HEADER PEPTIDE BINDING PROTEIN 01-AUG-07 2QT5
TITLE CRYSTAL STRUCTURE OF GRIP1 PDZ12 IN COMPLEX WITH THE FRAS1 PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE RECEPTOR-INTERACTING PROTEIN 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: PDZ12;
COMPND 5 SYNONYM: GRIP1 PROTEIN, AMPA RECEPTOR-INTERACTING PROTEIN GRIP1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: (ASN)(ASN)(LEU)(GLN)(ASP)(GLY)(THR)(GLU)(VAL);
COMPND 9 CHAIN: X, Y;
COMPND 10 SYNONYM: FRAS1;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 GENE: GRIP1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 MOL_ID: 2;
SOURCE 7 SYNTHETIC: YES;
SOURCE 8 OTHER_DETAILS: COMMERCIALLY SYNTHESIZED
KEYWDS PDZ-PEPTIDE COMPLEX, PDZ TANDEM, ALTERNATIVE SPLICING, CELL JUNCTION,
KEYWDS 2 CYTOPLASM, ENDOPLASMIC RETICULUM, MEMBRANE, POSTSYNAPTIC CELL
KEYWDS 3 MEMBRANE, SYNAPSE, PROTEIN BINDING, PEPTIDE BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LONG,Z.WEI,W.FENG,Y.ZHAO,M.ZHANG
REVDAT 3 13-MAR-24 2QT5 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2QT5 1 VERSN
REVDAT 1 03-JUN-08 2QT5 0
JRNL AUTH J.LONG,Z.WEI,W.FENG,C.YU,Y.X.ZHAO,M.ZHANG
JRNL TITL SUPRAMODULAR NATURE OF GRIP1 REVEALED BY THE STRUCTURE OF
JRNL TITL 2 ITS PDZ12 TANDEM IN COMPLEX WITH THE CARBOXYL TAIL OF FRAS1.
JRNL REF J.MOL.BIOL. V. 375 1457 2008
JRNL REFN ISSN 0022-2836
JRNL PMID 18155042
JRNL DOI 10.1016/J.JMB.2007.11.088
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.15
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 25976
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1344
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1747
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.46
REMARK 3 BIN R VALUE (WORKING SET) : 0.2350
REMARK 3 BIN FREE R VALUE SET COUNT : 102
REMARK 3 BIN FREE R VALUE : 0.2480
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2983
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 212
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.41000
REMARK 3 B22 (A**2) : -0.47000
REMARK 3 B33 (A**2) : 0.88000
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): 0.246
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.209
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.136
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.423
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.936
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.906
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3059 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4124 ; 1.087 ; 1.987
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 401 ; 5.685 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 126 ;37.234 ;23.810
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 560 ;14.002 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 27 ;14.585 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 484 ; 0.066 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2257 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1186 ; 0.179 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2057 ; 0.292 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 254 ; 0.127 ; 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): 33 ; 0.240 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 23 ; 0.126 ; 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): 2011 ; 1.148 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3162 ; 1.992 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1129 ; 2.607 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 957 ; 4.120 ; 6.000
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 2QT5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-AUG-07.
REMARK 100 THE DEPOSITION ID IS D_1000044022.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-FEB-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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 MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25986
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 26.157
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 8.200
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : 0.06000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.35500
REMARK 200 R SYM FOR SHELL (I) : 0.35500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER, RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MAGNESIUM ACETATE, 0.1M SODIUM
REMARK 280 CACODYLATE PH 6.5, 20% PEG 8K, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 29.55000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 63.19000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.96250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 63.19000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.55000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.96250
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, X
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, Y
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 44
REMARK 465 PRO A 45
REMARK 465 GLY A 46
REMARK 465 MET A 241
REMARK 465 ASP A 242
REMARK 465 SER A 243
REMARK 465 GLY B 44
REMARK 465 PRO B 45
REMARK 465 GLY B 46
REMARK 465 VAL B 240
REMARK 465 MET B 241
REMARK 465 ASP B 242
REMARK 465 SER B 243
REMARK 465 ASN X 1001
REMARK 465 ASN X 1002
REMARK 465 LEU X 1003
REMARK 465 GLN X 1004
REMARK 465 ASP X 1005
REMARK 465 ASN Y 2001
REMARK 465 ASN Y 2002
REMARK 465 LEU Y 2003
REMARK 465 GLN Y 2004
REMARK 465 ASP Y 2005
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 GLU A 60 -58.74 -27.96
REMARK 500 GLU B 126 -29.55 -143.93
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 EDO A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 244
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 2
DBREF 2QT5 A 48 243 UNP P97879 GRIP1_RAT 48 243
DBREF 2QT5 B 48 243 UNP P97879 GRIP1_RAT 48 243
DBREF 2QT5 X 1001 1009 PDB 2QT5 2QT5 1001 1009
DBREF 2QT5 Y 2001 2009 PDB 2QT5 2QT5 2001 2009
SEQADV 2QT5 GLY A 44 UNP P97879 EXPRESSION TAG
SEQADV 2QT5 PRO A 45 UNP P97879 EXPRESSION TAG
SEQADV 2QT5 GLY A 46 UNP P97879 EXPRESSION TAG
SEQADV 2QT5 SER A 47 UNP P97879 EXPRESSION TAG
SEQADV 2QT5 GLY B 44 UNP P97879 EXPRESSION TAG
SEQADV 2QT5 PRO B 45 UNP P97879 EXPRESSION TAG
SEQADV 2QT5 GLY B 46 UNP P97879 EXPRESSION TAG
SEQADV 2QT5 SER B 47 UNP P97879 EXPRESSION TAG
SEQRES 1 A 200 GLY PRO GLY SER PHE LYS GLY SER THR VAL VAL GLU LEU
SEQRES 2 A 200 MET LYS LYS GLU GLY THR THR LEU GLY LEU THR VAL SER
SEQRES 3 A 200 GLY GLY ILE ASP LYS ASP GLY LYS PRO ARG VAL SER ASN
SEQRES 4 A 200 LEU ARG GLN GLY GLY ILE ALA ALA ARG SER ASP GLN LEU
SEQRES 5 A 200 ASP VAL GLY ASP TYR ILE LYS ALA VAL ASN GLY ILE ASN
SEQRES 6 A 200 LEU ALA LYS PHE ARG HIS ASP GLU ILE ILE SER LEU LEU
SEQRES 7 A 200 LYS ASN VAL GLY GLU ARG VAL VAL LEU GLU VAL GLU TYR
SEQRES 8 A 200 GLU LEU PRO PRO VAL SER ILE GLN GLY SER SER VAL MET
SEQRES 9 A 200 PHE ARG THR VAL GLU VAL THR LEU HIS LYS GLU GLY ASN
SEQRES 10 A 200 THR PHE GLY PHE VAL ILE ARG GLY GLY ALA HIS ASP ASP
SEQRES 11 A 200 ARG ASN LYS SER ARG PRO VAL VAL ILE THR CYS VAL ARG
SEQRES 12 A 200 PRO GLY GLY PRO ALA ASP ARG GLU GLY THR ILE LYS PRO
SEQRES 13 A 200 GLY ASP ARG LEU LEU SER VAL ASP GLY ILE ARG LEU LEU
SEQRES 14 A 200 GLY THR THR HIS ALA GLU ALA MET SER ILE LEU LYS GLN
SEQRES 15 A 200 CYS GLY GLN GLU ALA THR LEU LEU ILE GLU TYR ASP VAL
SEQRES 16 A 200 SER VAL MET ASP SER
SEQRES 1 B 200 GLY PRO GLY SER PHE LYS GLY SER THR VAL VAL GLU LEU
SEQRES 2 B 200 MET LYS LYS GLU GLY THR THR LEU GLY LEU THR VAL SER
SEQRES 3 B 200 GLY GLY ILE ASP LYS ASP GLY LYS PRO ARG VAL SER ASN
SEQRES 4 B 200 LEU ARG GLN GLY GLY ILE ALA ALA ARG SER ASP GLN LEU
SEQRES 5 B 200 ASP VAL GLY ASP TYR ILE LYS ALA VAL ASN GLY ILE ASN
SEQRES 6 B 200 LEU ALA LYS PHE ARG HIS ASP GLU ILE ILE SER LEU LEU
SEQRES 7 B 200 LYS ASN VAL GLY GLU ARG VAL VAL LEU GLU VAL GLU TYR
SEQRES 8 B 200 GLU LEU PRO PRO VAL SER ILE GLN GLY SER SER VAL MET
SEQRES 9 B 200 PHE ARG THR VAL GLU VAL THR LEU HIS LYS GLU GLY ASN
SEQRES 10 B 200 THR PHE GLY PHE VAL ILE ARG GLY GLY ALA HIS ASP ASP
SEQRES 11 B 200 ARG ASN LYS SER ARG PRO VAL VAL ILE THR CYS VAL ARG
SEQRES 12 B 200 PRO GLY GLY PRO ALA ASP ARG GLU GLY THR ILE LYS PRO
SEQRES 13 B 200 GLY ASP ARG LEU LEU SER VAL ASP GLY ILE ARG LEU LEU
SEQRES 14 B 200 GLY THR THR HIS ALA GLU ALA MET SER ILE LEU LYS GLN
SEQRES 15 B 200 CYS GLY GLN GLU ALA THR LEU LEU ILE GLU TYR ASP VAL
SEQRES 16 B 200 SER VAL MET ASP SER
SEQRES 1 X 9 ASN ASN LEU GLN ASP GLY THR GLU VAL
SEQRES 1 Y 9 ASN ASN LEU GLN ASP GLY THR GLU VAL
HET EDO A 1 4
HET ACY A 244 4
HET ACY A 2 4
HET EDO B 2 4
HETNAM EDO 1,2-ETHANEDIOL
HETNAM ACY ACETIC ACID
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 EDO 2(C2 H6 O2)
FORMUL 6 ACY 2(C2 H4 O2)
FORMUL 9 HOH *212(H2 O)
HELIX 1 1 GLY A 87 SER A 92 1 6
HELIX 2 2 ARG A 113 ASN A 123 1 11
HELIX 3 3 GLY A 189 GLY A 195 1 7
HELIX 4 4 THR A 215 GLN A 225 1 11
HELIX 5 5 GLY B 87 SER B 92 1 6
HELIX 6 6 ARG B 113 VAL B 124 1 12
HELIX 7 7 GLY B 189 GLY B 195 1 7
HELIX 8 8 THR B 215 CYS B 226 1 12
SHEET 1 A 4 LYS A 49 MET A 57 0
SHEET 2 A 4 ARG A 127 GLU A 135 -1 O VAL A 132 N THR A 52
SHEET 3 A 4 TYR A 100 VAL A 104 -1 N TYR A 100 O GLU A 133
SHEET 4 A 4 ILE A 107 ASN A 108 -1 O ILE A 107 N VAL A 104
SHEET 1 B 3 ARG A 79 LEU A 83 0
SHEET 2 B 3 LEU A 66 SER A 69 -1 N THR A 67 O SER A 81
SHEET 3 B 3 THR X1007 VAL X1009 -1 O VAL X1009 N LEU A 66
SHEET 1 C 4 VAL A 146 HIS A 156 0
SHEET 2 C 4 GLU A 229 SER A 239 -1 O LEU A 232 N VAL A 153
SHEET 3 C 4 ARG A 202 VAL A 206 -1 N ARG A 202 O GLU A 235
SHEET 4 C 4 ILE A 209 ARG A 210 -1 O ILE A 209 N VAL A 206
SHEET 1 D 2 PHE A 164 GLY A 169 0
SHEET 2 D 2 ARG A 178 VAL A 185 -1 O VAL A 181 N ARG A 167
SHEET 1 E 4 LYS B 49 MET B 57 0
SHEET 2 E 4 ARG B 127 GLU B 135 -1 O LEU B 130 N VAL B 54
SHEET 3 E 4 TYR B 100 VAL B 104 -1 N TYR B 100 O GLU B 133
SHEET 4 E 4 ILE B 107 ASN B 108 -1 O ILE B 107 N VAL B 104
SHEET 1 F 3 ARG B 79 LEU B 83 0
SHEET 2 F 3 LEU B 66 SER B 69 -1 N THR B 67 O ASN B 82
SHEET 3 F 3 THR Y2007 VAL Y2009 -1 O VAL Y2009 N LEU B 66
SHEET 1 G 4 MET B 147 HIS B 156 0
SHEET 2 G 4 GLU B 229 VAL B 238 -1 O LEU B 232 N VAL B 153
SHEET 3 G 4 ARG B 202 VAL B 206 -1 N LEU B 204 O LEU B 233
SHEET 4 G 4 ILE B 209 ARG B 210 -1 O ILE B 209 N VAL B 206
SHEET 1 H 2 PHE B 164 GLY B 168 0
SHEET 2 H 2 VAL B 180 VAL B 185 -1 O VAL B 181 N ARG B 167
SITE 1 AC1 6 ASP A 93 PHE A 162 PHE A 164 MET A 220
SITE 2 AC1 6 HOH A 257 HOH A 312
SITE 1 AC2 6 ASP B 93 THR B 161 PHE B 162 PHE B 164
SITE 2 AC2 6 HOH B 283 HOH B 285
SITE 1 AC3 2 LYS A 49 ARG A 84
SITE 1 AC4 5 ARG A 174 ARG A 178 GLU B 152 GLU B 194
SITE 2 AC4 5 THR B 196
CRYST1 59.100 75.925 126.380 90.00 90.00 90.00 P 21 21 21 8
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 0.016920 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013171 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007913 0.00000
(ATOM LINES ARE NOT SHOWN.)
END