HEADER TRANSFERASE 21-JUL-09 2WO1
TITLE CRYSTAL STRUCTURE OF THE EPHA4 LIGAND BINDING DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPHRIN TYPE-A RECEPTOR;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: EPHRIN LIGAND BINDING DOMAIN, RESIDUES 30-202;
COMPND 5 SYNONYM: TYROSINE-PROTEIN KINASE RECEPTOR SEK, RECEPTOR PROTEIN-
COMPND 6 TYROSINE KINASE HEK8, TYROSINE-PROTEIN KINASE TYRO1;
COMPND 7 EC: 2.7.10.1;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293T;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PHLSEC
KEYWDS GLYCOPROTEIN, AXON GUIDANCE, VASCULAR DEVELOPMENT, CELL SURFACE
KEYWDS 2 RECEPTOR, TRANSFERASE, CELL SIGNALING
EXPDTA X-RAY DIFFRACTION
AUTHOR T.A.BOWDEN,A.R.ARICESCU,J.E.NETTLESHIP,C.SIEBOLD,N.RAHMAN-HUQ,
AUTHOR 2 R.J.OWENS,D.I.STUART,E.Y.JONES
REVDAT 5 20-DEC-23 2WO1 1 REMARK
REVDAT 4 28-FEB-18 2WO1 1 SOURCE
REVDAT 3 23-NOV-11 2WO1 1 JRNL
REVDAT 2 13-JUL-11 2WO1 1 VERSN
REVDAT 1 27-OCT-09 2WO1 0
JRNL AUTH T.A.BOWDEN,A.R.ARICESCU,J.E.NETTLESHIP,C.SIEBOLD,
JRNL AUTH 2 N.RAHMAN-HUQ,R.J.OWENS,D.I.STUART,E.Y.JONES
JRNL TITL STRUCTURAL PLASTICITY OF EPH-RECEPTOR A4 FACILITATES
JRNL TITL 2 CROSS-CLASS EPHRIN SIGNALLING
JRNL REF STRUCTURE V. 17 1386 2009
JRNL REFN ISSN 0969-2126
JRNL PMID 19836338
JRNL DOI 10.1016/J.STR.2009.07.018
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 30277
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1595
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2151
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.02
REMARK 3 BIN R VALUE (WORKING SET) : 0.2240
REMARK 3 BIN FREE R VALUE SET COUNT : 116
REMARK 3 BIN FREE R VALUE : 0.2910
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2890
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 297
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 26.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.34000
REMARK 3 B22 (A**2) : -1.17000
REMARK 3 B33 (A**2) : -0.09000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.30000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.153
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.145
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.095
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.851
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3018 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2073 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4083 ; 1.246 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5032 ; 0.771 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 366 ; 6.659 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 155 ;34.897 ;24.194
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 534 ;15.030 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;15.184 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 445 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3355 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 633 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1801 ; 0.786 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 734 ; 0.177 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2929 ; 1.424 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1217 ; 1.776 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1151 ; 2.923 ; 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 : 6
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 29 A 38 4
REMARK 3 1 B 29 B 38 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 114 ; 0.60 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 114 ; 0.60 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 114 ; 0.86 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 114 ; 0.86 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 46 A 56 4
REMARK 3 1 B 46 NULL 56 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 134 ; 0.37 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 B (A): 134 ; 0.37 ; 0.50
REMARK 3 MEDIUM THERMAL 2 A (A**2): 134 ; 0.62 ; 2.00
REMARK 3 MEDIUM THERMAL 2 B (A**2): 134 ; 0.62 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 67 A 103 4
REMARK 3 1 B 67 NULL 103 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 3 A (A): 512 ; 0.53 ; 0.50
REMARK 3 MEDIUM POSITIONAL 3 B (A): 512 ; 0.53 ; 0.50
REMARK 3 MEDIUM THERMAL 3 A (A**2): 512 ; 0.79 ; 2.00
REMARK 3 MEDIUM THERMAL 3 B (A**2): 512 ; 0.79 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 120 A 133 4
REMARK 3 1 B 120 NULL 133 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 4 A (A): 210 ; 0.31 ; 0.50
REMARK 3 MEDIUM POSITIONAL 4 B (A): 210 ; 0.31 ; 0.50
REMARK 3 MEDIUM THERMAL 4 A (A**2): 210 ; 0.53 ; 2.00
REMARK 3 MEDIUM THERMAL 4 B (A**2): 210 ; 0.53 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 141 A 155 4
REMARK 3 1 B 141 B 155 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 5 A (A): 193 ; 0.24 ; 0.50
REMARK 3 MEDIUM POSITIONAL 5 B (A): 193 ; 0.24 ; 0.50
REMARK 3 MEDIUM THERMAL 5 A (A**2): 193 ; 0.81 ; 2.00
REMARK 3 MEDIUM THERMAL 5 B (A**2): 193 ; 0.81 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 6
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 167 A 203 4
REMARK 3 1 B 167 B 203 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 6 A (A): 493 ; 0.43 ; 0.50
REMARK 3 MEDIUM POSITIONAL 6 B (A): 493 ; 0.43 ; 0.50
REMARK 3 MEDIUM THERMAL 6 A (A**2): 493 ; 0.59 ; 2.00
REMARK 3 MEDIUM THERMAL 6 B (A**2): 493 ; 0.59 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 27 A 209
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6750 27.0410 47.3350
REMARK 3 T TENSOR
REMARK 3 T11: 0.0235 T22: 0.0301
REMARK 3 T33: 0.0288 T12: -0.0002
REMARK 3 T13: 0.0136 T23: 0.0163
REMARK 3 L TENSOR
REMARK 3 L11: 3.2882 L22: 1.1074
REMARK 3 L33: 0.6438 L12: 0.1127
REMARK 3 L13: -0.0559 L23: 0.0329
REMARK 3 S TENSOR
REMARK 3 S11: -0.0700 S12: 0.0165 S13: 0.0770
REMARK 3 S21: -0.0608 S22: 0.0182 S23: 0.0478
REMARK 3 S31: 0.0751 S32: 0.0176 S33: 0.0518
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 29 B 203
REMARK 3 ORIGIN FOR THE GROUP (A): 36.8310 47.0230 33.0760
REMARK 3 T TENSOR
REMARK 3 T11: 0.1037 T22: 0.0412
REMARK 3 T33: 0.0455 T12: 0.0112
REMARK 3 T13: 0.0287 T23: 0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 0.8783 L22: 2.0254
REMARK 3 L33: 2.6505 L12: 0.4311
REMARK 3 L13: 0.0543 L23: 1.0135
REMARK 3 S TENSOR
REMARK 3 S11: -0.0223 S12: 0.0860 S13: 0.0854
REMARK 3 S21: -0.3585 S22: -0.0314 S23: 0.0208
REMARK 3 S31: -0.1255 S32: -0.1310 S33: 0.0537
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 2WO1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-JUL-09.
REMARK 100 THE DEPOSITION ID IS D_1290040489.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-DEC-05
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 : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.977
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31875
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.34000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.000
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 1NUK
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000, 8% PROPAN-1-OL, AND 100
REMARK 280 MM TRIS PH 8.5
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 36.61400
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
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 350
REMARK 350 BIOMOLECULE: 2
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: 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 GLU A 62
REMARK 465 ILE A 159
REMARK 465 GLY A 160
REMARK 465 HIS A 210
REMARK 465 HIS A 211
REMARK 465 GLU B 27
REMARK 465 THR B 28
REMARK 465 LYS B 205
REMARK 465 HIS B 206
REMARK 465 HIS B 207
REMARK 465 HIS B 208
REMARK 465 HIS B 209
REMARK 465 HIS B 210
REMARK 465 HIS B 211
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 CYS A 73 57.80 -155.16
REMARK 500 ASN A 74 49.03 -93.05
REMARK 500 ASN A 81 72.29 -150.53
REMARK 500 GLU A 92 -128.40 54.98
REMARK 500 ARG A 135 -95.69 -89.92
REMARK 500 ASP A 151 -127.81 -141.63
REMARK 500 THR A 204 53.29 -144.03
REMARK 500 ASP B 61 107.33 -160.49
REMARK 500 GLU B 62 32.72 -167.70
REMARK 500 LYS B 63 49.51 85.26
REMARK 500 CYS B 73 57.38 -155.29
REMARK 500 ASN B 74 49.44 -96.32
REMARK 500 ASN B 81 69.99 -153.82
REMARK 500 LYS B 133 56.12 -142.93
REMARK 500 ASP B 151 -141.79 -133.06
REMARK 500 ILE B 159 -62.03 -104.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2031 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH A2036 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH B2031 DISTANCE = 6.02 ANGSTROMS
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE POL B 1205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE POL A 1210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE POL A 1211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE POL A 1212
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE POL B 1206
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WO3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE EPHA4-EPHRINA2 COMPLEX
REMARK 900 RELATED ID: 2WO2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE EPHA4-EPHRINB2 COMPLEX
DBREF 2WO1 A 30 202 UNP P54764 EPHA4_HUMAN 30 202
DBREF 2WO1 B 30 202 UNP P54764 EPHA4_HUMAN 30 202
SEQADV 2WO1 GLU A 27 UNP P54764 EXPRESSION TAG
SEQADV 2WO1 THR A 28 UNP P54764 EXPRESSION TAG
SEQADV 2WO1 GLY A 29 UNP P54764 EXPRESSION TAG
SEQADV 2WO1 ARG A 203 UNP P54764 EXPRESSION TAG
SEQADV 2WO1 THR A 204 UNP P54764 EXPRESSION TAG
SEQADV 2WO1 LYS A 205 UNP P54764 EXPRESSION TAG
SEQADV 2WO1 HIS A 206 UNP P54764 EXPRESSION TAG
SEQADV 2WO1 HIS A 207 UNP P54764 EXPRESSION TAG
SEQADV 2WO1 HIS A 208 UNP P54764 EXPRESSION TAG
SEQADV 2WO1 HIS A 209 UNP P54764 EXPRESSION TAG
SEQADV 2WO1 HIS A 210 UNP P54764 EXPRESSION TAG
SEQADV 2WO1 HIS A 211 UNP P54764 EXPRESSION TAG
SEQADV 2WO1 GLU B 27 UNP P54764 EXPRESSION TAG
SEQADV 2WO1 THR B 28 UNP P54764 EXPRESSION TAG
SEQADV 2WO1 GLY B 29 UNP P54764 EXPRESSION TAG
SEQADV 2WO1 ARG B 203 UNP P54764 EXPRESSION TAG
SEQADV 2WO1 THR B 204 UNP P54764 EXPRESSION TAG
SEQADV 2WO1 LYS B 205 UNP P54764 EXPRESSION TAG
SEQADV 2WO1 HIS B 206 UNP P54764 EXPRESSION TAG
SEQADV 2WO1 HIS B 207 UNP P54764 EXPRESSION TAG
SEQADV 2WO1 HIS B 208 UNP P54764 EXPRESSION TAG
SEQADV 2WO1 HIS B 209 UNP P54764 EXPRESSION TAG
SEQADV 2WO1 HIS B 210 UNP P54764 EXPRESSION TAG
SEQADV 2WO1 HIS B 211 UNP P54764 EXPRESSION TAG
SEQRES 1 A 185 GLU THR GLY GLU VAL THR LEU LEU ASP SER ARG SER VAL
SEQRES 2 A 185 GLN GLY GLU LEU GLY TRP ILE ALA SER PRO LEU GLU GLY
SEQRES 3 A 185 GLY TRP GLU GLU VAL SER ILE MET ASP GLU LYS ASN THR
SEQRES 4 A 185 PRO ILE ARG THR TYR GLN VAL CYS ASN VAL MET GLU PRO
SEQRES 5 A 185 SER GLN ASN ASN TRP LEU ARG THR ASP TRP ILE THR ARG
SEQRES 6 A 185 GLU GLY ALA GLN ARG VAL TYR ILE GLU ILE LYS PHE THR
SEQRES 7 A 185 LEU ARG ASP CYS ASN SER LEU PRO GLY VAL MET GLY THR
SEQRES 8 A 185 CYS LYS GLU THR PHE ASN LEU TYR TYR TYR GLU SER ASP
SEQRES 9 A 185 ASN ASP LYS GLU ARG PHE ILE ARG GLU ASN GLN PHE VAL
SEQRES 10 A 185 LYS ILE ASP THR ILE ALA ALA ASP GLU SER PHE THR GLN
SEQRES 11 A 185 VAL ASP ILE GLY ASP ARG ILE MET LYS LEU ASN THR GLU
SEQRES 12 A 185 ILE ARG ASP VAL GLY PRO LEU SER LYS LYS GLY PHE TYR
SEQRES 13 A 185 LEU ALA PHE GLN ASP VAL GLY ALA CYS ILE ALA LEU VAL
SEQRES 14 A 185 SER VAL ARG VAL PHE TYR LYS ARG THR LYS HIS HIS HIS
SEQRES 15 A 185 HIS HIS HIS
SEQRES 1 B 185 GLU THR GLY GLU VAL THR LEU LEU ASP SER ARG SER VAL
SEQRES 2 B 185 GLN GLY GLU LEU GLY TRP ILE ALA SER PRO LEU GLU GLY
SEQRES 3 B 185 GLY TRP GLU GLU VAL SER ILE MET ASP GLU LYS ASN THR
SEQRES 4 B 185 PRO ILE ARG THR TYR GLN VAL CYS ASN VAL MET GLU PRO
SEQRES 5 B 185 SER GLN ASN ASN TRP LEU ARG THR ASP TRP ILE THR ARG
SEQRES 6 B 185 GLU GLY ALA GLN ARG VAL TYR ILE GLU ILE LYS PHE THR
SEQRES 7 B 185 LEU ARG ASP CYS ASN SER LEU PRO GLY VAL MET GLY THR
SEQRES 8 B 185 CYS LYS GLU THR PHE ASN LEU TYR TYR TYR GLU SER ASP
SEQRES 9 B 185 ASN ASP LYS GLU ARG PHE ILE ARG GLU ASN GLN PHE VAL
SEQRES 10 B 185 LYS ILE ASP THR ILE ALA ALA ASP GLU SER PHE THR GLN
SEQRES 11 B 185 VAL ASP ILE GLY ASP ARG ILE MET LYS LEU ASN THR GLU
SEQRES 12 B 185 ILE ARG ASP VAL GLY PRO LEU SER LYS LYS GLY PHE TYR
SEQRES 13 B 185 LEU ALA PHE GLN ASP VAL GLY ALA CYS ILE ALA LEU VAL
SEQRES 14 B 185 SER VAL ARG VAL PHE TYR LYS ARG THR LYS HIS HIS HIS
SEQRES 15 B 185 HIS HIS HIS
HET POL A1210 4
HET POL A1211 4
HET POL A1212 4
HET POL B1205 4
HET POL B1206 4
HETNAM POL N-PROPANOL
HETSYN POL 1-PROPONOL
FORMUL 3 POL 5(C3 H8 O)
FORMUL 8 HOH *297(H2 O)
HELIX 1 1 ARG A 37 VAL A 39 5 3
HELIX 2 2 ASP A 107 LEU A 111 5 5
HELIX 3 3 ARG A 138 PHE A 142 5 5
HELIX 4 4 ARG B 37 VAL B 39 5 3
HELIX 5 5 ASP B 107 LEU B 111 5 5
HELIX 6 6 ARG B 138 PHE B 142 5 5
SHEET 1 AA 4 VAL A 31 ASP A 35 0
SHEET 2 AA 4 CYS A 191 TYR A 201 -1 O VAL A 199 N LEU A 33
SHEET 3 AA 4 THR A 65 CYS A 73 -1 O TYR A 70 N LEU A 194
SHEET 4 AA 4 GLU A 55 ASP A 61 -1 O GLU A 55 N GLN A 71
SHEET 1 AB 2 VAL A 31 ASP A 35 0
SHEET 2 AB 2 CYS A 191 TYR A 201 -1 O VAL A 199 N LEU A 33
SHEET 1 AC 5 ILE A 46 SER A 48 0
SHEET 2 AC 5 ASN A 82 ARG A 85 -1 O TRP A 83 N SER A 48
SHEET 3 AC 5 TYR A 182 ASP A 187 -1 O PHE A 185 N LEU A 84
SHEET 4 AC 5 THR A 121 TYR A 127 -1 O ASN A 123 N GLN A 186
SHEET 5 AC 5 VAL A 143 ALA A 149 -1 O VAL A 143 N TYR A 126
SHEET 1 BA 4 VAL B 31 ASP B 35 0
SHEET 2 BA 4 CYS B 191 TYR B 201 -1 O VAL B 199 N LEU B 33
SHEET 3 BA 4 PRO B 66 CYS B 73 -1 O TYR B 70 N LEU B 194
SHEET 4 BA 4 GLU B 55 MET B 60 -1 O GLU B 55 N GLN B 71
SHEET 1 BB 2 VAL B 31 ASP B 35 0
SHEET 2 BB 2 CYS B 191 TYR B 201 -1 O VAL B 199 N LEU B 33
SHEET 1 BC 5 ILE B 46 SER B 48 0
SHEET 2 BC 5 ASN B 82 ARG B 85 -1 O TRP B 83 N SER B 48
SHEET 3 BC 5 TYR B 182 ASP B 187 -1 O PHE B 185 N LEU B 84
SHEET 4 BC 5 THR B 121 TYR B 127 -1 O ASN B 123 N GLN B 186
SHEET 5 BC 5 VAL B 143 ALA B 149 -1 O VAL B 143 N TYR B 126
SSBOND 1 CYS A 73 CYS A 191 1555 1555 2.08
SSBOND 2 CYS A 108 CYS A 118 1555 1555 2.03
SSBOND 3 CYS B 73 CYS B 191 1555 1555 2.07
SSBOND 4 CYS B 108 CYS B 118 1555 1555 2.06
CISPEP 1 SER A 48 PRO A 49 0 1.91
CISPEP 2 SER A 48 PRO A 49 0 2.06
CISPEP 3 GLY A 174 PRO A 175 0 2.34
CISPEP 4 SER B 48 PRO B 49 0 1.53
CISPEP 5 GLY B 174 PRO B 175 0 0.95
SITE 1 AC1 2 CYS B 73 HOH B2143
SITE 1 AC2 4 SER A 36 ARG A 37 LEU A 194 VAL A 195
SITE 1 AC3 5 TRP A 88 THR A 90 LYS A 179 HOH A2153
SITE 2 AC3 5 HOH B2101
SITE 1 AC4 6 ASP A 35 ARG A 37 GLU A 100 LYS A 102
SITE 2 AC4 6 SER A 196 ARG A 198
SITE 1 AC5 4 ARG B 96 TYR B 98 TYR B 201 LYS B 202
CRYST1 48.736 73.228 54.420 90.00 98.35 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 0.020519 0.000000 0.003012 0.00000
SCALE2 0.000000 0.013656 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018572 0.00000
(ATOM LINES ARE NOT SHOWN.)
END