HEADER STRUCTURAL PROTEIN 23-DEC-11 3V8O
TITLE HUMAN FILAMIN C IG - LIKE DOMAINS 4 AND 5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FILAMIN-C;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: DOMAINS 4 AND 5 (UNP RESIDUES 569-761);
COMPND 5 SYNONYM: FLN-C, FLNC, ABP-280-LIKE PROTEIN, ABP-L, ACTIN-BINDING-LIKE
COMPND 6 PROTEIN, FILAMIN-2, GAMMA-FILAMIN;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ABPL, FLN2, FLNC;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 GOLD
KEYWDS IMMUNOGLOBULIN LIKE FOLD, MUSCLE Z DISK, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.SETHI,J.YLANNE
REVDAT 4 13-SEP-23 3V8O 1 REMARK SEQADV LINK
REVDAT 3 08-OCT-14 3V8O 1 JRNL
REVDAT 2 12-FEB-14 3V8O 1 JRNL
REVDAT 1 17-JUL-13 3V8O 0
JRNL AUTH R.SETHI,J.SEPPALA,H.TOSSAVAINEN,M.YLILAURI,S.RUSKAMO,
JRNL AUTH 2 O.T.PENTIKAINEN,U.PENTIKAINEN,P.PERMI,J.YLANNE
JRNL TITL A NOVEL STRUCTURAL UNIT IN THE N-TERMINAL REGION OF
JRNL TITL 2 FILAMINS.
JRNL REF J.BIOL.CHEM. V. 289 8588 2014
JRNL REFN ISSN 0021-9258
JRNL PMID 24469451
JRNL DOI 10.1074/JBC.M113.537456
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.63
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 13602
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1512
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1012
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3340
REMARK 3 BIN FREE R VALUE SET COUNT : 113
REMARK 3 BIN FREE R VALUE : 0.4010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2854
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 47
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.52
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.80000
REMARK 3 B22 (A**2) : -2.57000
REMARK 3 B33 (A**2) : -0.23000
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): 0.701
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.342
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.221
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.288
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.921
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.880
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2929 ; 0.022 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3989 ; 1.925 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 378 ; 7.413 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 120 ;31.755 ;25.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 447 ;22.100 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;15.787 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 431 ; 0.127 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2276 ; 0.008 ; 0.022
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): 1893 ; 0.941 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3066 ; 1.839 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1036 ; 2.581 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 923 ; 4.695 ; 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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 575 A 612 2
REMARK 3 1 B 575 B 612 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 152 ; 0.05 ; 0.05
REMARK 3 MEDIUM POSITIONAL 1 A (A): 117 ; 0.06 ; 0.50
REMARK 3 TIGHT THERMAL 1 A (A**2): 152 ; 0.13 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 117 ; 0.13 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 618 A 760 2
REMARK 3 1 B 618 B 760 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 572 ; 0.09 ; 0.05
REMARK 3 MEDIUM POSITIONAL 2 A (A): 513 ; 0.15 ; 0.50
REMARK 3 TIGHT THERMAL 2 A (A**2): 572 ; 0.13 ; 0.50
REMARK 3 MEDIUM THERMAL 2 A (A**2): 513 ; 0.15 ; 2.00
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 3V8O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000069734.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-APR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.072270
REMARK 200 MONOCHROMATOR : SILICON
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15138
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 46.633
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 4.200
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) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
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: PHASER
REMARK 200 STARTING MODEL: 2NQC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M SODIUM POTASSIUM PHOSPHATE, PH 8,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 31.81000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.86000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.67500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.86000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.81000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.67500
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 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 761
REMARK 465 GLN B 568
REMARK 465 ALA B 569
REMARK 465 GLY B 570
REMARK 465 VAL B 571
REMARK 465 GLN B 572
REMARK 465 GLY B 761
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 ASP B 651 O HOH B 821 2.11
REMARK 500 OG SER B 743 O HOH B 820 2.17
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 LYS A 751 -24.44 89.65
REMARK 500 ASP B 651 -45.31 100.26
REMARK 500 ASP B 685 -2.68 80.60
REMARK 500 TRP B 744 -81.56 -122.59
REMARK 500 LYS B 751 8.15 97.43
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 K A 801 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 651 O
REMARK 620 2 PRO A 653 O 63.4
REMARK 620 3 ASP B 651 O 144.9 130.0
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 801
DBREF 3V8O A 569 761 UNP Q14315 FLNC_HUMAN 569 761
DBREF 3V8O B 569 761 UNP Q14315 FLNC_HUMAN 569 761
SEQADV 3V8O GLN A 568 UNP Q14315 EXPRESSION TAG
SEQADV 3V8O GLN B 568 UNP Q14315 EXPRESSION TAG
SEQRES 1 A 194 GLN ALA GLY VAL GLN LYS VAL ARG ALA TRP GLY PRO GLY
SEQRES 2 A 194 LEU GLU THR GLY GLN VAL GLY LYS SER ALA ASP PHE VAL
SEQRES 3 A 194 VAL GLU ALA ILE GLY THR GLU VAL GLY THR LEU GLY PHE
SEQRES 4 A 194 SER ILE GLU GLY PRO SER GLN ALA LYS ILE GLU CYS ASP
SEQRES 5 A 194 ASP LYS GLY ASP GLY SER CYS ASP VAL ARG TYR TRP PRO
SEQRES 6 A 194 THR GLU PRO GLY GLU TYR ALA VAL HIS VAL ILE CYS ASP
SEQRES 7 A 194 ASP GLU ASP ILE ARG ASP SER PRO PHE ILE ALA HIS ILE
SEQRES 8 A 194 LEU PRO ALA PRO PRO ASP CYS PHE PRO ASP LYS VAL LYS
SEQRES 9 A 194 ALA PHE GLY PRO GLY LEU GLU PRO THR GLY CYS ILE VAL
SEQRES 10 A 194 ASP LYS PRO ALA GLU PHE THR ILE ASP ALA ARG ALA ALA
SEQRES 11 A 194 GLY LYS GLY ASP LEU LYS LEU TYR ALA GLN ASP ALA ASP
SEQRES 12 A 194 GLY CYS PRO ILE ASP ILE LYS VAL ILE PRO ASN GLY ASP
SEQRES 13 A 194 GLY THR PHE ARG CYS SER TYR VAL PRO THR LYS PRO ILE
SEQRES 14 A 194 LYS HIS THR ILE ILE ILE SER TRP GLY GLY VAL ASN VAL
SEQRES 15 A 194 PRO LYS SER PRO PHE ARG VAL ASN VAL GLY GLU GLY
SEQRES 1 B 194 GLN ALA GLY VAL GLN LYS VAL ARG ALA TRP GLY PRO GLY
SEQRES 2 B 194 LEU GLU THR GLY GLN VAL GLY LYS SER ALA ASP PHE VAL
SEQRES 3 B 194 VAL GLU ALA ILE GLY THR GLU VAL GLY THR LEU GLY PHE
SEQRES 4 B 194 SER ILE GLU GLY PRO SER GLN ALA LYS ILE GLU CYS ASP
SEQRES 5 B 194 ASP LYS GLY ASP GLY SER CYS ASP VAL ARG TYR TRP PRO
SEQRES 6 B 194 THR GLU PRO GLY GLU TYR ALA VAL HIS VAL ILE CYS ASP
SEQRES 7 B 194 ASP GLU ASP ILE ARG ASP SER PRO PHE ILE ALA HIS ILE
SEQRES 8 B 194 LEU PRO ALA PRO PRO ASP CYS PHE PRO ASP LYS VAL LYS
SEQRES 9 B 194 ALA PHE GLY PRO GLY LEU GLU PRO THR GLY CYS ILE VAL
SEQRES 10 B 194 ASP LYS PRO ALA GLU PHE THR ILE ASP ALA ARG ALA ALA
SEQRES 11 B 194 GLY LYS GLY ASP LEU LYS LEU TYR ALA GLN ASP ALA ASP
SEQRES 12 B 194 GLY CYS PRO ILE ASP ILE LYS VAL ILE PRO ASN GLY ASP
SEQRES 13 B 194 GLY THR PHE ARG CYS SER TYR VAL PRO THR LYS PRO ILE
SEQRES 14 B 194 LYS HIS THR ILE ILE ILE SER TRP GLY GLY VAL ASN VAL
SEQRES 15 B 194 PRO LYS SER PRO PHE ARG VAL ASN VAL GLY GLU GLY
HET K A 801 1
HETNAM K POTASSIUM ION
FORMUL 3 K K 1+
FORMUL 4 HOH *47(H2 O)
HELIX 1 1 GLY A 578 LEU A 581 5 4
HELIX 2 2 GLU A 600 GLY A 602 5 3
HELIX 3 3 PHE A 666 VAL A 670 5 5
HELIX 4 4 GLY A 674 GLU A 678 5 5
HELIX 5 5 GLY B 578 LEU B 581 5 4
HELIX 6 6 GLU B 600 GLY B 602 5 3
HELIX 7 7 PHE B 666 VAL B 670 5 5
HELIX 8 8 GLY B 674 GLU B 678 5 5
SHEET 1 A 4 VAL A 574 TRP A 577 0
SHEET 2 A 4 ALA A 590 ALA A 596 -1 O VAL A 593 N TRP A 577
SHEET 3 A 4 SER A 625 TYR A 630 -1 O TYR A 630 N ALA A 590
SHEET 4 A 4 GLU A 617 ASP A 620 -1 N ASP A 619 O ASP A 627
SHEET 1 B 4 THR A 583 GLN A 585 0
SHEET 2 B 4 PHE A 654 LEU A 659 1 O LEU A 659 N GLY A 584
SHEET 3 B 4 GLY A 636 CYS A 644 -1 N VAL A 640 O PHE A 654
SHEET 4 B 4 LEU A 604 GLU A 609 -1 N GLU A 609 O ALA A 639
SHEET 1 C 4 THR A 583 GLN A 585 0
SHEET 2 C 4 PHE A 654 LEU A 659 1 O LEU A 659 N GLY A 584
SHEET 3 C 4 GLY A 636 CYS A 644 -1 N VAL A 640 O PHE A 654
SHEET 4 C 4 GLU A 647 ASP A 648 -1 O GLU A 647 N CYS A 644
SHEET 1 D 4 LYS A 671 PHE A 673 0
SHEET 2 D 4 ALA A 688 ASP A 693 -1 O THR A 691 N PHE A 673
SHEET 3 D 4 THR A 725 TYR A 730 -1 O TYR A 730 N ALA A 688
SHEET 4 D 4 LYS A 717 PRO A 720 -1 N ILE A 719 O ARG A 727
SHEET 1 E 4 CYS A 682 ILE A 683 0
SHEET 2 E 4 PHE A 754 GLY A 759 1 O GLY A 759 N CYS A 682
SHEET 3 E 4 LYS A 737 TRP A 744 -1 N ILE A 740 O PHE A 754
SHEET 4 E 4 LEU A 702 ASP A 708 -1 N TYR A 705 O ILE A 741
SHEET 1 F 4 CYS A 682 ILE A 683 0
SHEET 2 F 4 PHE A 754 GLY A 759 1 O GLY A 759 N CYS A 682
SHEET 3 F 4 LYS A 737 TRP A 744 -1 N ILE A 740 O PHE A 754
SHEET 4 F 4 VAL A 747 ASN A 748 -1 O VAL A 747 N TRP A 744
SHEET 1 G 4 VAL B 574 TRP B 577 0
SHEET 2 G 4 ALA B 590 ALA B 596 -1 O VAL B 593 N TRP B 577
SHEET 3 G 4 SER B 625 TYR B 630 -1 O VAL B 628 N PHE B 592
SHEET 4 G 4 ILE B 616 ASP B 620 -1 N ASP B 619 O ASP B 627
SHEET 1 H 4 THR B 583 GLN B 585 0
SHEET 2 H 4 PHE B 654 LEU B 659 1 O LEU B 659 N GLY B 584
SHEET 3 H 4 GLY B 636 CYS B 644 -1 N VAL B 640 O PHE B 654
SHEET 4 H 4 LEU B 604 GLU B 609 -1 N GLU B 609 O ALA B 639
SHEET 1 I 4 THR B 583 GLN B 585 0
SHEET 2 I 4 PHE B 654 LEU B 659 1 O LEU B 659 N GLY B 584
SHEET 3 I 4 GLY B 636 CYS B 644 -1 N VAL B 640 O PHE B 654
SHEET 4 I 4 GLU B 647 ASP B 648 -1 O GLU B 647 N CYS B 644
SHEET 1 J 4 LYS B 671 PHE B 673 0
SHEET 2 J 4 ALA B 688 ASP B 693 -1 O THR B 691 N PHE B 673
SHEET 3 J 4 THR B 725 TYR B 730 -1 O TYR B 730 N ALA B 688
SHEET 4 J 4 LYS B 717 PRO B 720 -1 N LYS B 717 O SER B 729
SHEET 1 K 4 CYS B 682 ILE B 683 0
SHEET 2 K 4 PHE B 754 GLY B 759 1 O GLY B 759 N CYS B 682
SHEET 3 K 4 LYS B 737 SER B 743 -1 N ILE B 740 O PHE B 754
SHEET 4 K 4 LYS B 703 ASP B 708 -1 N TYR B 705 O ILE B 741
LINK O ASP A 651 K K A 801 1555 1555 2.68
LINK O PRO A 653 K K A 801 1555 1555 2.56
LINK K K A 801 O ASP B 651 1555 1555 2.72
CISPEP 1 SER A 652 PRO A 653 0 2.53
CISPEP 2 SER A 752 PRO A 753 0 4.67
CISPEP 3 SER B 652 PRO B 653 0 -0.73
CISPEP 4 SER B 752 PRO B 753 0 10.85
SITE 1 AC1 3 ASP A 651 PRO A 653 ASP B 651
CRYST1 63.620 91.350 103.720 90.00 90.00 90.00 P 21 21 21 8
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 0.015718 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010947 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009641 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
