP A 1224 1 11
HELIX 10 10 PRO A 1235 TRP A 1246 1 12
HELIX 11 11 ASN A 1249 ARG A 1253 5 5
HELIX 12 12 THR A 1255 LYS A 1264 1 10
HELIX 13 13 ASP A 1265 LEU A 1267 5 3
HELIX 14 14 SER A 1270 SER A 1275 1 6
HELIX 15 15 ASN B 391 LYS B 408 1 18
SHEET 1 A 5 ILE A 996 GLU A1001 0
SHEET 2 A 5 GLY A1008 ARG A1016 -1 O GLU A1012 N ARG A1000
SHEET 3 A 5 GLU A1024 VAL A1032 -1 O VAL A1029 N TYR A1011
SHEET 4 A 5 THR A1072 GLU A1077 -1 O MET A1076 N ALA A1028
SHEET 5 A 5 LEU A1062 VAL A1066 -1 N LEU A1063 O VAL A1075
SHEET 1 B 2 PHE A1128 VAL A1129 0
SHEET 2 B 2 ARG A1155 ASP A1156 -1 O ARG A1155 N VAL A1129
SHEET 1 C 2 CYS A1138 VAL A1140 0
SHEET 2 C 2 VAL A1146 ILE A1148 -1 O LYS A1147 N MET A1139
SHEET 1 D 2 PTR A1163 ARG A1164 0
SHEET 2 D 2 VAL A1185 PHE A1186 -1 O PHE A1186 N PTR A1163
SHEET 1 E 2 LYS A1168 LEU A1171 0
SHEET 2 E 2 VAL B 377 ASP B 380 -1 O MET B 379 N GLY A1169
LINK CA CA A 1 OD1 ASP A1150 1555 1555 2.73
LINK CA CA A 1 CA CA A 2 1555 1555 2.79
LINK CA CA A 1 OD2 ASP A1150 1555 1555 2.32
LINK CA CA A 2 OD2 ASP A1150 1555 1555 3.29
LINK CA CA A 2 OE1 GLU A1047 1555 1555 2.90
LINK C ILE A1157 N PTR A1158 1555 1555 1.33
LINK C PTR A1158 N GLU A1159 1555 1555 1.32
LINK C ASP A1161 N PTR A1162 1555 1555 1.33
LINK C PTR A1162 N PTR A1163 1555 1555 1.33
LINK C PTR A1163 N ARG A1164 1555 1555 1.33
CISPEP 1 GLN A 1070 PRO A 1071 0 0.13
SITE 1 AC1 2 CA A 2 ASP A1150
SITE 1 AC2 3 CA A 1 GLU A1047 ASP A1150
CRYST1 127.182 127.182 65.925 90.00 90.00 120.00 P 62 6
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 0.007863 0.004540 0.000000 0.00000
SCALE2 0.000000 0.009079 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015169 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
