HEADER STRUCTURAL PROTEIN/CONTRACTILE PROTEIN 19-DEC-05 2FF3
TITLE CRYSTAL STRUCTURE OF GELSOLIN DOMAIN 1:N-WASP V2 MOTIF
TITLE 2 HYBRID IN COMPLEX WITH ACTIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GELSOLIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: GELSOLIN DOMAIN 1;
COMPND 5 SYNONYM: ACTIN-DEPOLYMERIZING FACTOR, ADF, BREVIN, AGEL;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: NEURAL WISKOTT-ALDRICH SYNDROME PROTEIN;
COMPND 9 CHAIN: C;
COMPND 10 FRAGMENT: N-WASP SECOND WH2 DOMAIN;
COMPND 11 SYNONYM: N-WASP;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: ACTIN, ALPHA SKELETAL MUSCLE;
COMPND 15 CHAIN: B;
COMPND 16 SYNONYM: ALPHA-ACTIN-1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 TISSUE: PLASMA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PHIS8-3;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 17 EXPRESSION_SYSTEM_PLASMID: PHIS8-3;
SOURCE 18 MOL_ID: 3;
SOURCE 19 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 20 ORGANISM_COMMON: RABBIT;
SOURCE 21 ORGANISM_TAXID: 9986;
SOURCE 22 TISSUE: SKELETAL MUSCLE
KEYWDS PROTEIN-PROTEIN COMPLEX, STRUCTURAL PROTEIN/CONTRACTILE
KEYWDS 2 PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.XUE,A.H.AGUDA,R.C.ROBINSON
REVDAT 3 24-FEB-09 2FF3 1 VERSN
REVDAT 2 28-MAR-06 2FF3 1 JRNL
REVDAT 1 21-MAR-06 2FF3 0
JRNL AUTH A.H.AGUDA,B.XUE,E.IROBI,T.PREAT,R.C.ROBINSON
JRNL TITL THE STRUCTURAL BASIS OF ACTIN INTERACTION WITH
JRNL TITL 2 MULTIPLE WH2/BETA-THYMOSIN MOTIF-CONTAINING
JRNL TITL 3 PROTEINS
JRNL REF STRUCTURE V. 14 469 2006
JRNL REFN ISSN 0969-2126
JRNL PMID 16531231
JRNL DOI 10.1016/J.STR.2005.12.011
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 54.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 45279
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) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2419
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3236
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.14
REMARK 3 BIN R VALUE (WORKING SET) : 0.2440
REMARK 3 BIN FREE R VALUE SET COUNT : 188
REMARK 3 BIN FREE R VALUE : 0.2820
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3819
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 339
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : -0.78000
REMARK 3 B33 (A**2) : 0.78000
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): 0.166
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.156
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.106
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.753
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.933
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.910
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3940 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5345 ; 1.052 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 483 ; 4.812 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 178 ;33.256 ;24.157
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 658 ;14.752 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;19.960 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 582 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2987 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1829 ; 0.180 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2641 ; 0.300 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 306 ; 0.120 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 12 ; 0.068 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 44 ; 0.196 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.160 ; 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): 2502 ; 0.799 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3885 ; 0.794 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1679 ; 1.513 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1460 ; 2.004 ; 4.500
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 : 1.20
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2FF3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-DEC-05.
REMARK 100 THE RCSB ID CODE IS RCSB035802.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-DEC-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9756
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45279
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.990
REMARK 200 RESOLUTION RANGE LOW (A) : 89.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% PEG 8000, 0.1M SODIUM ACETATE,
REMARK 280 10MM CALCIUM CHLORIDE, PH 6.5, MICROBATCH, TEMPERATURE 293.15K
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 28.49800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 89.93400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.67350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 89.93400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.49800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.67350
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 APPLY THE FOLLOWING TO CHAINS: A, C, 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 MET A 3
REMARK 465 LYS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 HIS A 11
REMARK 465 HIS A 12
REMARK 465 GLY A 13
REMARK 465 GLY A 14
REMARK 465 LEU A 15
REMARK 465 VAL A 16
REMARK 465 PRO A 17
REMARK 465 ARG A 18
REMARK 465 GLY A 19
REMARK 465 SER A 20
REMARK 465 HIS A 21
REMARK 465 GLY A 22
REMARK 465 GLY A 23
REMARK 465 SER A 24
REMARK 465 MET A 25
REMARK 465 VAL A 26
REMARK 465 VAL A 27
REMARK 465 GLN C 156
REMARK 465 GLU C 157
REMARK 465 SER C 158
REMARK 465 THR C 159
REMARK 465 PRO C 160
REMARK 465 PRO C 161
REMARK 465 THR C 162
REMARK 465 PRO C 163
REMARK 465 ALA C 164
REMARK 465 PRO C 165
REMARK 465 THR C 166
REMARK 465 SER C 167
REMARK 465 ASP B 1
REMARK 465 GLU B 2
REMARK 465 ASP B 3
REMARK 465 GLU B 4
REMARK 465 THR B 5
REMARK 465 ARG B 39
REMARK 465 HIS B 40
REMARK 465 GLN B 41
REMARK 465 GLY B 42
REMARK 465 VAL B 43
REMARK 465 MET B 44
REMARK 465 VAL B 45
REMARK 465 GLY B 46
REMARK 465 MET B 47
REMARK 465 GLY B 48
REMARK 465 GLN B 49
REMARK 465 LYS B 50
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 ASP B 154 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP B 244 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP B 288 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP B 292 CB - CG - OD2 ANGL. DEV. = 5.7 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 ASN A 80 -179.35 -66.68
REMARK 500 PHE A 125 23.00 -141.14
REMARK 500 GLU B 93 -60.38 -98.05
REMARK 500 ALA B 181 -156.53 -149.88
REMARK 500 VAL B 201 -38.68 -139.98
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 A 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 114 O
REMARK 620 2 HOH A 705 O 90.9
REMARK 620 3 HOH A 720 O 80.6 131.9
REMARK 620 4 HOH A 733 O 76.7 65.2 66.8
REMARK 620 5 ASP A 109 OD1 74.9 79.1 140.9 133.3
REMARK 620 6 ASP A 109 OD2 120.3 73.2 149.8 135.4 46.0
REMARK 620 7 ALA A 116 O 97.2 150.0 78.1 144.8 75.3 77.8
REMARK 620 8 GLU B 167 OE1 153.8 83.4 84.3 77.7 128.4 82.6 100.5
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 702 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 711 O
REMARK 620 2 ASP A 66 OD2 96.0
REMARK 620 3 GLU A 97 OE1 145.3 104.1
REMARK 620 4 GLU A 97 OE2 157.0 89.8 52.3
REMARK 620 5 VAL A 145 O 74.3 86.1 134.3 84.0
REMARK 620 6 HOH A 709 O 89.7 174.0 71.7 84.3 93.9
REMARK 620 7 GLY A 65 O 79.1 79.2 77.3 123.9 147.9 103.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 700 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 933 O
REMARK 620 2 HOH B 945 O 81.9
REMARK 620 3 ATP B 900 O3G 71.6 99.0
REMARK 620 4 ATP B 900 O2B 98.7 171.5 73.3
REMARK 620 5 HOH B 909 O 140.4 85.3 73.7 89.0
REMARK 620 6 HOH B 939 O 141.1 101.0 143.8 83.9 78.2
REMARK 620 7 HOH B 913 O 66.3 97.1 131.9 90.8 152.9 74.8
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 B 700
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 701
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 702
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 900
DBREF 2FF3 A 25 152 UNP P06396 GELS_HUMAN 52 179
DBREF 2FF3 C 153 167 UNP O00401 WASL_HUMAN 451 465
DBREF 2FF3 B 1 375 UNP P68135 ACTS_RABIT 3 377
SEQADV 2FF3 MET A 3 UNP P06396 EXPRESSION TAG
SEQADV 2FF3 LYS A 4 UNP P06396 EXPRESSION TAG
SEQADV 2FF3 HIS A 5 UNP P06396 EXPRESSION TAG
SEQADV 2FF3 HIS A 6 UNP P06396 EXPRESSION TAG
SEQADV 2FF3 HIS A 7 UNP P06396 EXPRESSION TAG
SEQADV 2FF3 HIS A 8 UNP P06396 EXPRESSION TAG
SEQADV 2FF3 HIS A 9 UNP P06396 EXPRESSION TAG
SEQADV 2FF3 HIS A 10 UNP P06396 EXPRESSION TAG
SEQADV 2FF3 HIS A 11 UNP P06396 EXPRESSION TAG
SEQADV 2FF3 HIS A 12 UNP P06396 EXPRESSION TAG
SEQADV 2FF3 GLY A 13 UNP P06396 EXPRESSION TAG
SEQADV 2FF3 GLY A 14 UNP P06396 EXPRESSION TAG
SEQADV 2FF3 LEU A 15 UNP P06396 EXPRESSION TAG
SEQADV 2FF3 VAL A 16 UNP P06396 EXPRESSION TAG
SEQADV 2FF3 PRO A 17 UNP P06396 EXPRESSION TAG
SEQADV 2FF3 ARG A 18 UNP P06396 EXPRESSION TAG
SEQADV 2FF3 GLY A 19 UNP P06396 EXPRESSION TAG
SEQADV 2FF3 SER A 20 UNP P06396 EXPRESSION TAG
SEQADV 2FF3 HIS A 21 UNP P06396 EXPRESSION TAG
SEQADV 2FF3 GLY A 22 UNP P06396 EXPRESSION TAG
SEQADV 2FF3 GLY A 23 UNP P06396 EXPRESSION TAG
SEQADV 2FF3 SER A 24 UNP P06396 EXPRESSION TAG
SEQRES 1 A 150 MET LYS HIS HIS HIS HIS HIS HIS HIS HIS GLY GLY LEU
SEQRES 2 A 150 VAL PRO ARG GLY SER HIS GLY GLY SER MET VAL VAL GLU
SEQRES 3 A 150 HIS PRO GLU PHE LEU LYS ALA GLY LYS GLU PRO GLY LEU
SEQRES 4 A 150 GLN ILE TRP ARG VAL GLU LYS PHE ASP LEU VAL PRO VAL
SEQRES 5 A 150 PRO THR ASN LEU TYR GLY ASP PHE PHE THR GLY ASP ALA
SEQRES 6 A 150 TYR VAL ILE LEU LYS THR VAL GLN LEU ARG ASN GLY ASN
SEQRES 7 A 150 LEU GLN TYR ASP LEU HIS TYR TRP LEU GLY ASN GLU CYS
SEQRES 8 A 150 SER GLN ASP GLU SER GLY ALA ALA ALA ILE PHE THR VAL
SEQRES 9 A 150 GLN LEU ASP ASP TYR LEU ASN GLY ARG ALA VAL GLN HIS
SEQRES 10 A 150 ARG GLU VAL GLN GLY PHE GLU SER ALA THR PHE LEU GLY
SEQRES 11 A 150 TYR PHE LYS SER GLY LEU LYS TYR LYS LYS GLY GLY VAL
SEQRES 12 A 150 ALA SER GLY PHE LYS HIS VAL
SEQRES 1 C 15 ALA ASP GLY GLN GLU SER THR PRO PRO THR PRO ALA PRO
SEQRES 2 C 15 THR SER
SEQRES 1 B 375 ASP GLU ASP GLU THR THR ALA LEU VAL CYS ASP ASN GLY
SEQRES 2 B 375 SER GLY LEU VAL LYS ALA GLY PHE ALA GLY ASP ASP ALA
SEQRES 3 B 375 PRO ARG ALA VAL PHE PRO SER ILE VAL GLY ARG PRO ARG
SEQRES 4 B 375 HIS GLN GLY VAL MET VAL GLY MET GLY GLN LYS ASP SER
SEQRES 5 B 375 TYR VAL GLY ASP GLU ALA GLN SER LYS ARG GLY ILE LEU
SEQRES 6 B 375 THR LEU LYS TYR PRO ILE GLU HIS GLY ILE ILE THR ASN
SEQRES 7 B 375 TRP ASP ASP MET GLU LYS ILE TRP HIS HIS THR PHE TYR
SEQRES 8 B 375 ASN GLU LEU ARG VAL ALA PRO GLU GLU HIS PRO THR LEU
SEQRES 9 B 375 LEU THR GLU ALA PRO LEU ASN PRO LYS ALA ASN ARG GLU
SEQRES 10 B 375 LYS MET THR GLN ILE MET PHE GLU THR PHE ASN VAL PRO
SEQRES 11 B 375 ALA MET TYR VAL ALA ILE GLN ALA VAL LEU SER LEU TYR
SEQRES 12 B 375 ALA SER GLY ARG THR THR GLY ILE VAL LEU ASP SER GLY
SEQRES 13 B 375 ASP GLY VAL THR HIS ASN VAL PRO ILE TYR GLU GLY TYR
SEQRES 14 B 375 ALA LEU PRO HIS ALA ILE MET ARG LEU ASP LEU ALA GLY
SEQRES 15 B 375 ARG ASP LEU THR ASP TYR LEU MET LYS ILE LEU THR GLU
SEQRES 16 B 375 ARG GLY TYR SER PHE VAL THR THR ALA GLU ARG GLU ILE
SEQRES 17 B 375 VAL ARG ASP ILE LYS GLU LYS LEU CYS TYR VAL ALA LEU
SEQRES 18 B 375 ASP PHE GLU ASN GLU MET ALA THR ALA ALA SER SER SER
SEQRES 19 B 375 SER LEU GLU LYS SER TYR GLU LEU PRO ASP GLY GLN VAL
SEQRES 20 B 375 ILE THR ILE GLY ASN GLU ARG PHE ARG CYS PRO GLU THR
SEQRES 21 B 375 LEU PHE GLN PRO SER PHE ILE GLY MET GLU SER ALA GLY
SEQRES 22 B 375 ILE HIS GLU THR THR TYR ASN SER ILE MET LYS CYS ASP
SEQRES 23 B 375 ILE ASP ILE ARG LYS ASP LEU TYR ALA ASN ASN VAL MET
SEQRES 24 B 375 SER GLY GLY THR THR MET TYR PRO GLY ILE ALA ASP ARG
SEQRES 25 B 375 MET GLN LYS GLU ILE THR ALA LEU ALA PRO SER THR MET
SEQRES 26 B 375 LYS ILE LYS ILE ILE ALA PRO PRO GLU ARG LYS TYR SER
SEQRES 27 B 375 VAL TRP ILE GLY GLY SER ILE LEU ALA SER LEU SER THR
SEQRES 28 B 375 PHE GLN GLN MET TRP ILE THR LYS GLN GLU TYR ASP GLU
SEQRES 29 B 375 ALA GLY PRO SER ILE VAL HIS ARG LYS CYS PHE
HET CA B 700 1
HET CA A 701 1
HET CA A 702 1
HET ATP B 900 31
HETNAM CA CALCIUM ION
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 4 CA 3(CA 2+)
FORMUL 7 ATP C10 H16 N5 O13 P3
FORMUL 8 HOH *339(H2 O)
HELIX 1 1 HIS A 29 ALA A 35 1 7
HELIX 2 2 PRO A 55 TYR A 59 5 5
HELIX 3 3 SER A 94 LEU A 112 1 19
HELIX 4 4 SER A 127 TYR A 133 1 7
HELIX 5 5 GLY B 55 LYS B 61 1 7
HELIX 6 6 ARG B 62 LEU B 65 5 4
HELIX 7 7 ASN B 78 ASN B 92 1 15
HELIX 8 8 ALA B 97 HIS B 101 5 5
HELIX 9 9 PRO B 112 THR B 126 1 15
HELIX 10 10 GLN B 137 SER B 145 1 9
HELIX 11 11 PRO B 172 ILE B 175 5 4
HELIX 12 12 ALA B 181 GLY B 197 1 17
HELIX 13 13 THR B 202 CYS B 217 1 16
HELIX 14 14 ASP B 222 SER B 233 1 12
HELIX 15 15 ASN B 252 THR B 260 1 9
HELIX 16 16 LEU B 261 PHE B 262 5 2
HELIX 17 17 GLN B 263 GLY B 268 5 6
HELIX 18 18 GLY B 273 LYS B 284 1 12
HELIX 19 19 CYS B 285 ASP B 288 5 4
HELIX 20 20 ILE B 289 ALA B 295 1 7
HELIX 21 21 GLY B 301 MET B 305 5 5
HELIX 22 22 GLY B 308 ALA B 321 1 14
HELIX 23 23 TYR B 337 LEU B 349 1 13
HELIX 24 24 SER B 350 GLN B 353 5 4
HELIX 25 25 LYS B 359 GLY B 366 1 8
HELIX 26 26 ILE B 369 CYS B 374 1 6
SHEET 1 A 5 ASP A 50 PRO A 53 0
SHEET 2 A 5 GLY A 40 GLU A 47 -1 N ARG A 45 O VAL A 52
SHEET 3 A 5 ALA A 67 GLN A 75 -1 O THR A 73 N GLY A 40
SHEET 4 A 5 LEU A 81 LEU A 89 -1 O HIS A 86 N ILE A 70
SHEET 5 A 5 VAL A 117 VAL A 122 1 O GLU A 121 N TYR A 87
SHEET 1 B 2 ASP A 61 PHE A 63 0
SHEET 2 B 2 LYS A 139 LYS A 141 1 O LYS A 139 N PHE A 62
SHEET 1 C 6 ALA B 29 PRO B 32 0
SHEET 2 C 6 LEU B 16 PHE B 21 -1 N ALA B 19 O ALA B 29
SHEET 3 C 6 LEU B 8 ASN B 12 -1 N ASP B 11 O LYS B 18
SHEET 4 C 6 THR B 103 GLU B 107 1 O LEU B 104 N LEU B 8
SHEET 5 C 6 ALA B 131 ILE B 136 1 O TYR B 133 N LEU B 105
SHEET 6 C 6 ILE B 357 THR B 358 -1 O ILE B 357 N MET B 132
SHEET 1 D 3 TYR B 53 VAL B 54 0
SHEET 2 D 3 VAL B 35 ARG B 37 -1 N GLY B 36 O TYR B 53
SHEET 3 D 3 THR B 66 LYS B 68 -1 O THR B 66 N ARG B 37
SHEET 1 E 2 ILE B 71 GLU B 72 0
SHEET 2 E 2 ILE B 75 ILE B 76 -1 O ILE B 75 N GLU B 72
SHEET 1 F 3 TYR B 169 ALA B 170 0
SHEET 2 F 3 THR B 160 TYR B 166 -1 N TYR B 166 O TYR B 169
SHEET 3 F 3 MET B 176 LEU B 178 -1 O LEU B 178 N THR B 160
SHEET 1 G 5 TYR B 169 ALA B 170 0
SHEET 2 G 5 THR B 160 TYR B 166 -1 N TYR B 166 O TYR B 169
SHEET 3 G 5 GLY B 150 SER B 155 -1 N VAL B 152 O VAL B 163
SHEET 4 G 5 ASN B 297 SER B 300 1 O SER B 300 N LEU B 153
SHEET 5 G 5 ILE B 329 ILE B 330 1 O ILE B 330 N ASN B 297
SHEET 1 H 2 LYS B 238 GLU B 241 0
SHEET 2 H 2 VAL B 247 ILE B 250 -1 O ILE B 250 N LYS B 238
LINK C VAL A 152 N ALA C 153 1555 1555 1.33
LINK CA CA A 701 O GLY A 114 1555 1555 2.42
LINK CA CA A 701 O HOH A 705 1555 1555 2.56
LINK CA CA A 701 O HOH A 720 1555 1555 2.39
LINK CA CA A 701 O HOH A 733 1555 1555 2.57
LINK CA CA A 701 OD1 ASP A 109 1555 1555 2.91
LINK CA CA A 701 OD2 ASP A 109 1555 1555 2.46
LINK CA CA A 701 O ALA A 116 1555 1555 2.37
LINK CA CA A 701 OE1 GLU B 167 1555 1555 2.39
LINK CA CA A 702 O HOH A 711 1555 1555 2.35
LINK CA CA A 702 OD2 ASP A 66 1555 1555 2.30
LINK CA CA A 702 OE1 GLU A 97 1555 1555 2.56
LINK CA CA A 702 OE2 GLU A 97 1555 1555 2.40
LINK CA CA A 702 O VAL A 145 1555 1555 2.36
LINK CA CA A 702 O HOH A 709 1555 1555 2.39
LINK CA CA A 702 O GLY A 65 1555 1555 2.28
LINK CA CA B 700 O HOH B 933 1555 1555 2.59
LINK CA CA B 700 O HOH B 945 1555 1555 2.45
LINK CA CA B 700 O3G ATP B 900 1555 1555 2.38
LINK CA CA B 700 O2B ATP B 900 1555 1555 2.34
LINK CA CA B 700 O HOH B 909 1555 1555 2.55
LINK CA CA B 700 O HOH B 939 1555 1555 2.49
LINK CA CA B 700 O HOH B 913 1555 1555 2.39
SITE 1 AC1 6 ATP B 900 HOH B 909 HOH B 913 HOH B 933
SITE 2 AC1 6 HOH B 939 HOH B 945
SITE 1 AC2 7 ASP A 109 GLY A 114 ALA A 116 HOH A 705
SITE 2 AC2 7 HOH A 720 HOH A 733 GLU B 167
SITE 1 AC3 6 GLY A 65 ASP A 66 GLU A 97 VAL A 145
SITE 2 AC3 6 HOH A 709 HOH A 711
SITE 1 AC4 25 GLY B 13 SER B 14 GLY B 15 LEU B 16
SITE 2 AC4 25 LYS B 18 GLY B 156 ASP B 157 GLY B 158
SITE 3 AC4 25 VAL B 159 GLY B 182 ARG B 210 LYS B 213
SITE 4 AC4 25 GLU B 214 GLY B 301 GLY B 302 THR B 303
SITE 5 AC4 25 MET B 305 TYR B 306 CA B 700 HOH B 909
SITE 6 AC4 25 HOH B 929 HOH B 932 HOH B 933 HOH B 969
SITE 7 AC4 25 HOH B 977
CRYST1 56.996 69.347 179.868 90.00 90.00 90.00 P 21 21 21 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 0.017545 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014420 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005560 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
