HEADER TRANSFERASE 29-FEB-16 5IH6
TITLE HUMAN CASEIN KINASE 1 ISOFORM DELTA (KINASE DOMAIN) IN COMPLEX WITH
TITLE 2 EPIBLASTIN A DERIVATIVE
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
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 5IH6 1 LINK
REVDAT 3 04-MAY-16 5IH6 1 JRNL
REVDAT 2 20-APR-16 5IH6 1 JRNL
REVDAT 1 13-APR-16 5IH6 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. 2.30 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 16405
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) : 0.234
REMARK 3 R VALUE (WORKING SET) : 0.233
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 : 864
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1071
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.67
REMARK 3 BIN R VALUE (WORKING SET) : 0.5420
REMARK 3 BIN FREE R VALUE SET COUNT : 56
REMARK 3 BIN FREE R VALUE : 0.4160
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2341
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 22
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 62.05
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 89.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.06000
REMARK 3 B22 (A**2) : 3.06000
REMARK 3 B33 (A**2) : -9.94000
REMARK 3 B12 (A**2) : 1.53000
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): 0.327
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.234
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.307
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.112
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2440 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2309 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3285 ; 1.552 ; 1.979
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5297 ; 0.994 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 286 ; 6.340 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 119 ;35.253 ;22.941
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 438 ;15.838 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;14.935 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 340 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2733 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 609 ; 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): 1144 ; 7.151 ; 8.537
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1143 ; 7.140 ; 8.531
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1427 ;10.457 ;12.763
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 : NULL
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 : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5IH6 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_1000218247.
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) : 1.76995
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 : 17269
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 37.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 14.10
REMARK 200 R MERGE (I) : 0.11500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.8
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 1.48100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.070
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 (%): 55.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79
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, SITTING 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 50.57333
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 101.14667
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 101.14667
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 50.57333
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: 700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14260 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 465 LYS A 294
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 NH1 ARG A 8 OD2 ASP A 28 1.55
REMARK 500 CE2 TYR A 9 OD1 ASP A 28 2.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 422 O HOH A 422 6555 1.78
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 ASN A 123 17.43 80.73
REMARK 500 ARG A 127 -3.83 76.35
REMARK 500 ASP A 149 91.55 73.47
REMARK 500 SER A 210 147.00 -175.89
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 119.9
REMARK 620 3 HIS A 278 NE2 85.3 46.3
REMARK 620 4 SRT A 302 O1 75.6 100.3 61.4
REMARK 620 5 SRT A 302 O11 114.7 104.6 95.4 50.1
REMARK 620 N 1 2 3 4
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 SRT A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 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 AUG A 305
DBREF 5IH6 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 SRT A 302 10
HET SO4 A 303 5
HET SO4 A 304 5
HET AUG A 305 20
HETNAM ZN ZINC ION
HETNAM SRT S,R MESO-TARTARIC ACID
HETNAM SO4 SULFATE ION
HETNAM AUG 6-(3-BROMOPHENYL)PTERIDINE-2,4,7-TRIAMINE
FORMUL 2 ZN ZN 2+
FORMUL 3 SRT C4 H6 O6
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 6 AUG C12 H10 BR N7
FORMUL 7 HOH *22(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 ILE A 23 N ILE A 15
SHEET 4 AA1 6 GLU A 33 CYS A 41 -1 O ILE A 37 N TYR A 24
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 GLU A 74 O TYR A 77
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 2.11
LINK SG CYS A 71 ZN ZN A 301 1555 1555 2.18
LINK NE2 HIS A 278 ZN ZN A 301 1555 2565 2.15
LINK ZN ZN A 301 O1 SRT A 302 1555 1555 2.66
LINK ZN ZN A 301 O11 SRT A 302 1555 1555 2.27
SITE 1 AC1 4 HIS A 50 CYS A 71 HIS A 278 SRT A 302
SITE 1 AC2 6 HIS A 50 CYS A 71 ARG A 259 HIS A 278
SITE 2 AC2 6 ARG A 279 ZN A 301
SITE 1 AC3 3 ARG A 127 LYS A 154 LYS A 171
SITE 1 AC4 4 ARG A 178 GLN A 214 GLY A 215 LYS A 224
SITE 1 AC5 10 ILE A 23 ALA A 36 MET A 80 MET A 82
SITE 2 AC5 10 GLU A 83 LEU A 84 LEU A 85 GLY A 86
SITE 3 AC5 10 LEU A 135 ILE A 148
CRYST1 65.720 65.720 151.720 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 0.015216 0.008785 0.000000 0.00000
SCALE2 0.000000 0.017570 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006591 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
