HEADER STRUCTURAL PROTEIN 28-MAR-07 2PBD
TITLE TERNARY COMPLEX OF PROFILIN-ACTIN WITH THE POLY-PRO-GAB DOMAIN OF
TITLE 2 VASP*
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACTIN, ALPHA SKELETAL MUSCLE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-377;
COMPND 5 SYNONYM: ALPHA-ACTIN-1;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PROFILIN-1;
COMPND 8 CHAIN: P;
COMPND 9 FRAGMENT: RESIDUES 2-140;
COMPND 10 SYNONYM: PROFILIN I;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: VASODILATOR-STIMULATED PHOSPHOPROTEIN;
COMPND 14 CHAIN: V;
COMPND 15 FRAGMENT: VASP LOADING POLY-PRO SITE AND GAB DOMAIN;
COMPND 16 SYNONYM: VASP;
COMPND 17 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 3 ORGANISM_COMMON: RABBIT;
SOURCE 4 ORGANISM_TAXID: 9986;
SOURCE 5 TISSUE: MUSCLE;
SOURCE 6 OTHER_DETAILS: GENE ACTA1, ACTA;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 ORGAN: BRAIN;
SOURCE 12 GENE: PFN1;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 17 EXPRESSION_SYSTEM_PLASMID: PET29;
SOURCE 18 MOL_ID: 3;
SOURCE 19 SYNTHETIC: YES;
SOURCE 20 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS, GENE VASP
KEYWDS TERNARY COMPLEX; PROFILIN; ACTIN; VASP; POLY-PROLINE; LOADING POLY-
KEYWDS 2 PRO SITE; GAB DOMAIN, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR F.FERRON,G.REBOWSKI,R.DOMINGUEZ
REVDAT 4 30-AUG-23 2PBD 1 REMARK SEQADV LINK
REVDAT 3 06-MAR-13 2PBD 1 REMARK VERSN
REVDAT 2 24-FEB-09 2PBD 1 VERSN
REVDAT 1 13-NOV-07 2PBD 0
JRNL AUTH F.FERRON,G.REBOWSKI,S.H.LEE,R.DOMINGUEZ
JRNL TITL STRUCTURAL BASIS FOR THE RECRUITMENT OF PROFILIN-ACTIN
JRNL TITL 2 COMPLEXES DURING FILAMENT ELONGATION BY ENA/VASP
JRNL REF EMBO J. V. 26 4597 2007
JRNL REFN ISSN 0261-4189
JRNL PMID 17914456
JRNL DOI 10.1038/SJ.EMBOJ.7601874
REMARK 2
REMARK 2 RESOLUTION. 1.50 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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.77
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 76665
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) : 0.158
REMARK 3 R VALUE (WORKING SET) : 0.156
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3855
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) : 5285
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.65
REMARK 3 BIN R VALUE (WORKING SET) : 0.1540
REMARK 3 BIN FREE R VALUE SET COUNT : 280
REMARK 3 BIN FREE R VALUE : 0.2210
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4049
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 732
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 10.87
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 10.85
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.04000
REMARK 3 B22 (A**2) : -0.08000
REMARK 3 B33 (A**2) : 0.09000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.09000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.074
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.076
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.045
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.249
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4421 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6051 ; 1.695 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 592 ; 6.447 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 182 ;34.582 ;23.956
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 777 ;13.356 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 27 ;17.353 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 678 ; 0.110 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3348 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2267 ; 0.229 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3089 ; 0.317 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 563 ; 0.200 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 4 ; 0.133 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 90 ; 0.250 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 74 ; 0.173 ; 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): 2796 ; 1.138 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4469 ; 1.737 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1819 ; 2.788 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1547 ; 4.118 ; 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 : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 9
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 5 A 32
REMARK 3 RESIDUE RANGE : A 33 A 70
REMARK 3 RESIDUE RANGE : A 71 A 130
REMARK 3 RESIDUE RANGE : A 131 A 148
REMARK 3 RESIDUE RANGE : A 149 A 181
REMARK 3 RESIDUE RANGE : A 182 A 262
REMARK 3 RESIDUE RANGE : A 263 A 274
REMARK 3 RESIDUE RANGE : A 275 A 336
REMARK 3 RESIDUE RANGE : A 337 A 375
REMARK 3 ORIGIN FOR THE GROUP (A): -1.5770 27.1260 23.0380
REMARK 3 T TENSOR
REMARK 3 T11: -0.0381 T22: 0.0033
REMARK 3 T33: -0.0428 T12: 0.0082
REMARK 3 T13: -0.0162 T23: 0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 0.2225 L22: 0.3522
REMARK 3 L33: 0.5614 L12: 0.0948
REMARK 3 L13: 0.1398 L23: 0.1081
REMARK 3 S TENSOR
REMARK 3 S11: 0.0003 S12: -0.0034 S13: -0.0487
REMARK 3 S21: 0.0277 S22: 0.0141 S23: -0.0137
REMARK 3 S31: 0.0187 S32: 0.0572 S33: -0.0144
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 5
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : P 1 P 15
REMARK 3 RESIDUE RANGE : P 16 P 38
REMARK 3 RESIDUE RANGE : P 39 P 92
REMARK 3 RESIDUE RANGE : P 93 P 116
REMARK 3 RESIDUE RANGE : P 117 P 139
REMARK 3 ORIGIN FOR THE GROUP (A): -20.8380 32.7280 -5.2230
REMARK 3 T TENSOR
REMARK 3 T11: -0.0464 T22: 0.0027
REMARK 3 T33: -0.0605 T12: 0.0043
REMARK 3 T13: -0.0161 T23: 0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 0.5568 L22: 0.7773
REMARK 3 L33: 1.1252 L12: 0.0030
REMARK 3 L13: 0.1186 L23: 0.2279
REMARK 3 S TENSOR
REMARK 3 S11: -0.0115 S12: 0.0605 S13: 0.0314
REMARK 3 S21: -0.0419 S22: 0.0017 S23: -0.0012
REMARK 3 S31: -0.0056 S32: -0.0178 S33: 0.0098
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : V 202 V 206
REMARK 3 RESIDUE RANGE : V 207 V 212
REMARK 3 RESIDUE RANGE : V 223 V 231
REMARK 3 RESIDUE RANGE : V 232 V 238
REMARK 3 ORIGIN FOR THE GROUP (A): -24.6130 23.6150 5.5150
REMARK 3 T TENSOR
REMARK 3 T11: -0.0008 T22: -0.0007
REMARK 3 T33: -0.0349 T12: -0.0009
REMARK 3 T13: -0.0147 T23: -0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 0.4587 L22: 0.1847
REMARK 3 L33: 4.2248 L12: 0.1216
REMARK 3 L13: 0.2680 L23: 0.8586
REMARK 3 S TENSOR
REMARK 3 S11: -0.0871 S12: 0.0086 S13: -0.0533
REMARK 3 S21: -0.0390 S22: -0.0889 S23: 0.0589
REMARK 3 S31: -0.0384 S32: -0.0062 S33: 0.1759
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 2PBD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-APR-07.
REMARK 100 THE DEPOSITION ID IS D_1000042189.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUN-06
REMARK 200 TEMPERATURE (KELVIN) : 200
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-BM-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.90020
REMARK 200 MONOCHROMATOR : BENT CONICAL SI-MIRROR (RH
REMARK 200 COATED)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 75393
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : 0.07100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 41.9000
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) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 7.50
REMARK 200 R MERGE FOR SHELL (I) : 0.29300
REMARK 200 R SYM FOR SHELL (I) : 0.29300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 9.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 2PAV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 150MM DL-MALIC ACID PH 7.0, 18% PEG
REMARK 280 3350, PH 7.4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 59.54700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.29450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 59.54700
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 28.29450
REMARK 290 SMTRY3 4 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, P, V
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1200 LIES ON A SPECIAL POSITION.
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 MET A -1
REMARK 465 CYS A 0
REMARK 465 ASP A 1
REMARK 465 GLU A 2
REMARK 465 ASP A 3
REMARK 465 GLU A 4
REMARK 465 GLN A 41
REMARK 465 GLY A 42
REMARK 465 VAL A 43
REMARK 465 MET A 44
REMARK 465 VAL A 45
REMARK 465 GLY A 46
REMARK 465 MET A 47
REMARK 465 GLY A 48
REMARK 465 GLN A 49
REMARK 465 LYS A 50
REMARK 465 ASP A 51
REMARK 465 GLN V 213
REMARK 465 GLY V 214
REMARK 465 PRO V 215
REMARK 465 GLY V 216
REMARK 465 GLY V 217
REMARK 465 GLY V 218
REMARK 465 GLY V 219
REMARK 465 ALA V 220
REMARK 465 GLY V 221
REMARK 465 LYS V 239
REMARK 465 GLN V 240
REMARK 465 GLU V 241
REMARK 465 GLU V 242
REMARK 465 ALA V 243
REMARK 465 SER V 244
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 CYS A 10 C O
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 NH1 ARG A 37 OD1 ASP A 81 2.15
REMARK 500 O HOH A 1106 O HOH A 1458 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD2 ASP P 80 O HOH A 1209 2555 2.15
REMARK 500 OD2 ASP P 80 O HOH A 1216 2555 2.16
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 116 NE - CZ - NH2 ANGL. DEV. = -3.6 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 ARG A 39 -45.09 104.14
REMARK 500 ASP A 179 41.66 -85.76
REMARK 500 ALA A 181 -151.10 -152.03
REMARK 500 ASP P 26 -66.80 67.58
REMARK 500 ASP P 26 -68.07 68.37
REMARK 500 SER P 29 167.32 179.48
REMARK 500 LYS P 37 -143.83 -101.84
REMARK 500 ASN P 61 28.28 -161.97
REMARK 500 ASN P 61 62.73 -161.52
REMARK 500 ASP P 80 84.44 10.42
REMARK 500 THR P 105 -163.12 -106.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLN P 79 ASP P 80 112.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP A1001 O2G
REMARK 620 2 ATP A1001 O2B 76.9
REMARK 620 3 HOH A1021 O 127.0 93.2
REMARK 620 4 HOH A1052 O 69.9 96.7 59.7
REMARK 620 5 HOH A1063 O 96.9 173.8 89.9 80.1
REMARK 620 6 HOH A1117 O 148.1 81.0 76.6 136.1 105.0
REMARK 620 7 HOH A1470 O 82.0 98.7 150.6 143.7 81.1 78.9
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PAV RELATED DB: PDB
REMARK 900 TERNARY COMPLEX OF PROFILIN ACTIN AND VASP LOADING POLY-PRO SITE
DBREF 2PBD A -1 375 UNP P68135 ACTS_RABIT 1 377
DBREF 2PBD P 1 139 UNP P07737 PROF1_HUMAN 2 140
DBREF 2PBD V 202 244 UNP P50552 VASP_HUMAN 203 245
SEQADV 2PBD HIC A 73 UNP P68135 HIS 75 MODIFIED RESIDUE
SEQRES 1 A 377 MET CYS ASP GLU ASP GLU THR THR ALA LEU VAL CYS ASP
SEQRES 2 A 377 ASN GLY SER GLY LEU VAL LYS ALA GLY PHE ALA GLY ASP
SEQRES 3 A 377 ASP ALA PRO ARG ALA VAL PHE PRO SER ILE VAL GLY ARG
SEQRES 4 A 377 PRO ARG HIS GLN GLY VAL MET VAL GLY MET GLY GLN LYS
SEQRES 5 A 377 ASP SER TYR VAL GLY ASP GLU ALA GLN SER LYS ARG GLY
SEQRES 6 A 377 ILE LEU THR LEU LYS TYR PRO ILE GLU HIC GLY ILE ILE
SEQRES 7 A 377 THR ASN TRP ASP ASP MET GLU LYS ILE TRP HIS HIS THR
SEQRES 8 A 377 PHE TYR ASN GLU LEU ARG VAL ALA PRO GLU GLU HIS PRO
SEQRES 9 A 377 THR LEU LEU THR GLU ALA PRO LEU ASN PRO LYS ALA ASN
SEQRES 10 A 377 ARG GLU LYS MET THR GLN ILE MET PHE GLU THR PHE ASN
SEQRES 11 A 377 VAL PRO ALA MET TYR VAL ALA ILE GLN ALA VAL LEU SER
SEQRES 12 A 377 LEU TYR ALA SER GLY ARG THR THR GLY ILE VAL LEU ASP
SEQRES 13 A 377 SER GLY ASP GLY VAL THR HIS ASN VAL PRO ILE TYR GLU
SEQRES 14 A 377 GLY TYR ALA LEU PRO HIS ALA ILE MET ARG LEU ASP LEU
SEQRES 15 A 377 ALA GLY ARG ASP LEU THR ASP TYR LEU MET LYS ILE LEU
SEQRES 16 A 377 THR GLU ARG GLY TYR SER PHE VAL THR THR ALA GLU ARG
SEQRES 17 A 377 GLU ILE VAL ARG ASP ILE LYS GLU LYS LEU CYS TYR VAL
SEQRES 18 A 377 ALA LEU ASP PHE GLU ASN GLU MET ALA THR ALA ALA SER
SEQRES 19 A 377 SER SER SER LEU GLU LYS SER TYR GLU LEU PRO ASP GLY
SEQRES 20 A 377 GLN VAL ILE THR ILE GLY ASN GLU ARG PHE ARG CYS PRO
SEQRES 21 A 377 GLU THR LEU PHE GLN PRO SER PHE ILE GLY MET GLU SER
SEQRES 22 A 377 ALA GLY ILE HIS GLU THR THR TYR ASN SER ILE MET LYS
SEQRES 23 A 377 CYS ASP ILE ASP ILE ARG LYS ASP LEU TYR ALA ASN ASN
SEQRES 24 A 377 VAL MET SER GLY GLY THR THR MET TYR PRO GLY ILE ALA
SEQRES 25 A 377 ASP ARG MET GLN LYS GLU ILE THR ALA LEU ALA PRO SER
SEQRES 26 A 377 THR MET LYS ILE LYS ILE ILE ALA PRO PRO GLU ARG LYS
SEQRES 27 A 377 TYR SER VAL TRP ILE GLY GLY SER ILE LEU ALA SER LEU
SEQRES 28 A 377 SER THR PHE GLN GLN MET TRP ILE THR LYS GLN GLU TYR
SEQRES 29 A 377 ASP GLU ALA GLY PRO SER ILE VAL HIS ARG LYS CYS PHE
SEQRES 1 P 139 ALA GLY TRP ASN ALA TYR ILE ASP ASN LEU MET ALA ASP
SEQRES 2 P 139 GLY THR CYS GLN ASP ALA ALA ILE VAL GLY TYR LYS ASP
SEQRES 3 P 139 SER PRO SER VAL TRP ALA ALA VAL PRO GLY LYS THR PHE
SEQRES 4 P 139 VAL ASN ILE THR PRO ALA GLU VAL GLY VAL LEU VAL GLY
SEQRES 5 P 139 LYS ASP ARG SER SER PHE TYR VAL ASN GLY LEU THR LEU
SEQRES 6 P 139 GLY GLY GLN LYS CYS SER VAL ILE ARG ASP SER LEU LEU
SEQRES 7 P 139 GLN ASP GLY GLU PHE SER MET ASP LEU ARG THR LYS SER
SEQRES 8 P 139 THR GLY GLY ALA PRO THR PHE ASN VAL THR VAL THR LYS
SEQRES 9 P 139 THR ASP LYS THR LEU VAL LEU LEU MET GLY LYS GLU GLY
SEQRES 10 P 139 VAL HIS GLY GLY LEU ILE ASN LYS LYS CYS TYR GLU MET
SEQRES 11 P 139 ALA SER HIS LEU ARG ARG SER GLN TYR
SEQRES 1 V 43 GLY PRO PRO PRO ALA PRO PRO LEU PRO ALA ALA GLN GLY
SEQRES 2 V 43 PRO GLY GLY GLY GLY ALA GLY ALA PRO GLY LEU ALA ALA
SEQRES 3 V 43 ALA ILE ALA GLY ALA LYS LEU ARG LYS VAL SER LYS GLN
SEQRES 4 V 43 GLU GLU ALA SER
MODRES 2PBD HIC A 73 HIS 4-METHYL-HISTIDINE
HET HIC A 73 11
HET CA A1002 1
HET ATP A1001 31
HETNAM HIC 4-METHYL-HISTIDINE
HETNAM CA CALCIUM ION
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 1 HIC C7 H11 N3 O2
FORMUL 4 CA CA 2+
FORMUL 5 ATP C10 H16 N5 O13 P3
FORMUL 6 HOH *732(H2 O)
HELIX 1 1 GLY A 55 LYS A 61 1 7
HELIX 2 2 ARG A 62 LEU A 65 5 4
HELIX 3 3 ASN A 78 ASN A 92 1 15
HELIX 4 4 ALA A 97 HIS A 101 5 5
HELIX 5 5 PRO A 112 THR A 126 1 15
HELIX 6 6 GLN A 137 SER A 145 1 9
HELIX 7 7 PRO A 172 ILE A 175 5 4
HELIX 8 8 ALA A 181 GLY A 197 1 17
HELIX 9 9 THR A 202 CYS A 217 1 16
HELIX 10 10 ASP A 222 ALA A 230 1 9
HELIX 11 11 ALA A 231 SER A 233 5 3
HELIX 12 12 ASN A 252 THR A 260 1 9
HELIX 13 13 LEU A 261 PHE A 262 5 2
HELIX 14 14 GLN A 263 GLY A 268 5 6
HELIX 15 15 GLY A 273 LYS A 284 1 12
HELIX 16 16 CYS A 285 ASP A 288 5 4
HELIX 17 17 ILE A 289 ALA A 295 1 7
HELIX 18 18 GLY A 301 MET A 305 5 5
HELIX 19 19 GLY A 308 ALA A 321 1 14
HELIX 20 20 PRO A 322 MET A 325 5 4
HELIX 21 21 TYR A 337 LEU A 349 1 13
HELIX 22 22 SER A 350 GLN A 353 5 4
HELIX 23 23 LYS A 359 GLY A 366 1 8
HELIX 24 24 SER A 368 CYS A 374 1 7
HELIX 25 25 TRP P 3 ALA P 12 1 10
HELIX 26 26 THR P 38 ILE P 42 5 5
HELIX 27 27 THR P 43 GLY P 52 1 10
HELIX 28 28 SER P 56 VAL P 60 5 5
HELIX 29 29 HIS P 119 SER P 137 1 19
HELIX 30 30 GLY V 224 GLY V 231 1 8
SHEET 1 A 6 ALA A 29 PRO A 32 0
SHEET 2 A 6 LEU A 16 PHE A 21 -1 N VAL A 17 O PHE A 31
SHEET 3 A 6 LEU A 8 ASN A 12 -1 N ASP A 11 O LYS A 18
SHEET 4 A 6 THR A 103 GLU A 107 1 O LEU A 104 N LEU A 8
SHEET 5 A 6 ALA A 131 ILE A 136 1 O TYR A 133 N LEU A 105
SHEET 6 A 6 ILE A 357 THR A 358 -1 O ILE A 357 N MET A 132
SHEET 1 B 3 TYR A 53 VAL A 54 0
SHEET 2 B 3 VAL A 35 ARG A 37 -1 N GLY A 36 O TYR A 53
SHEET 3 B 3 THR A 66 LYS A 68 -1 O LYS A 68 N VAL A 35
SHEET 1 C 2 ILE A 71 GLU A 72 0
SHEET 2 C 2 ILE A 75 ILE A 76 -1 O ILE A 75 N GLU A 72
SHEET 1 D 3 TYR A 169 ALA A 170 0
SHEET 2 D 3 THR A 160 TYR A 166 -1 N TYR A 166 O TYR A 169
SHEET 3 D 3 MET A 176 LEU A 178 -1 O LEU A 178 N THR A 160
SHEET 1 E 4 TYR A 169 ALA A 170 0
SHEET 2 E 4 THR A 160 TYR A 166 -1 N TYR A 166 O TYR A 169
SHEET 3 E 4 GLY A 150 SER A 155 -1 N ASP A 154 O HIS A 161
SHEET 4 E 4 ASN A 297 SER A 300 1 O VAL A 298 N ILE A 151
SHEET 1 F 2 LYS A 238 GLU A 241 0
SHEET 2 F 2 VAL A 247 ILE A 250 -1 O ILE A 250 N LYS A 238
SHEET 1 G 7 SER P 29 ALA P 33 0
SHEET 2 G 7 CYS P 16 GLY P 23 -1 N ILE P 21 O ALA P 32
SHEET 3 G 7 THR P 108 GLY P 114 -1 O LEU P 109 N VAL P 22
SHEET 4 G 7 ASN P 99 LYS P 104 -1 N ASN P 99 O GLY P 114
SHEET 5 G 7 SER P 84 THR P 89 -1 N LEU P 87 O VAL P 100
SHEET 6 G 7 GLN P 68 SER P 76 -1 N SER P 71 O ARG P 88
SHEET 7 G 7 LEU P 63 LEU P 65 -1 N LEU P 63 O CYS P 70
LINK C GLU A 72 N HIC A 73 1555 1555 1.34
LINK C HIC A 73 N GLY A 74 1555 1555 1.33
LINK O2G ATP A1001 CA CA A1002 1555 1555 2.28
LINK O2B ATP A1001 CA CA A1002 1555 1555 2.33
LINK CA CA A1002 O HOH A1021 1555 1555 2.30
LINK CA CA A1002 O HOH A1052 1555 1555 2.96
LINK CA CA A1002 O HOH A1063 1555 1555 2.25
LINK CA CA A1002 O HOH A1117 1555 1555 2.56
LINK CA CA A1002 O HOH A1470 1555 1555 2.52
CISPEP 1 PRO A 38 ARG A 39 0 25.76
CISPEP 2 VAL V 237 SER V 238 0 -2.92
SITE 1 AC1 6 ATP A1001 HOH A1021 HOH A1052 HOH A1063
SITE 2 AC1 6 HOH A1117 HOH A1470
SITE 1 AC2 31 GLY A 13 SER A 14 GLY A 15 LEU A 16
SITE 2 AC2 31 LYS A 18 GLY A 156 ASP A 157 GLY A 158
SITE 3 AC2 31 VAL A 159 GLY A 182 ARG A 210 LYS A 213
SITE 4 AC2 31 GLU A 214 GLY A 301 GLY A 302 THR A 303
SITE 5 AC2 31 MET A 305 TYR A 306 LYS A 336 CA A1002
SITE 6 AC2 31 HOH A1003 HOH A1052 HOH A1071 HOH A1086
SITE 7 AC2 31 HOH A1132 HOH A1183 HOH A1256 HOH A1375
SITE 8 AC2 31 HOH A1450 HOH A1463 HOH A1470
CRYST1 119.094 56.589 75.227 90.00 104.75 90.00 C 1 2 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 0.008397 0.000000 0.002211 0.00000
SCALE2 0.000000 0.017671 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013746 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
