HEADER TRANSFERASE 13-JUN-09 3HUB
TITLE HUMAN P38 MAP KINASE IN COMPLEX WITH SCIOS-469
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 14;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MITOGEN-ACTIVATED PROTEIN KINASE P38 ALPHA, MAP KINASE P38
COMPND 5 ALPHA, CYTOKINE SUPPRESSIVE ANTI-INFLAMMATORY DRUG-BINDING PROTEIN,
COMPND 6 CSAID-BINDING PROTEIN, CSBP, MAX-INTERACTING PROTEIN 2, MAP KINASE
COMPND 7 MXI2, SAPK2A;
COMPND 8 EC: 2.7.11.24;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MAPK14, CSBP, CSBP1, CSBP2, CSPB1, MXI2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX 6P-1
KEYWDS DFG-IN, GLYCINE-RICH LOOP, SCIOS-469, ALTERNATIVE SPLICING, ATP-
KEYWDS 2 BINDING, CYTOPLASM, KINASE, NUCLEOTIDE-BINDING, NUCLEUS,
KEYWDS 3 PHOSPHOPROTEIN, POLYMORPHISM, SERINE/THREONINE-PROTEIN KINASE,
KEYWDS 4 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.GRUETTER,J.R.SIMARD,D.RAUH
REVDAT 5 21-FEB-24 3HUB 1 REMARK
REVDAT 4 13-OCT-21 3HUB 1 SEQADV HETSYN
REVDAT 3 29-JUL-20 3HUB 1 COMPND REMARK SEQADV HETNAM
REVDAT 3 2 1 SITE
REVDAT 2 28-APR-10 3HUB 1 JRNL
REVDAT 1 09-MAR-10 3HUB 0
JRNL AUTH J.R.SIMARD,M.GETLIK,C.GRUTTER,R.SCHNEIDER,S.WULFERT,D.RAUH
JRNL TITL FLUOROPHORE LABELING OF THE GLYCINE-RICH LOOP AS A METHOD OF
JRNL TITL 2 IDENTIFYING INHIBITORS THAT BIND TO ACTIVE AND INACTIVE
JRNL TITL 3 KINASE CONFORMATIONS.
JRNL REF J.AM.CHEM.SOC. V. 132 4152 2010
JRNL REFN ISSN 0002-7863
JRNL PMID 20201574
JRNL DOI 10.1021/JA908083E
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 17296
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) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.292
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 865
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) : 2.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1184
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2360
REMARK 3 BIN FREE R VALUE SET COUNT : 62
REMARK 3 BIN FREE R VALUE : 0.3540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2694
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 96
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.74
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.87
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.88000
REMARK 3 B22 (A**2) : -0.46000
REMARK 3 B33 (A**2) : -0.42000
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): 0.366
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.278
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.212
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.414
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.879
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2817 ; 0.019 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3829 ; 1.842 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 333 ; 6.810 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 128 ;35.571 ;24.062
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 481 ;18.635 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;21.858 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 430 ; 0.112 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2112 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1256 ; 0.221 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1898 ; 0.312 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 125 ; 0.191 ; 0.200
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): 41 ; 0.238 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 10 ; 0.122 ; 0.200
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): 1732 ; 1.072 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2720 ; 1.753 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1272 ; 2.540 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1109 ; 3.695 ; 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 : 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 : 1.20
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 3HUB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUN-09.
REMARK 100 THE DEPOSITION ID IS D_1000053591.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97910
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : DYNAMICALLY BENDABLE MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE, XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17297
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 40.720
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.050
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.3400
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) : 2.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.41800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 1.3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES, 20-30% PEG4000, 50 MM N
REMARK 280 -BOG, PH 6.0, 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 34.00500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.22000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.80500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.22000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.00500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.80500
REMARK 290 SMTRY3 4 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 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 1
REMARK 465 SER A 2
REMARK 465 GLN A 3
REMARK 465 LEU A 171
REMARK 465 CYS A 172
REMARK 465 ARG A 173
REMARK 465 HIS A 174
REMARK 465 THR A 175
REMARK 465 ASP A 176
REMARK 465 ASP A 177
REMARK 465 GLU A 178
REMARK 465 MET A 179
REMARK 465 THR A 180
REMARK 465 GLY A 181
REMARK 465 TYR A 182
REMARK 465 VAL A 183
REMARK 465 ALA A 184
REMARK 465 LEU A 353
REMARK 465 ASP A 354
REMARK 465 GLN A 355
REMARK 465 GLU A 356
REMARK 465 GLU A 357
REMARK 465 MET A 358
REMARK 465 GLU A 359
REMARK 465 SER A 360
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 GLU A 4 CG CD OE1 OE2
REMARK 470 ARG A 10 CG CD NE CZ NH1 NH2
REMARK 470 PRO A 352 O
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 LEU A 164 CA - CB - CG ANGL. DEV. = 13.9 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 SER A 32 54.26 36.38
REMARK 500 PHE A 99 108.48 -51.08
REMARK 500 ARG A 149 -16.58 80.73
REMARK 500 ASP A 150 50.90 -142.32
REMARK 500 ASP A 168 37.10 74.87
REMARK 500 ASP A 227 -176.15 -170.46
REMARK 500 SER A 261 -6.07 -58.48
REMARK 500 PHE A 274 60.23 -109.14
REMARK 500 ALA A 277 153.99 -48.89
REMARK 500 LEU A 289 66.00 -107.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3GCP RELATED DB: PDB
REMARK 900 RELATED ID: 3GCQ RELATED DB: PDB
REMARK 900 RELATED ID: 3GCS RELATED DB: PDB
REMARK 900 RELATED ID: 3GCU RELATED DB: PDB
REMARK 900 RELATED ID: 3GCV RELATED DB: PDB
REMARK 900 RELATED ID: 3HUC RELATED DB: PDB
DBREF 3HUB A 2 360 UNP Q16539 MK14_HUMAN 2 360
SEQADV 3HUB GLY A 1 UNP Q16539 EXPRESSION TAG
SEQADV 3HUB SER A 119 UNP Q16539 CYS 119 ENGINEERED MUTATION
SEQADV 3HUB SER A 162 UNP Q16539 CYS 162 ENGINEERED MUTATION
SEQADV 3HUB CYS A 172 UNP Q16539 ALA 172 ENGINEERED MUTATION
SEQADV 3HUB LEU A 327 UNP Q16539 PHE 327 ENGINEERED MUTATION
SEQRES 1 A 360 GLY SER GLN GLU ARG PRO THR PHE TYR ARG GLN GLU LEU
SEQRES 2 A 360 ASN LYS THR ILE TRP GLU VAL PRO GLU ARG TYR GLN ASN
SEQRES 3 A 360 LEU SER PRO VAL GLY SER GLY ALA TYR GLY SER VAL CYS
SEQRES 4 A 360 ALA ALA PHE ASP THR LYS THR GLY LEU ARG VAL ALA VAL
SEQRES 5 A 360 LYS LYS LEU SER ARG PRO PHE GLN SER ILE ILE HIS ALA
SEQRES 6 A 360 LYS ARG THR TYR ARG GLU LEU ARG LEU LEU LYS HIS MET
SEQRES 7 A 360 LYS HIS GLU ASN VAL ILE GLY LEU LEU ASP VAL PHE THR
SEQRES 8 A 360 PRO ALA ARG SER LEU GLU GLU PHE ASN ASP VAL TYR LEU
SEQRES 9 A 360 VAL THR HIS LEU MET GLY ALA ASP LEU ASN ASN ILE VAL
SEQRES 10 A 360 LYS SER GLN LYS LEU THR ASP ASP HIS VAL GLN PHE LEU
SEQRES 11 A 360 ILE TYR GLN ILE LEU ARG GLY LEU LYS TYR ILE HIS SER
SEQRES 12 A 360 ALA ASP ILE ILE HIS ARG ASP LEU LYS PRO SER ASN LEU
SEQRES 13 A 360 ALA VAL ASN GLU ASP SER GLU LEU LYS ILE LEU ASP PHE
SEQRES 14 A 360 GLY LEU CYS ARG HIS THR ASP ASP GLU MET THR GLY TYR
SEQRES 15 A 360 VAL ALA THR ARG TRP TYR ARG ALA PRO GLU ILE MET LEU
SEQRES 16 A 360 ASN TRP MET HIS TYR ASN GLN THR VAL ASP ILE TRP SER
SEQRES 17 A 360 VAL GLY CYS ILE MET ALA GLU LEU LEU THR GLY ARG THR
SEQRES 18 A 360 LEU PHE PRO GLY THR ASP HIS ILE ASP GLN LEU LYS LEU
SEQRES 19 A 360 ILE LEU ARG LEU VAL GLY THR PRO GLY ALA GLU LEU LEU
SEQRES 20 A 360 LYS LYS ILE SER SER GLU SER ALA ARG ASN TYR ILE GLN
SEQRES 21 A 360 SER LEU THR GLN MET PRO LYS MET ASN PHE ALA ASN VAL
SEQRES 22 A 360 PHE ILE GLY ALA ASN PRO LEU ALA VAL ASP LEU LEU GLU
SEQRES 23 A 360 LYS MET LEU VAL LEU ASP SER ASP LYS ARG ILE THR ALA
SEQRES 24 A 360 ALA GLN ALA LEU ALA HIS ALA TYR PHE ALA GLN TYR HIS
SEQRES 25 A 360 ASP PRO ASP ASP GLU PRO VAL ALA ASP PRO TYR ASP GLN
SEQRES 26 A 360 SER LEU GLU SER ARG ASP LEU LEU ILE ASP GLU TRP LYS
SEQRES 27 A 360 SER LEU THR TYR ASP GLU VAL ILE SER PHE VAL PRO PRO
SEQRES 28 A 360 PRO LEU ASP GLN GLU GLU MET GLU SER
HET BOG A1000 20
HET 469 A 361 36
HETNAM BOG OCTYL BETA-D-GLUCOPYRANOSIDE
HETNAM 469 2-(6-CHLORO-5-{[(2R,5S)-4-(4-FLUOROBENZYL)-2,5-
HETNAM 2 469 DIMETHYLPIPERAZIN-1-YL]CARBONYL}-1-METHYL-1H-INDOL-3-
HETNAM 3 469 YL)-N,N-DIMETHYL-2-OXOACETAMIDE
HETSYN BOG BETA-OCTYLGLUCOSIDE; OCTYL BETA-D-GLUCOSIDE; OCTYL D-
HETSYN 2 BOG GLUCOSIDE; OCTYL GLUCOSIDE
FORMUL 2 BOG C14 H28 O6
FORMUL 3 469 C27 H30 CL F N4 O3
FORMUL 4 HOH *96(H2 O)
HELIX 1 1 GLY A 31 ALA A 34 5 4
HELIX 2 2 SER A 61 MET A 78 1 18
HELIX 3 3 LEU A 113 LYS A 118 1 6
HELIX 4 4 THR A 123 ALA A 144 1 22
HELIX 5 5 LYS A 152 SER A 154 5 3
HELIX 6 6 ALA A 190 LEU A 195 1 6
HELIX 7 7 THR A 203 GLY A 219 1 17
HELIX 8 8 ASP A 227 GLY A 240 1 14
HELIX 9 9 GLY A 243 LYS A 249 1 7
HELIX 10 10 SER A 252 SER A 261 1 10
HELIX 11 11 ASN A 269 VAL A 273 5 5
HELIX 12 12 ASN A 278 LEU A 289 1 12
HELIX 13 13 ASP A 292 ARG A 296 5 5
HELIX 14 14 THR A 298 ALA A 304 1 7
HELIX 15 15 HIS A 305 ALA A 309 5 5
HELIX 16 16 ASP A 324 SER A 329 1 6
HELIX 17 17 LEU A 333 SER A 347 1 15
SHEET 1 A 2 PHE A 8 LEU A 13 0
SHEET 2 A 2 THR A 16 PRO A 21 -1 O THR A 16 N LEU A 13
SHEET 1 B 5 TYR A 24 PRO A 29 0
SHEET 2 B 5 VAL A 38 ASP A 43 -1 O PHE A 42 N GLN A 25
SHEET 3 B 5 LEU A 48 LYS A 54 -1 O VAL A 52 N CYS A 39
SHEET 4 B 5 TYR A 103 HIS A 107 -1 O THR A 106 N ALA A 51
SHEET 5 B 5 ASP A 88 PHE A 90 -1 N ASP A 88 O VAL A 105
SHEET 1 C 2 LEU A 156 VAL A 158 0
SHEET 2 C 2 LEU A 164 ILE A 166 -1 O LYS A 165 N ALA A 157
CRYST1 68.010 69.610 74.440 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 0.014704 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014366 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013434 0.00000
(ATOM LINES ARE NOT SHOWN.)
END