HEADER TRANSFERASE 13-JUL-12 4G3C
TITLE CRYSTAL STRUCTURE OF APO MURINE NF-KAPPAB INDUCING KINASE (NIK)
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-KABBAB 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, MAP3K14,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.G.HYMOWITZ,G.DE LEON-BOENIG
REVDAT 3 24-JAN-18 4G3C 1 AUTHOR
REVDAT 2 23-JAN-13 4G3C 1 JRNL
REVDAT 1 08-AUG-12 4G3C 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. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 44453
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 5003
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) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.20
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2470
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.78
REMARK 3 BIN R VALUE (WORKING SET) : 0.2550
REMARK 3 BIN FREE R VALUE SET COUNT : 280
REMARK 3 BIN FREE R VALUE : 0.2850
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4990
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 192
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.24000
REMARK 3 B22 (A**2) : -0.24000
REMARK 3 B33 (A**2) : 0.49000
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): 0.196
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.173
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.113
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.892
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
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): 6972 ; 1.102 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 645 ; 5.378 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 215 ;32.774 ;23.442
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 899 ;13.995 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 37 ;19.666 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 755 ; 0.070 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3857 ; 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): 45.6611 39.8679 -3.2365
REMARK 3 T TENSOR
REMARK 3 T11: 0.0492 T22: 0.0517
REMARK 3 T33: 0.1295 T12: 0.0468
REMARK 3 T13: 0.0523 T23: 0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 1.8312 L22: 2.5824
REMARK 3 L33: 0.8857 L12: -0.1817
REMARK 3 L13: 0.1128 L23: 0.4378
REMARK 3 S TENSOR
REMARK 3 S11: 0.0609 S12: 0.0242 S13: 0.2484
REMARK 3 S21: 0.0209 S22: -0.0711 S23: -0.0842
REMARK 3 S31: 0.0201 S32: -0.0113 S33: 0.0102
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): 52.6668 12.6661 -4.2930
REMARK 3 T TENSOR
REMARK 3 T11: 0.1261 T22: 0.0335
REMARK 3 T33: 0.0094 T12: 0.0466
REMARK 3 T13: 0.0202 T23: 0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 1.1725 L22: 2.0695
REMARK 3 L33: 1.4715 L12: -0.1094
REMARK 3 L13: -0.4203 L23: -0.8527
REMARK 3 S TENSOR
REMARK 3 S11: 0.0207 S12: 0.0980 S13: -0.0630
REMARK 3 S21: -0.0918 S22: -0.0829 S23: -0.0738
REMARK 3 S31: 0.1698 S32: 0.0461 S33: 0.0622
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): 30.8999 66.9831 2.5281
REMARK 3 T TENSOR
REMARK 3 T11: 0.0160 T22: 0.0141
REMARK 3 T33: 0.1124 T12: 0.0007
REMARK 3 T13: 0.0098 T23: -0.0277
REMARK 3 L TENSOR
REMARK 3 L11: 2.0351 L22: 2.5433
REMARK 3 L33: 1.5748 L12: 0.5796
REMARK 3 L13: 0.0906 L23: 0.2812
REMARK 3 S TENSOR
REMARK 3 S11: -0.0073 S12: -0.0448 S13: 0.0323
REMARK 3 S21: 0.0192 S22: -0.0085 S23: -0.2448
REMARK 3 S31: -0.0211 S32: 0.0478 S33: 0.0158
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): 17.4444 42.7844 1.0765
REMARK 3 T TENSOR
REMARK 3 T11: 0.0459 T22: 0.0792
REMARK 3 T33: 0.0127 T12: -0.0220
REMARK 3 T13: -0.0061 T23: 0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 1.4675 L22: 2.0214
REMARK 3 L33: 2.4482 L12: 0.0014
REMARK 3 L13: 0.1007 L23: 0.0261
REMARK 3 S TENSOR
REMARK 3 S11: 0.1088 S12: -0.0490 S13: -0.0518
REMARK 3 S21: 0.0152 S22: -0.0585 S23: 0.0195
REMARK 3 S31: 0.2715 S32: 0.0106 S33: -0.0503
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 4G3C 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_1000073685.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-08
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 : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97740
REMARK 200 MONOCHROMATOR : SI(220) ASYMMETRIC CUT SINGLE
REMARK 200 CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49462
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
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 : 3.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.58400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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: HOMOLOGY MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
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 , PH 6.2, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 276K
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 22.54150
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 33.81225
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 11.27075
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 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 ARG B 675
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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 VAL A 430 CB - CA - C ANGL. DEV. = -11.7 DEGREES
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 GLN A 405 -135.86 35.97
REMARK 500 ASP A 517 56.91 -149.07
REMARK 500 ASP A 536 97.29 68.68
REMARK 500 TYR A 601 -29.11 73.19
REMARK 500 PRO A 616 36.27 -73.72
REMARK 500 LYS A 668 -113.80 65.58
REMARK 500 GLU B 398 -0.12 67.12
REMARK 500 GLN B 405 -132.69 34.30
REMARK 500 VAL B 408 -75.94 -103.01
REMARK 500 ARG B 410 -169.21 -123.33
REMARK 500 ASP B 517 55.42 -151.20
REMARK 500 ASP B 536 96.03 66.80
REMARK 500 PRO B 545 -18.25 -47.32
REMARK 500 LEU B 553 48.59 76.41
REMARK 500 ASP B 576 -164.67 -125.01
REMARK 500 PRO B 616 41.24 -75.63
REMARK 500 LYS B 668 -141.65 66.59
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 SO4 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 SO4 B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 703
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4G3D RELATED DB: PDB
REMARK 900 RELATED ID: 4G3E RELATED DB: PDB
REMARK 900 RELATED ID: 4G3F RELATED DB: PDB
REMARK 900 RELATED ID: 4G3G RELATED DB: PDB
DBREF 4G3C A 329 675 UNP Q9WUL6 M3K14_MOUSE 329 675
DBREF 4G3C B 329 675 UNP Q9WUL6 M3K14_MOUSE 329 675
SEQADV 4G3C GLY A 327 UNP Q9WUL6 EXPRESSION TAG
SEQADV 4G3C SER A 328 UNP Q9WUL6 EXPRESSION TAG
SEQADV 4G3C GLY A 676 UNP Q9WUL6 EXPRESSION TAG
SEQADV 4G3C ASN A 677 UNP Q9WUL6 EXPRESSION TAG
SEQADV 4G3C SER A 678 UNP Q9WUL6 EXPRESSION TAG
SEQADV 4G3C GLY B 327 UNP Q9WUL6 EXPRESSION TAG
SEQADV 4G3C SER B 328 UNP Q9WUL6 EXPRESSION TAG
SEQADV 4G3C GLY B 676 UNP Q9WUL6 EXPRESSION TAG
SEQADV 4G3C ASN B 677 UNP Q9WUL6 EXPRESSION TAG
SEQADV 4G3C 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 SO4 A 703 5
HET SO4 B 701 5
HET SO4 B 702 5
HET SO4 B 703 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 6(O4 S 2-)
FORMUL 9 HOH *192(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 THR A 361 SER A 363 5 3
HELIX 4 4 GLU A 436 ARG A 439 5 4
HELIX 5 5 VAL A 440 ALA A 445 1 6
HELIX 6 6 LEU A 479 GLY A 487 1 9
HELIX 7 7 PRO A 490 ARG A 511 1 22
HELIX 8 8 LYS A 519 ASP A 521 5 3
HELIX 9 9 THR A 561 MET A 565 5 5
HELIX 10 10 ALA A 566 MET A 571 1 6
HELIX 11 11 ALA A 577 GLY A 594 1 18
HELIX 12 12 PRO A 605 GLU A 613 1 9
HELIX 13 13 PRO A 615 ILE A 620 5 6
HELIX 14 14 ALA A 625 LEU A 636 1 12
HELIX 15 15 GLU A 639 ARG A 643 5 5
HELIX 16 16 SER A 645 VAL A 660 1 16
HELIX 17 17 VAL B 335 GLN B 344 1 10
HELIX 18 18 GLN B 351 LYS B 360 1 10
HELIX 19 19 THR B 361 SER B 363 5 3
HELIX 20 20 GLU B 436 ARG B 439 5 4
HELIX 21 21 VAL B 440 ALA B 445 1 6
HELIX 22 22 SER B 478 GLY B 487 1 10
HELIX 23 23 PRO B 490 ARG B 511 1 22
HELIX 24 24 LYS B 519 ASP B 521 5 3
HELIX 25 25 THR B 561 MET B 565 5 5
HELIX 26 26 ALA B 566 MET B 571 1 6
HELIX 27 27 ALA B 577 GLY B 594 1 18
HELIX 28 28 PRO B 605 GLU B 613 1 9
HELIX 29 29 PRO B 616 ILE B 620 5 5
HELIX 30 30 ALA B 625 LEU B 636 1 12
HELIX 31 31 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 VAL A 433 O VAL A 467
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 3 GLY A 477 SER A 478 0
SHEET 2 B 3 VAL A 523 LEU A 525 -1 O LEU A 525 N GLY A 477
SHEET 3 B 3 ALA A 532 LEU A 534 -1 O ALA A 533 N LEU A 524
SHEET 1 C 2 ILE A 513 LEU A 514 0
SHEET 2 C 2 LEU A 541 CYS A 542 -1 O LEU A 541 N LEU A 514
SHEET 1 D 7 VAL B 347 SER B 349 0
SHEET 2 D 7 ASN B 379 LEU B 383 1 O LEU B 383 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 LYS B 431 O ILE B 469
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 8 CYS A 446 VAL A 455 MET A 471 LEU A 534
SITE 2 AC1 8 CYS A 535 ASP A 536 PHE A 537 HOH A 873
SITE 1 AC2 2 ARG A 650 ARG A 651
SITE 1 AC3 4 ARG A 637 LYS A 638 GLU A 639 HIS A 642
SITE 1 AC4 8 CYS B 446 VAL B 455 MET B 471 LEU B 534
SITE 2 AC4 8 CYS B 535 ASP B 536 PHE B 537 HOH B 883
SITE 1 AC5 2 TYR B 507 ARG B 511
SITE 1 AC6 4 ARG B 637 LYS B 638 GLU B 639 HIS B 642
CRYST1 142.211 142.211 45.083 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 0.007032 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007032 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022181 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
