HEADER CELL ADHESION 31-JUL-08 2VZC
TITLE CRYSTAL STRUCTURE OF THE C-TERMINAL CALPONIN HOMOLOGY DOMAIN OF ALPHA
TITLE 2 PARVIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-PARVIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: C-TERMINAL CALPONIN HOMOLOGY DOMAIN, RESIDUES 242-372;
COMPND 5 SYNONYM: CALPONIN-LIKE INTEGRIN-LINKED KINASE-BINDING PROTEIN, CH-
COMPND 6 ILKBP, MATRIX-REMODELING-ASSOCIATED PROTEIN 2, ACTOPAXIN;
COMPND 7 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: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX-6P1
KEYWDS MEMBRANE, CYTOPLASM, CYTOSKELETON, CELL JUNCTION, ALTERNATIVE
KEYWDS 2 SPLICING, CALPONIN HOMOLOGY DOMAIN, ACTIN-BINDING, CELL MEMBRANE,
KEYWDS 3 CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LORENZ,I.VAKONAKIS,E.D.LOWE,I.D.CAMPBELL,M.E.M.NOBLE,M.K.HOELLERER
REVDAT 4 13-DEC-23 2VZC 1 REMARK
REVDAT 3 28-MAR-12 2VZC 1 JRNL REMARK VERSN HETSYN
REVDAT 3 2 1 FORMUL
REVDAT 2 24-FEB-09 2VZC 1 VERSN
REVDAT 1 28-OCT-08 2VZC 0
JRNL AUTH S.LORENZ,I.VAKONAKIS,E.D.LOWE,I.D.CAMPBELL,M.E.M.NOBLE,
JRNL AUTH 2 M.K.HOELLERER
JRNL TITL STRUCTURAL ANALYSIS OF THE INTERACTIONS BETWEEN PAXILLIN LD
JRNL TITL 2 MOTIFS AND ALPHA-PARVIN
JRNL REF STRUCTURE V. 16 1521 2008
JRNL REFN ISSN 0969-2126
JRNL PMID 18940607
JRNL DOI 10.1016/J.STR.2008.08.007
REMARK 2
REMARK 2 RESOLUTION. 1.05 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) : 1.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.5
REMARK 3 NUMBER OF REFLECTIONS : 118544
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) : 0.144
REMARK 3 R VALUE (WORKING SET) : 0.143
REMARK 3 FREE R VALUE : 0.159
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6274
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) : 1.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6271
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2800
REMARK 3 BIN FREE R VALUE SET COUNT : 320
REMARK 3 BIN FREE R VALUE : 0.2990
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2069
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 279
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 9.28
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.09000
REMARK 3 B22 (A**2) : -0.87000
REMARK 3 B33 (A**2) : -0.07000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.43000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.029
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.028
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.018
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.805
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.974
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.970
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2927 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2038 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4047 ; 1.690 ; 2.009
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5050 ; 1.041 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 393 ; 5.319 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 130 ;36.608 ;24.615
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 562 ;12.363 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;15.908 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 441 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3442 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 604 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 754 ; 0.261 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2155 ; 0.195 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1530 ; 0.190 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1365 ; 0.090 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 216 ; 0.192 ; 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): 14 ; 0.241 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 61 ; 0.244 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 26 ; 0.192 ; 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): 2310 ; 1.655 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2944 ; 2.058 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1359 ; 2.946 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1101 ; 3.605 ; 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 : 1.40
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 2VZC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-JUL-08.
REMARK 100 THE DEPOSITION ID IS D_1290037076.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-NOV-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 : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 124910
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.050
REMARK 200 RESOLUTION RANGE LOW (A) : 23.740
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.46000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
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 ENTRIES 1WKU, 1TJT, 2EYI, 1MB8
REMARK 200
REMARK 200 REMARK: MOLECULAR REPLACEMENT WITH ENSEMBLE OF CH1 DOMAINS FROM
REMARK 200 PDB ENTRIES 1WKU, 1TJT, 2EYI AND 1MB8
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% (W/V) PEG 8000, 35% (V/V) MPD,
REMARK 280 0.1M HEPES PH 7.5
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 35.59850
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 SER A 242
REMARK 465 GLY A 243
REMARK 465 ARG A 244
REMARK 465 HIS A 245
REMARK 465 SER B 242
REMARK 465 GLY B 243
REMARK 465 ARG B 244
REMARK 465 HIS B 245
REMARK 465 GLU B 246
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 NZ LYS B 265 O HOH B 2011 1.65
REMARK 500 NH2 ARG A 247 O HOH A 2002 1.79
REMARK 500 NH2 ARG A 247 OD2 ASP A 255 1.89
REMARK 500 NZ LYS A 260 O HOH A 2012 2.00
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 345 NE - CZ - NH2 ANGL. DEV. = -3.2 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 GLU A 340 151.10 -48.09
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 MRD B 1373
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 1374
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 1373
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1374
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VZD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE C-TERMINAL CALPONIN HOMOLOGY DOMAIN OF
REMARK 900 ALPHA PARVIN IN COMPLEX WITH PAXILLIN LD1 MOTIF
REMARK 900 RELATED ID: 2VZI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE C-TERMINAL CALPONIN HOMOLOGY DOMAIN OF
REMARK 900 ALPHA-PARVIN IN COMPLEX WITH PAXILLIN LD4 MOTIF
REMARK 900 RELATED ID: 2VZG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE C-TERMINAL CALPONIN HOMOLOGY DOMAIN OF
REMARK 900 ALPHA-PARVIN IN COMPLEX WITH PAXILLIN LD2 MOTIF
DBREF 2VZC A 242 372 UNP Q9NVD7 PARVA_HUMAN 242 372
DBREF 2VZC B 242 372 UNP Q9NVD7 PARVA_HUMAN 242 372
SEQRES 1 A 131 SER GLY ARG HIS GLU ARG ASP ALA PHE ASP THR LEU PHE
SEQRES 2 A 131 ASP HIS ALA PRO ASP LYS LEU ASN VAL VAL LYS LYS THR
SEQRES 3 A 131 LEU ILE THR PHE VAL ASN LYS HIS LEU ASN LYS LEU ASN
SEQRES 4 A 131 LEU GLU VAL THR GLU LEU GLU THR GLN PHE ALA ASP GLY
SEQRES 5 A 131 VAL TYR LEU VAL LEU LEU MET GLY LEU LEU GLU GLY TYR
SEQRES 6 A 131 PHE VAL PRO LEU HIS SER PHE PHE LEU THR PRO ASP SER
SEQRES 7 A 131 PHE GLU GLN LYS VAL LEU ASN VAL SER PHE ALA PHE GLU
SEQRES 8 A 131 LEU MET GLN ASP GLY GLY LEU GLU LYS PRO LYS PRO ARG
SEQRES 9 A 131 PRO GLU ASP ILE VAL ASN CYS ASP LEU LYS SER THR LEU
SEQRES 10 A 131 ARG VAL LEU TYR ASN LEU PHE THR LYS TYR ARG ASN VAL
SEQRES 11 A 131 GLU
SEQRES 1 B 131 SER GLY ARG HIS GLU ARG ASP ALA PHE ASP THR LEU PHE
SEQRES 2 B 131 ASP HIS ALA PRO ASP LYS LEU ASN VAL VAL LYS LYS THR
SEQRES 3 B 131 LEU ILE THR PHE VAL ASN LYS HIS LEU ASN LYS LEU ASN
SEQRES 4 B 131 LEU GLU VAL THR GLU LEU GLU THR GLN PHE ALA ASP GLY
SEQRES 5 B 131 VAL TYR LEU VAL LEU LEU MET GLY LEU LEU GLU GLY TYR
SEQRES 6 B 131 PHE VAL PRO LEU HIS SER PHE PHE LEU THR PRO ASP SER
SEQRES 7 B 131 PHE GLU GLN LYS VAL LEU ASN VAL SER PHE ALA PHE GLU
SEQRES 8 B 131 LEU MET GLN ASP GLY GLY LEU GLU LYS PRO LYS PRO ARG
SEQRES 9 B 131 PRO GLU ASP ILE VAL ASN CYS ASP LEU LYS SER THR LEU
SEQRES 10 B 131 ARG VAL LEU TYR ASN LEU PHE THR LYS TYR ARG ASN VAL
SEQRES 11 B 131 GLU
HET TRS A1373 8
HET GOL A1374 6
HET MRD B1373 8
HET MPD B1374 8
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM GOL GLYCEROL
HETNAM MRD (4R)-2-METHYLPENTANE-2,4-DIOL
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETSYN TRS TRIS BUFFER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 TRS C4 H12 N O3 1+
FORMUL 4 GOL C3 H8 O3
FORMUL 5 MRD C6 H14 O2
FORMUL 6 MPD C6 H14 O2
FORMUL 7 HOH *279(H2 O)
HELIX 1 1 ASP A 248 ALA A 257 1 10
HELIX 2 2 ALA A 257 ASN A 277 1 21
HELIX 3 3 LYS A 278 ASN A 280 5 3
HELIX 4 4 GLY A 293 GLU A 304 1 12
HELIX 5 5 SER A 319 GLY A 337 1 19
HELIX 6 6 ARG A 345 ASN A 351 1 7
HELIX 7 7 ASP A 353 ARG A 369 1 17
HELIX 8 8 ASP B 248 ALA B 257 1 10
HELIX 9 9 ALA B 257 ASN B 277 1 21
HELIX 10 10 LYS B 278 ASN B 280 5 3
HELIX 11 11 GLY B 293 GLY B 305 1 13
HELIX 12 12 PRO B 309 PHE B 313 5 5
HELIX 13 13 SER B 319 GLY B 337 1 19
HELIX 14 14 ARG B 345 ASN B 351 1 7
HELIX 15 15 ASP B 353 ARG B 369 1 17
SITE 1 AC1 7 GLU A 347 HOH A2104 SER B 312 PHE B 314
SITE 2 AC1 7 LEU B 325 HOH B2062 HOH B2139
SITE 1 AC2 6 SER A 312 HOH A2050 ARG B 345 GLU B 347
SITE 2 AC2 6 HOH B2110 HOH B2140
SITE 1 AC3 8 ASP A 255 HIS A 256 ASP A 318 GLN A 322
SITE 2 AC3 8 HOH A2057 HOH A2138 HOH A2139 GLU B 321
SITE 1 AC4 5 GLN A 289 ASP A 292 TYR A 295 HOH A2036
SITE 2 AC4 5 HOH A2040
CRYST1 44.144 71.197 47.146 90.00 99.88 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 0.022653 0.000000 0.003945 0.00000
SCALE2 0.000000 0.014046 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021530 0.00000
(ATOM LINES ARE NOT SHOWN.)
END