HEADER TRANSFERASE/TRANSFERASE INHIBITOR 03-NOV-15 5EKO
TITLE CRYSTAL STRUCTURE OF MAPK13 COMPLEX WITH INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 13;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MAPK 13,MITOGEN-ACTIVATED PROTEIN KINASE P38 DELTA,MAP
COMPND 5 KINASE P38 DELTA,STRESS-ACTIVATED PROTEIN KINASE 4;
COMPND 6 EC: 2.7.11.24;
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: MAPK13, PRKM13, SAPK4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS KINASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.J.BRETT,C.A.MILLER,Z.YURTSEVER
REVDAT 7 27-SEP-23 5EKO 1 REMARK
REVDAT 6 04-DEC-19 5EKO 1 REMARK
REVDAT 5 01-NOV-17 5EKO 1 REMARK
REVDAT 4 20-SEP-17 5EKO 1 JRNL REMARK
REVDAT 3 14-SEP-16 5EKO 1 JRNL
REVDAT 2 20-JUL-16 5EKO 1 JRNL
REVDAT 1 06-JUL-16 5EKO 0
JRNL AUTH Z.YURTSEVER,D.A.PATEL,D.L.KOBER,A.SU,C.A.MILLER,A.G.ROMERO,
JRNL AUTH 2 M.J.HOLTZMAN,T.J.BRETT
JRNL TITL FIRST COMPREHENSIVE STRUCTURAL AND BIOPHYSICAL ANALYSIS OF
JRNL TITL 2 MAPK13 INHIBITORS TARGETING DFG-IN AND DFG-OUT BINDING
JRNL TITL 3 MODES.
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1860 2335 2016
JRNL REFN ISSN 0006-3002
JRNL PMID 27369736
JRNL DOI 10.1016/J.BBAGEN.2016.06.023
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_2155: ???)
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 81.1
REMARK 3 NUMBER OF REFLECTIONS : 22368
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 : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 1142
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 32.7206 - 3.9980 0.82 2859 136 0.1782 0.2158
REMARK 3 2 3.9980 - 3.1742 0.67 2206 119 0.1828 0.2145
REMARK 3 3 3.1742 - 2.7732 0.89 2892 157 0.2042 0.2311
REMARK 3 4 2.7732 - 2.5197 0.90 2937 141 0.2106 0.2601
REMARK 3 5 2.5197 - 2.3392 0.91 2927 169 0.2166 0.2563
REMARK 3 6 2.3392 - 2.2013 0.51 1640 75 0.2415 0.3059
REMARK 3 7 2.2013 - 2.0911 0.92 2956 172 0.2441 0.2956
REMARK 3 8 2.0911 - 2.0001 0.88 2809 173 0.2648 0.3246
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.890
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.30
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 2870
REMARK 3 ANGLE : 0.904 3878
REMARK 3 CHIRALITY : 0.043 418
REMARK 3 PLANARITY : 0.004 491
REMARK 3 DIHEDRAL : 16.885 1720
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 5EKO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215079.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-AUG-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0070
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK HIGH-RESOLUTION
REMARK 200 DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22441
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 81.2
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : 0.05500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.36900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
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: 4YNO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM AMMONIUM TARTRATE, 18% PEG3350,
REMARK 280 PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K
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 30.63150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.53400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.83450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 46.53400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.63150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.83450
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 300 REMARK: MONOMER ACCORDING TO SIZE EXCLUSION CHROMATOGRAPHY
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 MET A -18
REMARK 465 GLY A -17
REMARK 465 SER A -16
REMARK 465 SER A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 SER A -8
REMARK 465 SER A -7
REMARK 465 GLY A -6
REMARK 465 LEU A -5
REMARK 465 VAL A -4
REMARK 465 PRO A -3
REMARK 465 ARG A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 ALA A 172
REMARK 465 ARG A 173
REMARK 465 HIS A 174
REMARK 465 ALA A 175
REMARK 465 ASP A 176
REMARK 465 ALA A 177
REMARK 465 GLU A 178
REMARK 465 MET A 179
REMARK 465 THR A 180
REMARK 465 ILE A 352
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 LYS A 268 O HOH A 501 1.91
REMARK 500 O HOH A 665 O HOH A 702 1.99
REMARK 500 O HOH A 658 O HOH A 673 2.00
REMARK 500 O HOH A 610 O HOH A 678 2.00
REMARK 500 O HOH A 686 O HOH A 709 2.05
REMARK 500 NH2 ARG A 58 O HOH A 502 2.06
REMARK 500 OH TYR A 101 O HOH A 503 2.10
REMARK 500 O HOH A 525 O HOH A 700 2.11
REMARK 500 NZ LYS A 7 O HOH A 504 2.12
REMARK 500 O HOH A 512 O HOH A 689 2.14
REMARK 500 O HOH A 533 O HOH A 695 2.18
REMARK 500 O LEU A 250 O HOH A 505 2.19
REMARK 500 NE2 GLN A 115 O HOH A 506 2.19
REMARK 500 N LEU A 171 O HOH A 507 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 663 O HOH A 670 3544 2.08
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 47 -1.44 -147.55
REMARK 500 ARG A 58 62.28 39.82
REMARK 500 THR A 112 -159.01 -150.34
REMARK 500 MET A 118 -153.66 -78.02
REMARK 500 ARG A 149 -16.86 81.13
REMARK 500 TYR A 182 -134.48 38.30
REMARK 500 SER A 196 45.33 37.68
REMARK 500 LYS A 224 -152.02 -127.55
REMARK 500 ARG A 267 -90.79 -83.42
REMARK 500 LYS A 268 -102.14 -109.15
REMARK 500 ASP A 269 70.81 42.73
REMARK 500 PHE A 274 78.96 -114.22
REMARK 500 SER A 327 -65.21 107.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ARG A 267 LYS A 268 -139.61
REMARK 500 LYS A 268 ASP A 269 -143.31
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 712 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH A 713 DISTANCE = 6.67 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue N17 A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4YNO RELATED DB: PDB
REMARK 900 SAME MOLECULE WITHOUT INHIBITOR
REMARK 900 RELATED ID: 4MYG RELATED DB: PDB
REMARK 900 SAME MOLECULE WITHOUT INHIBITOR IN ACTIVE FORM
REMARK 900 RELATED ID: 4EYJ RELATED DB: PDB
REMARK 900 SAME MOLECULE IN COMPLEX WITH A DIFFERENT INHIBITOR
REMARK 900 RELATED ID: 4EYM RELATED DB: PDB
REMARK 900 SAME MOLECULE IN COMPLEX WITH A DIFFERENT INHIBITOR
REMARK 900 RELATED ID: 5EKN RELATED DB: PDB
REMARK 900 SAME MOLECULE IN COMPLEX WITH A DIFFERENT INHIBITOR
DBREF 5EKO A 1 352 UNP O15264 MK13_HUMAN 1 352
SEQADV 5EKO MET A -18 UNP O15264 EXPRESSION TAG
SEQADV 5EKO GLY A -17 UNP O15264 EXPRESSION TAG
SEQADV 5EKO SER A -16 UNP O15264 EXPRESSION TAG
SEQADV 5EKO SER A -15 UNP O15264 EXPRESSION TAG
SEQADV 5EKO HIS A -14 UNP O15264 EXPRESSION TAG
SEQADV 5EKO HIS A -13 UNP O15264 EXPRESSION TAG
SEQADV 5EKO HIS A -12 UNP O15264 EXPRESSION TAG
SEQADV 5EKO HIS A -11 UNP O15264 EXPRESSION TAG
SEQADV 5EKO HIS A -10 UNP O15264 EXPRESSION TAG
SEQADV 5EKO HIS A -9 UNP O15264 EXPRESSION TAG
SEQADV 5EKO SER A -8 UNP O15264 EXPRESSION TAG
SEQADV 5EKO SER A -7 UNP O15264 EXPRESSION TAG
SEQADV 5EKO GLY A -6 UNP O15264 EXPRESSION TAG
SEQADV 5EKO LEU A -5 UNP O15264 EXPRESSION TAG
SEQADV 5EKO VAL A -4 UNP O15264 EXPRESSION TAG
SEQADV 5EKO PRO A -3 UNP O15264 EXPRESSION TAG
SEQADV 5EKO ARG A -2 UNP O15264 EXPRESSION TAG
SEQADV 5EKO GLY A -1 UNP O15264 EXPRESSION TAG
SEQADV 5EKO SER A 0 UNP O15264 EXPRESSION TAG
SEQRES 1 A 371 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 371 LEU VAL PRO ARG GLY SER MET SER LEU ILE ARG LYS LYS
SEQRES 3 A 371 GLY PHE TYR LYS GLN ASP VAL ASN LYS THR ALA TRP GLU
SEQRES 4 A 371 LEU PRO LYS THR TYR VAL SER PRO THR HIS VAL GLY SER
SEQRES 5 A 371 GLY ALA TYR GLY SER VAL CYS SER ALA ILE ASP LYS ARG
SEQRES 6 A 371 SER GLY GLU LYS VAL ALA ILE LYS LYS LEU SER ARG PRO
SEQRES 7 A 371 PHE GLN SER GLU ILE PHE ALA LYS ARG ALA TYR ARG GLU
SEQRES 8 A 371 LEU LEU LEU LEU LYS HIS MET GLN HIS GLU ASN VAL ILE
SEQRES 9 A 371 GLY LEU LEU ASP VAL PHE THR PRO ALA SER SER LEU ARG
SEQRES 10 A 371 ASN PHE TYR ASP PHE TYR LEU VAL MET PRO PHE MET GLN
SEQRES 11 A 371 THR ASP LEU GLN LYS ILE MET GLY MET GLU PHE SER GLU
SEQRES 12 A 371 GLU LYS ILE GLN TYR LEU VAL TYR GLN MET LEU LYS GLY
SEQRES 13 A 371 LEU LYS TYR ILE HIS SER ALA GLY VAL VAL HIS ARG ASP
SEQRES 14 A 371 LEU LYS PRO GLY ASN LEU ALA VAL ASN GLU ASP CYS GLU
SEQRES 15 A 371 LEU LYS ILE LEU ASP PHE GLY LEU ALA ARG HIS ALA ASP
SEQRES 16 A 371 ALA GLU MET THR GLY TYR VAL VAL THR ARG TRP TYR ARG
SEQRES 17 A 371 ALA PRO GLU VAL ILE LEU SER TRP MET HIS TYR ASN GLN
SEQRES 18 A 371 THR VAL ASP ILE TRP SER VAL GLY CYS ILE MET ALA GLU
SEQRES 19 A 371 MET LEU THR GLY LYS THR LEU PHE LYS GLY LYS ASP TYR
SEQRES 20 A 371 LEU ASP GLN LEU THR GLN ILE LEU LYS VAL THR GLY VAL
SEQRES 21 A 371 PRO GLY THR GLU PHE VAL GLN LYS LEU ASN ASP LYS ALA
SEQRES 22 A 371 ALA LYS SER TYR ILE GLN SER LEU PRO GLN THR PRO ARG
SEQRES 23 A 371 LYS ASP PHE THR GLN LEU PHE PRO ARG ALA SER PRO GLN
SEQRES 24 A 371 ALA ALA ASP LEU LEU GLU LYS MET LEU GLU LEU ASP VAL
SEQRES 25 A 371 ASP LYS ARG LEU THR ALA ALA GLN ALA LEU THR HIS PRO
SEQRES 26 A 371 PHE PHE GLU PRO PHE ARG ASP PRO GLU GLU GLU THR GLU
SEQRES 27 A 371 ALA GLN GLN PRO PHE ASP ASP SER LEU GLU HIS GLU LYS
SEQRES 28 A 371 LEU THR VAL ASP GLU TRP LYS GLN HIS ILE TYR LYS GLU
SEQRES 29 A 371 ILE VAL ASN PHE SER PRO ILE
HET N17 A 401 28
HETNAM N17 3-(4-METHYL-1H-IMIDAZOL-1-YL)-N-[4-(PYRIDIN-4-YLOXY)
HETNAM 2 N17 PHENYL]BENZAMIDE
FORMUL 2 N17 C22 H18 N4 O2
FORMUL 3 HOH *213(H2 O)
HELIX 1 AA1 SER A 62 MET A 79 1 18
HELIX 2 AA2 LEU A 114 MET A 118 1 5
HELIX 3 AA3 SER A 123 ALA A 144 1 22
HELIX 4 AA4 LYS A 152 GLY A 154 5 3
HELIX 5 AA5 ALA A 190 SER A 196 1 7
HELIX 6 AA6 THR A 203 GLY A 219 1 17
HELIX 7 AA7 ASP A 227 GLY A 240 1 14
HELIX 8 AA8 GLY A 243 LEU A 250 1 8
HELIX 9 AA9 ASP A 252 LEU A 262 1 11
HELIX 10 AB1 ASP A 269 PHE A 274 1 6
HELIX 11 AB2 SER A 278 LEU A 289 1 12
HELIX 12 AB3 THR A 298 THR A 304 1 7
HELIX 13 AB4 HIS A 305 GLU A 309 5 5
HELIX 14 AB5 ASP A 313 GLU A 317 5 5
HELIX 15 AB6 THR A 334 PHE A 349 1 16
SHEET 1 AA1 2 PHE A 9 VAL A 14 0
SHEET 2 AA1 2 THR A 17 PRO A 22 -1 O THR A 17 N VAL A 14
SHEET 1 AA2 5 TYR A 25 SER A 33 0
SHEET 2 AA2 5 GLY A 37 ASP A 44 -1 O VAL A 39 N GLY A 32
SHEET 3 AA2 5 LYS A 50 LEU A 56 -1 O ILE A 53 N CYS A 40
SHEET 4 AA2 5 TYR A 104 PRO A 108 -1 O MET A 107 N ALA A 52
SHEET 5 AA2 5 ASP A 89 PHE A 91 -1 N PHE A 91 O TYR A 104
SHEET 1 AA3 3 THR A 112 ASP A 113 0
SHEET 2 AA3 3 LEU A 156 VAL A 158 -1 O VAL A 158 N THR A 112
SHEET 3 AA3 3 LEU A 164 ILE A 166 -1 O LYS A 165 N ALA A 157
CISPEP 1 ASP A 326 SER A 327 0 15.62
SITE 1 AC1 13 VAL A 39 ALA A 52 ARG A 68 GLU A 72
SITE 2 AC1 13 LEU A 76 ILE A 85 MET A 107 PRO A 108
SITE 3 AC1 13 MET A 110 LEU A 167 ASP A 168 PHE A 169
SITE 4 AC1 13 LEU A 171
CRYST1 61.263 69.669 93.068 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 0.016323 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014354 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010745 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
