HEADER PROTEIN BINDING 12-NOV-09 3AAA
TITLE CRYSTAL STRUCTURE OF ACTIN CAPPING PROTEIN IN COMPLEX WITH V-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: F-ACTIN-CAPPING PROTEIN SUBUNIT ALPHA-1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CAPZ 36/32, BETA-ACTININ SUBUNIT I;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: F-ACTIN-CAPPING PROTEIN SUBUNIT BETA ISOFORMS 1 AND 2;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: CAPZ B1 AND B2, CAPZ 36/32, BETA-ACTININ SUBUNIT II;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: MYOTROPHIN;
COMPND 13 CHAIN: C;
COMPND 14 SYNONYM: PROTEIN V-1;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 GENE: CAPZA1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETDUET1;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 13 ORGANISM_COMMON: CHICKEN;
SOURCE 14 ORGANISM_TAXID: 9031;
SOURCE 15 GENE: CAPZB;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: ROSETTA2 (DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PETDUET1;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 23 ORGANISM_COMMON: HUMAN;
SOURCE 24 ORGANISM_TAXID: 9606;
SOURCE 25 GENE: MTPN;
SOURCE 26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 28 EXPRESSION_SYSTEM_STRAIN: ROSETTA2 (DE3);
SOURCE 29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 30 EXPRESSION_SYSTEM_PLASMID: PGEX6P1
KEYWDS ACTIN CAPPING PROTEIN, BARBED END CAPPING, INHIBITION, PROTEIN
KEYWDS 2 BINDING, ACTIN CAPPING, ACTIN-BINDING, CYTOSKELETON, ANK REPEAT
EXPDTA X-RAY DIFFRACTION
AUTHOR S.TAKEDA,S.MINAKATA,A.NARITA,M.KITAZAWA,T.YAMAKUNI,Y.MAEDA,Y.NITANAI
REVDAT 2 01-NOV-23 3AAA 1 REMARK SEQADV
REVDAT 1 04-AUG-10 3AAA 0
JRNL AUTH S.TAKEDA,S.MINAKATA,R.KOIKE,I.KAWAHATA,A.NARITA,M.KITAZAWA,
JRNL AUTH 2 M.OTA,T.YAMAKUNI,Y.MAEDA,Y.NITANAI
JRNL TITL TWO DISTINCT MECHANISMS FOR ACTIN CAPPING PROTEIN
JRNL TITL 2 REGULATION--STERIC AND ALLOSTERIC INHIBITION
JRNL REF PLOS BIOL. V. 8 00416 2010
JRNL REFN ISSN 1544-9173
JRNL PMID 20625546
JRNL DOI 10.1371/JOURNAL.PBIO.1000416
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 36744
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1941
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) : 2.21
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2640
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.82
REMARK 3 BIN R VALUE (WORKING SET) : 0.1770
REMARK 3 BIN FREE R VALUE SET COUNT : 139
REMARK 3 BIN FREE R VALUE : 0.2720
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5034
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 354
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.07000
REMARK 3 B22 (A**2) : 0.05000
REMARK 3 B33 (A**2) : -0.12000
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): 0.248
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.204
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.127
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.813
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5140 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6953 ; 1.419 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 631 ; 5.490 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 254 ;38.546 ;25.118
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 911 ;14.446 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;15.767 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 763 ; 0.105 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3911 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 3154 ; 0.956 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5085 ; 1.831 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1986 ; 2.773 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1868 ; 4.591 ; 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 3AAA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-NOV-09.
REMARK 100 THE DEPOSITION ID IS D_1000029008.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-NOV-07
REMARK 200 TEMPERATURE (KELVIN) : 90.0
REMARK 200 PH : 8.35
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL26B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU JUPITER 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38745
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.10
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.6200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 13.80
REMARK 200 R MERGE FOR SHELL (I) : 0.30400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.680
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1IZN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 4000, 20% ISOPROPANOL, 20MM
REMARK 280 EDTA, 0.1M TRIS-HCL, PH 8.35, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293.0K
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 35.71200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.51750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.50300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.51750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.71200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.50300
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 300 REMARK: THE ORIGOMETRIC STATE OF THE ACTIN CAPPING PROTEIN IS A
REMARK 300 HETERO DIMER COMPOSE OF SUBUNIT A (CHAIN A) AND SUBUNIT B (CHAIN B)
REMARK 300 IN VIVO AND IN VITRO.
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: 7490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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: C
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 1
REMARK 465 ALA A 2
REMARK 465 ASP A 3
REMARK 465 PHE A 4
REMARK 465 GLU A 5
REMARK 465 ASP A 6
REMARK 465 ARG A 7
REMARK 465 VAL A 8
REMARK 465 SER A 276
REMARK 465 TYR A 277
REMARK 465 LYS A 278
REMARK 465 ILE A 279
REMARK 465 GLY A 280
REMARK 465 LYS A 281
REMARK 465 GLU A 282
REMARK 465 MET A 283
REMARK 465 GLN A 284
REMARK 465 ASN A 285
REMARK 465 ALA A 286
REMARK 465 MET B 1
REMARK 465 ASN B 252
REMARK 465 GLN B 253
REMARK 465 LYS B 254
REMARK 465 TYR B 255
REMARK 465 LYS B 256
REMARK 465 GLN B 257
REMARK 465 LEU B 258
REMARK 465 GLN B 259
REMARK 465 ARG B 260
REMARK 465 GLU B 261
REMARK 465 LEU B 262
REMARK 465 SER B 263
REMARK 465 GLN B 264
REMARK 465 VAL B 265
REMARK 465 LEU B 266
REMARK 465 THR B 267
REMARK 465 GLN B 268
REMARK 465 ARG B 269
REMARK 465 GLN B 270
REMARK 465 ILE B 271
REMARK 465 TYR B 272
REMARK 465 ILE B 273
REMARK 465 GLN B 274
REMARK 465 PRO B 275
REMARK 465 ASP B 276
REMARK 465 ASN B 277
REMARK 465 GLY C -4
REMARK 465 PRO C -3
REMARK 465 LEU C -2
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 MET C 1
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 B 72 NE - CZ - NH2 ANGL. DEV. = -3.1 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 ASP A 72 -155.44 -77.58
REMARK 500 SER A 115 26.52 -60.11
REMARK 500 TYR A 199 33.24 -143.73
REMARK 500 SER A 219 -110.15 -127.19
REMARK 500 THR A 253 -58.06 -126.06
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 IPA B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA B 1002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IZN RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN APO-FORM
REMARK 900 RELATED ID: 3AA0 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEXED WITH THE 21 AA LENGTH CARMIL FRAGMENT
REMARK 900 RELATED ID: 3AA1 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEXED WITH THE 23 AA LENGTH CKIP-1 FRAGMENT
REMARK 900 RELATED ID: 3AA6 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEXED WITH THE 23 AA LENGTH CD2AP FRAGMENT
REMARK 900 RELATED ID: 3AA7 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN APO-FORM
REMARK 900 RELATED ID: 3AAE RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEXED WITH THE 32 AA LENGTH CARMIL FRAGMENT
DBREF 3AAA A 1 286 UNP P13127 CAZA1_CHICK 1 286
DBREF 3AAA B 1 277 UNP P14315 CAPZB_CHICK 1 277
DBREF 3AAA C 1 118 UNP P58546 MTPN_HUMAN 1 118
SEQADV 3AAA GLY C -4 UNP P58546 EXPRESSION TAG
SEQADV 3AAA PRO C -3 UNP P58546 EXPRESSION TAG
SEQADV 3AAA LEU C -2 UNP P58546 EXPRESSION TAG
SEQADV 3AAA GLY C -1 UNP P58546 EXPRESSION TAG
SEQADV 3AAA SER C 0 UNP P58546 EXPRESSION TAG
SEQRES 1 A 286 MET ALA ASP PHE GLU ASP ARG VAL SER ASP GLU GLU LYS
SEQRES 2 A 286 VAL ARG ILE ALA ALA LYS PHE ILE THR HIS ALA PRO PRO
SEQRES 3 A 286 GLY GLU PHE ASN GLU VAL PHE ASN ASP VAL ARG LEU LEU
SEQRES 4 A 286 LEU ASN ASN ASP ASN LEU LEU ARG GLU GLY ALA ALA HIS
SEQRES 5 A 286 ALA PHE ALA GLN TYR ASN MET ASP GLN PHE THR PRO VAL
SEQRES 6 A 286 LYS ILE GLU GLY TYR ASP ASP GLN VAL LEU ILE THR GLU
SEQRES 7 A 286 HIS GLY ASP LEU GLY ASN GLY ARG PHE LEU ASP PRO ARG
SEQRES 8 A 286 ASN LYS ILE SER PHE LYS PHE ASP HIS LEU ARG LYS GLU
SEQRES 9 A 286 ALA SER ASP PRO GLN PRO GLU ASP THR GLU SER ALA LEU
SEQRES 10 A 286 LYS GLN TRP ARG ASP ALA CYS ASP SER ALA LEU ARG ALA
SEQRES 11 A 286 TYR VAL LYS ASP HIS TYR PRO ASN GLY PHE CYS THR VAL
SEQRES 12 A 286 TYR GLY LYS SER ILE ASP GLY GLN GLN THR ILE ILE ALA
SEQRES 13 A 286 CYS ILE GLU SER HIS GLN PHE GLN PRO LYS ASN PHE TRP
SEQRES 14 A 286 ASN GLY ARG TRP ARG SER GLU TRP LYS PHE THR ILE THR
SEQRES 15 A 286 PRO PRO THR ALA GLN VAL ALA ALA VAL LEU LYS ILE GLN
SEQRES 16 A 286 VAL HIS TYR TYR GLU ASP GLY ASN VAL GLN LEU VAL SER
SEQRES 17 A 286 HIS LYS ASP ILE GLN ASP SER VAL GLN VAL SER SER ASP
SEQRES 18 A 286 VAL GLN THR ALA LYS GLU PHE ILE LYS ILE ILE GLU ASN
SEQRES 19 A 286 ALA GLU ASN GLU TYR GLN THR ALA ILE SER GLU ASN TYR
SEQRES 20 A 286 GLN THR MET SER ASP THR THR PHE LYS ALA LEU ARG ARG
SEQRES 21 A 286 GLN LEU PRO VAL THR ARG THR LYS ILE ASP TRP ASN LYS
SEQRES 22 A 286 ILE LEU SER TYR LYS ILE GLY LYS GLU MET GLN ASN ALA
SEQRES 1 B 277 MET SER ASP GLN GLN LEU ASP CYS ALA LEU ASP LEU MET
SEQRES 2 B 277 ARG ARG LEU PRO PRO GLN GLN ILE GLU LYS ASN LEU SER
SEQRES 3 B 277 ASP LEU ILE ASP LEU VAL PRO SER LEU CYS GLU ASP LEU
SEQRES 4 B 277 LEU SER SER VAL ASP GLN PRO LEU LYS ILE ALA ARG ASP
SEQRES 5 B 277 LYS VAL VAL GLY LYS ASP TYR LEU LEU CYS ASP TYR ASN
SEQRES 6 B 277 ARG ASP GLY ASP SER TYR ARG SER PRO TRP SER ASN LYS
SEQRES 7 B 277 TYR ASP PRO PRO LEU GLU ASP GLY ALA MET PRO SER ALA
SEQRES 8 B 277 ARG LEU ARG LYS LEU GLU VAL GLU ALA ASN ASN ALA PHE
SEQRES 9 B 277 ASP GLN TYR ARG ASP LEU TYR PHE GLU GLY GLY VAL SER
SEQRES 10 B 277 SER VAL TYR LEU TRP ASP LEU ASP HIS GLY PHE ALA GLY
SEQRES 11 B 277 VAL ILE LEU ILE LYS LYS ALA GLY ASP GLY SER LYS LYS
SEQRES 12 B 277 ILE LYS GLY CYS TRP ASP SER ILE HIS VAL VAL GLU VAL
SEQRES 13 B 277 GLN GLU LYS SER SER GLY ARG THR ALA HIS TYR LYS LEU
SEQRES 14 B 277 THR SER THR VAL MET LEU TRP LEU GLN THR ASN LYS THR
SEQRES 15 B 277 GLY SER GLY THR MET ASN LEU GLY GLY SER LEU THR ARG
SEQRES 16 B 277 GLN MET GLU LYS ASP GLU THR VAL SER ASP SER SER PRO
SEQRES 17 B 277 HIS ILE ALA ASN ILE GLY ARG LEU VAL GLU ASP MET GLU
SEQRES 18 B 277 ASN LYS ILE ARG SER THR LEU ASN GLU ILE TYR PHE GLY
SEQRES 19 B 277 LYS THR LYS ASP ILE VAL ASN GLY LEU ARG SER ILE ASP
SEQRES 20 B 277 ALA ILE PRO ASP ASN GLN LYS TYR LYS GLN LEU GLN ARG
SEQRES 21 B 277 GLU LEU SER GLN VAL LEU THR GLN ARG GLN ILE TYR ILE
SEQRES 22 B 277 GLN PRO ASP ASN
SEQRES 1 C 123 GLY PRO LEU GLY SER MET CYS ASP LYS GLU PHE MET TRP
SEQRES 2 C 123 ALA LEU LYS ASN GLY ASP LEU ASP GLU VAL LYS ASP TYR
SEQRES 3 C 123 VAL ALA LYS GLY GLU ASP VAL ASN ARG THR LEU GLU GLY
SEQRES 4 C 123 GLY ARG LYS PRO LEU HIS TYR ALA ALA ASP CYS GLY GLN
SEQRES 5 C 123 LEU GLU ILE LEU GLU PHE LEU LEU LEU LYS GLY ALA ASP
SEQRES 6 C 123 ILE ASN ALA PRO ASP LYS HIS HIS ILE THR PRO LEU LEU
SEQRES 7 C 123 SER ALA VAL TYR GLU GLY HIS VAL SER CYS VAL LYS LEU
SEQRES 8 C 123 LEU LEU SER LYS GLY ALA ASP LYS THR VAL LYS GLY PRO
SEQRES 9 C 123 ASP GLY LEU THR ALA PHE GLU ALA THR ASP ASN GLN ALA
SEQRES 10 C 123 ILE LYS ALA LEU LEU GLN
HET IPA B1001 4
HET IPA B1002 4
HETNAM IPA ISOPROPYL ALCOHOL
HETSYN IPA 2-PROPANOL
FORMUL 4 IPA 2(C3 H8 O)
FORMUL 6 HOH *354(H2 O)
HELIX 1 1 SER A 9 HIS A 23 1 15
HELIX 2 2 GLU A 28 ASN A 41 1 14
HELIX 3 3 ASN A 42 ALA A 50 1 9
HELIX 4 4 ALA A 51 GLN A 61 1 11
HELIX 5 5 THR A 77 HIS A 79 5 3
HELIX 6 6 LEU A 117 TYR A 136 1 20
HELIX 7 7 PRO A 165 ASN A 167 5 3
HELIX 8 8 SER A 220 THR A 253 1 34
HELIX 9 9 THR A 253 ARG A 259 1 7
HELIX 10 10 ASP A 270 LEU A 275 1 6
HELIX 11 11 SER B 2 LEU B 16 1 15
HELIX 12 12 PRO B 17 GLN B 19 5 3
HELIX 13 13 GLN B 20 ASP B 30 1 11
HELIX 14 14 VAL B 32 SER B 34 5 3
HELIX 15 15 LEU B 35 VAL B 43 1 9
HELIX 16 16 CYS B 62 TYR B 64 5 3
HELIX 17 17 SER B 90 GLU B 113 1 24
HELIX 18 18 SER B 160 GLY B 162 5 3
HELIX 19 19 PRO B 208 GLY B 234 1 27
HELIX 20 20 GLY B 234 ARG B 244 1 11
HELIX 21 21 CYS C 2 ASN C 12 1 11
HELIX 22 22 ASP C 14 LYS C 24 1 11
HELIX 23 23 LYS C 37 CYS C 45 1 9
HELIX 24 24 GLN C 47 LEU C 56 1 10
HELIX 25 25 THR C 70 GLY C 79 1 10
HELIX 26 26 HIS C 80 LYS C 90 1 11
HELIX 27 27 THR C 103 THR C 108 1 6
HELIX 28 28 ASN C 110 GLN C 118 1 9
SHEET 1 A 2 THR A 63 VAL A 65 0
SHEET 2 A 2 VAL A 74 ILE A 76 -1 O ILE A 76 N THR A 63
SHEET 1 B 4 ASP A 81 GLY A 83 0
SHEET 2 B 4 ARG A 86 ASP A 89 -1 O ARG A 86 N LEU A 82
SHEET 3 B 4 ILE A 94 ASP A 99 -1 O ILE A 94 N ASP A 89
SHEET 4 B 4 GLU A 104 PRO A 110 -1 O SER A 106 N LYS A 97
SHEET 1 C10 GLY A 139 ILE A 148 0
SHEET 2 C10 GLN A 151 GLN A 164 -1 O ILE A 155 N TYR A 144
SHEET 3 C10 TRP A 169 THR A 182 -1 O PHE A 179 N ILE A 154
SHEET 4 C10 THR A 185 TYR A 198 -1 O ALA A 189 N LYS A 178
SHEET 5 C10 ASN A 203 GLN A 217 -1 O ASP A 214 N VAL A 188
SHEET 6 C10 GLY B 185 THR B 202 -1 O ASN B 188 N VAL A 207
SHEET 7 C10 THR B 164 LYS B 181 -1 N SER B 171 O ARG B 195
SHEET 8 C10 ILE B 144 LYS B 159 -1 N GLN B 157 O HIS B 166
SHEET 9 C10 GLY B 127 GLY B 138 -1 N PHE B 128 O VAL B 156
SHEET 10 C10 VAL B 116 LEU B 124 -1 N VAL B 116 O LYS B 135
SHEET 1 D 2 ILE B 49 ARG B 51 0
SHEET 2 D 2 ASP B 58 LEU B 60 -1 O TYR B 59 N ALA B 50
SHEET 1 E 3 ARG B 66 ASP B 67 0
SHEET 2 E 3 SER B 70 ARG B 72 -1 O SER B 70 N ASP B 67
SHEET 3 E 3 TYR B 79 ASP B 80 -1 O ASP B 80 N TYR B 71
CISPEP 1 PRO A 183 PRO A 184 0 11.06
CISPEP 2 ASP B 80 PRO B 81 0 -4.44
SITE 1 AC1 5 GLN A 213 ASN B 77 PRO B 89 ALA B 91
SITE 2 AC1 5 HOH B1029
SITE 1 AC2 5 ASP A 214 VAL A 216 HOH A 288 SER B 76
SITE 2 AC2 5 LYS B 78
CRYST1 71.424 87.006 121.035 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 0.014001 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011493 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008262 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
