HEADER TRANSFERASE 10-MAY-17 5NXC
TITLE LIM DOMAIN KINASE 1 (LIMK1) IN COMPLEX WITH PF-00477736
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIM DOMAIN KINASE 1;
COMPND 3 CHAIN: L;
COMPND 4 FRAGMENT: UNP RESIDUES 330-637;
COMPND 5 SYNONYM: LIMK-1;
COMPND 6 EC: 2.7.11.1;
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: LIMK1, LIMK;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS KINASE ACTIN CYTOSKELETON INHIBITOR, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MATHEA,E.SALAH,A.C.W.PIKE,S.BUSHELL,E.P.CARPENTER,F.VON DELFT,
AUTHOR 2 C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,A.N.BULLOCK,S.KNAPP
REVDAT 2 17-JAN-24 5NXC 1 REMARK
REVDAT 1 24-MAY-17 5NXC 0
JRNL AUTH S.MATHEA,E.SALAH,A.C.W.PIKE,S.BUSHELL,E.P.CARPENTER,
JRNL AUTH 2 F.VON DELFT,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,
JRNL AUTH 3 A.N.BULLOCK,S.KNAPP
JRNL TITL LIM DOMAIN KINASE (LIMK1) IN COMPLEX WITH PF-00477736
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 64.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 16629
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) : 0.242
REMARK 3 R VALUE (WORKING SET) : 0.239
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 815
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) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.30
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1186
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.92
REMARK 3 BIN R VALUE (WORKING SET) : 0.2710
REMARK 3 BIN FREE R VALUE SET COUNT : 58
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2133
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 44
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.19
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.61000
REMARK 3 B22 (A**2) : 1.96000
REMARK 3 B33 (A**2) : -1.35000
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): 0.290
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.248
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.198
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.153
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.908
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.866
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2224 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2057 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3022 ; 1.749 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4716 ; 1.087 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 272 ; 7.000 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 96 ;37.157 ;23.229
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 351 ;14.788 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;17.989 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 327 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2606 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 520 ; 0.002 ; 0.020
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): 1095 ; 2.247 ; 2.873
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1096 ; 2.246 ; 2.873
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1364 ; 3.532 ; 4.300
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1365 ; 3.531 ; 4.300
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1129 ; 2.294 ; 2.960
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1130 ; 2.293 ; 2.961
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1659 ; 3.547 ; 4.368
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2468 ; 5.052 ;22.040
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2457 ; 5.054 ;22.032
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 : NULL
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5NXC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1200004882.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUL-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9686
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17463
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 84.390
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.22000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : 0.92000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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: 1YI6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.0 0.2 M MGCL2 10%
REMARK 280 PEG8K, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 42.19600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.19600
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 44.19350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.91800
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 44.19350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.91800
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 42.19600
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 44.19350
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 47.91800
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 42.19600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 44.19350
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 47.91800
REMARK 290 SMTRY3 8 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L
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 L 480
REMARK 465 LEU L 481
REMARK 465 ALA L 482
REMARK 465 ARG L 483
REMARK 465 LEU L 484
REMARK 465 MET L 485
REMARK 465 VAL L 486
REMARK 465 ASP L 487
REMARK 465 GLU L 488
REMARK 465 LYS L 489
REMARK 465 THR L 490
REMARK 465 GLN L 491
REMARK 465 PRO L 492
REMARK 465 GLU L 493
REMARK 465 GLY L 494
REMARK 465 LEU L 495
REMARK 465 ARG L 496
REMARK 465 SER L 497
REMARK 465 LEU L 498
REMARK 465 LYS L 499
REMARK 465 LYS L 500
REMARK 465 PRO L 501
REMARK 465 ASP L 502
REMARK 465 ARG L 503
REMARK 465 LYS L 504
REMARK 465 LYS L 505
REMARK 465 ARG L 506
REMARK 465 TYR L 507
REMARK 465 THR L 508
REMARK 465 VAL L 509
REMARK 465 VAL L 510
REMARK 465 ARG L 633
REMARK 465 ARG L 634
REMARK 465 GLY L 635
REMARK 465 GLU L 636
REMARK 465 SER L 637
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 LYS L 347 CG CD CE NZ
REMARK 470 CYS L 349 SG
REMARK 470 PHE L 350 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG L 359 CZ NH1 NH2
REMARK 470 ILE L 371 CG1 CG2 CD1
REMARK 470 ARG L 372 CG CD NE CZ NH1 NH2
REMARK 470 ASP L 374 CG OD1 OD2
REMARK 470 GLU L 375 CG CD OE1 OE2
REMARK 470 GLU L 376 CG CD OE1 OE2
REMARK 470 THR L 377 OG1 CG2
REMARK 470 ARG L 379 CG CD NE CZ NH1 NH2
REMARK 470 LYS L 383 CD CE NZ
REMARK 470 LYS L 386 CE NZ
REMARK 470 LYS L 398 NZ
REMARK 470 TYR L 404 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS L 405 CG CD CE NZ
REMARK 470 ASP L 406 CG OD1 OD2
REMARK 470 LYS L 407 CG CD CE NZ
REMARK 470 LYS L 417 CE NZ
REMARK 470 GLN L 431 CG CD OE1 NE2
REMARK 470 ARG L 459 NE CZ NH1 NH2
REMARK 470 GLU L 470 CG CD OE1 OE2
REMARK 470 ARG L 569 CG CD NE CZ NH1 NH2
REMARK 470 ARG L 585 NE CZ NH1 NH2
REMARK 470 LYS L 599 CD CE NZ
REMARK 470 GLN L 623 CG CD OE1 NE2
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 L 389 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG L 422 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 CYS L 586 CA - CB - SG ANGL. DEV. = 6.6 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 L 372 128.47 98.13
REMARK 500 ASP L 374 140.45 -37.30
REMARK 500 LYS L 405 -72.63 -105.72
REMARK 500 ASP L 406 -90.67 -116.02
REMARK 500 ASN L 455 29.90 46.77
REMARK 500 ARG L 459 -18.62 78.54
REMARK 500 LYS L 472 1.89 85.10
REMARK 500 SER L 578 -22.66 84.85
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 9DB L 701
DBREF 5NXC L 330 637 UNP P53667 LIMK1_HUMAN 330 637
SEQADV 5NXC SER L 328 UNP P53667 EXPRESSION TAG
SEQADV 5NXC MET L 329 UNP P53667 EXPRESSION TAG
SEQRES 1 L 310 SER MET PRO HIS ARG ILE PHE ARG PRO SER ASP LEU ILE
SEQRES 2 L 310 HIS GLY GLU VAL LEU GLY LYS GLY CYS PHE GLY GLN ALA
SEQRES 3 L 310 ILE LYS VAL THR HIS ARG GLU THR GLY GLU VAL MET VAL
SEQRES 4 L 310 MET LYS GLU LEU ILE ARG PHE ASP GLU GLU THR GLN ARG
SEQRES 5 L 310 THR PHE LEU LYS GLU VAL LYS VAL MET ARG CYS LEU GLU
SEQRES 6 L 310 HIS PRO ASN VAL LEU LYS PHE ILE GLY VAL LEU TYR LYS
SEQRES 7 L 310 ASP LYS ARG LEU ASN PHE ILE THR GLU TYR ILE LYS GLY
SEQRES 8 L 310 GLY THR LEU ARG GLY ILE ILE LYS SER MET ASP SER GLN
SEQRES 9 L 310 TYR PRO TRP SER GLN ARG VAL SER PHE ALA LYS ASP ILE
SEQRES 10 L 310 ALA SER GLY MET ALA TYR LEU HIS SER MET ASN ILE ILE
SEQRES 11 L 310 HIS ARG ASP LEU ASN SER HIS ASN CYS LEU VAL ARG GLU
SEQRES 12 L 310 ASN LYS ASN VAL VAL VAL ALA ASP PHE GLY LEU ALA ARG
SEQRES 13 L 310 LEU MET VAL ASP GLU LYS THR GLN PRO GLU GLY LEU ARG
SEQRES 14 L 310 SER LEU LYS LYS PRO ASP ARG LYS LYS ARG TYR THR VAL
SEQRES 15 L 310 VAL GLY ASN PRO TYR TRP MET ALA PRO GLU MET ILE ASN
SEQRES 16 L 310 GLY ARG SER TYR ASP GLU LYS VAL ASP VAL PHE SER PHE
SEQRES 17 L 310 GLY ILE VAL LEU CYS GLU ILE ILE GLY ARG VAL ASN ALA
SEQRES 18 L 310 ASP PRO ASP TYR LEU PRO ARG THR MET ASP PHE GLY LEU
SEQRES 19 L 310 ASN VAL ARG GLY PHE LEU ASP ARG TYR CYS PRO PRO ASN
SEQRES 20 L 310 CYS PRO PRO SER PHE PHE PRO ILE THR VAL ARG CYS CYS
SEQRES 21 L 310 ASP LEU ASP PRO GLU LYS ARG PRO SER PHE VAL LYS LEU
SEQRES 22 L 310 GLU HIS TRP LEU GLU THR LEU ARG MET HIS LEU ALA GLY
SEQRES 23 L 310 HIS LEU PRO LEU GLY PRO GLN LEU GLU GLN LEU ASP ARG
SEQRES 24 L 310 GLY PHE TRP GLU THR TYR ARG ARG GLY GLU SER
HET 9DB L 701 31
HETNAM 9DB (2~{R})-2-AZANYL-2-CYCLOHEXYL-~{N}-[2-(1-METHYLPYRAZOL-
HETNAM 2 9DB 4-YL)-9-OXIDANYLIDENE-3,10,11-
HETNAM 3 9DB TRIAZATRICYCLO[6.4.1.0^{4,13}]TRIDECA-1,4,6,8(13),11-
HETNAM 4 9DB PENTAEN-6-YL]ETHANAMIDE
FORMUL 2 9DB C22 H25 N7 O2
FORMUL 3 HOH *44(H2 O)
HELIX 1 AA1 ARG L 335 SER L 337 5 3
HELIX 2 AA2 ASP L 374 LEU L 391 1 18
HELIX 3 AA3 THR L 420 SER L 427 1 8
HELIX 4 AA4 PRO L 433 MET L 454 1 22
HELIX 5 AA5 ALA L 517 ASN L 522 1 6
HELIX 6 AA6 GLU L 528 ARG L 545 1 18
HELIX 7 AA7 ASN L 562 TYR L 570 1 9
HELIX 8 AA8 SER L 578 CYS L 587 1 10
HELIX 9 AA9 ASP L 590 ARG L 594 5 5
HELIX 10 AB1 SER L 596 HIS L 614 1 19
HELIX 11 AB2 GLY L 618 TYR L 632 1 15
SHEET 1 AA1 5 LEU L 339 LYS L 347 0
SHEET 2 AA1 5 GLY L 351 HIS L 358 -1 O ALA L 353 N LEU L 345
SHEET 3 AA1 5 VAL L 364 LEU L 370 -1 O MET L 365 N VAL L 356
SHEET 4 AA1 5 LEU L 409 GLU L 414 -1 O THR L 413 N VAL L 366
SHEET 5 AA1 5 PHE L 399 TYR L 404 -1 N LEU L 403 O ASN L 410
SHEET 1 AA2 2 CYS L 466 VAL L 468 0
SHEET 2 AA2 2 VAL L 474 VAL L 476 -1 O VAL L 475 N LEU L 467
SITE 1 AC1 14 GLY L 346 LYS L 347 GLY L 351 GLN L 352
SITE 2 AC1 14 VAL L 366 LYS L 368 LEU L 397 THR L 413
SITE 3 AC1 14 GLU L 414 TYR L 415 ILE L 416 GLY L 419
SITE 4 AC1 14 LEU L 467 ASP L 478
CRYST1 88.387 95.836 84.392 90.00 90.00 90.00 C 2 2 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 0.011314 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010434 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011849 0.00000
(ATOM LINES ARE NOT SHOWN.)
END