HEADER TRANSFERASE/TRANSFERASE INHIBITOR 26-JUL-14 4QYY
TITLE DISCOVERY OF NOVEL, DUAL MECHANISM ERK INHIBITORS BY AFFINITY
TITLE 2 SELECTION SCREENING OF AN INACTIVE KINASE STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MAP KINASE 1, MAPK 1, ERT1, EXTRACELLULAR SIGNAL-REGULATED
COMPND 5 KINASE 2, ERK-2, MAP KINASE ISOFORM P42, P42-MAPK, MITOGEN-ACTIVATED
COMPND 6 PROTEIN KINASE 2, MAP KINASE 2, MAPK 2;
COMPND 7 EC: 2.7.11.24;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: MAPK1, ERK2, MAPK, PRKM1;
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
KEYWDS TRANSFERASE, SERINE/THREONINE-PROTEIN KINASE, MAP KINASE,
KEYWDS 2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.DENG,G.W.SHIPPS,A.COOPER,J.M.ENGLISH,D.A.ANNIS,D.CARR,Y.NAN,T.WANG,
AUTHOR 2 Y.H.ZHU,C.CHUANG,P.DAYANANTH,A.W.HRUZA,L.XIAO,W.JIN,P.KIRSCHMEIER,
AUTHOR 3 W.T.WINDSOR,A.A.SAMATAR
REVDAT 2 17-DEC-14 4QYY 1 JRNL
REVDAT 1 12-NOV-14 4QYY 0
JRNL AUTH Y.DENG,G.W.SHIPPS,A.COOPER,J.M.ENGLISH,D.A.ANNIS,D.CARR,
JRNL AUTH 2 Y.NAN,T.WANG,H.Y.ZHU,C.C.CHUANG,P.DAYANANTH,A.W.HRUZA,
JRNL AUTH 3 L.XIAO,W.JIN,P.KIRSCHMEIER,W.T.WINDSOR,A.A.SAMATAR
JRNL TITL DISCOVERY OF NOVEL, DUAL MECHANISM ERK INHIBITORS BY
JRNL TITL 2 AFFINITY SELECTION SCREENING OF AN INACTIVE KINASE.
JRNL REF J.MED.CHEM. V. 57 8817 2014
JRNL REFN ISSN 0022-2623
JRNL PMID 25313996
JRNL DOI 10.1021/JM500847M
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.4
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 49215
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) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 2464
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.69
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.60
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3380
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2584
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3216
REMARK 3 BIN R VALUE (WORKING SET) : 0.2576
REMARK 3 BIN FREE R VALUE : 0.2741
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.85
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 164
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2757
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 49
REMARK 3 SOLVENT ATOMS : 188
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.19
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.03
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.71520
REMARK 3 B22 (A**2) : 0.10470
REMARK 3 B33 (A**2) : 1.61050
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.215
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.128
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.915
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 5667 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 10247 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1262 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 73 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 834 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 5667 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : 3 ; 0.000 ; HARMONIC
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 367 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 6315 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.04
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.63
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 15.17
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|13 - A|353 A|401 - A|404 A|601 - A|788 }
REMARK 3 ORIGIN FOR THE GROUP (A): 52.9821 19.0412 19.4617
REMARK 3 T TENSOR
REMARK 3 T11: -0.0482 T22: -0.0769
REMARK 3 T33: -0.0711 T12: 0.0106
REMARK 3 T13: -0.0041 T23: -0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 1.2063 L22: 0.7987
REMARK 3 L33: 0.9119 L12: -0.5050
REMARK 3 L13: -0.4974 L23: 0.0852
REMARK 3 S TENSOR
REMARK 3 S11: 0.0690 S12: 0.2118 S13: -0.0808
REMARK 3 S21: -0.0470 S22: -0.0809 S23: 0.1003
REMARK 3 S31: -0.0307 S32: -0.0917 S33: 0.0119
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4QYY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-AUG-14.
REMARK 100 THE RCSB ID CODE IS RCSB086689.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-SEP-04
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 6.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49215
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 29.880
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.700
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.60200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1ERK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, PH 6.4, 2.0M AMMONIUM
REMARK 280 SULFATE, 5% PEG 400, 0.5% DMSO, 1% GLYEROL, 0.0005M OLOMOUCINE,
REMARK 280 10 DAY SOAK WITH NEW COMPOUND, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 35.60100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.70450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.60100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.70450
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 ALA A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 6
REMARK 465 ALA A 7
REMARK 465 GLY A 8
REMARK 465 PRO A 9
REMARK 465 GLU A 10
REMARK 465 MET A 11
REMARK 465 VAL A 12
REMARK 465 PHE A 329
REMARK 465 ASP A 330
REMARK 465 MET A 331
REMARK 465 GLU A 332
REMARK 465 PRO A 354
REMARK 465 GLY A 355
REMARK 465 TYR A 356
REMARK 465 ARG A 357
REMARK 465 SER A 358
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET A 291 SD MET A 291 CE -0.401
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 VAL A 16 122.52 125.40
REMARK 500 ASN A 25 80.57 56.14
REMARK 500 LYS A 46 -65.18 68.41
REMARK 500 THR A 108 -169.20 -160.13
REMARK 500 ASP A 147 42.37 -152.84
REMARK 500 ASP A 165 86.57 70.00
REMARK 500 ASP A 173 68.74 -152.77
REMARK 500 ASN A 199 12.18 -164.20
REMARK 500 ILE A 254 -63.84 75.52
REMARK 500 LEU A 292 43.40 -95.99
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 3G7 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 404
DBREF 4QYY A 1 358 UNP P63086 MK01_RAT 1 358
SEQADV 4QYY ALA A -6 UNP P63086 EXPRESSION TAG
SEQADV 4QYY HIS A -5 UNP P63086 EXPRESSION TAG
SEQADV 4QYY HIS A -4 UNP P63086 EXPRESSION TAG
SEQADV 4QYY HIS A -3 UNP P63086 EXPRESSION TAG
SEQADV 4QYY HIS A -2 UNP P63086 EXPRESSION TAG
SEQADV 4QYY HIS A -1 UNP P63086 EXPRESSION TAG
SEQADV 4QYY HIS A 0 UNP P63086 EXPRESSION TAG
SEQRES 1 A 365 ALA HIS HIS HIS HIS HIS HIS MET ALA ALA ALA ALA ALA
SEQRES 2 A 365 ALA GLY PRO GLU MET VAL ARG GLY GLN VAL PHE ASP VAL
SEQRES 3 A 365 GLY PRO ARG TYR THR ASN LEU SER TYR ILE GLY GLU GLY
SEQRES 4 A 365 ALA TYR GLY MET VAL CYS SER ALA TYR ASP ASN LEU ASN
SEQRES 5 A 365 LYS VAL ARG VAL ALA ILE LYS LYS ILE SER PRO PHE GLU
SEQRES 6 A 365 HIS GLN THR TYR CYS GLN ARG THR LEU ARG GLU ILE LYS
SEQRES 7 A 365 ILE LEU LEU ARG PHE ARG HIS GLU ASN ILE ILE GLY ILE
SEQRES 8 A 365 ASN ASP ILE ILE ARG ALA PRO THR ILE GLU GLN MET LYS
SEQRES 9 A 365 ASP VAL TYR ILE VAL GLN ASP LEU MET GLU THR ASP LEU
SEQRES 10 A 365 TYR LYS LEU LEU LYS THR GLN HIS LEU SER ASN ASP HIS
SEQRES 11 A 365 ILE CYS TYR PHE LEU TYR GLN ILE LEU ARG GLY LEU LYS
SEQRES 12 A 365 TYR ILE HIS SER ALA ASN VAL LEU HIS ARG ASP LEU LYS
SEQRES 13 A 365 PRO SER ASN LEU LEU LEU ASN THR THR CYS ASP LEU LYS
SEQRES 14 A 365 ILE CYS ASP PHE GLY LEU ALA ARG VAL ALA ASP PRO ASP
SEQRES 15 A 365 HIS ASP HIS THR GLY PHE LEU THR GLU TYR VAL ALA THR
SEQRES 16 A 365 ARG TRP TYR ARG ALA PRO GLU ILE MET LEU ASN SER LYS
SEQRES 17 A 365 GLY TYR THR LYS SER ILE ASP ILE TRP SER VAL GLY CYS
SEQRES 18 A 365 ILE LEU ALA GLU MET LEU SER ASN ARG PRO ILE PHE PRO
SEQRES 19 A 365 GLY LYS HIS TYR LEU ASP GLN LEU ASN HIS ILE LEU GLY
SEQRES 20 A 365 ILE LEU GLY SER PRO SER GLN GLU ASP LEU ASN CYS ILE
SEQRES 21 A 365 ILE ASN LEU LYS ALA ARG ASN TYR LEU LEU SER LEU PRO
SEQRES 22 A 365 HIS LYS ASN LYS VAL PRO TRP ASN ARG LEU PHE PRO ASN
SEQRES 23 A 365 ALA ASP SER LYS ALA LEU ASP LEU LEU ASP LYS MET LEU
SEQRES 24 A 365 THR PHE ASN PRO HIS LYS ARG ILE GLU VAL GLU GLN ALA
SEQRES 25 A 365 LEU ALA HIS PRO TYR LEU GLU GLN TYR TYR ASP PRO SER
SEQRES 26 A 365 ASP GLU PRO ILE ALA GLU ALA PRO PHE LYS PHE ASP MET
SEQRES 27 A 365 GLU LEU ASP ASP LEU PRO LYS GLU LYS LEU LYS GLU LEU
SEQRES 28 A 365 ILE PHE GLU GLU THR ALA ARG PHE GLN PRO GLY TYR ARG
SEQRES 29 A 365 SER
HET 3G7 A 401 34
HET SO4 A 402 5
HET SO4 A 403 5
HET SO4 A 404 5
HETNAM 3G7 (3R)-1-{2-[4-(4-ACETYLPHENYL)PIPERAZIN-1-YL]-2-
HETNAM 2 3G7 OXOETHYL}-N-(3-CHLORO-4-HYDROXYPHENYL)PYRROLIDINE-3-
HETNAM 3 3G7 CARBOXAMIDE
HETNAM SO4 SULFATE ION
FORMUL 2 3G7 C25 H29 CL N4 O4
FORMUL 3 SO4 3(O4 S 2-)
FORMUL 6 HOH *188(H2 O)
HELIX 1 1 HIS A 59 PHE A 76 1 18
HELIX 2 2 LEU A 110 GLN A 117 1 8
HELIX 3 3 SER A 120 ALA A 141 1 22
HELIX 4 4 LYS A 149 SER A 151 5 3
HELIX 5 5 ASP A 173 ASP A 177 5 5
HELIX 6 6 THR A 188 ALA A 193 5 6
HELIX 7 7 PRO A 194 ASN A 199 1 6
HELIX 8 8 LYS A 205 ASN A 222 1 18
HELIX 9 9 HIS A 230 GLY A 243 1 14
HELIX 10 10 SER A 246 CYS A 252 1 7
HELIX 11 11 ASN A 255 LEU A 265 1 11
HELIX 12 12 PRO A 272 PHE A 277 1 6
HELIX 13 13 ASP A 281 LEU A 292 1 12
HELIX 14 14 GLU A 301 ALA A 307 1 7
HELIX 15 15 HIS A 308 GLU A 312 5 5
HELIX 16 16 ASP A 316 GLU A 320 5 5
HELIX 17 17 PRO A 337 ALA A 350 1 14
HELIX 18 18 ARG A 351 GLN A 353 5 3
SHEET 1 A 5 TYR A 23 GLY A 32 0
SHEET 2 A 5 GLY A 35 ASP A 42 -1 O TYR A 41 N THR A 24
SHEET 3 A 5 ARG A 48 ILE A 54 -1 O VAL A 49 N ALA A 40
SHEET 4 A 5 VAL A 99 ASP A 104 -1 O GLN A 103 N ALA A 50
SHEET 5 A 5 ASP A 86 ILE A 88 -1 N ASP A 86 O VAL A 102
SHEET 1 B 3 THR A 108 ASP A 109 0
SHEET 2 B 3 LEU A 153 LEU A 155 -1 O LEU A 155 N THR A 108
SHEET 3 B 3 LEU A 161 ILE A 163 -1 O LYS A 162 N LEU A 154
SHEET 1 C 2 VAL A 143 LEU A 144 0
SHEET 2 C 2 ARG A 170 VAL A 171 -1 O ARG A 170 N LEU A 144
CISPEP 1 GLY A 20 PRO A 21 0 -0.36
SITE 1 AC1 15 ALA A 33 TYR A 34 ALA A 50 LYS A 52
SITE 2 AC1 15 ILE A 54 TYR A 62 GLU A 69 GLN A 103
SITE 3 AC1 15 ASP A 104 LEU A 105 MET A 106 LEU A 154
SITE 4 AC1 15 ASP A 165 GLY A 167 HOH A 766
SITE 1 AC2 6 TYR A 185 ARG A 189 ARG A 192 TYR A 231
SITE 2 AC2 6 HOH A 722 HOH A 731
SITE 1 AC3 6 ASN A 121 GLY A 180 LYS A 257 HOH A 637
SITE 2 AC3 6 HOH A 644 HOH A 708
SITE 1 AC4 3 GLN A 64 ARG A 65 LEU A 168
CRYST1 71.202 91.409 63.316 90.00 90.00 90.00 P 21 21 2 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 0.014045 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010940 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015794 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
