HEADER TRANSFERASE/TRANSFERASE INHIBITOR 13-AUG-15 5D7A
TITLE CRYSTAL STRUCTURE OF THE KINASE DOMAIN OF TRAF2 AND NCK-INTERACTING
TITLE 2 PROTEIN KINASE WITH NCB-0846
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRAF2 AND NCK-INTERACTING PROTEIN KINASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 EC: 2.7.11.1;
COMPND 5 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: TNIK, KIAA0551;
SOURCE 6 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PFASTBAC1-HM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 274590
KEYWDS KINASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR N.OHBAYASHI,M.KUKIMOTO-NIINO,T.YAMADA,M.SHIROUZU
REVDAT 5 08-NOV-23 5D7A 1 REMARK
REVDAT 4 19-FEB-20 5D7A 1 REMARK
REVDAT 3 28-SEP-16 5D7A 1 TITLE
REVDAT 2 07-SEP-16 5D7A 1 TITLE JRNL
REVDAT 1 17-AUG-16 5D7A 0
JRNL AUTH M.MASUDA,Y.UNO,N.OHBAYASHI,H.OHATA,A.MIMATA,
JRNL AUTH 2 M.KUKIMOTO-NIINO,H.MORIYAMA,S.KASHIMOTO,T.INOUE,N.GOTO,
JRNL AUTH 3 K.OKAMOTO,M.SHIROUZU,M.SAWA,T.YAMADA
JRNL TITL TNIK INHIBITION ABROGATES COLORECTAL CANCER STEMNESS
JRNL REF NAT COMMUN V. 7 12586 2016
JRNL REFN ESSN 2041-1723
JRNL PMID 27562646
JRNL DOI 10.1038/NCOMMS12586
REMARK 2
REMARK 2 RESOLUTION. 2.90 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.92
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 28789
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 1426
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 46.9306 - 6.2435 1.00 2793 121 0.1598 0.1829
REMARK 3 2 6.2435 - 4.9574 1.00 2761 137 0.1855 0.2737
REMARK 3 3 4.9574 - 4.3312 1.00 2769 126 0.1603 0.2079
REMARK 3 4 4.3312 - 3.9354 1.00 2750 130 0.1646 0.2171
REMARK 3 5 3.9354 - 3.6535 1.00 2751 129 0.1784 0.2535
REMARK 3 6 3.6535 - 3.4382 1.00 2684 171 0.1869 0.2086
REMARK 3 7 3.4382 - 3.2660 1.00 2687 178 0.2067 0.2835
REMARK 3 8 3.2660 - 3.1239 1.00 2653 166 0.2253 0.2775
REMARK 3 9 3.1239 - 3.0036 1.00 2765 149 0.2511 0.3156
REMARK 3 10 3.0036 - 2.9000 1.00 2750 119 0.2972 0.3692
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.410
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.020
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 : 0.004 7179
REMARK 3 ANGLE : 0.822 9703
REMARK 3 CHIRALITY : 0.032 1042
REMARK 3 PLANARITY : 0.003 1239
REMARK 3 DIHEDRAL : 13.972 2711
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 5D7A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-AUG-15.
REMARK 100 THE DEPOSITION ID IS D_1000212484.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL26B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28803
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 46.920
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.700
REMARK 200 R MERGE (I) : 0.11700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 2X7F
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULFATE 0.1M BIS-TRIS
REMARK 280 (5.6) 15% PEG3350 7% ETHYLENEGLYCOL, PH 5.6, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 106.31000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 62.48600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 106.31000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 62.48600
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, 3
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 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 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 7
REMARK 465 SER A 8
REMARK 465 GLY A 9
REMARK 465 ALA A 10
REMARK 465 SER A 175
REMARK 465 ALA A 176
REMARK 465 GLN A 177
REMARK 465 LEU A 178
REMARK 465 ASP A 179
REMARK 465 ARG A 180
REMARK 465 THR A 181
REMARK 465 VAL A 182
REMARK 465 GLY A 183
REMARK 465 ARG A 184
REMARK 465 ARG A 185
REMARK 465 LYS A 311
REMARK 465 LYS A 312
REMARK 465 ARG A 313
REMARK 465 GLY A 314
REMARK 465 GLY B 7
REMARK 465 SER B 8
REMARK 465 GLY B 9
REMARK 465 ALA B 10
REMARK 465 SER B 175
REMARK 465 ALA B 176
REMARK 465 GLN B 177
REMARK 465 LEU B 178
REMARK 465 ASP B 179
REMARK 465 ARG B 180
REMARK 465 THR B 181
REMARK 465 VAL B 182
REMARK 465 GLY B 183
REMARK 465 ARG B 184
REMARK 465 ARG B 185
REMARK 465 ARG B 308
REMARK 465 THR B 309
REMARK 465 LYS B 310
REMARK 465 LYS B 311
REMARK 465 LYS B 312
REMARK 465 ARG B 313
REMARK 465 GLY B 314
REMARK 465 GLY C 7
REMARK 465 SER C 8
REMARK 465 GLY C 9
REMARK 465 ALA C 10
REMARK 465 ASP C 11
REMARK 465 GLU C 12
REMARK 465 VAL C 174
REMARK 465 SER C 175
REMARK 465 ALA C 176
REMARK 465 GLN C 177
REMARK 465 LEU C 178
REMARK 465 ASP C 179
REMARK 465 ARG C 180
REMARK 465 THR C 181
REMARK 465 VAL C 182
REMARK 465 GLY C 183
REMARK 465 ARG C 184
REMARK 465 ARG C 185
REMARK 465 LYS C 311
REMARK 465 LYS C 312
REMARK 465 ARG C 313
REMARK 465 GLY C 314
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 OE1 GLU B 166 NH1 ARG C 290 2.19
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 GLU A 12 38.11 -92.70
REMARK 500 VAL A 28 -80.86 -92.83
REMARK 500 THR A 35 93.69 -68.96
REMARK 500 THR A 59 -144.83 -135.58
REMARK 500 PRO A 94 152.90 -45.44
REMARK 500 ARG A 152 -15.16 75.38
REMARK 500 ASP A 153 48.45 -145.78
REMARK 500 CYS A 202 -163.38 -163.44
REMARK 500 ASN A 205 81.44 -152.91
REMARK 500 GLU A 228 -5.18 -141.63
REMARK 500 ASP A 235 37.98 -87.02
REMARK 500 LEU A 270 68.04 -102.12
REMARK 500 ASP A 291 76.84 -69.77
REMARK 500 THR B 35 99.83 -63.02
REMARK 500 TYR B 36 75.67 55.15
REMARK 500 PRO B 94 155.32 -42.82
REMARK 500 ARG B 152 -4.54 73.98
REMARK 500 ASP B 153 47.47 -155.90
REMARK 500 CYS B 202 -156.36 -158.03
REMARK 500 ASP B 291 37.35 -85.88
REMARK 500 ARG C 80 3.08 -64.05
REMARK 500 ARG C 152 -1.61 72.07
REMARK 500 ASP C 153 58.90 -158.84
REMARK 500 ASP C 171 71.57 58.46
REMARK 500 CYS C 202 -168.16 -168.88
REMARK 500 ASN C 205 72.46 -153.78
REMARK 500 ASP C 207 79.17 -101.51
REMARK 500 ASN C 294 55.07 -111.60
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 58C 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 58C B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 58C C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5CWZ RELATED DB: PDB
REMARK 900 RELATED ID: 5AX9 RELATED DB: PDB
DBREF 5D7A A 11 314 UNP Q9UKE5 TNIK_HUMAN 11 314
DBREF 5D7A B 11 314 UNP Q9UKE5 TNIK_HUMAN 11 314
DBREF 5D7A C 11 314 UNP Q9UKE5 TNIK_HUMAN 11 314
SEQADV 5D7A GLY A 7 UNP Q9UKE5 EXPRESSION TAG
SEQADV 5D7A SER A 8 UNP Q9UKE5 EXPRESSION TAG
SEQADV 5D7A GLY A 9 UNP Q9UKE5 EXPRESSION TAG
SEQADV 5D7A ALA A 10 UNP Q9UKE5 EXPRESSION TAG
SEQADV 5D7A GLY B 7 UNP Q9UKE5 EXPRESSION TAG
SEQADV 5D7A SER B 8 UNP Q9UKE5 EXPRESSION TAG
SEQADV 5D7A GLY B 9 UNP Q9UKE5 EXPRESSION TAG
SEQADV 5D7A ALA B 10 UNP Q9UKE5 EXPRESSION TAG
SEQADV 5D7A GLY C 7 UNP Q9UKE5 EXPRESSION TAG
SEQADV 5D7A SER C 8 UNP Q9UKE5 EXPRESSION TAG
SEQADV 5D7A GLY C 9 UNP Q9UKE5 EXPRESSION TAG
SEQADV 5D7A ALA C 10 UNP Q9UKE5 EXPRESSION TAG
SEQRES 1 A 308 GLY SER GLY ALA ASP GLU ILE ASP LEU SER ALA LEU ARG
SEQRES 2 A 308 ASP PRO ALA GLY ILE PHE GLU LEU VAL GLU LEU VAL GLY
SEQRES 3 A 308 ASN GLY THR TYR GLY GLN VAL TYR LYS GLY ARG HIS VAL
SEQRES 4 A 308 LYS THR GLY GLN LEU ALA ALA ILE LYS VAL MET ASP VAL
SEQRES 5 A 308 THR GLY ASP GLU GLU GLU GLU ILE LYS GLN GLU ILE ASN
SEQRES 6 A 308 MET LEU LYS LYS TYR SER HIS HIS ARG ASN ILE ALA THR
SEQRES 7 A 308 TYR TYR GLY ALA PHE ILE LYS LYS ASN PRO PRO GLY MET
SEQRES 8 A 308 ASP ASP GLN LEU TRP LEU VAL MET GLU PHE CYS GLY ALA
SEQRES 9 A 308 GLY SER VAL THR ASP LEU ILE LYS ASN THR LYS GLY ASN
SEQRES 10 A 308 THR LEU LYS GLU GLU TRP ILE ALA TYR ILE CYS ARG GLU
SEQRES 11 A 308 ILE LEU ARG GLY LEU SER HIS LEU HIS GLN HIS LYS VAL
SEQRES 12 A 308 ILE HIS ARG ASP ILE LYS GLY GLN ASN VAL LEU LEU THR
SEQRES 13 A 308 GLU ASN ALA GLU VAL LYS LEU VAL ASP PHE GLY VAL SER
SEQRES 14 A 308 ALA GLN LEU ASP ARG THR VAL GLY ARG ARG ASN THR PHE
SEQRES 15 A 308 ILE GLY THR PRO TYR TRP MET ALA PRO GLU VAL ILE ALA
SEQRES 16 A 308 CYS ASP GLU ASN PRO ASP ALA THR TYR ASP PHE LYS SER
SEQRES 17 A 308 ASP LEU TRP SER LEU GLY ILE THR ALA ILE GLU MET ALA
SEQRES 18 A 308 GLU GLY ALA PRO PRO LEU CYS ASP MET HIS PRO MET ARG
SEQRES 19 A 308 ALA LEU PHE LEU ILE PRO ARG ASN PRO ALA PRO ARG LEU
SEQRES 20 A 308 LYS SER LYS LYS TRP SER LYS LYS PHE GLN SER PHE ILE
SEQRES 21 A 308 GLU SER CYS LEU VAL LYS ASN HIS SER GLN ARG PRO ALA
SEQRES 22 A 308 THR GLU GLN LEU MET LYS HIS PRO PHE ILE ARG ASP GLN
SEQRES 23 A 308 PRO ASN GLU ARG GLN VAL ARG ILE GLN LEU LYS ASP HIS
SEQRES 24 A 308 ILE ASP ARG THR LYS LYS LYS ARG GLY
SEQRES 1 B 308 GLY SER GLY ALA ASP GLU ILE ASP LEU SER ALA LEU ARG
SEQRES 2 B 308 ASP PRO ALA GLY ILE PHE GLU LEU VAL GLU LEU VAL GLY
SEQRES 3 B 308 ASN GLY THR TYR GLY GLN VAL TYR LYS GLY ARG HIS VAL
SEQRES 4 B 308 LYS THR GLY GLN LEU ALA ALA ILE LYS VAL MET ASP VAL
SEQRES 5 B 308 THR GLY ASP GLU GLU GLU GLU ILE LYS GLN GLU ILE ASN
SEQRES 6 B 308 MET LEU LYS LYS TYR SER HIS HIS ARG ASN ILE ALA THR
SEQRES 7 B 308 TYR TYR GLY ALA PHE ILE LYS LYS ASN PRO PRO GLY MET
SEQRES 8 B 308 ASP ASP GLN LEU TRP LEU VAL MET GLU PHE CYS GLY ALA
SEQRES 9 B 308 GLY SER VAL THR ASP LEU ILE LYS ASN THR LYS GLY ASN
SEQRES 10 B 308 THR LEU LYS GLU GLU TRP ILE ALA TYR ILE CYS ARG GLU
SEQRES 11 B 308 ILE LEU ARG GLY LEU SER HIS LEU HIS GLN HIS LYS VAL
SEQRES 12 B 308 ILE HIS ARG ASP ILE LYS GLY GLN ASN VAL LEU LEU THR
SEQRES 13 B 308 GLU ASN ALA GLU VAL LYS LEU VAL ASP PHE GLY VAL SER
SEQRES 14 B 308 ALA GLN LEU ASP ARG THR VAL GLY ARG ARG ASN THR PHE
SEQRES 15 B 308 ILE GLY THR PRO TYR TRP MET ALA PRO GLU VAL ILE ALA
SEQRES 16 B 308 CYS ASP GLU ASN PRO ASP ALA THR TYR ASP PHE LYS SER
SEQRES 17 B 308 ASP LEU TRP SER LEU GLY ILE THR ALA ILE GLU MET ALA
SEQRES 18 B 308 GLU GLY ALA PRO PRO LEU CYS ASP MET HIS PRO MET ARG
SEQRES 19 B 308 ALA LEU PHE LEU ILE PRO ARG ASN PRO ALA PRO ARG LEU
SEQRES 20 B 308 LYS SER LYS LYS TRP SER LYS LYS PHE GLN SER PHE ILE
SEQRES 21 B 308 GLU SER CYS LEU VAL LYS ASN HIS SER GLN ARG PRO ALA
SEQRES 22 B 308 THR GLU GLN LEU MET LYS HIS PRO PHE ILE ARG ASP GLN
SEQRES 23 B 308 PRO ASN GLU ARG GLN VAL ARG ILE GLN LEU LYS ASP HIS
SEQRES 24 B 308 ILE ASP ARG THR LYS LYS LYS ARG GLY
SEQRES 1 C 308 GLY SER GLY ALA ASP GLU ILE ASP LEU SER ALA LEU ARG
SEQRES 2 C 308 ASP PRO ALA GLY ILE PHE GLU LEU VAL GLU LEU VAL GLY
SEQRES 3 C 308 ASN GLY THR TYR GLY GLN VAL TYR LYS GLY ARG HIS VAL
SEQRES 4 C 308 LYS THR GLY GLN LEU ALA ALA ILE LYS VAL MET ASP VAL
SEQRES 5 C 308 THR GLY ASP GLU GLU GLU GLU ILE LYS GLN GLU ILE ASN
SEQRES 6 C 308 MET LEU LYS LYS TYR SER HIS HIS ARG ASN ILE ALA THR
SEQRES 7 C 308 TYR TYR GLY ALA PHE ILE LYS LYS ASN PRO PRO GLY MET
SEQRES 8 C 308 ASP ASP GLN LEU TRP LEU VAL MET GLU PHE CYS GLY ALA
SEQRES 9 C 308 GLY SER VAL THR ASP LEU ILE LYS ASN THR LYS GLY ASN
SEQRES 10 C 308 THR LEU LYS GLU GLU TRP ILE ALA TYR ILE CYS ARG GLU
SEQRES 11 C 308 ILE LEU ARG GLY LEU SER HIS LEU HIS GLN HIS LYS VAL
SEQRES 12 C 308 ILE HIS ARG ASP ILE LYS GLY GLN ASN VAL LEU LEU THR
SEQRES 13 C 308 GLU ASN ALA GLU VAL LYS LEU VAL ASP PHE GLY VAL SER
SEQRES 14 C 308 ALA GLN LEU ASP ARG THR VAL GLY ARG ARG ASN THR PHE
SEQRES 15 C 308 ILE GLY THR PRO TYR TRP MET ALA PRO GLU VAL ILE ALA
SEQRES 16 C 308 CYS ASP GLU ASN PRO ASP ALA THR TYR ASP PHE LYS SER
SEQRES 17 C 308 ASP LEU TRP SER LEU GLY ILE THR ALA ILE GLU MET ALA
SEQRES 18 C 308 GLU GLY ALA PRO PRO LEU CYS ASP MET HIS PRO MET ARG
SEQRES 19 C 308 ALA LEU PHE LEU ILE PRO ARG ASN PRO ALA PRO ARG LEU
SEQRES 20 C 308 LYS SER LYS LYS TRP SER LYS LYS PHE GLN SER PHE ILE
SEQRES 21 C 308 GLU SER CYS LEU VAL LYS ASN HIS SER GLN ARG PRO ALA
SEQRES 22 C 308 THR GLU GLN LEU MET LYS HIS PRO PHE ILE ARG ASP GLN
SEQRES 23 C 308 PRO ASN GLU ARG GLN VAL ARG ILE GLN LEU LYS ASP HIS
SEQRES 24 C 308 ILE ASP ARG THR LYS LYS LYS ARG GLY
HET 58C A 401 28
HET SO4 A 402 5
HET 58C B 401 28
HET 58C C 401 28
HET SO4 C 402 5
HET SO4 C 403 5
HETNAM 58C CIS-4-{[2-(1H-BENZIMIDAZOL-5-YLAMINO)QUINAZOLIN-8-
HETNAM 2 58C YL]OXY}CYCLOHEXANOL
HETNAM SO4 SULFATE ION
FORMUL 4 58C 3(C21 H21 N5 O2)
FORMUL 5 SO4 3(O4 S 2-)
FORMUL 10 HOH *7(H2 O)
HELIX 1 AA1 ASP A 14 LEU A 18 5 5
HELIX 2 AA2 ASP A 61 SER A 77 1 17
HELIX 3 AA3 SER A 112 ASN A 119 1 8
HELIX 4 AA4 THR A 120 THR A 124 5 5
HELIX 5 AA5 LYS A 126 HIS A 147 1 22
HELIX 6 AA6 ALA A 196 ILE A 200 5 5
HELIX 7 AA7 ASP A 211 GLY A 229 1 19
HELIX 8 AA8 HIS A 237 ASN A 248 1 12
HELIX 9 AA9 SER A 259 LEU A 270 1 12
HELIX 10 AB1 ASN A 273 ARG A 277 5 5
HELIX 11 AB2 ALA A 279 LYS A 285 1 7
HELIX 12 AB3 HIS A 286 ASP A 291 1 6
HELIX 13 AB4 ASN A 294 THR A 309 1 16
HELIX 14 AB5 ASP B 14 LEU B 18 5 5
HELIX 15 AB6 THR B 59 ASP B 61 5 3
HELIX 16 AB7 GLU B 62 SER B 77 1 16
HELIX 17 AB8 SER B 112 ASN B 119 1 8
HELIX 18 AB9 LYS B 126 HIS B 147 1 22
HELIX 19 AC1 ASP B 211 GLY B 229 1 19
HELIX 20 AC2 HIS B 237 ASN B 248 1 12
HELIX 21 AC3 SER B 259 LEU B 270 1 12
HELIX 22 AC4 ALA B 279 LYS B 285 1 7
HELIX 23 AC5 HIS B 286 ASP B 291 1 6
HELIX 24 AC6 ASN B 294 ASP B 307 1 14
HELIX 25 AC7 GLU C 62 SER C 77 1 16
HELIX 26 AC8 VAL C 113 ASN C 119 1 7
HELIX 27 AC9 LYS C 126 HIS C 147 1 22
HELIX 28 AD1 LYS C 155 GLN C 157 5 3
HELIX 29 AD2 ASP C 211 GLY C 229 1 19
HELIX 30 AD3 HIS C 237 ILE C 245 1 9
HELIX 31 AD4 SER C 259 LEU C 270 1 12
HELIX 32 AD5 ALA C 279 LYS C 285 1 7
HELIX 33 AD6 HIS C 286 ASP C 291 1 6
HELIX 34 AD7 ASN C 294 THR C 309 1 16
SHEET 1 AA1 5 PHE A 25 GLY A 34 0
SHEET 2 AA1 5 GLY A 37 HIS A 44 -1 O VAL A 39 N GLY A 32
SHEET 3 AA1 5 LEU A 50 VAL A 58 -1 O VAL A 55 N GLN A 38
SHEET 4 AA1 5 ASP A 99 MET A 105 -1 O ASP A 99 N VAL A 58
SHEET 5 AA1 5 TYR A 85 LYS A 91 -1 N PHE A 89 O TRP A 102
SHEET 1 AA2 2 VAL A 159 LEU A 161 0
SHEET 2 AA2 2 VAL A 167 LEU A 169 -1 O LYS A 168 N LEU A 160
SHEET 1 AA3 5 PHE B 25 GLY B 34 0
SHEET 2 AA3 5 GLY B 37 HIS B 44 -1 O LYS B 41 N GLU B 29
SHEET 3 AA3 5 LEU B 50 VAL B 58 -1 O ILE B 53 N TYR B 40
SHEET 4 AA3 5 ASP B 99 MET B 105 -1 O MET B 105 N ALA B 52
SHEET 5 AA3 5 TYR B 85 LYS B 91 -1 N PHE B 89 O TRP B 102
SHEET 1 AA4 2 VAL B 159 LEU B 161 0
SHEET 2 AA4 2 VAL B 167 LEU B 169 -1 O LYS B 168 N LEU B 160
SHEET 1 AA5 5 PHE C 25 GLY C 32 0
SHEET 2 AA5 5 GLN C 38 HIS C 44 -1 O VAL C 39 N GLY C 32
SHEET 3 AA5 5 LEU C 50 VAL C 58 -1 O ILE C 53 N TYR C 40
SHEET 4 AA5 5 ASP C 99 MET C 105 -1 O LEU C 101 N MET C 56
SHEET 5 AA5 5 TYR C 85 LYS C 91 -1 N PHE C 89 O TRP C 102
SHEET 1 AA6 3 GLY C 111 SER C 112 0
SHEET 2 AA6 3 VAL C 159 LEU C 161 -1 O LEU C 161 N GLY C 111
SHEET 3 AA6 3 VAL C 167 LEU C 169 -1 O LYS C 168 N LEU C 160
SITE 1 AC1 13 VAL A 31 ASN A 33 VAL A 39 ALA A 52
SITE 2 AC1 13 MET A 105 GLU A 106 CYS A 108 GLY A 111
SITE 3 AC1 13 SER A 112 ASP A 115 GLN A 157 LEU A 160
SITE 4 AC1 13 VAL A 170
SITE 1 AC2 5 ARG A 19 ASP B 211 LYS B 213 HIS B 274
SITE 2 AC2 5 SER B 275
SITE 1 AC3 12 VAL B 31 VAL B 39 ALA B 52 MET B 105
SITE 2 AC3 12 GLU B 106 PHE B 107 CYS B 108 GLY B 111
SITE 3 AC3 12 ASP B 115 GLN B 157 LEU B 160 VAL B 170
SITE 1 AC4 11 VAL C 31 ALA C 52 MET C 105 GLU C 106
SITE 2 AC4 11 CYS C 108 GLY C 111 ASP C 115 GLN C 157
SITE 3 AC4 11 LEU C 160 VAL C 170 ASP C 171
SITE 1 AC5 5 ARG B 19 ASP C 211 LYS C 213 HIS C 274
SITE 2 AC5 5 SER C 275
SITE 1 AC6 4 LYS A 213 HIS A 274 SER A 275 ARG C 19
CRYST1 212.620 124.972 49.897 90.00 96.32 90.00 C 1 2 1 12
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 0.004703 0.000000 0.000521 0.00000
SCALE2 0.000000 0.008002 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020164 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
