HEADER TRANSFERASE/TRANSFERASE INHIBITOR 23-APR-13 4KBA
TITLE CK1D IN COMPLEX WITH 9-[3-(4-FLUOROPHENYL)-1-METHYL-1H-PYRAZOL-4-YL]-
TITLE 2 2,3,4,5-TETRAHYDROPYRIDO[2,3-F][1,4]OXAZEPINE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASEIN KINASE I ISOFORM DELTA;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: CKI-DELTA, CKID, TAU-PROTEIN KINASE CSNK1D;
COMPND 5 EC: 2.7.11.1, 2.7.11.26;
COMPND 6 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: CSNK1D, HCKID;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9
KEYWDS SER/THR KINASE, INHIBITOR, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LIU
REVDAT 3 28-FEB-24 4KBA 1 REMARK SEQADV
REVDAT 2 25-SEP-13 4KBA 1 JRNL
REVDAT 1 18-SEP-13 4KBA 0
JRNL AUTH S.MENTE,E.ARNOLD,T.BUTLER,S.CHAKRAPANI,R.CHANDRASEKARAN,
JRNL AUTH 2 K.CHERRY,K.DIRICO,A.DORAN,K.FISHER,P.GALATSIS,M.GREEN,
JRNL AUTH 3 M.HAYWARD,J.HUMPHREY,J.KNAFELS,J.LI,S.LIU,M.MARCONI,
JRNL AUTH 4 S.MCDONALD,J.OHREN,V.PARADIS,B.SNEED,K.WALTON,T.WAGER
JRNL TITL LIGAND-PROTEIN INTERACTIONS OF SELECTIVE CASEIN KINASE 1
JRNL TITL 2 DELTA INHIBITORS.
JRNL REF J.MED.CHEM. V. 56 6819 2013
JRNL REFN ISSN 0022-2623
JRNL PMID 23919824
JRNL DOI 10.1021/JM4006324
REMARK 2
REMARK 2 RESOLUTION. 1.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.2
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) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 85598
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) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 4379
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) : 1.98
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.03
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.09
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 6066
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2036
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5766
REMARK 3 BIN R VALUE (WORKING SET) : 0.2017
REMARK 3 BIN FREE R VALUE : 0.2412
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.95
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 300
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 : 8948
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 141
REMARK 3 SOLVENT ATOMS : 176
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.34
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.27830
REMARK 3 B22 (A**2) : 1.22240
REMARK 3 B33 (A**2) : 1.05590
REMARK 3 B12 (A**2) : 2.35690
REMARK 3 B13 (A**2) : -0.35220
REMARK 3 B23 (A**2) : -2.54990
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.314
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) : 0.183
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 : 0.916
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.889
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 9375 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 12663 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 3318 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 200 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1460 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 9375 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1119 ; 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 : 10501 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.03
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.79
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 19.36
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|3 - A|293 A|401 - A|401 }
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0296 -0.6303 0.9696
REMARK 3 T TENSOR
REMARK 3 T11: -0.1313 T22: 0.2673
REMARK 3 T33: -0.1210 T12: 0.0776
REMARK 3 T13: 0.0695 T23: 0.1714
REMARK 3 L TENSOR
REMARK 3 L11: 1.3537 L22: 0.4488
REMARK 3 L33: 1.5409 L12: 0.3266
REMARK 3 L13: -0.2486 L23: -0.1355
REMARK 3 S TENSOR
REMARK 3 S11: 0.0490 S12: -0.0816 S13: 0.0550
REMARK 3 S21: -0.0466 S22: 0.0378 S23: 0.0810
REMARK 3 S31: -0.1014 S32: -0.1127 S33: -0.0868
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|3 - B|293 B|401 - B|401 }
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6874 16.7904 -37.7309
REMARK 3 T TENSOR
REMARK 3 T11: -0.0416 T22: 0.2419
REMARK 3 T33: -0.1611 T12: -0.0360
REMARK 3 T13: 0.0552 T23: 0.1141
REMARK 3 L TENSOR
REMARK 3 L11: 0.8011 L22: 0.7185
REMARK 3 L33: 2.2919 L12: 0.1373
REMARK 3 L13: -0.3724 L23: -0.9404
REMARK 3 S TENSOR
REMARK 3 S11: 0.0355 S12: -0.1200 S13: 0.0334
REMARK 3 S21: 0.0959 S22: -0.0446 S23: 0.0230
REMARK 3 S31: -0.3553 S32: 0.3263 S33: 0.0090
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { C|7 - C|293 C|401 - C|401 }
REMARK 3 ORIGIN FOR THE GROUP (A): -0.4596 -22.8877 -41.1461
REMARK 3 T TENSOR
REMARK 3 T11: -0.0974 T22: 0.2211
REMARK 3 T33: -0.1372 T12: 0.0451
REMARK 3 T13: -0.0083 T23: 0.1637
REMARK 3 L TENSOR
REMARK 3 L11: 1.6459 L22: 0.2867
REMARK 3 L33: 1.5680 L12: -0.3364
REMARK 3 L13: 0.2590 L23: 0.0197
REMARK 3 S TENSOR
REMARK 3 S11: 0.0615 S12: 0.0435 S13: -0.0687
REMARK 3 S21: 0.0628 S22: 0.0417 S23: 0.0741
REMARK 3 S31: 0.0945 S32: -0.1800 S33: -0.1031
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { D|3 - D|293 D|401 - D|401 }
REMARK 3 ORIGIN FOR THE GROUP (A): 17.1413 -39.1352 -2.8801
REMARK 3 T TENSOR
REMARK 3 T11: -0.0322 T22: 0.2594
REMARK 3 T33: -0.1740 T12: 0.1413
REMARK 3 T13: -0.0174 T23: 0.1296
REMARK 3 L TENSOR
REMARK 3 L11: 0.8780 L22: 0.6241
REMARK 3 L33: 2.1290 L12: -0.1847
REMARK 3 L13: 0.2028 L23: -0.8238
REMARK 3 S TENSOR
REMARK 3 S11: 0.0263 S12: 0.0857 S13: -0.0353
REMARK 3 S21: -0.0853 S22: -0.0253 S23: 0.0330
REMARK 3 S31: 0.2955 S32: 0.3183 S33: -0.0010
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4KBA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-APR-13.
REMARK 100 THE DEPOSITION ID IS D_1000079123.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
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 : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85686
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.980
REMARK 200 RESOLUTION RANGE LOW (A) : 80.950
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL
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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -24.17692
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -28.89705
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 80.95147
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 24.51208
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -28.89705
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 80.95147
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 -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 SER A -6
REMARK 465 SER A -5
REMARK 465 GLY A -4
REMARK 465 LEU A -3
REMARK 465 VAL A -2
REMARK 465 PRO A -1
REMARK 465 ARG A 0
REMARK 465 GLY A 1
REMARK 465 SER A 2
REMARK 465 ARG A 157
REMARK 465 ASP A 158
REMARK 465 ALA A 159
REMARK 465 ARG A 160
REMARK 465 THR A 161
REMARK 465 HIS A 162
REMARK 465 GLN A 163
REMARK 465 HIS A 164
REMARK 465 ILE A 165
REMARK 465 PRO A 166
REMARK 465 TYR A 167
REMARK 465 ARG A 168
REMARK 465 GLU A 169
REMARK 465 ASN A 170
REMARK 465 LYS A 171
REMARK 465 ASN A 172
REMARK 465 LEU A 173
REMARK 465 THR A 174
REMARK 465 LYS A 217
REMARK 465 ALA A 218
REMARK 465 ALA A 219
REMARK 465 THR A 220
REMARK 465 LYS A 221
REMARK 465 ARG A 222
REMARK 465 GLN A 223
REMARK 465 LYS A 224
REMARK 465 TYR A 225
REMARK 465 GLU A 226
REMARK 465 LYS A 294
REMARK 465 PHE A 295
REMARK 465 GLY A 296
REMARK 465 ALA A 297
REMARK 465 SER A 298
REMARK 465 ARG A 299
REMARK 465 ALA A 300
REMARK 465 ALA A 301
REMARK 465 ASP A 302
REMARK 465 ASP A 303
REMARK 465 ALA A 304
REMARK 465 GLU A 305
REMARK 465 ARG A 306
REMARK 465 GLU A 307
REMARK 465 ARG A 308
REMARK 465 ARG A 309
REMARK 465 ASP A 310
REMARK 465 ARG A 311
REMARK 465 GLU A 312
REMARK 465 GLU A 313
REMARK 465 ARG A 314
REMARK 465 LEU A 315
REMARK 465 ARG A 316
REMARK 465 HIS A 317
REMARK 465 MET B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 SER B -6
REMARK 465 SER B -5
REMARK 465 GLY B -4
REMARK 465 LEU B -3
REMARK 465 VAL B -2
REMARK 465 PRO B -1
REMARK 465 ARG B 0
REMARK 465 GLY B 1
REMARK 465 SER B 2
REMARK 465 VAL B 42
REMARK 465 LYS B 43
REMARK 465 THR B 44
REMARK 465 LYS B 45
REMARK 465 HIS B 46
REMARK 465 PRO B 47
REMARK 465 LYS B 294
REMARK 465 PHE B 295
REMARK 465 GLY B 296
REMARK 465 ALA B 297
REMARK 465 SER B 298
REMARK 465 ARG B 299
REMARK 465 ALA B 300
REMARK 465 ALA B 301
REMARK 465 ASP B 302
REMARK 465 ASP B 303
REMARK 465 ALA B 304
REMARK 465 GLU B 305
REMARK 465 ARG B 306
REMARK 465 GLU B 307
REMARK 465 ARG B 308
REMARK 465 ARG B 309
REMARK 465 ASP B 310
REMARK 465 ARG B 311
REMARK 465 GLU B 312
REMARK 465 GLU B 313
REMARK 465 ARG B 314
REMARK 465 LEU B 315
REMARK 465 ARG B 316
REMARK 465 HIS B 317
REMARK 465 MET C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 HIS C -9
REMARK 465 HIS C -8
REMARK 465 HIS C -7
REMARK 465 SER C -6
REMARK 465 SER C -5
REMARK 465 GLY C -4
REMARK 465 LEU C -3
REMARK 465 VAL C -2
REMARK 465 PRO C -1
REMARK 465 ARG C 0
REMARK 465 GLY C 1
REMARK 465 SER C 2
REMARK 465 LEU C 3
REMARK 465 ARG C 4
REMARK 465 VAL C 5
REMARK 465 GLY C 6
REMARK 465 ARG C 157
REMARK 465 ASP C 158
REMARK 465 ALA C 159
REMARK 465 ARG C 160
REMARK 465 THR C 161
REMARK 465 HIS C 162
REMARK 465 GLN C 163
REMARK 465 HIS C 164
REMARK 465 ILE C 165
REMARK 465 PRO C 166
REMARK 465 LYS C 294
REMARK 465 PHE C 295
REMARK 465 GLY C 296
REMARK 465 ALA C 297
REMARK 465 SER C 298
REMARK 465 ARG C 299
REMARK 465 ALA C 300
REMARK 465 ALA C 301
REMARK 465 ASP C 302
REMARK 465 ASP C 303
REMARK 465 ALA C 304
REMARK 465 GLU C 305
REMARK 465 ARG C 306
REMARK 465 GLU C 307
REMARK 465 ARG C 308
REMARK 465 ARG C 309
REMARK 465 ASP C 310
REMARK 465 ARG C 311
REMARK 465 GLU C 312
REMARK 465 GLU C 313
REMARK 465 ARG C 314
REMARK 465 LEU C 315
REMARK 465 ARG C 316
REMARK 465 HIS C 317
REMARK 465 MET D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 HIS D -9
REMARK 465 HIS D -8
REMARK 465 HIS D -7
REMARK 465 SER D -6
REMARK 465 SER D -5
REMARK 465 GLY D -4
REMARK 465 LEU D -3
REMARK 465 VAL D -2
REMARK 465 PRO D -1
REMARK 465 ARG D 0
REMARK 465 GLY D 1
REMARK 465 SER D 2
REMARK 465 SER D 17
REMARK 465 GLY D 18
REMARK 465 SER D 19
REMARK 465 PHE D 20
REMARK 465 GLY D 21
REMARK 465 VAL D 42
REMARK 465 LYS D 43
REMARK 465 THR D 44
REMARK 465 LYS D 45
REMARK 465 HIS D 46
REMARK 465 ARG D 157
REMARK 465 ASP D 158
REMARK 465 ALA D 159
REMARK 465 ARG D 160
REMARK 465 THR D 161
REMARK 465 HIS D 162
REMARK 465 GLN D 163
REMARK 465 LYS D 294
REMARK 465 PHE D 295
REMARK 465 GLY D 296
REMARK 465 ALA D 297
REMARK 465 SER D 298
REMARK 465 ARG D 299
REMARK 465 ALA D 300
REMARK 465 ALA D 301
REMARK 465 ASP D 302
REMARK 465 ASP D 303
REMARK 465 ALA D 304
REMARK 465 GLU D 305
REMARK 465 ARG D 306
REMARK 465 GLU D 307
REMARK 465 ARG D 308
REMARK 465 ARG D 309
REMARK 465 ASP D 310
REMARK 465 ARG D 311
REMARK 465 GLU D 312
REMARK 465 GLU D 313
REMARK 465 ARG D 314
REMARK 465 LEU D 315
REMARK 465 ARG D 316
REMARK 465 HIS D 317
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 LEU A 3 CG CD1 CD2
REMARK 470 ARG A 4 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 3 CG CD1 CD2
REMARK 470 ARG B 4 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 48 CG CD OE1 NE2
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 ASN A 7 -23.36 68.94
REMARK 500 PHE A 20 52.21 -146.46
REMARK 500 GLU A 40 -62.17 -108.22
REMARK 500 CYS A 41 109.39 122.53
REMARK 500 HIS A 46 75.76 -117.50
REMARK 500 ARG A 127 -6.31 78.43
REMARK 500 ASP A 149 105.13 65.02
REMARK 500 ASN B 7 -25.38 69.17
REMARK 500 ARG B 127 -3.35 76.93
REMARK 500 ASP B 128 52.52 -141.49
REMARK 500 ASP B 149 106.50 62.39
REMARK 500 PHE C 20 22.92 -141.81
REMARK 500 CYS C 41 109.68 112.04
REMARK 500 HIS C 46 78.09 -117.70
REMARK 500 GLN C 48 -7.63 -147.81
REMARK 500 ARG C 127 -4.92 78.99
REMARK 500 ASP C 128 51.61 -140.77
REMARK 500 ASP C 149 104.02 65.26
REMARK 500 LEU C 173 89.66 -68.42
REMARK 500 ALA C 219 -29.38 -157.16
REMARK 500 ASN D 7 -24.48 68.84
REMARK 500 GLU D 74 -96.19 -73.03
REMARK 500 ASP D 76 42.60 -100.22
REMARK 500 ARG D 127 -4.45 77.53
REMARK 500 ASP D 128 52.21 -141.49
REMARK 500 ASP D 149 106.14 62.47
REMARK 500 LEU D 173 94.84 -66.86
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 1QM 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 1QM B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1QM C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1QM D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KB8 RELATED DB: PDB
REMARK 900 RELATED ID: 4KBC RELATED DB: PDB
REMARK 900 RELATED ID: 4KBH RELATED DB: PDB
REMARK 900 RELATED ID: 4KBK RELATED DB: PDB
DBREF 4KBA A 3 317 UNP P48730 KC1D_HUMAN 3 317
DBREF 4KBA B 3 317 UNP P48730 KC1D_HUMAN 3 317
DBREF 4KBA C 3 317 UNP P48730 KC1D_HUMAN 3 317
DBREF 4KBA D 3 317 UNP P48730 KC1D_HUMAN 3 317
SEQADV 4KBA MET A -13 UNP P48730 EXPRESSION TAG
SEQADV 4KBA HIS A -12 UNP P48730 EXPRESSION TAG
SEQADV 4KBA HIS A -11 UNP P48730 EXPRESSION TAG
SEQADV 4KBA HIS A -10 UNP P48730 EXPRESSION TAG
SEQADV 4KBA HIS A -9 UNP P48730 EXPRESSION TAG
SEQADV 4KBA HIS A -8 UNP P48730 EXPRESSION TAG
SEQADV 4KBA HIS A -7 UNP P48730 EXPRESSION TAG
SEQADV 4KBA SER A -6 UNP P48730 EXPRESSION TAG
SEQADV 4KBA SER A -5 UNP P48730 EXPRESSION TAG
SEQADV 4KBA GLY A -4 UNP P48730 EXPRESSION TAG
SEQADV 4KBA LEU A -3 UNP P48730 EXPRESSION TAG
SEQADV 4KBA VAL A -2 UNP P48730 EXPRESSION TAG
SEQADV 4KBA PRO A -1 UNP P48730 EXPRESSION TAG
SEQADV 4KBA ARG A 0 UNP P48730 EXPRESSION TAG
SEQADV 4KBA GLY A 1 UNP P48730 EXPRESSION TAG
SEQADV 4KBA SER A 2 UNP P48730 EXPRESSION TAG
SEQADV 4KBA MET B -13 UNP P48730 EXPRESSION TAG
SEQADV 4KBA HIS B -12 UNP P48730 EXPRESSION TAG
SEQADV 4KBA HIS B -11 UNP P48730 EXPRESSION TAG
SEQADV 4KBA HIS B -10 UNP P48730 EXPRESSION TAG
SEQADV 4KBA HIS B -9 UNP P48730 EXPRESSION TAG
SEQADV 4KBA HIS B -8 UNP P48730 EXPRESSION TAG
SEQADV 4KBA HIS B -7 UNP P48730 EXPRESSION TAG
SEQADV 4KBA SER B -6 UNP P48730 EXPRESSION TAG
SEQADV 4KBA SER B -5 UNP P48730 EXPRESSION TAG
SEQADV 4KBA GLY B -4 UNP P48730 EXPRESSION TAG
SEQADV 4KBA LEU B -3 UNP P48730 EXPRESSION TAG
SEQADV 4KBA VAL B -2 UNP P48730 EXPRESSION TAG
SEQADV 4KBA PRO B -1 UNP P48730 EXPRESSION TAG
SEQADV 4KBA ARG B 0 UNP P48730 EXPRESSION TAG
SEQADV 4KBA GLY B 1 UNP P48730 EXPRESSION TAG
SEQADV 4KBA SER B 2 UNP P48730 EXPRESSION TAG
SEQADV 4KBA MET C -13 UNP P48730 EXPRESSION TAG
SEQADV 4KBA HIS C -12 UNP P48730 EXPRESSION TAG
SEQADV 4KBA HIS C -11 UNP P48730 EXPRESSION TAG
SEQADV 4KBA HIS C -10 UNP P48730 EXPRESSION TAG
SEQADV 4KBA HIS C -9 UNP P48730 EXPRESSION TAG
SEQADV 4KBA HIS C -8 UNP P48730 EXPRESSION TAG
SEQADV 4KBA HIS C -7 UNP P48730 EXPRESSION TAG
SEQADV 4KBA SER C -6 UNP P48730 EXPRESSION TAG
SEQADV 4KBA SER C -5 UNP P48730 EXPRESSION TAG
SEQADV 4KBA GLY C -4 UNP P48730 EXPRESSION TAG
SEQADV 4KBA LEU C -3 UNP P48730 EXPRESSION TAG
SEQADV 4KBA VAL C -2 UNP P48730 EXPRESSION TAG
SEQADV 4KBA PRO C -1 UNP P48730 EXPRESSION TAG
SEQADV 4KBA ARG C 0 UNP P48730 EXPRESSION TAG
SEQADV 4KBA GLY C 1 UNP P48730 EXPRESSION TAG
SEQADV 4KBA SER C 2 UNP P48730 EXPRESSION TAG
SEQADV 4KBA MET D -13 UNP P48730 EXPRESSION TAG
SEQADV 4KBA HIS D -12 UNP P48730 EXPRESSION TAG
SEQADV 4KBA HIS D -11 UNP P48730 EXPRESSION TAG
SEQADV 4KBA HIS D -10 UNP P48730 EXPRESSION TAG
SEQADV 4KBA HIS D -9 UNP P48730 EXPRESSION TAG
SEQADV 4KBA HIS D -8 UNP P48730 EXPRESSION TAG
SEQADV 4KBA HIS D -7 UNP P48730 EXPRESSION TAG
SEQADV 4KBA SER D -6 UNP P48730 EXPRESSION TAG
SEQADV 4KBA SER D -5 UNP P48730 EXPRESSION TAG
SEQADV 4KBA GLY D -4 UNP P48730 EXPRESSION TAG
SEQADV 4KBA LEU D -3 UNP P48730 EXPRESSION TAG
SEQADV 4KBA VAL D -2 UNP P48730 EXPRESSION TAG
SEQADV 4KBA PRO D -1 UNP P48730 EXPRESSION TAG
SEQADV 4KBA ARG D 0 UNP P48730 EXPRESSION TAG
SEQADV 4KBA GLY D 1 UNP P48730 EXPRESSION TAG
SEQADV 4KBA SER D 2 UNP P48730 EXPRESSION TAG
SEQRES 1 A 331 MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO
SEQRES 2 A 331 ARG GLY SER LEU ARG VAL GLY ASN ARG TYR ARG LEU GLY
SEQRES 3 A 331 ARG LYS ILE GLY SER GLY SER PHE GLY ASP ILE TYR LEU
SEQRES 4 A 331 GLY THR ASP ILE ALA ALA GLY GLU GLU VAL ALA ILE LYS
SEQRES 5 A 331 LEU GLU CYS VAL LYS THR LYS HIS PRO GLN LEU HIS ILE
SEQRES 6 A 331 GLU SER LYS ILE TYR LYS MET MET GLN GLY GLY VAL GLY
SEQRES 7 A 331 ILE PRO THR ILE ARG TRP CYS GLY ALA GLU GLY ASP TYR
SEQRES 8 A 331 ASN VAL MET VAL MET GLU LEU LEU GLY PRO SER LEU GLU
SEQRES 9 A 331 ASP LEU PHE ASN PHE CYS SER ARG LYS PHE SER LEU LYS
SEQRES 10 A 331 THR VAL LEU LEU LEU ALA ASP GLN MET ILE SER ARG ILE
SEQRES 11 A 331 GLU TYR ILE HIS SER LYS ASN PHE ILE HIS ARG ASP VAL
SEQRES 12 A 331 LYS PRO ASP ASN PHE LEU MET GLY LEU GLY LYS LYS GLY
SEQRES 13 A 331 ASN LEU VAL TYR ILE ILE ASP PHE GLY LEU ALA LYS LYS
SEQRES 14 A 331 TYR ARG ASP ALA ARG THR HIS GLN HIS ILE PRO TYR ARG
SEQRES 15 A 331 GLU ASN LYS ASN LEU THR GLY THR ALA ARG TYR ALA SER
SEQRES 16 A 331 ILE ASN THR HIS LEU GLY ILE GLU GLN SER ARG ARG ASP
SEQRES 17 A 331 ASP LEU GLU SER LEU GLY TYR VAL LEU MET TYR PHE ASN
SEQRES 18 A 331 LEU GLY SER LEU PRO TRP GLN GLY LEU LYS ALA ALA THR
SEQRES 19 A 331 LYS ARG GLN LYS TYR GLU ARG ILE SER GLU LYS LYS MET
SEQRES 20 A 331 SER THR PRO ILE GLU VAL LEU CYS LYS GLY TYR PRO SER
SEQRES 21 A 331 GLU PHE ALA THR TYR LEU ASN PHE CYS ARG SER LEU ARG
SEQRES 22 A 331 PHE ASP ASP LYS PRO ASP TYR SER TYR LEU ARG GLN LEU
SEQRES 23 A 331 PHE ARG ASN LEU PHE HIS ARG GLN GLY PHE SER TYR ASP
SEQRES 24 A 331 TYR VAL PHE ASP TRP ASN MET LEU LYS PHE GLY ALA SER
SEQRES 25 A 331 ARG ALA ALA ASP ASP ALA GLU ARG GLU ARG ARG ASP ARG
SEQRES 26 A 331 GLU GLU ARG LEU ARG HIS
SEQRES 1 B 331 MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO
SEQRES 2 B 331 ARG GLY SER LEU ARG VAL GLY ASN ARG TYR ARG LEU GLY
SEQRES 3 B 331 ARG LYS ILE GLY SER GLY SER PHE GLY ASP ILE TYR LEU
SEQRES 4 B 331 GLY THR ASP ILE ALA ALA GLY GLU GLU VAL ALA ILE LYS
SEQRES 5 B 331 LEU GLU CYS VAL LYS THR LYS HIS PRO GLN LEU HIS ILE
SEQRES 6 B 331 GLU SER LYS ILE TYR LYS MET MET GLN GLY GLY VAL GLY
SEQRES 7 B 331 ILE PRO THR ILE ARG TRP CYS GLY ALA GLU GLY ASP TYR
SEQRES 8 B 331 ASN VAL MET VAL MET GLU LEU LEU GLY PRO SER LEU GLU
SEQRES 9 B 331 ASP LEU PHE ASN PHE CYS SER ARG LYS PHE SER LEU LYS
SEQRES 10 B 331 THR VAL LEU LEU LEU ALA ASP GLN MET ILE SER ARG ILE
SEQRES 11 B 331 GLU TYR ILE HIS SER LYS ASN PHE ILE HIS ARG ASP VAL
SEQRES 12 B 331 LYS PRO ASP ASN PHE LEU MET GLY LEU GLY LYS LYS GLY
SEQRES 13 B 331 ASN LEU VAL TYR ILE ILE ASP PHE GLY LEU ALA LYS LYS
SEQRES 14 B 331 TYR ARG ASP ALA ARG THR HIS GLN HIS ILE PRO TYR ARG
SEQRES 15 B 331 GLU ASN LYS ASN LEU THR GLY THR ALA ARG TYR ALA SER
SEQRES 16 B 331 ILE ASN THR HIS LEU GLY ILE GLU GLN SER ARG ARG ASP
SEQRES 17 B 331 ASP LEU GLU SER LEU GLY TYR VAL LEU MET TYR PHE ASN
SEQRES 18 B 331 LEU GLY SER LEU PRO TRP GLN GLY LEU LYS ALA ALA THR
SEQRES 19 B 331 LYS ARG GLN LYS TYR GLU ARG ILE SER GLU LYS LYS MET
SEQRES 20 B 331 SER THR PRO ILE GLU VAL LEU CYS LYS GLY TYR PRO SER
SEQRES 21 B 331 GLU PHE ALA THR TYR LEU ASN PHE CYS ARG SER LEU ARG
SEQRES 22 B 331 PHE ASP ASP LYS PRO ASP TYR SER TYR LEU ARG GLN LEU
SEQRES 23 B 331 PHE ARG ASN LEU PHE HIS ARG GLN GLY PHE SER TYR ASP
SEQRES 24 B 331 TYR VAL PHE ASP TRP ASN MET LEU LYS PHE GLY ALA SER
SEQRES 25 B 331 ARG ALA ALA ASP ASP ALA GLU ARG GLU ARG ARG ASP ARG
SEQRES 26 B 331 GLU GLU ARG LEU ARG HIS
SEQRES 1 C 331 MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO
SEQRES 2 C 331 ARG GLY SER LEU ARG VAL GLY ASN ARG TYR ARG LEU GLY
SEQRES 3 C 331 ARG LYS ILE GLY SER GLY SER PHE GLY ASP ILE TYR LEU
SEQRES 4 C 331 GLY THR ASP ILE ALA ALA GLY GLU GLU VAL ALA ILE LYS
SEQRES 5 C 331 LEU GLU CYS VAL LYS THR LYS HIS PRO GLN LEU HIS ILE
SEQRES 6 C 331 GLU SER LYS ILE TYR LYS MET MET GLN GLY GLY VAL GLY
SEQRES 7 C 331 ILE PRO THR ILE ARG TRP CYS GLY ALA GLU GLY ASP TYR
SEQRES 8 C 331 ASN VAL MET VAL MET GLU LEU LEU GLY PRO SER LEU GLU
SEQRES 9 C 331 ASP LEU PHE ASN PHE CYS SER ARG LYS PHE SER LEU LYS
SEQRES 10 C 331 THR VAL LEU LEU LEU ALA ASP GLN MET ILE SER ARG ILE
SEQRES 11 C 331 GLU TYR ILE HIS SER LYS ASN PHE ILE HIS ARG ASP VAL
SEQRES 12 C 331 LYS PRO ASP ASN PHE LEU MET GLY LEU GLY LYS LYS GLY
SEQRES 13 C 331 ASN LEU VAL TYR ILE ILE ASP PHE GLY LEU ALA LYS LYS
SEQRES 14 C 331 TYR ARG ASP ALA ARG THR HIS GLN HIS ILE PRO TYR ARG
SEQRES 15 C 331 GLU ASN LYS ASN LEU THR GLY THR ALA ARG TYR ALA SER
SEQRES 16 C 331 ILE ASN THR HIS LEU GLY ILE GLU GLN SER ARG ARG ASP
SEQRES 17 C 331 ASP LEU GLU SER LEU GLY TYR VAL LEU MET TYR PHE ASN
SEQRES 18 C 331 LEU GLY SER LEU PRO TRP GLN GLY LEU LYS ALA ALA THR
SEQRES 19 C 331 LYS ARG GLN LYS TYR GLU ARG ILE SER GLU LYS LYS MET
SEQRES 20 C 331 SER THR PRO ILE GLU VAL LEU CYS LYS GLY TYR PRO SER
SEQRES 21 C 331 GLU PHE ALA THR TYR LEU ASN PHE CYS ARG SER LEU ARG
SEQRES 22 C 331 PHE ASP ASP LYS PRO ASP TYR SER TYR LEU ARG GLN LEU
SEQRES 23 C 331 PHE ARG ASN LEU PHE HIS ARG GLN GLY PHE SER TYR ASP
SEQRES 24 C 331 TYR VAL PHE ASP TRP ASN MET LEU LYS PHE GLY ALA SER
SEQRES 25 C 331 ARG ALA ALA ASP ASP ALA GLU ARG GLU ARG ARG ASP ARG
SEQRES 26 C 331 GLU GLU ARG LEU ARG HIS
SEQRES 1 D 331 MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO
SEQRES 2 D 331 ARG GLY SER LEU ARG VAL GLY ASN ARG TYR ARG LEU GLY
SEQRES 3 D 331 ARG LYS ILE GLY SER GLY SER PHE GLY ASP ILE TYR LEU
SEQRES 4 D 331 GLY THR ASP ILE ALA ALA GLY GLU GLU VAL ALA ILE LYS
SEQRES 5 D 331 LEU GLU CYS VAL LYS THR LYS HIS PRO GLN LEU HIS ILE
SEQRES 6 D 331 GLU SER LYS ILE TYR LYS MET MET GLN GLY GLY VAL GLY
SEQRES 7 D 331 ILE PRO THR ILE ARG TRP CYS GLY ALA GLU GLY ASP TYR
SEQRES 8 D 331 ASN VAL MET VAL MET GLU LEU LEU GLY PRO SER LEU GLU
SEQRES 9 D 331 ASP LEU PHE ASN PHE CYS SER ARG LYS PHE SER LEU LYS
SEQRES 10 D 331 THR VAL LEU LEU LEU ALA ASP GLN MET ILE SER ARG ILE
SEQRES 11 D 331 GLU TYR ILE HIS SER LYS ASN PHE ILE HIS ARG ASP VAL
SEQRES 12 D 331 LYS PRO ASP ASN PHE LEU MET GLY LEU GLY LYS LYS GLY
SEQRES 13 D 331 ASN LEU VAL TYR ILE ILE ASP PHE GLY LEU ALA LYS LYS
SEQRES 14 D 331 TYR ARG ASP ALA ARG THR HIS GLN HIS ILE PRO TYR ARG
SEQRES 15 D 331 GLU ASN LYS ASN LEU THR GLY THR ALA ARG TYR ALA SER
SEQRES 16 D 331 ILE ASN THR HIS LEU GLY ILE GLU GLN SER ARG ARG ASP
SEQRES 17 D 331 ASP LEU GLU SER LEU GLY TYR VAL LEU MET TYR PHE ASN
SEQRES 18 D 331 LEU GLY SER LEU PRO TRP GLN GLY LEU LYS ALA ALA THR
SEQRES 19 D 331 LYS ARG GLN LYS TYR GLU ARG ILE SER GLU LYS LYS MET
SEQRES 20 D 331 SER THR PRO ILE GLU VAL LEU CYS LYS GLY TYR PRO SER
SEQRES 21 D 331 GLU PHE ALA THR TYR LEU ASN PHE CYS ARG SER LEU ARG
SEQRES 22 D 331 PHE ASP ASP LYS PRO ASP TYR SER TYR LEU ARG GLN LEU
SEQRES 23 D 331 PHE ARG ASN LEU PHE HIS ARG GLN GLY PHE SER TYR ASP
SEQRES 24 D 331 TYR VAL PHE ASP TRP ASN MET LEU LYS PHE GLY ALA SER
SEQRES 25 D 331 ARG ALA ALA ASP ASP ALA GLU ARG GLU ARG ARG ASP ARG
SEQRES 26 D 331 GLU GLU ARG LEU ARG HIS
HET 1QM A 401 41
HET SO4 A 402 5
HET SO4 A 403 5
HET 1QM B 401 41
HET SO4 B 402 5
HET SO4 B 403 5
HET 1QM C 401 41
HET SO4 C 402 5
HET SO4 C 403 5
HET 1QM D 401 41
HET SO4 D 402 5
HET SO4 D 403 5
HET SO4 D 404 5
HETNAM 1QM 9-[3-(4-FLUOROPHENYL)-1-METHYL-1H-PYRAZOL-4-YL]-2,3,4,
HETNAM 2 1QM 5-TETRAHYDROPYRIDO[2,3-F][1,4]OXAZEPINE
HETNAM SO4 SULFATE ION
FORMUL 5 1QM 4(C18 H17 F N4 O)
FORMUL 6 SO4 9(O4 S 2-)
FORMUL 18 HOH *176(H2 O)
HELIX 1 1 GLN A 48 GLN A 60 1 13
HELIX 2 2 SER A 88 CYS A 96 1 9
HELIX 3 3 SER A 101 LYS A 122 1 22
HELIX 4 4 LYS A 130 ASP A 132 5 3
HELIX 5 5 LEU A 138 GLY A 142 5 5
HELIX 6 6 SER A 181 LEU A 186 1 6
HELIX 7 7 SER A 191 GLY A 209 1 19
HELIX 8 8 ILE A 228 THR A 235 1 8
HELIX 9 9 PRO A 236 CYS A 241 1 6
HELIX 10 10 SER A 246 LEU A 258 1 13
HELIX 11 11 ASP A 265 GLN A 280 1 16
HELIX 12 12 PHE A 288 LEU A 293 5 6
HELIX 13 13 LEU B 49 GLN B 60 1 12
HELIX 14 14 SER B 88 CYS B 96 1 9
HELIX 15 15 SER B 101 LYS B 122 1 22
HELIX 16 16 LYS B 130 ASP B 132 5 3
HELIX 17 17 LEU B 138 GLY B 142 5 5
HELIX 18 18 SER B 181 LEU B 186 1 6
HELIX 19 19 SER B 191 GLY B 209 1 19
HELIX 20 20 THR B 220 THR B 235 1 16
HELIX 21 21 PRO B 236 CYS B 241 1 6
HELIX 22 22 SER B 246 LEU B 258 1 13
HELIX 23 23 ASP B 265 GLN B 280 1 16
HELIX 24 24 PHE B 288 LEU B 293 5 6
HELIX 25 25 GLN C 48 GLN C 60 1 13
HELIX 26 26 SER C 88 CYS C 96 1 9
HELIX 27 27 SER C 101 LYS C 122 1 22
HELIX 28 28 LYS C 130 ASP C 132 5 3
HELIX 29 29 LEU C 138 GLY C 142 5 5
HELIX 30 30 SER C 181 LEU C 186 1 6
HELIX 31 31 SER C 191 GLY C 209 1 19
HELIX 32 32 THR C 220 THR C 235 1 16
HELIX 33 33 PRO C 236 CYS C 241 1 6
HELIX 34 34 SER C 246 LEU C 258 1 13
HELIX 35 35 ASP C 265 GLN C 280 1 16
HELIX 36 36 PHE C 288 LEU C 293 5 6
HELIX 37 37 GLN D 48 GLN D 60 1 13
HELIX 38 38 SER D 88 CYS D 96 1 9
HELIX 39 39 SER D 101 LYS D 122 1 22
HELIX 40 40 LYS D 130 ASP D 132 5 3
HELIX 41 41 LEU D 138 GLY D 142 5 5
HELIX 42 42 SER D 181 LEU D 186 1 6
HELIX 43 43 SER D 191 GLY D 209 1 19
HELIX 44 44 THR D 220 THR D 235 1 16
HELIX 45 45 PRO D 236 CYS D 241 1 6
HELIX 46 46 SER D 246 LEU D 258 1 13
HELIX 47 47 ASP D 265 GLN D 280 1 16
HELIX 48 48 PHE D 288 LEU D 293 5 6
SHEET 1 A 6 ARG A 4 VAL A 5 0
SHEET 2 A 6 TYR A 9 GLY A 18 -1 O TYR A 9 N VAL A 5
SHEET 3 A 6 GLY A 21 ASP A 28 -1 O GLY A 21 N GLY A 18
SHEET 4 A 6 GLU A 33 LEU A 39 -1 O GLU A 33 N ASP A 28
SHEET 5 A 6 TYR A 77 GLU A 83 -1 O MET A 82 N ALA A 36
SHEET 6 A 6 ILE A 68 GLU A 74 -1 N GLY A 72 O VAL A 79
SHEET 1 B 2 PHE A 124 ILE A 125 0
SHEET 2 B 2 LYS A 154 LYS A 155 -1 O LYS A 154 N ILE A 125
SHEET 1 C 2 PHE A 134 MET A 136 0
SHEET 2 C 2 VAL A 145 ILE A 147 -1 O TYR A 146 N LEU A 135
SHEET 1 D 6 ARG B 4 VAL B 5 0
SHEET 2 D 6 TYR B 9 GLY B 16 -1 O TYR B 9 N VAL B 5
SHEET 3 D 6 ILE B 23 ASP B 28 -1 O ILE B 23 N ILE B 15
SHEET 4 D 6 GLU B 33 GLU B 40 -1 O GLU B 33 N ASP B 28
SHEET 5 D 6 TYR B 77 GLU B 83 -1 O ASN B 78 N GLU B 40
SHEET 6 D 6 ILE B 68 GLU B 74 -1 N TRP B 70 O VAL B 81
SHEET 1 E 2 PHE B 124 ILE B 125 0
SHEET 2 E 2 LYS B 154 LYS B 155 -1 O LYS B 154 N ILE B 125
SHEET 1 F 2 PHE B 134 MET B 136 0
SHEET 2 F 2 VAL B 145 ILE B 147 -1 O TYR B 146 N LEU B 135
SHEET 1 G 5 TYR C 9 SER C 17 0
SHEET 2 G 5 ASP C 22 ASP C 28 -1 O LEU C 25 N GLY C 12
SHEET 3 G 5 GLU C 33 LEU C 39 -1 O GLU C 33 N ASP C 28
SHEET 4 G 5 TYR C 77 GLU C 83 -1 O MET C 82 N ALA C 36
SHEET 5 G 5 ILE C 68 GLU C 74 -1 N GLY C 72 O VAL C 79
SHEET 1 H 2 PHE C 124 ILE C 125 0
SHEET 2 H 2 LYS C 154 LYS C 155 -1 O LYS C 154 N ILE C 125
SHEET 1 I 2 PHE C 134 MET C 136 0
SHEET 2 I 2 VAL C 145 ILE C 147 -1 O TYR C 146 N LEU C 135
SHEET 1 J 6 ARG D 4 VAL D 5 0
SHEET 2 J 6 TYR D 9 LYS D 14 -1 O TYR D 9 N VAL D 5
SHEET 3 J 6 ILE D 23 ASP D 28 -1 O LEU D 25 N GLY D 12
SHEET 4 J 6 GLU D 33 GLU D 40 -1 O GLU D 33 N ASP D 28
SHEET 5 J 6 ASN D 78 GLU D 83 -1 O ASN D 78 N GLU D 40
SHEET 6 J 6 ILE D 68 ALA D 73 -1 N TRP D 70 O VAL D 81
SHEET 1 K 2 PHE D 124 ILE D 125 0
SHEET 2 K 2 LYS D 154 LYS D 155 -1 O LYS D 154 N ILE D 125
SHEET 1 L 2 PHE D 134 MET D 136 0
SHEET 2 L 2 VAL D 145 ILE D 147 -1 O TYR D 146 N LEU D 135
CISPEP 1 GLY B 21 ASP B 22 0 -5.11
SITE 1 AC1 11 ILE A 15 SER A 17 ILE A 23 ALA A 36
SITE 2 AC1 11 LYS A 38 MET A 80 MET A 82 LEU A 85
SITE 3 AC1 11 GLY A 86 LEU A 135 ILE A 148
SITE 1 AC2 4 ARG A 178 GLN A 214 GLY A 215 HOH A 543
SITE 1 AC3 5 SER A 267 ARG A 270 ARG A 274 ASN D 275
SITE 2 AC3 5 ARG D 279
SITE 1 AC4 11 ILE B 15 SER B 17 ILE B 23 ALA B 36
SITE 2 AC4 11 LYS B 38 MET B 80 MET B 82 LEU B 85
SITE 3 AC4 11 GLY B 86 LEU B 135 ILE B 148
SITE 1 AC5 4 ARG B 178 GLN B 214 GLY B 215 LYS B 224
SITE 1 AC6 3 ARG B 127 LYS B 154 LYS B 171
SITE 1 AC7 10 ILE C 15 SER C 17 ILE C 23 ALA C 36
SITE 2 AC7 10 MET C 80 MET C 82 LEU C 85 GLY C 86
SITE 3 AC7 10 LEU C 135 ILE C 148
SITE 1 AC8 5 ASN B 275 ARG B 279 SER C 267 ARG C 270
SITE 2 AC8 5 ARG C 274
SITE 1 AC9 5 ARG C 178 GLN C 214 GLY C 215 LYS C 224
SITE 2 AC9 5 HOH C 545
SITE 1 BC1 12 ILE D 15 ILE D 23 ALA D 36 LYS D 38
SITE 2 BC1 12 MET D 80 MET D 82 GLU D 83 LEU D 84
SITE 3 BC1 12 LEU D 85 GLY D 86 LEU D 135 ILE D 148
SITE 1 BC2 4 ARG D 178 GLN D 214 GLY D 215 LYS D 224
SITE 1 BC3 3 ARG D 127 LYS D 154 LYS D 171
SITE 1 BC4 2 ARG D 192 LYS D 263
CRYST1 48.689 83.964 89.290 108.00 105.71 93.00 P 1 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 0.020539 0.001076 0.006518 0.00000
SCALE2 0.000000 0.011926 0.004257 0.00000
SCALE3 0.000000 0.000000 0.012353 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
