HEADER TRANSFERASE/TRANSFERASE INHIBITOR 13-JUL-12 4G3E
TITLE CRYSTAL STRUCTURE OF MURINE NF-KAPPAB INDUCING KINASE (NIK) BOUND TO A
TITLE 2 6-ALKYNYLINDOLINE (CMP1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NF-KAPPA-BETA-INDUCING KINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: SERINE/THREONINE-PROTEIN KINASE NIK;
COMPND 5 EC: 2.7.11.25;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: MAP3K14, NF-KAPPAB INDUCING KINASE, NIK;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS TRANSFER VECTOR;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PACGP67
KEYWDS NON-RD KINASE, PROTEIN SERINE/THREONINE KINASE, NF-KAPPAB, STRUCTURE-
KEYWDS 2 BASED DRUG DESIGN, MAP3K14, TRANSFERASE, TRANSFERASE-TRANSFERASE
KEYWDS 3 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.G.HYMOWITZ,G.DE LEON-BOENIG
REVDAT 5 03-APR-24 4G3E 1 REMARK
REVDAT 4 28-FEB-24 4G3E 1 REMARK SEQADV
REVDAT 3 24-JAN-18 4G3E 1 AUTHOR REMARK
REVDAT 2 23-JAN-13 4G3E 1 JRNL
REVDAT 1 15-AUG-12 4G3E 0
JRNL AUTH G.DE LEON-BOENIG,K.K.BOWMAN,J.A.FENG,T.CRAWFORD,C.EVERETT,
JRNL AUTH 2 Y.FRANKE,A.OH,M.STANLEY,S.T.STABEN,M.A.STAROVASNIK,
JRNL AUTH 3 H.J.WALLWEBER,J.WU,L.C.WU,A.R.JOHNSON,S.G.HYMOWITZ
JRNL TITL THE CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF THE
JRNL TITL 2 NF-KAPPAB INDUCING KINASE REVEALS A NARROW BUT FLEXIBLE
JRNL TITL 3 ACTIVE SITE.
JRNL REF STRUCTURE V. 20 1704 2012
JRNL REFN ISSN 0969-2126
JRNL PMID 22921830
JRNL DOI 10.1016/J.STR.2012.07.013
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 32110
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3259
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 25
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1574
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.14
REMARK 3 BIN R VALUE (WORKING SET) : 0.2950
REMARK 3 BIN FREE R VALUE SET COUNT : 163
REMARK 3 BIN FREE R VALUE : 0.3650
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4956
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 69
REMARK 3 SOLVENT ATOMS : 61
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.28000
REMARK 3 B22 (A**2) : -0.28000
REMARK 3 B33 (A**2) : 0.57000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.381
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.262
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.190
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.602
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5150 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6969 ; 1.224 ; 1.992
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 634 ; 5.697 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 212 ;38.370 ;23.443
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 892 ;16.331 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 37 ;18.466 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 748 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3858 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 334 A 472
REMARK 3 ORIGIN FOR THE GROUP (A): 46.3999 40.0639 -3.0370
REMARK 3 T TENSOR
REMARK 3 T11: 0.0576 T22: 0.0915
REMARK 3 T33: 0.2102 T12: 0.0679
REMARK 3 T13: 0.0136 T23: 0.0208
REMARK 3 L TENSOR
REMARK 3 L11: 3.0346 L22: 5.4137
REMARK 3 L33: 1.6367 L12: -0.7101
REMARK 3 L13: -1.6015 L23: 0.1059
REMARK 3 S TENSOR
REMARK 3 S11: 0.0670 S12: 0.0915 S13: 0.2536
REMARK 3 S21: -0.0639 S22: -0.0858 S23: -0.2112
REMARK 3 S31: 0.0415 S32: -0.0361 S33: 0.0188
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 473 A 671
REMARK 3 ORIGIN FOR THE GROUP (A): 53.0599 12.4309 -4.2842
REMARK 3 T TENSOR
REMARK 3 T11: 0.1887 T22: 0.0426
REMARK 3 T33: 0.0170 T12: 0.0560
REMARK 3 T13: 0.0378 T23: 0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 2.7396 L22: 4.3899
REMARK 3 L33: 3.9335 L12: 0.4319
REMARK 3 L13: -0.1751 L23: -0.3596
REMARK 3 S TENSOR
REMARK 3 S11: -0.0918 S12: 0.1618 S13: -0.1261
REMARK 3 S21: -0.2607 S22: 0.0187 S23: -0.2023
REMARK 3 S31: 0.1244 S32: 0.2347 S33: 0.0731
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 334 B 472
REMARK 3 ORIGIN FOR THE GROUP (A): 31.3036 67.0408 2.6789
REMARK 3 T TENSOR
REMARK 3 T11: 0.0089 T22: 0.0927
REMARK 3 T33: 0.1800 T12: 0.0202
REMARK 3 T13: -0.0229 T23: -0.0300
REMARK 3 L TENSOR
REMARK 3 L11: 3.5853 L22: 5.4904
REMARK 3 L33: 2.3037 L12: 1.3026
REMARK 3 L13: -1.1479 L23: 0.6700
REMARK 3 S TENSOR
REMARK 3 S11: 0.1000 S12: 0.0162 S13: 0.0281
REMARK 3 S21: 0.0406 S22: -0.0803 S23: -0.2389
REMARK 3 S31: -0.0432 S32: 0.0091 S33: -0.0197
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 473 B 674
REMARK 3 ORIGIN FOR THE GROUP (A): 17.3244 42.9371 1.0622
REMARK 3 T TENSOR
REMARK 3 T11: 0.0810 T22: 0.1124
REMARK 3 T33: 0.0546 T12: -0.0391
REMARK 3 T13: -0.0290 T23: 0.0435
REMARK 3 L TENSOR
REMARK 3 L11: 3.4109 L22: 4.1307
REMARK 3 L33: 4.7559 L12: 0.1693
REMARK 3 L13: 0.5093 L23: 0.4486
REMARK 3 S TENSOR
REMARK 3 S11: 0.2121 S12: 0.0146 S13: -0.1720
REMARK 3 S21: 0.0469 S22: -0.0633 S23: -0.0196
REMARK 3 S31: 0.4816 S32: 0.0103 S33: -0.1488
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4G3E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-12.
REMARK 100 THE DEPOSITION ID IS D_1000073687.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAY-12
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32116
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06800
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) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.59800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: APO MURINE NIK KINASE DOMAIN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2UL PROTEIN WITH 2UL WELL SOLUTION OF
REMARK 280 0.5 M AMMONIUM SULFATE, 0.9 M LITHIUM SULFATE,0.1M SODIUM
REMARK 280 CITRATE TRIBASIC DIHYDRATE THEN SOAKED IN WELL SOLUTION WITH 1
REMARK 280 MM CMP1, PH 6.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
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 22.57550
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 33.86325
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 11.28775
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: 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 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 327
REMARK 465 SER A 328
REMARK 465 ALA A 329
REMARK 465 LEU A 330
REMARK 465 GLU A 331
REMARK 465 LYS A 332
REMARK 465 VAL A 333
REMARK 465 SER A 364
REMARK 465 GLY A 365
REMARK 465 SER A 366
REMARK 465 ALA A 367
REMARK 465 LYS A 368
REMARK 465 LEU A 369
REMARK 465 GLN A 370
REMARK 465 ARG A 371
REMARK 465 LEU A 372
REMARK 465 GLY A 373
REMARK 465 PRO A 374
REMARK 465 GLU A 375
REMARK 465 THR A 376
REMARK 465 GLU A 377
REMARK 465 PRO A 545
REMARK 465 ASP A 546
REMARK 465 GLY A 547
REMARK 465 LEU A 548
REMARK 465 GLY A 549
REMARK 465 LYS A 550
REMARK 465 SER A 551
REMARK 465 LEU A 552
REMARK 465 LEU A 553
REMARK 465 THR A 554
REMARK 465 GLY A 555
REMARK 465 ASP A 556
REMARK 465 TYR A 557
REMARK 465 ARG A 603
REMARK 465 GLY A 676
REMARK 465 ASN A 677
REMARK 465 SER A 678
REMARK 465 GLY B 327
REMARK 465 SER B 328
REMARK 465 ALA B 329
REMARK 465 LEU B 330
REMARK 465 GLU B 331
REMARK 465 LYS B 332
REMARK 465 VAL B 333
REMARK 465 SER B 364
REMARK 465 GLY B 365
REMARK 465 SER B 366
REMARK 465 ALA B 367
REMARK 465 LYS B 368
REMARK 465 LEU B 369
REMARK 465 GLN B 370
REMARK 465 ARG B 371
REMARK 465 LEU B 372
REMARK 465 GLY B 373
REMARK 465 PRO B 374
REMARK 465 GLU B 375
REMARK 465 THR B 376
REMARK 465 GLU B 377
REMARK 465 TYR B 601
REMARK 465 PHE B 602
REMARK 465 ARG B 603
REMARK 465 GLY B 676
REMARK 465 ASN B 677
REMARK 465 SER B 678
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 TRP A 362 31.68 -82.69
REMARK 500 VAL A 399 -50.10 -125.00
REMARK 500 GLN A 405 -76.73 -45.85
REMARK 500 ARG A 407 95.31 -64.99
REMARK 500 CYS A 428 -155.23 -144.04
REMARK 500 CYS A 446 -49.34 178.15
REMARK 500 ASP A 517 50.26 -150.78
REMARK 500 ASP A 536 82.98 63.15
REMARK 500 ASP A 576 -168.44 -129.94
REMARK 500 TRP A 598 -19.75 73.53
REMARK 500 PRO A 616 35.58 -73.86
REMARK 500 LYS A 668 76.68 -119.85
REMARK 500 GLN B 405 -132.19 25.31
REMARK 500 CYS B 428 -157.25 -143.92
REMARK 500 ASP B 517 52.08 -150.72
REMARK 500 ASP B 536 90.15 70.18
REMARK 500 PRO B 545 27.95 -70.29
REMARK 500 ASP B 546 -10.96 -146.77
REMARK 500 ASP B 576 -166.40 -128.99
REMARK 500 PRO B 616 37.85 -70.55
REMARK 500 LYS B 668 -119.47 -122.83
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 GLN B 405 PRO B 406 149.04
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 SO4 A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0WC A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0WC B 702
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4G3C RELATED DB: PDB
REMARK 900 RELATED ID: 4G3D RELATED DB: PDB
REMARK 900 RELATED ID: 4G3F RELATED DB: PDB
REMARK 900 RELATED ID: 4G3G RELATED DB: PDB
DBREF 4G3E A 329 675 UNP Q9WUL6 M3K14_MOUSE 329 675
DBREF 4G3E B 329 675 UNP Q9WUL6 M3K14_MOUSE 329 675
SEQADV 4G3E GLY A 327 UNP Q9WUL6 EXPRESSION TAG
SEQADV 4G3E SER A 328 UNP Q9WUL6 EXPRESSION TAG
SEQADV 4G3E GLY A 676 UNP Q9WUL6 EXPRESSION TAG
SEQADV 4G3E ASN A 677 UNP Q9WUL6 EXPRESSION TAG
SEQADV 4G3E SER A 678 UNP Q9WUL6 EXPRESSION TAG
SEQADV 4G3E GLY B 327 UNP Q9WUL6 EXPRESSION TAG
SEQADV 4G3E SER B 328 UNP Q9WUL6 EXPRESSION TAG
SEQADV 4G3E GLY B 676 UNP Q9WUL6 EXPRESSION TAG
SEQADV 4G3E ASN B 677 UNP Q9WUL6 EXPRESSION TAG
SEQADV 4G3E SER B 678 UNP Q9WUL6 EXPRESSION TAG
SEQRES 1 A 352 GLY SER ALA LEU GLU LYS VAL PRO VAL GLU GLU TYR LEU
SEQRES 2 A 352 VAL HIS ALA LEU GLN GLY SER VAL SER SER GLY GLN ALA
SEQRES 3 A 352 HIS SER LEU ALA SER LEU ALA LYS THR TRP SER SER GLY
SEQRES 4 A 352 SER ALA LYS LEU GLN ARG LEU GLY PRO GLU THR GLU ASP
SEQRES 5 A 352 ASN GLU GLY VAL LEU LEU THR GLU LYS LEU LYS PRO VAL
SEQRES 6 A 352 ASP TYR GLU TYR ARG GLU GLU VAL HIS TRP MET THR HIS
SEQRES 7 A 352 GLN PRO ARG VAL GLY ARG GLY SER PHE GLY GLU VAL HIS
SEQRES 8 A 352 ARG MET LYS ASP LYS GLN THR GLY PHE GLN CYS ALA VAL
SEQRES 9 A 352 LYS LYS VAL ARG LEU GLU VAL PHE ARG VAL GLU GLU LEU
SEQRES 10 A 352 VAL ALA CYS ALA GLY LEU SER SER PRO ARG ILE VAL PRO
SEQRES 11 A 352 LEU TYR GLY ALA VAL ARG GLU GLY PRO TRP VAL ASN ILE
SEQRES 12 A 352 PHE MET GLU LEU LEU GLU GLY GLY SER LEU GLY GLN LEU
SEQRES 13 A 352 ILE LYS GLN MET GLY CYS LEU PRO GLU ASP ARG ALA LEU
SEQRES 14 A 352 TYR TYR LEU GLY GLN ALA LEU GLU GLY LEU GLU TYR LEU
SEQRES 15 A 352 HIS THR ARG ARG ILE LEU HIS GLY ASP VAL LYS ALA ASP
SEQRES 16 A 352 ASN VAL LEU LEU SER SER ASP GLY SER ARG ALA ALA LEU
SEQRES 17 A 352 CYS ASP PHE GLY HIS ALA LEU CYS LEU GLN PRO ASP GLY
SEQRES 18 A 352 LEU GLY LYS SER LEU LEU THR GLY ASP TYR ILE PRO GLY
SEQRES 19 A 352 THR GLU THR HIS MET ALA PRO GLU VAL VAL MET GLY LYS
SEQRES 20 A 352 PRO CYS ASP ALA LYS VAL ASP ILE TRP SER SER CYS CYS
SEQRES 21 A 352 MET MET LEU HIS MET LEU ASN GLY CYS HIS PRO TRP THR
SEQRES 22 A 352 GLN TYR PHE ARG GLY PRO LEU CYS LEU LYS ILE ALA SER
SEQRES 23 A 352 GLU PRO PRO PRO ILE ARG GLU ILE PRO PRO SER CYS ALA
SEQRES 24 A 352 PRO LEU THR ALA GLN ALA ILE GLN GLU GLY LEU ARG LYS
SEQRES 25 A 352 GLU PRO VAL HIS ARG ALA SER ALA MET GLU LEU ARG ARG
SEQRES 26 A 352 LYS VAL GLY LYS ALA LEU GLN GLU VAL GLY GLY LEU LYS
SEQRES 27 A 352 SER PRO TRP LYS GLY GLU TYR LYS GLU PRO ARG GLY ASN
SEQRES 28 A 352 SER
SEQRES 1 B 352 GLY SER ALA LEU GLU LYS VAL PRO VAL GLU GLU TYR LEU
SEQRES 2 B 352 VAL HIS ALA LEU GLN GLY SER VAL SER SER GLY GLN ALA
SEQRES 3 B 352 HIS SER LEU ALA SER LEU ALA LYS THR TRP SER SER GLY
SEQRES 4 B 352 SER ALA LYS LEU GLN ARG LEU GLY PRO GLU THR GLU ASP
SEQRES 5 B 352 ASN GLU GLY VAL LEU LEU THR GLU LYS LEU LYS PRO VAL
SEQRES 6 B 352 ASP TYR GLU TYR ARG GLU GLU VAL HIS TRP MET THR HIS
SEQRES 7 B 352 GLN PRO ARG VAL GLY ARG GLY SER PHE GLY GLU VAL HIS
SEQRES 8 B 352 ARG MET LYS ASP LYS GLN THR GLY PHE GLN CYS ALA VAL
SEQRES 9 B 352 LYS LYS VAL ARG LEU GLU VAL PHE ARG VAL GLU GLU LEU
SEQRES 10 B 352 VAL ALA CYS ALA GLY LEU SER SER PRO ARG ILE VAL PRO
SEQRES 11 B 352 LEU TYR GLY ALA VAL ARG GLU GLY PRO TRP VAL ASN ILE
SEQRES 12 B 352 PHE MET GLU LEU LEU GLU GLY GLY SER LEU GLY GLN LEU
SEQRES 13 B 352 ILE LYS GLN MET GLY CYS LEU PRO GLU ASP ARG ALA LEU
SEQRES 14 B 352 TYR TYR LEU GLY GLN ALA LEU GLU GLY LEU GLU TYR LEU
SEQRES 15 B 352 HIS THR ARG ARG ILE LEU HIS GLY ASP VAL LYS ALA ASP
SEQRES 16 B 352 ASN VAL LEU LEU SER SER ASP GLY SER ARG ALA ALA LEU
SEQRES 17 B 352 CYS ASP PHE GLY HIS ALA LEU CYS LEU GLN PRO ASP GLY
SEQRES 18 B 352 LEU GLY LYS SER LEU LEU THR GLY ASP TYR ILE PRO GLY
SEQRES 19 B 352 THR GLU THR HIS MET ALA PRO GLU VAL VAL MET GLY LYS
SEQRES 20 B 352 PRO CYS ASP ALA LYS VAL ASP ILE TRP SER SER CYS CYS
SEQRES 21 B 352 MET MET LEU HIS MET LEU ASN GLY CYS HIS PRO TRP THR
SEQRES 22 B 352 GLN TYR PHE ARG GLY PRO LEU CYS LEU LYS ILE ALA SER
SEQRES 23 B 352 GLU PRO PRO PRO ILE ARG GLU ILE PRO PRO SER CYS ALA
SEQRES 24 B 352 PRO LEU THR ALA GLN ALA ILE GLN GLU GLY LEU ARG LYS
SEQRES 25 B 352 GLU PRO VAL HIS ARG ALA SER ALA MET GLU LEU ARG ARG
SEQRES 26 B 352 LYS VAL GLY LYS ALA LEU GLN GLU VAL GLY GLY LEU LYS
SEQRES 27 B 352 SER PRO TRP LYS GLY GLU TYR LYS GLU PRO ARG GLY ASN
SEQRES 28 B 352 SER
HET SO4 A 701 5
HET SO4 A 702 5
HET 0WC A 703 27
HET SO4 B 701 5
HET 0WC B 702 27
HETNAM SO4 SULFATE ION
HETNAM 0WC (2R)-4-[1-(2-AMINO-5-CHLOROPYRIMIDIN-4-YL)-2,3-DIHYDRO-
HETNAM 2 0WC 1H-INDOL-6-YL]-2-(1,3-THIAZOL-2-YL)BUT-3-YN-2-OL
FORMUL 3 SO4 3(O4 S 2-)
FORMUL 5 0WC 2(C19 H16 CL N5 O S)
FORMUL 8 HOH *61(H2 O)
HELIX 1 1 PRO A 334 GLN A 344 1 11
HELIX 2 2 GLN A 351 LYS A 360 1 10
HELIX 3 3 GLU A 436 PHE A 438 5 3
HELIX 4 4 ARG A 439 ALA A 445 1 7
HELIX 5 5 SER A 478 GLY A 487 1 10
HELIX 6 6 PRO A 490 ARG A 511 1 22
HELIX 7 7 LYS A 519 ASP A 521 5 3
HELIX 8 8 THR A 561 MET A 565 5 5
HELIX 9 9 ALA A 566 MET A 571 1 6
HELIX 10 10 ALA A 577 GLY A 594 1 18
HELIX 11 11 PRO A 605 GLU A 613 1 9
HELIX 12 12 PRO A 615 ILE A 620 5 6
HELIX 13 13 ALA A 625 LEU A 636 1 12
HELIX 14 14 GLU A 639 ARG A 643 5 5
HELIX 15 15 SER A 645 VAL A 660 1 16
HELIX 16 16 VAL B 335 GLN B 344 1 10
HELIX 17 17 GLN B 351 LYS B 360 1 10
HELIX 18 18 THR B 361 SER B 363 5 3
HELIX 19 19 GLU B 436 ARG B 439 5 4
HELIX 20 20 VAL B 440 ALA B 445 1 6
HELIX 21 21 SER B 478 GLY B 487 1 10
HELIX 22 22 PRO B 490 ARG B 511 1 22
HELIX 23 23 LYS B 519 ASP B 521 5 3
HELIX 24 24 THR B 561 MET B 565 5 5
HELIX 25 25 ALA B 566 MET B 571 1 6
HELIX 26 26 ALA B 577 GLY B 594 1 18
HELIX 27 27 PRO B 605 GLU B 613 1 9
HELIX 28 28 PRO B 615 ILE B 620 5 6
HELIX 29 29 ALA B 625 LEU B 636 1 12
HELIX 30 30 SER B 645 VAL B 660 1 16
SHEET 1 A 7 VAL A 347 SER A 349 0
SHEET 2 A 7 ASN A 379 LEU A 383 1 O LEU A 383 N SER A 348
SHEET 3 A 7 LEU A 457 GLU A 463 -1 O ARG A 462 N GLU A 380
SHEET 4 A 7 TRP A 466 MET A 471 -1 O ASN A 468 N VAL A 461
SHEET 5 A 7 GLN A 427 ARG A 434 -1 N LYS A 431 O ILE A 469
SHEET 6 A 7 VAL A 416 ASP A 421 -1 N MET A 419 O CYS A 428
SHEET 7 A 7 TRP A 401 THR A 403 -1 N MET A 402 O LYS A 420
SHEET 1 B 2 ILE A 513 LEU A 514 0
SHEET 2 B 2 LEU A 541 CYS A 542 -1 O LEU A 541 N LEU A 514
SHEET 1 C 2 VAL A 523 LEU A 525 0
SHEET 2 C 2 ALA A 532 LEU A 534 -1 O ALA A 533 N LEU A 524
SHEET 1 D 7 VAL B 347 SER B 349 0
SHEET 2 D 7 ASN B 379 LEU B 383 1 O GLY B 381 N SER B 348
SHEET 3 D 7 LEU B 457 GLU B 463 -1 O ARG B 462 N GLU B 380
SHEET 4 D 7 TRP B 466 MET B 471 -1 O PHE B 470 N TYR B 458
SHEET 5 D 7 GLN B 427 ARG B 434 -1 N VAL B 433 O VAL B 467
SHEET 6 D 7 VAL B 416 ASP B 421 -1 N MET B 419 O CYS B 428
SHEET 7 D 7 TRP B 401 THR B 403 -1 N MET B 402 O LYS B 420
SHEET 1 E 2 ILE B 513 LEU B 514 0
SHEET 2 E 2 LEU B 541 CYS B 542 -1 O LEU B 541 N LEU B 514
SHEET 1 F 2 VAL B 523 LEU B 525 0
SHEET 2 F 2 ALA B 532 LEU B 534 -1 O ALA B 533 N LEU B 524
SITE 1 AC1 3 MET A 647 ARG A 650 ARG A 651
SITE 1 AC2 4 ARG A 637 LYS A 638 GLU A 639 HIS A 642
SITE 1 AC3 14 ARG A 410 VAL A 416 ALA A 429 GLU A 442
SITE 2 AC3 14 VAL A 455 ILE A 469 MET A 471 GLU A 472
SITE 3 AC3 14 LEU A 474 GLN A 481 LEU A 524 CYS A 535
SITE 4 AC3 14 ASP A 536 PHE A 537
SITE 1 AC4 4 ARG B 637 LYS B 638 GLU B 639 HIS B 642
SITE 1 AC5 16 ARG B 410 GLY B 411 VAL B 416 ALA B 429
SITE 2 AC5 16 LYS B 431 GLU B 442 VAL B 455 ILE B 469
SITE 3 AC5 16 MET B 471 GLU B 472 LEU B 474 GLN B 481
SITE 4 AC5 16 LEU B 524 CYS B 535 ASP B 536 PHE B 537
CRYST1 143.145 143.145 45.151 90.00 90.00 90.00 P 43 8
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 0.006986 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006986 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022148 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 0.732896 -0.680151 -0.016050 69.10763 1
MTRIX2 2 0.680038 0.733070 -0.012527 -30.25893 1
MTRIX3 2 0.020286 -0.001733 0.999793 -6.31223 1
(ATOM LINES ARE NOT SHOWN.)
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