HEADER TRANSFERASE 29-FEB-16 5IH5
TITLE HUMAN CASEIN KINASE 1 ISOFORM DELTA (KINASE DOMAIN) IN COMPLEX WITH
TITLE 2 EPIBLASTIN A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASEIN KINASE I ISOFORM DELTA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CKID,TAU-PROTEIN KINASE CSNK1D;
COMPND 5 EC: 2.7.11.1,2.7.11.26;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: N-TERMINAL CLONING ARTIFACT: GP
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: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET19-NHIS
KEYWDS KINASE DOMAIN, STEM CELL REPROGRAMMING, KINASE INHIBITOR COMPLEX,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.URSU,D.J.ILLICH,Y.TAKEMOTO,A.T.PORFETYE,M.ZHANG,A.BROCKMEYER,
AUTHOR 2 P.JANNING,N.WATANABE,H.OSADA,I.R.VETTER,S.ZIEGLER,H.R.SCHOELER,
AUTHOR 3 H.WALDMANN
REVDAT 4 10-JAN-24 5IH5 1 LINK
REVDAT 3 04-MAY-16 5IH5 1 JRNL
REVDAT 2 20-APR-16 5IH5 1 JRNL
REVDAT 1 13-APR-16 5IH5 0
JRNL AUTH A.URSU,D.J.ILLICH,Y.TAKEMOTO,A.T.PORFETYE,M.ZHANG,
JRNL AUTH 2 A.BROCKMEYER,P.JANNING,N.WATANABE,H.OSADA,I.R.VETTER,
JRNL AUTH 3 S.ZIEGLER,H.R.SCHOLER,H.WALDMANN
JRNL TITL EPIBLASTIN A INDUCES REPROGRAMMING OF EPIBLAST STEM CELLS
JRNL TITL 2 INTO EMBRYONIC STEM CELLS BY INHIBITION OF CASEIN KINASE 1.
JRNL REF CELL CHEM BIOL V. 23 494 2016
JRNL REFN ESSN 2451-9456
JRNL PMID 27049670
JRNL DOI 10.1016/J.CHEMBIOL.2016.02.015
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.21
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 16897
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) : 0.241
REMARK 3 R VALUE (WORKING SET) : 0.240
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 890
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 795
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 64.73
REMARK 3 BIN R VALUE (WORKING SET) : 0.5890
REMARK 3 BIN FREE R VALUE SET COUNT : 42
REMARK 3 BIN FREE R VALUE : 0.6650
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2350
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 37
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.64
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 73.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.12000
REMARK 3 B22 (A**2) : 4.12000
REMARK 3 B33 (A**2) : -13.37000
REMARK 3 B12 (A**2) : 2.06000
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): 0.325
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.229
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.274
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.893
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
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): 2465 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2341 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3321 ; 1.836 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5377 ; 1.036 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 293 ; 6.436 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 119 ;36.104 ;22.941
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 449 ;16.162 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;15.424 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 344 ; 0.108 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2761 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 613 ; 0.002 ; 0.020
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): 1153 ; 2.355 ; 3.763
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1152 ; 2.341 ; 3.760
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1441 ; 3.844 ; 5.639
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 : 1
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 2 A 294
REMARK 3 ORIGIN FOR THE GROUP (A): -34.0433 27.0410 8.2141
REMARK 3 T TENSOR
REMARK 3 T11: 0.0909 T22: 0.0714
REMARK 3 T33: 0.4760 T12: -0.0019
REMARK 3 T13: -0.0482 T23: 0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 1.9948 L22: 1.5468
REMARK 3 L33: 5.9228 L12: 0.4800
REMARK 3 L13: 0.3171 L23: 0.9412
REMARK 3 S TENSOR
REMARK 3 S11: -0.1007 S12: 0.1792 S13: 0.1396
REMARK 3 S21: -0.3719 S22: 0.0443 S23: 0.1496
REMARK 3 S31: -0.2982 S32: -0.5152 S33: 0.0563
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 5IH5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-FEB-16.
REMARK 100 THE DEPOSITION ID IS D_1000218232.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-MAR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.3-9.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92019
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17788
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 45.210
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 19.00
REMARK 200 R MERGE (I) : 0.18600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.1900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 64.8
REMARK 200 DATA REDUNDANCY IN SHELL : 9.70
REMARK 200 R MERGE FOR SHELL (I) : 1.29700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.590
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: 5IH4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M LI2SO4, 0.7 - 0.8 M NA-K
REMARK 280 TARTRATE, 0.1 M CHES, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.49333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 100.98667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 100.98667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 50.49333
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 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 TOTAL BURIED SURFACE AREA: 690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 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 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 1
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 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 ND2 ASN A 183 O HOH A 401 2.13
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 N GLN A 223 N GLN A 223 4465 1.64
REMARK 500 O HOH A 430 O HOH A 430 4465 1.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 197 CG GLU A 197 CD 0.111
REMARK 500 GLU A 197 CD GLU A 197 OE1 0.093
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 69 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 193 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 GLU A 197 OE1 - CD - OE2 ANGL. DEV. = 8.4 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 ARG A 127 -4.04 72.61
REMARK 500 ASP A 149 96.84 70.56
REMARK 500 SER A 210 147.94 -174.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 50 ND1
REMARK 620 2 CYS A 71 SG 115.7
REMARK 620 3 HIS A 278 NE2 82.0 46.6
REMARK 620 4 SRT A 303 O11 98.6 126.1 105.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AUE A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SRT A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 305
DBREF 5IH5 A 1 294 UNP P48730 KC1D_HUMAN 1 294
SEQRES 1 A 294 MET GLU LEU ARG VAL GLY ASN ARG TYR ARG LEU GLY ARG
SEQRES 2 A 294 LYS ILE GLY SER GLY SER PHE GLY ASP ILE TYR LEU GLY
SEQRES 3 A 294 THR ASP ILE ALA ALA GLY GLU GLU VAL ALA ILE LYS LEU
SEQRES 4 A 294 GLU CYS VAL LYS THR LYS HIS PRO GLN LEU HIS ILE GLU
SEQRES 5 A 294 SER LYS ILE TYR LYS MET MET GLN GLY GLY VAL GLY ILE
SEQRES 6 A 294 PRO THR ILE ARG TRP CYS GLY ALA GLU GLY ASP TYR ASN
SEQRES 7 A 294 VAL MET VAL MET GLU LEU LEU GLY PRO SER LEU GLU ASP
SEQRES 8 A 294 LEU PHE ASN PHE CYS SER ARG LYS PHE SER LEU LYS THR
SEQRES 9 A 294 VAL LEU LEU LEU ALA ASP GLN MET ILE SER ARG ILE GLU
SEQRES 10 A 294 TYR ILE HIS SER LYS ASN PHE ILE HIS ARG ASP VAL LYS
SEQRES 11 A 294 PRO ASP ASN PHE LEU MET GLY LEU GLY LYS LYS GLY ASN
SEQRES 12 A 294 LEU VAL TYR ILE ILE ASP PHE GLY LEU ALA LYS LYS TYR
SEQRES 13 A 294 ARG ASP ALA ARG THR HIS GLN HIS ILE PRO TYR ARG GLU
SEQRES 14 A 294 ASN LYS ASN LEU THR GLY THR ALA ARG TYR ALA SER ILE
SEQRES 15 A 294 ASN THR HIS LEU GLY ILE GLU GLN SER ARG ARG ASP ASP
SEQRES 16 A 294 LEU GLU SER LEU GLY TYR VAL LEU MET TYR PHE ASN LEU
SEQRES 17 A 294 GLY SER LEU PRO TRP GLN GLY LEU LYS ALA ALA THR LYS
SEQRES 18 A 294 ARG GLN LYS TYR GLU ARG ILE SER GLU LYS LYS MET SER
SEQRES 19 A 294 THR PRO ILE GLU VAL LEU CYS LYS GLY TYR PRO SER GLU
SEQRES 20 A 294 PHE ALA THR TYR LEU ASN PHE CYS ARG SER LEU ARG PHE
SEQRES 21 A 294 ASP ASP LYS PRO ASP TYR SER TYR LEU ARG GLN LEU PHE
SEQRES 22 A 294 ARG ASN LEU PHE HIS ARG GLN GLY PHE SER TYR ASP TYR
SEQRES 23 A 294 VAL PHE ASP TRP ASN MET LEU LYS
HET ZN A 301 1
HET AUE A 302 20
HET SRT A 303 10
HET SO4 A 304 5
HET SO4 A 305 5
HETNAM ZN ZINC ION
HETNAM AUE 6-(3-CHLOROPHENYL)PTERIDINE-2,4,7-TRIAMINE
HETNAM SRT S,R MESO-TARTARIC ACID
HETNAM SO4 SULFATE ION
FORMUL 2 ZN ZN 2+
FORMUL 3 AUE C12 H10 CL N7
FORMUL 4 SRT C4 H6 O6
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 7 HOH *37(H2 O)
HELIX 1 AA1 GLN A 48 MET A 59 1 12
HELIX 2 AA2 SER A 88 CYS A 96 1 9
HELIX 3 AA3 SER A 101 LYS A 122 1 22
HELIX 4 AA4 LYS A 130 ASP A 132 5 3
HELIX 5 AA5 LEU A 138 GLY A 142 5 5
HELIX 6 AA6 THR A 176 ALA A 180 5 5
HELIX 7 AA7 SER A 181 LEU A 186 1 6
HELIX 8 AA8 SER A 191 GLY A 209 1 19
HELIX 9 AA9 LYS A 224 THR A 235 1 12
HELIX 10 AB1 PRO A 236 LYS A 242 1 7
HELIX 11 AB2 SER A 246 LEU A 258 1 13
HELIX 12 AB3 ASP A 265 GLN A 280 1 16
SHEET 1 AA1 6 ARG A 4 VAL A 5 0
SHEET 2 AA1 6 TYR A 9 SER A 17 -1 O TYR A 9 N VAL A 5
SHEET 3 AA1 6 ASP A 22 ASP A 28 -1 O LEU A 25 N GLY A 12
SHEET 4 AA1 6 GLU A 33 CYS A 41 -1 O GLU A 33 N ASP A 28
SHEET 5 AA1 6 TYR A 77 GLU A 83 -1 O ASN A 78 N GLU A 40
SHEET 6 AA1 6 ILE A 68 GLU A 74 -1 N GLY A 72 O VAL A 79
SHEET 1 AA2 2 PHE A 124 ILE A 125 0
SHEET 2 AA2 2 LYS A 154 LYS A 155 -1 O LYS A 154 N ILE A 125
SHEET 1 AA3 2 PHE A 134 MET A 136 0
SHEET 2 AA3 2 VAL A 145 ILE A 147 -1 O TYR A 146 N LEU A 135
LINK ND1 HIS A 50 ZN ZN A 301 1555 1555 2.07
LINK SG CYS A 71 ZN ZN A 301 1555 1555 2.18
LINK NE2 HIS A 278 ZN ZN A 301 1555 2565 2.10
LINK ZN ZN A 301 O11 SRT A 303 1555 1555 2.11
SITE 1 AC1 4 HIS A 50 CYS A 71 HIS A 278 SRT A 303
SITE 1 AC2 10 ILE A 23 ALA A 36 LYS A 38 GLU A 52
SITE 2 AC2 10 TYR A 56 MET A 80 MET A 82 GLU A 83
SITE 3 AC2 10 LEU A 84 LEU A 85
SITE 1 AC3 7 HIS A 50 LYS A 57 CYS A 71 ARG A 259
SITE 2 AC3 7 HIS A 278 ARG A 279 ZN A 301
SITE 1 AC4 3 ARG A 127 LYS A 154 LYS A 171
SITE 1 AC5 5 ARG A 178 GLN A 214 GLY A 215 LYS A 224
SITE 2 AC5 5 HOH A 426
CRYST1 65.070 65.070 151.480 90.00 90.00 120.00 P 31 2 1 6
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 0.015368 0.008873 0.000000 0.00000
SCALE2 0.000000 0.017746 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006602 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
