HEADER TRANSFERASE 08-FEB-17 5N2N
TITLE CRYSTAL STRUCTURE OF THE RECEIVER DOMAIN OF THE HISTIDINE KINASE CKI1
TITLE 2 FROM ARABIDOPSIS THALIANA COMPLEXED WITH MG2+ AND BEF3-
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTIDINE KINASE CKI1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PROTEIN CYTOKININ-INDEPENDENT 1;
COMPND 5 EC: 2.7.13.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: THALE CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: CKI1, AT2G47430, T30B22.27;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS RECEIVER DOMAIN, HISTIDINE KINASE CKI1, (ALPHA/BETA)5 FOLD,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR O.OTRUSINOVA,G.DEMO,P.PADRTA,Z.JASENAKOVA,B.PEKAROVA,Z.GELOVA,
AUTHOR 2 A.SZMITKOWSKA,P.KADERAVEK,S.JANSEN,M.ZACHRDLA,T.KLUMPLER,J.MAREK,
AUTHOR 3 J.HRITZ,L.JANDA,H.IWAI,M.WIMMEROVA,J.HEJATKO,L.ZIDEK
REVDAT 3 17-JAN-24 5N2N 1 LINK
REVDAT 2 01-NOV-17 5N2N 1 JRNL
REVDAT 1 13-SEP-17 5N2N 0
JRNL AUTH O.OTRUSINOVA,G.DEMO,P.PADRTA,Z.JASENAKOVA,B.PEKAROVA,
JRNL AUTH 2 Z.GELOVA,A.SZMITKOWSKA,P.KADERAVEK,S.JANSEN,M.ZACHRDLA,
JRNL AUTH 3 T.KLUMPLER,J.MAREK,J.HRITZ,L.JANDA,H.IWAI,M.WIMMEROVA,
JRNL AUTH 4 J.HEJATKO,L.ZIDEK
JRNL TITL CONFORMATIONAL DYNAMICS ARE A KEY FACTOR IN SIGNALING
JRNL TITL 2 MEDIATED BY THE RECEIVER DOMAIN OF A SENSOR HISTIDINE KINASE
JRNL TITL 3 FROM ARABIDOPSIS THALIANA.
JRNL REF J. BIOL. CHEM. V. 292 17525 2017
JRNL REFN ESSN 1083-351X
JRNL PMID 28860196
JRNL DOI 10.1074/JBC.M117.790212
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.47
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 13028
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 658
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) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10
REMARK 3 REFLECTION IN BIN (WORKING SET) : 936
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2020
REMARK 3 BIN FREE R VALUE SET COUNT : 55
REMARK 3 BIN FREE R VALUE : 0.2740
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1160
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 53
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.23000
REMARK 3 B22 (A**2) : -0.15000
REMARK 3 B33 (A**2) : -3.08000
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): 0.146
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.144
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.110
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.034
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
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): 1182 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1136 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1573 ; 1.850 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2629 ; 1.020 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 147 ; 6.029 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 56 ;39.178 ;24.821
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 228 ;16.178 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;22.273 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 176 ; 0.158 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1315 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 241 ; 0.001 ; 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): 594 ; 4.159 ; 4.102
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 593 ; 4.150 ; 4.098
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 739 ; 5.479 ; 6.123
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 740 ; 5.478 ; 6.128
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 588 ; 6.212 ; 4.957
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 583 ; 6.220 ; 4.969
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 832 ; 9.337 ; 7.108
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 1337 ;11.288 ;33.282
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 1329 ;11.301 ;33.238
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 : NULL
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
REMARK 4
REMARK 4 5N2N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1200003359.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.05
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13705
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 46.740
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.47000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3MM4
REMARK 200
REMARK 200 REMARK: PRISM
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.54 M (NH4)2(SO4), 0.1 M MES PH 5.05,
REMARK 280 12% GLYCEROL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 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 40.06950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.06950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 26.42500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.07600
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 26.42500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.07600
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 40.06950
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 26.42500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 50.07600
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 40.06950
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 26.42500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 50.07600
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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: 350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1342 LIES ON A SPECIAL POSITION.
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 925
REMARK 465 SER A 926
REMARK 465 SER A 927
REMARK 465 HIS A 928
REMARK 465 HIS A 929
REMARK 465 HIS A 930
REMARK 465 HIS A 931
REMARK 465 HIS A 932
REMARK 465 HIS A 933
REMARK 465 ARG A 940
REMARK 465 GLY A 941
REMARK 465 SER A 942
REMARK 465 HIS A 943
REMARK 465 MET A 944
REMARK 465 ALA A 945
REMARK 465 SER A 946
REMARK 465 THR A 947
REMARK 465 ASP A 948
REMARK 465 SER A 949
REMARK 465 GLU A 950
REMARK 465 SER A 951
REMARK 465 GLU A 952
REMARK 465 THR A 953
REMARK 465 ARG A 954
REMARK 465 VAL A 955
REMARK 465 LYS A 956
REMARK 465 SER A 957
REMARK 465 VAL A 958
REMARK 465 ARG A 959
REMARK 465 THR A 960
REMARK 465 GLY A 961
REMARK 465 ARG A 962
REMARK 465 LYS A 963
REMARK 465 PRO A 964
REMARK 465 ILE A 965
REMARK 465 GLY A 966
REMARK 465 ASN A 967
REMARK 465 PRO A 968
REMARK 465 GLU A 969
REMARK 465 ASP A 970
REMARK 465 GLU A 971
REMARK 465 GLN A 972
REMARK 465 GLU A 973
REMARK 465 THR A 974
REMARK 465 SER A 975
REMARK 465 LYS A 976
REMARK 465 PRO A 977
REMARK 465 ARG A 1121
REMARK 465 HIS A 1122
REMARK 465 LEU A 1123
REMARK 465 GLU A 1124
REMARK 465 HIS A 1125
REMARK 465 HIS A 1126
REMARK 465 HIS A 1127
REMARK 465 HIS A 1128
REMARK 465 HIS A 1129
REMARK 465 HIS A 1130
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 O HOH A 1347 O HOH A 1348 2.15
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 998 NE - CZ - NH2 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ASP A1050 CB - CG - OD2 ANGL. DEV. = -7.1 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 ASP A 979 30.13 -140.95
REMARK 500 GLU A1055 -68.74 75.86
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 MG A1201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 993 OD1
REMARK 620 2 ASP A1050 OD2 78.5
REMARK 620 3 GLN A1052 O 93.7 84.4
REMARK 620 4 HOH A1305 O 91.4 84.8 166.9
REMARK 620 5 HOH A1309 O 104.7 159.1 74.8 115.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 BEF A1202 BE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A1050 OD1
REMARK 620 2 BEF A1202 F1 93.3
REMARK 620 3 BEF A1202 F2 99.7 112.4
REMARK 620 4 BEF A1202 F3 96.6 121.1 122.6
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 MG A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BEF A 1202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3MM4 RELATED DB: PDB
REMARK 900 RELATED ID: 3MMN RELATED DB: PDB
REMARK 900 RELATED ID: 5LNM RELATED DB: PDB
REMARK 900 RELATED ID: 5LNN RELATED DB: PDB
DBREF 5N2N A 944 1122 UNP O22267 CKI1_ARATH 944 1122
SEQADV 5N2N GLY A 925 UNP O22267 EXPRESSION TAG
SEQADV 5N2N SER A 926 UNP O22267 EXPRESSION TAG
SEQADV 5N2N SER A 927 UNP O22267 EXPRESSION TAG
SEQADV 5N2N HIS A 928 UNP O22267 EXPRESSION TAG
SEQADV 5N2N HIS A 929 UNP O22267 EXPRESSION TAG
SEQADV 5N2N HIS A 930 UNP O22267 EXPRESSION TAG
SEQADV 5N2N HIS A 931 UNP O22267 EXPRESSION TAG
SEQADV 5N2N HIS A 932 UNP O22267 EXPRESSION TAG
SEQADV 5N2N HIS A 933 UNP O22267 EXPRESSION TAG
SEQADV 5N2N SER A 934 UNP O22267 EXPRESSION TAG
SEQADV 5N2N SER A 935 UNP O22267 EXPRESSION TAG
SEQADV 5N2N GLY A 936 UNP O22267 EXPRESSION TAG
SEQADV 5N2N LEU A 937 UNP O22267 EXPRESSION TAG
SEQADV 5N2N VAL A 938 UNP O22267 EXPRESSION TAG
SEQADV 5N2N PRO A 939 UNP O22267 EXPRESSION TAG
SEQADV 5N2N ARG A 940 UNP O22267 EXPRESSION TAG
SEQADV 5N2N GLY A 941 UNP O22267 EXPRESSION TAG
SEQADV 5N2N SER A 942 UNP O22267 EXPRESSION TAG
SEQADV 5N2N HIS A 943 UNP O22267 EXPRESSION TAG
SEQADV 5N2N LEU A 1123 UNP O22267 EXPRESSION TAG
SEQADV 5N2N GLU A 1124 UNP O22267 EXPRESSION TAG
SEQADV 5N2N HIS A 1125 UNP O22267 EXPRESSION TAG
SEQADV 5N2N HIS A 1126 UNP O22267 EXPRESSION TAG
SEQADV 5N2N HIS A 1127 UNP O22267 EXPRESSION TAG
SEQADV 5N2N HIS A 1128 UNP O22267 EXPRESSION TAG
SEQADV 5N2N HIS A 1129 UNP O22267 EXPRESSION TAG
SEQADV 5N2N HIS A 1130 UNP O22267 EXPRESSION TAG
SEQRES 1 A 206 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 A 206 VAL PRO ARG GLY SER HIS MET ALA SER THR ASP SER GLU
SEQRES 3 A 206 SER GLU THR ARG VAL LYS SER VAL ARG THR GLY ARG LYS
SEQRES 4 A 206 PRO ILE GLY ASN PRO GLU ASP GLU GLN GLU THR SER LYS
SEQRES 5 A 206 PRO SER ASP ASP GLU PHE LEU ARG GLY LYS ARG VAL LEU
SEQRES 6 A 206 VAL VAL ASP ASP ASN PHE ILE SER ARG LYS VAL ALA THR
SEQRES 7 A 206 GLY LYS LEU LYS LYS MET GLY VAL SER GLU VAL GLU GLN
SEQRES 8 A 206 CYS ASP SER GLY LYS GLU ALA LEU ARG LEU VAL THR GLU
SEQRES 9 A 206 GLY LEU THR GLN ARG GLU GLU GLN GLY SER VAL ASP LYS
SEQRES 10 A 206 LEU PRO PHE ASP TYR ILE PHE MET ASP CYS GLN MET PRO
SEQRES 11 A 206 GLU MET ASP GLY TYR GLU ALA THR ARG GLU ILE ARG LYS
SEQRES 12 A 206 VAL GLU LYS SER TYR GLY VAL ARG THR PRO ILE ILE ALA
SEQRES 13 A 206 VAL SER GLY HIS ASP PRO GLY SER GLU GLU ALA ARG GLU
SEQRES 14 A 206 THR ILE GLN ALA GLY MET ASP ALA PHE LEU ASP LYS SER
SEQRES 15 A 206 LEU ASN GLN LEU ALA ASN VAL ILE ARG GLU ILE GLU SER
SEQRES 16 A 206 LYS ARG HIS LEU GLU HIS HIS HIS HIS HIS HIS
HET MG A1201 1
HET BEF A1202 4
HETNAM MG MAGNESIUM ION
HETNAM BEF BERYLLIUM TRIFLUORIDE ION
FORMUL 2 MG MG 2+
FORMUL 3 BEF BE F3 1-
FORMUL 4 HOH *53(H2 O)
HELIX 1 AA1 ASN A 994 MET A 1008 1 15
HELIX 2 AA2 SER A 1018 GLY A 1037 1 20
HELIX 3 AA3 ASP A 1057 SER A 1071 1 15
HELIX 4 AA4 GLY A 1087 GLY A 1098 1 12
HELIX 5 AA5 GLN A 1109 LYS A 1120 1 12
SHEET 1 AA1 6 GLY A 936 LEU A 937 0
SHEET 2 AA1 6 ALA A1101 ASP A1104 -1 O PHE A1102 N GLY A 936
SHEET 3 AA1 6 ILE A1078 SER A1082 1 N ALA A1080 O LEU A1103
SHEET 4 AA1 6 TYR A1046 ASP A1050 1 N ILE A1047 O ILE A1079
SHEET 5 AA1 6 ARG A 987 VAL A 991 1 N LEU A 989 O PHE A1048
SHEET 6 AA1 6 GLU A1012 CYS A1016 1 O GLU A1012 N VAL A 988
LINK OD1 ASP A 993 MG MG A1201 1555 1555 2.10
LINK OD2 ASP A1050 MG MG A1201 1555 1555 2.18
LINK OD1 ASP A1050 BE BEF A1202 1555 1555 1.76
LINK O GLN A1052 MG MG A1201 1555 1555 2.14
LINK MG MG A1201 O HOH A1305 1555 1555 2.19
LINK MG MG A1201 O HOH A1309 1555 1555 2.20
SITE 1 AC1 6 ASP A 993 ASP A1050 GLN A1052 BEF A1202
SITE 2 AC1 6 HOH A1305 HOH A1309
SITE 1 AC2 10 ASP A1050 CYS A1051 GLN A1052 VAL A1081
SITE 2 AC2 10 SER A1082 GLY A1083 LYS A1105 MG A1201
SITE 3 AC2 10 HOH A1305 HOH A1309
CRYST1 52.850 100.152 80.139 90.00 90.00 90.00 C 2 2 21 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 0.018921 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009985 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012478 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
