HEADER STRUCTURAL PROTEIN 15-MAY-01 1J72
TITLE CRYSTAL STRUCTURE OF MUTANT MACROPHAGE CAPPING PROTEIN (CAP G) WITH
TITLE 2 ACTIN-SEVERING ACTIVITY IN THE CA2+-FREE FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MACROPHAGE CAPPING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACTIN-REGULATORY PROTEIN CAP-G;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: 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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS ACTIN, HUMAN, CAPPING, CAP G, MACROPHAGE, GCAP39, MBHL, GELSOLIN,
KEYWDS 2 STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.M.VOROBIEV,F.S.SOUTHWICK,B.STOROKOPYTOV,S.C.ALMO
REVDAT 4 07-FEB-24 1J72 1 REMARK
REVDAT 3 13-JUL-11 1J72 1 VERSN
REVDAT 2 24-FEB-09 1J72 1 VERSN
REVDAT 1 24-JUN-03 1J72 0
JRNL AUTH S.M.VOROBIEV,F.S.SOUTHWICK,B.STOROKOPYTOV,S.C.ALMO
JRNL TITL CRYSTAL STRUCTURE OF MUTANT HUMAN MACROPHAGE CAPPING PROTEIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.S.SOUTHWICK
REMARK 1 TITL GAIN-OF-FUNCTION MUTATIONS CONFERRING ACTIN-SEVERING
REMARK 1 TITL 2 ACTIVITY TO HUMAN MACROPHAGE CAP G
REMARK 1 REF J.BIOL.CHEM. V. 270 45 1995
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2189205.080
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.2
REMARK 3 NUMBER OF REFLECTIONS : 22664
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 SET) : 0.243
REMARK 3 FREE R VALUE : 0.299
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.800
REMARK 3 FREE R VALUE TEST SET COUNT : 862
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 75.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2945
REMARK 3 BIN R VALUE (WORKING SET) : 0.4020
REMARK 3 BIN FREE R VALUE : 0.3990
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 107
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.039
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2506
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 82
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 65.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.60000
REMARK 3 B22 (A**2) : 5.60000
REMARK 3 B33 (A**2) : -11.20000
REMARK 3 B12 (A**2) : 5.03000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.43
REMARK 3 ESD FROM SIGMAA (A) : 0.66
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.52
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.67
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.018
REMARK 3 BOND ANGLES (DEGREES) : 2.000
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.180
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 7.170 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 10.550; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 9.450 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 12.650; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.31
REMARK 3 BSOL : 53.11
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1J72 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAY-01.
REMARK 100 THE DEPOSITION ID IS D_1000013440.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JAN-99
REMARK 200 TEMPERATURE (KELVIN) : 100.00
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X9B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24873
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 5.860
REMARK 200 R MERGE (I) : 0.09700
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) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.54
REMARK 200 R MERGE FOR SHELL (I) : 0.43100
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: MIR
REMARK 200 SOFTWARE USED: SOLVE, ROTPTF V. 6D
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL, PH 7.0-8.0, 3.5 - 4.0
REMARK 280 AMMONIUM FORMATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z+1/2
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/2
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 28.08700
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 28.08700
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 28.08700
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 28.08700
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 28.08700
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 28.08700
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 5950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
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 BIOMT1 2 0.500000 0.866025 0.000000 -103.31150
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 178.94077
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 28.08700
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 TYR A 2
REMARK 465 THR A 3
REMARK 465 ALA A 4
REMARK 465 ILE A 5
REMARK 465 PRO A 6
REMARK 465 GLN A 7
REMARK 465 SER A 8
REMARK 465 GLY A 9
REMARK 465 SER A 10
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 17 CG CD OE1 NE2
REMARK 470 ASP A 18 CG OD1 OD2
REMARK 470 LYS A 28 CG CD CE NZ
REMARK 470 LYS A 30 CG CD CE NZ
REMARK 470 GLN A 36 CG CD OE1 NE2
REMARK 470 GLU A 37 CG CD OE1 OE2
REMARK 470 GLU A 56 CG CD OE1 OE2
REMARK 470 GLU A 57 CG CD OE1 OE2
REMARK 470 GLU A 73 CG CD OE1 OE2
REMARK 470 ARG A 112 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 122 CG CD OE1 OE2
REMARK 470 GLU A 132 CG CD OE1 OE2
REMARK 470 LYS A 144 CG CD CE NZ
REMARK 470 LYS A 145 CG CD CE NZ
REMARK 470 SER A 199 OG
REMARK 470 GLU A 200 CG CD OE1 OE2
REMARK 470 ARG A 201 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 202 CG CD OE1 NE2
REMARK 470 LYS A 204 CG CD CE NZ
REMARK 470 GLN A 206 CG CD OE1 NE2
REMARK 470 GLN A 221 CG CD OE1 NE2
REMARK 470 LYS A 230 CG CD CE NZ
REMARK 470 GLU A 231 CG CD OE1 OE2
REMARK 470 ASN A 233 CG OD1 ND2
REMARK 470 GLU A 235 CG CD OE1 OE2
REMARK 470 GLU A 236 CG CD OE1 OE2
REMARK 470 ASP A 237 CG OD1 OD2
REMARK 470 LEU A 238 CG CD1 CD2
REMARK 470 THR A 239 OG1 CG2
REMARK 470 ASP A 241 CG OD1 OD2
REMARK 470 LYS A 242 CG CD CE NZ
REMARK 470 ASN A 244 CG OD1 ND2
REMARK 470 LYS A 291 CG CD CE NZ
REMARK 470 LYS A 296 CG CD CE NZ
REMARK 470 LYS A 299 CG CD CE NZ
REMARK 470 ARG A 305 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 345 CG OD1 OD2
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 O LYS A 344 N TRP A 346 1.99
REMARK 500 O LEU A 105 OG SER A 108 2.16
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 O GLY A 100 NH1 ARG A 148 12565 1.99
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 PRO A 55 C - N - CA ANGL. DEV. = 10.3 DEGREES
REMARK 500 LEU A 167 CA - CB - CG ANGL. DEV. = 17.4 DEGREES
REMARK 500 TRP A 346 C - N - CA ANGL. DEV. = -15.4 DEGREES
REMARK 500 TRP A 346 CA - CB - CG ANGL. DEV. = -18.7 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 PRO A 13 4.86 -54.19
REMARK 500 SER A 15 29.35 -74.91
REMARK 500 ASP A 18 154.28 -37.88
REMARK 500 GLU A 27 -113.59 -85.61
REMARK 500 LYS A 28 -86.44 -67.59
REMARK 500 PRO A 55 -74.00 12.71
REMARK 500 GLU A 56 20.05 -74.19
REMARK 500 GLU A 102 -167.85 -55.36
REMARK 500 LYS A 145 -76.94 -77.88
REMARK 500 ILE A 196 -80.07 -43.75
REMARK 500 ARG A 197 -60.10 -27.14
REMARK 500 ASP A 198 -94.75 -75.14
REMARK 500 SER A 199 -61.37 -29.95
REMARK 500 ARG A 201 89.84 55.05
REMARK 500 LYS A 204 100.62 -167.80
REMARK 500 ASP A 212 106.06 -42.46
REMARK 500 GLU A 214 44.21 -105.31
REMARK 500 GLU A 231 -95.90 -49.42
REMARK 500 PRO A 234 -99.80 -77.65
REMARK 500 GLU A 235 154.78 -29.87
REMARK 500 GLU A 236 78.70 -105.60
REMARK 500 LEU A 238 -151.94 -124.77
REMARK 500 ALA A 243 -107.58 -127.93
REMARK 500 ASN A 244 -54.65 -133.14
REMARK 500 ALA A 245 -93.19 -95.44
REMARK 500 GLN A 246 -124.75 -90.49
REMARK 500 ALA A 247 28.26 -178.65
REMARK 500 GLN A 259 -169.00 -115.07
REMARK 500 ASP A 267 20.58 -143.32
REMARK 500 SER A 269 -75.70 -79.80
REMARK 500 CYS A 289 53.17 -110.41
REMARK 500 LYS A 299 32.78 -96.20
REMARK 500 SER A 317 -83.00 -62.53
REMARK 500 ARG A 318 -53.58 -26.14
REMARK 500 PRO A 323 -6.76 -50.69
REMARK 500 ARG A 334 36.46 -98.22
REMARK 500 PHE A 343 -165.24 -35.92
REMARK 500 LYS A 344 -96.23 -53.48
REMARK 500 ASP A 345 4.66 -30.07
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1J72 A 1 347 UNP P40121 CAPG_HUMAN 1 348
SEQADV 1J72 GLN A 83 UNP P40121 SEE REMARK 999
SEQADV 1J72 LEU A 84 UNP P40121 SEE REMARK 999
SEQADV 1J72 ASP A 85 UNP P40121 SEE REMARK 999
SEQADV 1J72 ASP A 86 UNP P40121 SEE REMARK 999
SEQADV 1J72 TYR A 87 UNP P40121 SEE REMARK 999
SEQADV 1J72 LEU A 88 UNP P40121 SEE REMARK 999
SEQADV 1J72 GLY A 89 UNP P40121 SEE REMARK 999
SEQADV 1J72 GLY A 90 UNP P40121 SEE REMARK 999
SEQADV 1J72 GLY A 124 UNP P40121 SEE REMARK 999
SEQADV 1J72 PHE A 125 UNP P40121 SEE REMARK 999
SEQADV 1J72 LYS A 126 UNP P40121 SEE REMARK 999
SEQADV 1J72 HIS A 127 UNP P40121 SEE REMARK 999
SEQADV 1J72 VAL A 128 UNP P40121 SEE REMARK 999
SEQADV 1J72 VAL A 129 UNP P40121 SEE REMARK 999
SEQADV 1J72 PRO A 130 UNP P40121 SEE REMARK 999
SEQADV 1J72 ASN A 131 UNP P40121 SEE REMARK 999
SEQADV 1J72 GLU A 132 UNP P40121 SEE REMARK 999
SEQADV 1J72 VAL A 133 UNP P40121 SEE REMARK 999
SEQADV 1J72 VAL A 134 UNP P40121 SEE REMARK 999
SEQADV 1J72 VAL A 135 UNP P40121 SEE REMARK 999
SEQADV 1J72 GLN A 136 UNP P40121 SEE REMARK 999
SEQADV 1J72 ARG A 137 UNP P40121 SEE REMARK 999
SEQRES 1 A 347 MET TYR THR ALA ILE PRO GLN SER GLY SER PRO PHE PRO
SEQRES 2 A 347 GLY SER VAL GLN ASP PRO GLY LEU HIS VAL TRP ARG VAL
SEQRES 3 A 347 GLU LYS LEU LYS PRO VAL PRO VAL ALA GLN GLU ASN GLN
SEQRES 4 A 347 GLY VAL PHE PHE SER GLY ASP SER TYR LEU VAL LEU HIS
SEQRES 5 A 347 ASN GLY PRO GLU GLU VAL SER HIS LEU HIS LEU TRP ILE
SEQRES 6 A 347 GLY GLN GLN SER SER ARG ASP GLU GLN GLY ALA CYS ALA
SEQRES 7 A 347 VAL LEU ALA VAL GLN LEU ASP ASP TYR LEU GLY GLY ARG
SEQRES 8 A 347 PRO VAL GLN HIS ARG GLU VAL GLN GLY ASN GLU SER ASP
SEQRES 9 A 347 LEU PHE MET SER TYR PHE PRO ARG GLY LEU LYS TYR GLN
SEQRES 10 A 347 GLU GLY GLY VAL GLU SER GLY PHE LYS HIS VAL VAL PRO
SEQRES 11 A 347 ASN GLU VAL VAL VAL GLN ARG LEU TYR GLN VAL LYS GLY
SEQRES 12 A 347 LYS LYS ASN ILE ARG ALA THR GLU ARG ALA LEU ASN TRP
SEQRES 13 A 347 ASP SER PHE ASN THR GLY ASP CYS PHE ILE LEU ASP LEU
SEQRES 14 A 347 GLY GLN ASN ILE PHE ALA TRP CYS GLY GLY LYS SER ASN
SEQRES 15 A 347 ILE LEU GLU ARG ASN LYS ALA ARG ASP LEU ALA LEU ALA
SEQRES 16 A 347 ILE ARG ASP SER GLU ARG GLN GLY LYS ALA GLN VAL GLU
SEQRES 17 A 347 ILE VAL THR ASP GLY GLU GLU PRO ALA GLU MET ILE GLN
SEQRES 18 A 347 VAL LEU GLY PRO LYS PRO ALA LEU LYS GLU GLY ASN PRO
SEQRES 19 A 347 GLU GLU ASP LEU THR ALA ASP LYS ALA ASN ALA GLN ALA
SEQRES 20 A 347 ALA ALA LEU TYR LYS VAL SER ASP ALA THR GLY GLN MET
SEQRES 21 A 347 ASN LEU THR LYS VAL ALA ASP SER SER PRO PHE ALA LEU
SEQRES 22 A 347 GLU LEU LEU ILE SER ASP ASP CYS PHE VAL LEU ASP ASN
SEQRES 23 A 347 GLY LEU CYS GLY LYS ILE TYR ILE TRP LYS GLY ARG LYS
SEQRES 24 A 347 ALA ASN GLU LYS GLU ARG GLN ALA ALA LEU GLN VAL ALA
SEQRES 25 A 347 GLU GLY PHE ILE SER ARG MET GLN TYR ALA PRO ASN THR
SEQRES 26 A 347 GLN VAL GLU ILE LEU PRO GLN GLY ARG GLU SER PRO ILE
SEQRES 27 A 347 PHE LYS GLN PHE PHE LYS ASP TRP LYS
FORMUL 2 HOH *82(H2 O)
HELIX 1 1 SER A 70 LEU A 88 1 19
HELIX 2 2 SER A 103 SER A 108 1 6
HELIX 3 3 ASN A 155 PHE A 159 5 5
HELIX 4 4 ASN A 182 ASP A 198 1 17
HELIX 5 5 PRO A 216 GLY A 224 1 9
HELIX 6 6 ALA A 272 LEU A 276 5 5
HELIX 7 7 GLY A 287 CYS A 289 5 3
HELIX 8 8 ASN A 301 GLN A 320 1 20
SHEET 1 A 5 PRO A 31 PRO A 33 0
SHEET 2 A 5 GLY A 20 VAL A 26 -1 N ARG A 25 O VAL A 32
SHEET 3 A 5 SER A 47 ASN A 53 -1 O SER A 47 N VAL A 26
SHEET 4 A 5 SER A 59 ILE A 65 -1 O HIS A 60 N HIS A 52
SHEET 5 A 5 VAL A 93 VAL A 98 1 N VAL A 93 O SER A 59
SHEET 1 B 2 VAL A 41 PHE A 43 0
SHEET 2 B 2 LYS A 115 GLN A 117 1 O LYS A 115 N PHE A 42
SHEET 1 C 5 GLN A 206 THR A 211 0
SHEET 2 C 5 ASN A 172 CYS A 177 1 O ILE A 173 N GLU A 208
SHEET 3 C 5 CYS A 164 LEU A 169 -1 N PHE A 165 O TRP A 176
SHEET 4 C 5 VAL A 134 LYS A 142 -1 O ARG A 137 N ASP A 168
SHEET 5 C 5 ARG A 148 ARG A 152 -1 N ARG A 148 O LYS A 142
SHEET 1 D 9 GLN A 206 THR A 211 0
SHEET 2 D 9 ASN A 172 CYS A 177 1 O ILE A 173 N GLU A 208
SHEET 3 D 9 CYS A 164 LEU A 169 -1 N PHE A 165 O TRP A 176
SHEET 4 D 9 VAL A 134 LYS A 142 -1 O ARG A 137 N ASP A 168
SHEET 5 D 9 ASN A 261 ALA A 266 1 O LEU A 262 N GLN A 136
SHEET 6 D 9 ALA A 249 SER A 254 -1 N LEU A 250 O ALA A 266
SHEET 7 D 9 CYS A 281 ASP A 285 -1 O CYS A 281 N VAL A 253
SHEET 8 D 9 LYS A 291 LYS A 296 -1 N TYR A 293 O LEU A 284
SHEET 9 D 9 GLN A 326 PRO A 331 1 O GLN A 326 N ILE A 292
CRYST1 206.623 206.623 56.174 90.00 90.00 120.00 P 63 2 2 12
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 0.004840 0.002794 0.000000 0.00000
SCALE2 0.000000 0.005588 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017802 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
