HEADER MEMBRANE PROTEIN 28-JUN-07 2JIL
TITLE CRYSTAL STRUCTURE OF 2ND PDZ DOMAIN OF GLUTAMATE RECEPTOR INTERACTING
TITLE 2 PROTEIN-1 (GRIP1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE RECEPTOR INTERACTING PROTEIN-1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: PDZ DOMAIN 2, RESIDUES 149-239;
COMPND 5 SYNONYM: GRIP1 PROTEIN;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: R3-PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS ENDOPLASMIC RETICULUM, POSTSYNAPTIC MEMBRANE, MEMBRANE, MEMBRANE
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.TICKLE,J.ELKINS,A.C.W.PIKE,C.COOPER,E.SALAH,E.PAPAGRIGORIOU,F.VON
AUTHOR 2 DELFT,A.EDWARDS,C.H.ARROWSMITH,J.WEIGELT,M.SUNDSTROM,D.DOYLE
REVDAT 5 13-DEC-23 2JIL 1 REMARK
REVDAT 4 24-JAN-18 2JIL 1 JRNL
REVDAT 3 13-JUL-11 2JIL 1 VERSN
REVDAT 2 24-FEB-09 2JIL 1 VERSN
REVDAT 1 10-JUL-07 2JIL 0
JRNL AUTH J.TICKLE,J.ELKINS,A.C.W.PIKE,C.COOPER,E.SALAH,
JRNL AUTH 2 E.PAPAGRIGORIOU,F.VON DELFT,A.EDWARDS,C.H.ARROWSMITH,
JRNL AUTH 3 J.WEIGELT,M.SUNDSTROM,D.DOYLE
JRNL TITL CRYSTAL STRUCTURE OF 2ND PDZ DOMAIN OF GLUTAMATE RECEPTOR
JRNL TITL 2 INTERACTING PROTEIN-1 (GRIP1)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0037
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.22
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 24603
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.300
REMARK 3 FREE R VALUE TEST SET COUNT : 2226
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1792
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3140
REMARK 3 BIN FREE R VALUE SET COUNT : 166
REMARK 3 BIN FREE R VALUE : 0.4030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1411
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 151
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 21.03
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.94
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.89000
REMARK 3 B22 (A**2) : 0.19000
REMARK 3 B33 (A**2) : -1.08000
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): 0.087
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.090
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.069
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.642
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1487 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1020 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2004 ; 1.519 ; 1.981
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2490 ; 1.678 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 193 ; 5.920 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 58 ;29.306 ;21.724
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 259 ;13.705 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;20.649 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 242 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1635 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 295 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 306 ; 0.264 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1077 ; 0.228 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 706 ; 0.164 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 854 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 93 ; 0.156 ; 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): 39 ; 0.367 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 91 ; 0.377 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 21 ; 0.139 ; 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): 960 ; 2.646 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1552 ; 4.035 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 527 ; 6.146 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 450 ; 8.437 ;11.000
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 : 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 -1 A 243
REMARK 3 ORIGIN FOR THE GROUP (A): 10.8215 6.9709 11.5215
REMARK 3 T TENSOR
REMARK 3 T11: -0.1571 T22: -0.0509
REMARK 3 T33: -0.0958 T12: -0.0130
REMARK 3 T13: -0.0049 T23: -0.0494
REMARK 3 L TENSOR
REMARK 3 L11: 0.8740 L22: 3.9928
REMARK 3 L33: 2.6101 L12: 0.0166
REMARK 3 L13: 0.3868 L23: 0.7546
REMARK 3 S TENSOR
REMARK 3 S11: 0.0200 S12: 0.2144 S13: -0.0857
REMARK 3 S21: -0.1810 S22: -0.2518 S23: 0.2378
REMARK 3 S31: -0.1133 S32: -0.3423 S33: 0.2318
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 -1 B 243
REMARK 3 ORIGIN FOR THE GROUP (A): 35.2416 13.1015 13.0577
REMARK 3 T TENSOR
REMARK 3 T11: -0.0514 T22: -0.1381
REMARK 3 T33: -0.1490 T12: -0.0051
REMARK 3 T13: 0.0106 T23: -0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 4.3902 L22: 0.9962
REMARK 3 L33: 1.9275 L12: 0.3029
REMARK 3 L13: -0.5280 L23: -0.2298
REMARK 3 S TENSOR
REMARK 3 S11: -0.1171 S12: 0.0613 S13: -0.1948
REMARK 3 S21: -0.0728 S22: 0.1167 S23: -0.1363
REMARK 3 S31: 0.2859 S32: 0.1776 S33: 0.0004
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 2JIL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JUN-07.
REMARK 100 THE DEPOSITION ID IS D_1290033052.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAY-07
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9999
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26857
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 41.310
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.56000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
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 1N7E 1TQ3 1BE9 1MFG 2HE2 1N7F
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.20M POTASSIUM
REMARK 280 THIOCYANATE, 10% ETHYLENE GLYCOL, 0.1M BIS TRIS PROPANE PH 7.5,
REMARK 280 PH 7.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 48.19850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.19850
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 1.000000 0.000000 0.000000 28.03000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 30.52850
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 28.03000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 30.52850
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 48.19850
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 28.03000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 30.52850
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 48.19850
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 28.03000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 30.52850
REMARK 290 SMTRY3 8 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: PQS
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: PQS
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 184 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, CYS 184 TO SER
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 ASN A 175
REMARK 465 LYS A 176
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 172 CG OD1 OD2
REMARK 470 ARG A 174 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 224 CD CE NZ
REMARK 470 GLN A 228 CG CD OE1 NE2
REMARK 470 GLU B 158 OE1 OE2
REMARK 470 ASP B 172 CG OD1 OD2
REMARK 470 ASN B 175 OD1 ND2
REMARK 470 LYS B 176 CD CE NZ
REMARK 470 LYS B 224 CD CE NZ
REMARK 470 GLN B 225 CD OE1 NE2
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 LEU A 211 36.23 -96.37
REMARK 500 ASN B 160 13.26 58.45
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 SCN A1244
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A1245
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1246
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1244
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1245
DBREF 2JIL A -1 0 PDB 2JIL 2JIL -1 0
DBREF 2JIL A 149 239 UNP Q9Y3R0 GRIP1_HUMAN 149 239
DBREF 2JIL A 240 243 PDB 2JIL 2JIL 240 243
DBREF 2JIL B -1 0 PDB 2JIL 2JIL -1 0
DBREF 2JIL B 149 239 UNP Q9Y3R0 GRIP1_HUMAN 149 239
DBREF 2JIL B 240 243 PDB 2JIL 2JIL 240 243
SEQADV 2JIL SER A 184 UNP Q9Y3R0 CYS 184 ENGINEERED MUTATION
SEQADV 2JIL SER B 184 UNP Q9Y3R0 CYS 184 ENGINEERED MUTATION
SEQRES 1 A 97 SER MET ARG THR VAL GLU VAL THR LEU HIS LYS GLU GLY
SEQRES 2 A 97 ASN THR PHE GLY PHE VAL ILE ARG GLY GLY ALA HIS ASP
SEQRES 3 A 97 ASP ARG ASN LYS SER ARG PRO VAL VAL ILE THR SER VAL
SEQRES 4 A 97 ARG PRO GLY GLY PRO ALA ASP ARG GLU GLY THR ILE LYS
SEQRES 5 A 97 PRO GLY ASP ARG LEU LEU SER VAL ASP GLY ILE ARG LEU
SEQRES 6 A 97 LEU GLY THR THR HIS ALA GLU ALA MET SER ILE LEU LYS
SEQRES 7 A 97 GLN CYS GLY GLN GLU ALA ALA LEU LEU ILE GLU TYR ASP
SEQRES 8 A 97 VAL SER GLU THR ALA VAL
SEQRES 1 B 97 SER MET ARG THR VAL GLU VAL THR LEU HIS LYS GLU GLY
SEQRES 2 B 97 ASN THR PHE GLY PHE VAL ILE ARG GLY GLY ALA HIS ASP
SEQRES 3 B 97 ASP ARG ASN LYS SER ARG PRO VAL VAL ILE THR SER VAL
SEQRES 4 B 97 ARG PRO GLY GLY PRO ALA ASP ARG GLU GLY THR ILE LYS
SEQRES 5 B 97 PRO GLY ASP ARG LEU LEU SER VAL ASP GLY ILE ARG LEU
SEQRES 6 B 97 LEU GLY THR THR HIS ALA GLU ALA MET SER ILE LEU LYS
SEQRES 7 B 97 GLN CYS GLY GLN GLU ALA ALA LEU LEU ILE GLU TYR ASP
SEQRES 8 B 97 VAL SER GLU THR ALA VAL
HET SCN A1244 3
HET SCN A1245 3
HET EDO A1246 4
HET EDO B1244 4
HET EDO B1245 4
HETNAM SCN THIOCYANATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 SCN 2(C N S 1-)
FORMUL 5 EDO 3(C2 H6 O2)
FORMUL 8 HOH *151(H2 O)
HELIX 1 1 GLY A 189 GLY A 195 1 7
HELIX 2 2 THR A 215 CYS A 226 1 12
HELIX 3 3 ASP B 173 SER B 177 5 5
HELIX 4 4 GLY B 189 GLY B 195 1 7
HELIX 5 5 THR B 215 CYS B 226 1 12
SHEET 1 AA 4 MET A 0 HIS A 156 0
SHEET 2 AA 4 GLU A 229 ASP A 237 -1 O ALA A 230 N LEU A 155
SHEET 3 AA 4 ARG A 202 VAL A 206 -1 O ARG A 202 N GLU A 235
SHEET 4 AA 4 ILE A 209 ARG A 210 -1 O ILE A 209 N VAL A 206
SHEET 1 AB 3 ARG A 178 VAL A 185 0
SHEET 2 AB 3 PHE A 164 GLY A 169 -1 O VAL A 165 N THR A 183
SHEET 3 AB 3 GLU B 240 ALA B 242 -1 O THR B 241 N ILE A 166
SHEET 1 BA 4 MET B 0 HIS B 156 0
SHEET 2 BA 4 GLU B 229 ASP B 237 -1 O ALA B 230 N LEU B 155
SHEET 3 BA 4 ARG B 202 VAL B 206 -1 O ARG B 202 N GLU B 235
SHEET 4 BA 4 ILE B 209 ARG B 210 -1 O ILE B 209 N VAL B 206
SHEET 1 BB 2 PHE B 164 GLY B 169 0
SHEET 2 BB 2 ARG B 178 VAL B 185 -1 O ARG B 178 N GLY B 169
SITE 1 AC1 4 ARG A 167 GLY A 168 TYR B 236 SER B 239
SITE 1 AC2 4 TYR A 236 SER A 239 ARG B 167 GLY B 168
SITE 1 AC3 6 THR A 150 VAL A 151 VAL A 238 GLU A 240
SITE 2 AC3 6 ARG B 167 THR B 183
SITE 1 AC4 4 MET B 0 ARG B 149 THR B 150 GLU B 235
SITE 1 AC5 8 ARG A 210 LEU A 212 GLY B 163 PHE B 164
SITE 2 AC5 8 VAL B 165 SER B 184 ARG B 186 HOH B2078
CRYST1 56.060 61.057 96.397 90.00 90.00 90.00 C 2 2 21 16
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 0.017838 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016378 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010374 0.00000
MTRIX1 1 -0.083570 0.996490 -0.004910 28.96959 1
MTRIX2 1 0.995870 0.083690 0.035180 1.05976 1
MTRIX3 1 0.035460 -0.001950 -0.999370 23.91029 1
(ATOM LINES ARE NOT SHOWN.)
END
