HEADER TRANSFERASE 04-APR-17 5VEF
TITLE PAK4 KINASE DOMAIN IN COMPLEX WITH FASUDIL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PAK 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 286-591;
COMPND 5 SYNONYM: P21-ACTIVATED KINASE 4,PAK-4;
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: PAK4, KIAA1142;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RILP;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET VECTOR
KEYWDS KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.Y.ZHANG,B.H.HA,T.J.BOGGON
REVDAT 5 04-OCT-23 5VEF 1 HETSYN
REVDAT 4 26-FEB-20 5VEF 1 REMARK
REVDAT 3 01-JAN-20 5VEF 1 REMARK
REVDAT 2 03-JAN-18 5VEF 1 JRNL
REVDAT 1 18-OCT-17 5VEF 0
JRNL AUTH E.Y.ZHANG,B.H.HA,T.J.BOGGON
JRNL TITL PAK4 CRYSTAL STRUCTURES SUGGEST UNUSUAL KINASE
JRNL TITL 2 CONFORMATIONAL MOVEMENTS.
JRNL REF BIOCHIM. BIOPHYS. ACTA V.1866 356 2018
JRNL REFN ISSN 0006-3002
JRNL PMID 28993291
JRNL DOI 10.1016/J.BBAPAP.2017.10.004
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.80
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 35251
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.920
REMARK 3 FREE R VALUE TEST SET COUNT : 1733
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 43.8119 - 4.0092 1.00 3177 168 0.1420 0.1839
REMARK 3 2 4.0092 - 3.1825 1.00 2970 181 0.1689 0.1964
REMARK 3 3 3.1825 - 2.7803 1.00 2946 143 0.2010 0.2303
REMARK 3 4 2.7803 - 2.5261 0.99 2899 160 0.1968 0.2157
REMARK 3 5 2.5261 - 2.3451 0.99 2889 138 0.2060 0.2425
REMARK 3 6 2.3451 - 2.2068 0.96 2741 152 0.2794 0.3984
REMARK 3 7 2.2068 - 2.0963 0.98 2833 142 0.2278 0.2566
REMARK 3 8 2.0963 - 2.0051 0.97 2760 152 0.2214 0.2386
REMARK 3 9 2.0051 - 1.9279 0.92 2648 119 0.3432 0.4021
REMARK 3 10 1.9279 - 1.8614 0.84 2389 140 0.4881 0.5632
REMARK 3 11 1.8614 - 1.8031 0.92 2666 120 0.3185 0.3790
REMARK 3 12 1.8031 - 1.7516 0.91 2600 118 0.2987 0.3159
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.590
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 2385
REMARK 3 ANGLE : 1.080 3237
REMARK 3 CHIRALITY : 0.042 363
REMARK 3 PLANARITY : 0.005 415
REMARK 3 DIHEDRAL : 12.963 910
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 11.6285 40.6932 7.6838
REMARK 3 T TENSOR
REMARK 3 T11: 0.1787 T22: 0.1391
REMARK 3 T33: 0.1390 T12: -0.0263
REMARK 3 T13: 0.0164 T23: -0.0237
REMARK 3 L TENSOR
REMARK 3 L11: 0.6510 L22: 1.4467
REMARK 3 L33: 1.3843 L12: 0.1047
REMARK 3 L13: 0.4356 L23: -0.1394
REMARK 3 S TENSOR
REMARK 3 S11: -0.0503 S12: 0.0500 S13: -0.0549
REMARK 3 S21: -0.2075 S22: 0.0960 S23: -0.0391
REMARK 3 S31: -0.0664 S32: 0.0220 S33: -0.0442
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5VEF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-APR-17.
REMARK 100 THE DEPOSITION ID IS D_1000227225.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-NOV-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97919
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35807
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 12.20
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.4
REMARK 200 DATA REDUNDANCY IN SHELL : 10.40
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: 4FIJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL (PH 7.5) AND 1.5 - 2.0
REMARK 280 M NA ACETATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 -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 91.37050
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 30.97000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 30.97000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 45.68525
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 30.97000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 30.97000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 137.05575
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 30.97000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 30.97000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 45.68525
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 30.97000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 30.97000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 137.05575
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 91.37050
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 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 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 273
REMARK 465 ALA A 274
REMARK 465 ARG A 275
REMARK 465 ALA A 276
REMARK 465 ARG A 277
REMARK 465 GLN A 278
REMARK 465 GLU A 279
REMARK 465 ASN A 280
REMARK 465 GLY A 281
REMARK 465 MET A 282
REMARK 465 PRO A 283
REMARK 465 GLU A 284
REMARK 465 LYS A 285
REMARK 465 PRO A 286
REMARK 465 PRO A 287
REMARK 465 GLY A 288
REMARK 465 PRO A 289
REMARK 465 ARG A 290
REMARK 465 SER A 291
REMARK 465 PRO A 292
REMARK 465 GLN A 293
REMARK 465 ARG A 294
REMARK 465 GLU A 295
REMARK 465 PRO A 296
REMARK 465 GLN A 297
REMARK 465 ARG A 298
REMARK 465 VAL A 299
REMARK 465 THR A 590
REMARK 465 ARG A 591
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 HOH A 702 O HOH A 817 2.09
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 440 43.97 -147.38
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 M77 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5VED RELATED DB: PDB
REMARK 900 RELATED ID: 5VEF RELATED DB: PDB
DBREF 5VEF A 286 591 UNP O96013 PAK4_HUMAN 286 591
SEQADV 5VEF GLY A 273 UNP O96013 EXPRESSION TAG
SEQADV 5VEF ALA A 274 UNP O96013 EXPRESSION TAG
SEQADV 5VEF ARG A 275 UNP O96013 EXPRESSION TAG
SEQADV 5VEF ALA A 276 UNP O96013 EXPRESSION TAG
SEQADV 5VEF ARG A 277 UNP O96013 EXPRESSION TAG
SEQADV 5VEF GLN A 278 UNP O96013 EXPRESSION TAG
SEQADV 5VEF GLU A 279 UNP O96013 EXPRESSION TAG
SEQADV 5VEF ASN A 280 UNP O96013 EXPRESSION TAG
SEQADV 5VEF GLY A 281 UNP O96013 EXPRESSION TAG
SEQADV 5VEF MET A 282 UNP O96013 EXPRESSION TAG
SEQADV 5VEF PRO A 283 UNP O96013 EXPRESSION TAG
SEQADV 5VEF GLU A 284 UNP O96013 EXPRESSION TAG
SEQADV 5VEF LYS A 285 UNP O96013 EXPRESSION TAG
SEQRES 1 A 319 GLY ALA ARG ALA ARG GLN GLU ASN GLY MET PRO GLU LYS
SEQRES 2 A 319 PRO PRO GLY PRO ARG SER PRO GLN ARG GLU PRO GLN ARG
SEQRES 3 A 319 VAL SER HIS GLU GLN PHE ARG ALA ALA LEU GLN LEU VAL
SEQRES 4 A 319 VAL ASP PRO GLY ASP PRO ARG SER TYR LEU ASP ASN PHE
SEQRES 5 A 319 ILE LYS ILE GLY GLU GLY SER THR GLY ILE VAL CYS ILE
SEQRES 6 A 319 ALA THR VAL ARG SER SER GLY LYS LEU VAL ALA VAL LYS
SEQRES 7 A 319 LYS MET ASP LEU ARG LYS GLN GLN ARG ARG GLU LEU LEU
SEQRES 8 A 319 PHE ASN GLU VAL VAL ILE MET ARG ASP TYR GLN HIS GLU
SEQRES 9 A 319 ASN VAL VAL GLU MET TYR ASN SER TYR LEU VAL GLY ASP
SEQRES 10 A 319 GLU LEU TRP VAL VAL MET GLU PHE LEU GLU GLY GLY ALA
SEQRES 11 A 319 LEU THR ASP ILE VAL THR HIS THR ARG MET ASN GLU GLU
SEQRES 12 A 319 GLN ILE ALA ALA VAL CYS LEU ALA VAL LEU GLN ALA LEU
SEQRES 13 A 319 SER VAL LEU HIS ALA GLN GLY VAL ILE HIS ARG ASP ILE
SEQRES 14 A 319 LYS SER ASP SER ILE LEU LEU THR HIS ASP GLY ARG VAL
SEQRES 15 A 319 LYS LEU SER ASP PHE GLY PHE CYS ALA GLN VAL SER LYS
SEQRES 16 A 319 GLU VAL PRO ARG ARG LYS SEP LEU VAL GLY THR PRO TYR
SEQRES 17 A 319 TRP MET ALA PRO GLU LEU ILE SER ARG LEU PRO TYR GLY
SEQRES 18 A 319 PRO GLU VAL ASP ILE TRP SER LEU GLY ILE MET VAL ILE
SEQRES 19 A 319 GLU MET VAL ASP GLY GLU PRO PRO TYR PHE ASN GLU PRO
SEQRES 20 A 319 PRO LEU LYS ALA MET LYS MET ILE ARG ASP ASN LEU PRO
SEQRES 21 A 319 PRO ARG LEU LYS ASN LEU HIS LYS VAL SER PRO SER LEU
SEQRES 22 A 319 LYS GLY PHE LEU ASP ARG LEU LEU VAL ARG ASP PRO ALA
SEQRES 23 A 319 GLN ARG ALA THR ALA ALA GLU LEU LEU LYS HIS PRO PHE
SEQRES 24 A 319 LEU ALA LYS ALA GLY PRO PRO ALA SER ILE VAL PRO LEU
SEQRES 25 A 319 MET ARG GLN ASN ARG THR ARG
MODRES 5VEF SEP A 474 SER MODIFIED RESIDUE
HET SEP A 474 14
HET M77 A 601 37
HET ACT A 602 7
HETNAM SEP PHOSPHOSERINE
HETNAM M77 5-(1,4-DIAZEPAN-1-SULFONYL)ISOQUINOLINE
HETNAM ACT ACETATE ION
HETSYN SEP PHOSPHONOSERINE
HETSYN M77 FASUDIL; (5-ISOQUINOLINESULFONYL)HOMOPIPERAZINE
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 2 M77 C14 H17 N3 O2 S
FORMUL 3 ACT C2 H3 O2 1-
FORMUL 4 HOH *136(H2 O)
HELIX 1 AA1 SER A 300 VAL A 312 1 13
HELIX 2 AA2 ASP A 316 SER A 319 5 4
HELIX 3 AA3 ARG A 355 GLN A 357 5 3
HELIX 4 AA4 ARG A 359 LEU A 362 5 4
HELIX 5 AA5 LEU A 363 TYR A 373 1 11
HELIX 6 AA6 LEU A 403 THR A 410 1 8
HELIX 7 AA7 ASN A 413 GLN A 434 1 22
HELIX 8 AA8 LYS A 442 ASP A 444 5 3
HELIX 9 AA9 THR A 478 MET A 482 5 5
HELIX 10 AB1 ALA A 483 SER A 488 1 6
HELIX 11 AB2 PRO A 494 GLY A 511 1 18
HELIX 12 AB3 PRO A 519 ASN A 530 1 12
HELIX 13 AB4 ASN A 537 VAL A 541 5 5
HELIX 14 AB5 SER A 542 LEU A 553 1 12
HELIX 15 AB6 THR A 562 LEU A 567 1 6
HELIX 16 AB7 LYS A 568 ALA A 575 5 8
HELIX 17 AB8 PRO A 577 MET A 585 5 9
SHEET 1 AA1 5 LEU A 321 GLU A 329 0
SHEET 2 AA1 5 ILE A 334 VAL A 340 -1 O THR A 339 N ASP A 322
SHEET 3 AA1 5 LEU A 346 ASP A 353 -1 O LYS A 351 N ILE A 334
SHEET 4 AA1 5 GLU A 390 GLU A 396 -1 O VAL A 393 N LYS A 350
SHEET 5 AA1 5 MET A 381 VAL A 387 -1 N VAL A 387 O GLU A 390
SHEET 1 AA2 3 GLY A 401 ALA A 402 0
SHEET 2 AA2 3 ILE A 446 LEU A 448 -1 O LEU A 448 N GLY A 401
SHEET 3 AA2 3 VAL A 454 LEU A 456 -1 O LYS A 455 N LEU A 447
SHEET 1 AA3 2 VAL A 436 ILE A 437 0
SHEET 2 AA3 2 ALA A 463 GLN A 464 -1 O ALA A 463 N ILE A 437
LINK C LYS A 473 N SEP A 474 1555 1555 1.32
LINK C SEP A 474 N LEU A 475 1555 1555 1.33
SITE 1 AC1 10 GLY A 328 GLU A 329 GLY A 330 VAL A 335
SITE 2 AC1 10 GLU A 396 PHE A 397 LEU A 398 ASP A 444
SITE 3 AC1 10 LEU A 447 SER A 457
SITE 1 AC2 6 THR A 404 SER A 443 ASP A 444 TRP A 481
SITE 2 AC2 6 GLU A 507 HOH A 760
CRYST1 61.940 61.940 182.741 90.00 90.00 90.00 P 41 21 2 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 0.016145 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016145 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005472 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
