HEADER TRANSFERASE 20-JUL-07 2QOD
TITLE HUMAN EPHA3 KINASE AND JUXTAMEMBRANE REGION, Y602F MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPHRIN RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: JUXTAMEMBRANE SEGMENT AND KINASE DOMAIN: RESIDUES 577-947;
COMPND 5 EC: 2.7.10.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 TISSUE: PLACENTA;
SOURCE 6 GENE: EPHA3;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET28A-LIC
KEYWDS RECEPTOR TYROSINE KINASE, JUXTAMEMBRANE SEGMENT, STRUCTURAL GENOMICS,
KEYWDS 2 STRUCTURAL GENOMICS CONSORTIUM, SGC, ATP-BINDING, NUCLEOTIDE-
KEYWDS 3 BINDING, PHOSPHORYLATION, TRANSFERASE, TRANSMEMBRANE, TYROSINE-
KEYWDS 4 PROTEIN KINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.DAVIS,J.R.WALKER,E.M.NEWMAN,F.MACKENZIE,C.BUTLER-COLE,J.WEIGELT,
AUTHOR 2 M.SUNDSTROM,C.H.ARROWSMITH,A.M.EDWARDS,A.BOCHKAREV,S.DHE-PAGANON,
AUTHOR 3 STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 6 30-AUG-23 2QOD 1 REMARK
REVDAT 5 20-OCT-21 2QOD 1 SEQADV
REVDAT 4 25-OCT-17 2QOD 1 REMARK
REVDAT 3 24-FEB-09 2QOD 1 VERSN
REVDAT 2 01-JUL-08 2QOD 1 JRNL
REVDAT 1 21-AUG-07 2QOD 0
JRNL AUTH T.L.DAVIS,J.R.WALKER,P.LOPPNAU,C.BUTLER-COLE,
JRNL AUTH 2 A.ALLALI-HASSANI,S.DHE-PAGANON
JRNL TITL AUTOREGULATION BY THE JUXTAMEMBRANE REGION OF THE HUMAN
JRNL TITL 2 EPHRIN RECEPTOR TYROSINE KINASE A3 (EPHA3).
JRNL REF STRUCTURE V. 16 873 2008
JRNL REFN ISSN 0969-2126
JRNL PMID 18547520
JRNL DOI 10.1016/J.STR.2008.03.008
REMARK 2
REMARK 2 RESOLUTION. 1.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 107702
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) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5412
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.18
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7402
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.23
REMARK 3 BIN R VALUE (WORKING SET) : 0.3060
REMARK 3 BIN FREE R VALUE SET COUNT : 402
REMARK 3 BIN FREE R VALUE : 0.3280
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2181
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 370
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.038
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.039
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.028
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.595
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.963
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2368 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1662 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3224 ; 1.139 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4079 ; 0.819 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 310 ; 4.958 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 106 ;32.701 ;24.057
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 449 ;11.140 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;13.927 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 358 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2634 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 474 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 495 ; 0.207 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1820 ; 0.179 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1212 ; 0.176 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1175 ; 0.083 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 243 ; 0.126 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 16 ; 0.212 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 69 ; 0.174 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 44 ; 0.134 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1909 ; 0.864 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 577 ; 0.138 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2358 ; 1.039 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1092 ; 1.530 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 852 ; 1.947 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2QOD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-AUG-07.
REMARK 100 THE DEPOSITION ID IS D_1000043851.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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) : 1.00000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 107783
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.150
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.03600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.62500
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: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2GSF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 33.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MG/ML PROTEIN, 25% PEG 3350, 0.2M
REMARK 280 AMMONIUM SULFATE, 0.1M HEPES, PH 7.5, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 298K
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 19.14450
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 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 GLY A 575
REMARK 465 SER A 576
REMARK 465 ASP A 577
REMARK 465 GLU A 578
REMARK 465 LYS A 579
REMARK 465 ARG A 580
REMARK 465 LEU A 581
REMARK 465 HIS A 582
REMARK 465 PHE A 583
REMARK 465 GLY A 584
REMARK 465 ASN A 585
REMARK 465 GLY A 586
REMARK 465 HIS A 587
REMARK 465 LEU A 588
REMARK 465 LYS A 589
REMARK 465 LEU A 590
REMARK 465 PRO A 591
REMARK 465 GLY A 592
REMARK 465 LEU A 593
REMARK 465 ARG A 594
REMARK 465 HIS A 600
REMARK 465 THR A 601
REMARK 465 PHE A 602
REMARK 465 GLU A 603
REMARK 465 ASP A 604
REMARK 465 PRO A 605
REMARK 465 THR A 606
REMARK 465 GLN A 607
REMARK 465 THR A 608
REMARK 465 GLY A 766
REMARK 465 LEU A 767
REMARK 465 SER A 768
REMARK 465 ARG A 769
REMARK 465 VAL A 770
REMARK 465 LEU A 771
REMARK 465 GLU A 772
REMARK 465 ASP A 773
REMARK 465 ASP A 774
REMARK 465 PRO A 775
REMARK 465 GLU A 776
REMARK 465 ALA A 777
REMARK 465 ALA A 778
REMARK 465 TYR A 779
REMARK 465 THR A 780
REMARK 465 THR A 781
REMARK 465 ARG A 782
REMARK 465 GLY A 783
REMARK 465 GLY A 784
REMARK 465 LYS A 785
REMARK 465 ILE A 786
REMARK 465 SER A 893
REMARK 465 ALA A 894
REMARK 465 ALA A 895
REMARK 465 ALA A 896
REMARK 465 ARG A 897
REMARK 465 PRO A 898
REMARK 465 GLN A 905
REMARK 465 SER A 906
REMARK 465 ASN A 907
REMARK 465 VAL A 908
REMARK 465 ASP A 909
REMARK 465 ILE A 910
REMARK 465 THR A 911
REMARK 465 THR A 912
REMARK 465 PHE A 913
REMARK 465 ARG A 914
REMARK 465 THR A 915
REMARK 465 THR A 916
REMARK 465 GLY A 917
REMARK 465 ASP A 918
REMARK 465 TRP A 919
REMARK 465 LEU A 920
REMARK 465 ASN A 921
REMARK 465 GLY A 922
REMARK 465 VAL A 923
REMARK 465 TRP A 924
REMARK 465 THR A 925
REMARK 465 ALA A 926
REMARK 465 HIS A 927
REMARK 465 CYS A 928
REMARK 465 LYS A 929
REMARK 465 GLU A 930
REMARK 465 ILE A 931
REMARK 465 PHE A 932
REMARK 465 THR A 933
REMARK 465 GLY A 934
REMARK 465 VAL A 935
REMARK 465 GLU A 936
REMARK 465 TYR A 937
REMARK 465 SER A 938
REMARK 465 SER A 939
REMARK 465 CYS A 940
REMARK 465 ASP A 941
REMARK 465 THR A 942
REMARK 465 ILE A 943
REMARK 465 ALA A 944
REMARK 465 LYS A 945
REMARK 465 ILE A 946
REMARK 465 SER A 947
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 102 O HOH A 369 1.57
REMARK 500 O HOH A 356 O HOH A 367 1.68
REMARK 500 O HOH A 277 O HOH A 369 1.73
REMARK 500 O HOH A 198 O HOH A 359 1.86
REMARK 500 SG CYS A 636 O HOH A 299 2.17
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 750 NE - CZ - NH1 ANGL. DEV. = 3.5 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 LYS A 645 -5.38 81.97
REMARK 500 ARG A 745 -14.41 75.02
REMARK 500 ASP A 764 69.41 68.49
REMARK 500 ASP A 764 70.51 67.44
REMARK 500 TYR A 798 31.66 -149.77
REMARK 500 TRP A 826 -129.62 48.79
REMARK 500 TRP A 826 -129.39 48.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GSF RELATED DB: PDB
REMARK 900 THE HUMAN EPHA3 RECEPTOR TYROSINE KINASE AND JUXTAMEMBRANE REGION
REMARK 900 RELATED ID: 2QO2 RELATED DB: PDB
REMARK 900 HUMAN EPHA3 KINASE AND JUXTAMEMBRANE REGION, DEPHOSPHORYLATED, APO
REMARK 900 STRUCTURE
REMARK 900 RELATED ID: 2QO7 RELATED DB: PDB
REMARK 900 HUMAN EPHA3 KINASE AND JUXTAMEMBRANE REGION, DEPHOSPHORYLATED, AMP-
REMARK 900 PNP BOUND
REMARK 900 RELATED ID: 2QO9 RELATED DB: PDB
REMARK 900 HUMAN EPHA3 KINASE AND JUXTAMEMBRANE REGION, PHOSPHORYLATED, AMP-
REMARK 900 PNP BOUND
REMARK 900 RELATED ID: 2QOB RELATED DB: PDB
REMARK 900 HUMAN EPHA3 KINASE DOMAIN, BASE STRUCTURE
REMARK 900 RELATED ID: 2QOC RELATED DB: PDB
REMARK 900 HUMAN EPHA3 KINASE DOMAIN, PHOSPHORYLATED, AMP-PNP BOUND STRUCTURE
REMARK 900 RELATED ID: 2QOF RELATED DB: PDB
REMARK 900 HUMAN EPHA3 KINASE AND JUXTAMEMBRANE REGION, Y596F MUTANT
REMARK 900 RELATED ID: 2QOI RELATED DB: PDB
REMARK 900 HUMAN EPHA3 KINASE AND JUXTAMEMBRANE REGION, Y596F:Y602F DOUBLE
REMARK 900 MUTANT
REMARK 900 RELATED ID: 2QOK RELATED DB: PDB
REMARK 900 HUMAN EPHA3 KINASE AND JUXTAMEMBRANE REGION, Y596F:Y602F:S768A
REMARK 900 TRIPLE MUTANT
REMARK 900 RELATED ID: 2QOL RELATED DB: PDB
REMARK 900 HUMAN EPHA3 KINASE AND JUXTAMEMBRANE REGION, Y596:Y602:S768G TRIPLE
REMARK 900 MUTANT
REMARK 900 RELATED ID: 2QON RELATED DB: PDB
REMARK 900 HUMAN EPHA3 KINASE AND JUXTAMEMBRANE REGION, Y596F:Y602F:Y742A
REMARK 900 TRIPLE MUTANT
REMARK 900 RELATED ID: 2QOO RELATED DB: PDB
REMARK 900 HUMAN EPHA3 KINASE AND JUXTAMEMBRANE REGION, Y596F:Y602F:Y742F
REMARK 900 TRIPLE MUTANT
REMARK 900 RELATED ID: 2QOQ RELATED DB: PDB
REMARK 900 HUMAN EPHA3 KINASE AND JUXTAMEMBRANE REGION, BASE, AMP-PNP BOUND
REMARK 900 STRUCTURE
DBREF 2QOD A 577 947 UNP Q6P4R6 Q6P4R6_HUMAN 577 947
SEQADV 2QOD GLY A 575 UNP Q6P4R6 EXPRESSION TAG
SEQADV 2QOD SER A 576 UNP Q6P4R6 EXPRESSION TAG
SEQADV 2QOD PHE A 602 UNP Q6P4R6 TYR 602 ENGINEERED MUTATION
SEQRES 1 A 373 GLY SER ASP GLU LYS ARG LEU HIS PHE GLY ASN GLY HIS
SEQRES 2 A 373 LEU LYS LEU PRO GLY LEU ARG THR TYR VAL ASP PRO HIS
SEQRES 3 A 373 THR PHE GLU ASP PRO THR GLN THR VAL HIS GLU PHE ALA
SEQRES 4 A 373 LYS GLU LEU ASP ALA THR ASN ILE SER ILE ASP LYS VAL
SEQRES 5 A 373 VAL GLY ALA GLY GLU PHE GLY GLU VAL CYS SER GLY ARG
SEQRES 6 A 373 LEU LYS LEU PRO SER LYS LYS GLU ILE SER VAL ALA ILE
SEQRES 7 A 373 LYS THR LEU LYS VAL GLY TYR THR GLU LYS GLN ARG ARG
SEQRES 8 A 373 ASP PHE LEU GLY GLU ALA SER ILE MET GLY GLN PHE ASP
SEQRES 9 A 373 HIS PRO ASN ILE ILE ARG LEU GLU GLY VAL VAL THR LYS
SEQRES 10 A 373 SER LYS PRO VAL MET ILE VAL THR GLU TYR MET GLU ASN
SEQRES 11 A 373 GLY SER LEU ASP SER PHE LEU ARG LYS HIS ASP ALA GLN
SEQRES 12 A 373 PHE THR VAL ILE GLN LEU VAL GLY MET LEU ARG GLY ILE
SEQRES 13 A 373 ALA SER GLY MET LYS TYR LEU SER ASP MET GLY TYR VAL
SEQRES 14 A 373 HIS ARG ASP LEU ALA ALA ARG ASN ILE LEU ILE ASN SER
SEQRES 15 A 373 ASN LEU VAL CYS LYS VAL SER ASP PHE GLY LEU SER ARG
SEQRES 16 A 373 VAL LEU GLU ASP ASP PRO GLU ALA ALA TYR THR THR ARG
SEQRES 17 A 373 GLY GLY LYS ILE PRO ILE ARG TRP THR SER PRO GLU ALA
SEQRES 18 A 373 ILE ALA TYR ARG LYS PHE THR SER ALA SER ASP VAL TRP
SEQRES 19 A 373 SER TYR GLY ILE VAL LEU TRP GLU VAL MET SER TYR GLY
SEQRES 20 A 373 GLU ARG PRO TYR TRP GLU MET SER ASN GLN ASP VAL ILE
SEQRES 21 A 373 LYS ALA VAL ASP GLU GLY TYR ARG LEU PRO PRO PRO MET
SEQRES 22 A 373 ASP CYS PRO ALA ALA LEU TYR GLN LEU MET LEU ASP CYS
SEQRES 23 A 373 TRP GLN LYS ASP ARG ASN ASN ARG PRO LYS PHE GLU GLN
SEQRES 24 A 373 ILE VAL SER ILE LEU ASP LYS LEU ILE ARG ASN PRO GLY
SEQRES 25 A 373 SER LEU LYS ILE ILE THR SER ALA ALA ALA ARG PRO SER
SEQRES 26 A 373 ASN LEU LEU LEU ASP GLN SER ASN VAL ASP ILE THR THR
SEQRES 27 A 373 PHE ARG THR THR GLY ASP TRP LEU ASN GLY VAL TRP THR
SEQRES 28 A 373 ALA HIS CYS LYS GLU ILE PHE THR GLY VAL GLU TYR SER
SEQRES 29 A 373 SER CYS ASP THR ILE ALA LYS ILE SER
FORMUL 2 HOH *370(H2 O)
HELIX 1 1 ASP A 617 THR A 619 5 3
HELIX 2 2 THR A 660 GLY A 675 1 16
HELIX 3 3 SER A 706 LYS A 713 1 8
HELIX 4 4 THR A 719 MET A 740 1 22
HELIX 5 5 ALA A 748 ARG A 750 5 3
HELIX 6 6 PRO A 787 THR A 791 5 5
HELIX 7 7 SER A 792 ARG A 799 1 8
HELIX 8 8 THR A 802 SER A 819 1 18
HELIX 9 9 SER A 829 GLU A 839 1 11
HELIX 10 10 PRO A 850 TRP A 861 1 12
HELIX 11 11 ASP A 864 ARG A 868 5 5
HELIX 12 12 LYS A 870 ASN A 884 1 15
HELIX 13 13 PRO A 885 ILE A 890 5 6
SHEET 1 A 5 ILE A 621 ALA A 629 0
SHEET 2 A 5 GLU A 634 LYS A 641 -1 O VAL A 635 N GLY A 628
SHEET 3 A 5 GLU A 647 THR A 654 -1 O ILE A 652 N CYS A 636
SHEET 4 A 5 MET A 696 GLU A 700 -1 O THR A 699 N ALA A 651
SHEET 5 A 5 LEU A 685 VAL A 689 -1 N GLY A 687 O VAL A 698
SHEET 1 B 2 ILE A 752 ILE A 754 0
SHEET 2 B 2 CYS A 760 VAL A 762 -1 O LYS A 761 N LEU A 753
SHEET 1 C 2 TYR A 841 ARG A 842 0
SHEET 2 C 2 LEU A 902 LEU A 903 -1 O LEU A 902 N ARG A 842
CISPEP 1 LYS A 693 PRO A 694 0 4.60
CRYST1 54.215 38.289 76.004 90.00 102.43 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 0.018445 0.000000 0.004064 0.00000
SCALE2 0.000000 0.026117 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013473 0.00000
(ATOM LINES ARE NOT SHOWN.)
END