HEADER METAL BINDING PROTEIN/TRANSFERASE 29-OCT-04 1WRZ
TITLE CALMODULIN COMPLEXED WITH A PEPTIDE FROM A HUMAN DEATH-ASSOCIATED
TITLE 2 PROTEIN KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DEATH-ASSOCIATED PROTEIN KINASE 2;
COMPND 7 CHAIN: B;
COMPND 8 FRAGMENT: RESIDUES 302-320;
COMPND 9 SYNONYM: DAP KINASE 2, DAP- KINASE RELATED PROTEIN 1, DRP-1;
COMPND 10 EC: 2.7.1.37;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3)PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET8A;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 13 OF THE PEPTIDE IS NATURALLY FOUND IN HOMO SAPIENS (HUMAN).
KEYWDS CALMODULIN, PROTEIN KINASE, METAL BINDING PROTEIN-TRANSFERASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.KURSULA,J.VAHOKOSKI,M.WILMANNS
REVDAT 5 13-MAR-24 1WRZ 1 REMARK
REVDAT 4 20-NOV-19 1WRZ 1 REMARK LINK
REVDAT 3 13-JUL-11 1WRZ 1 VERSN
REVDAT 2 24-FEB-09 1WRZ 1 VERSN
REVDAT 1 21-MAR-06 1WRZ 0
JRNL AUTH P.KURSULA,J.VAHOKOSKI,M.WILMANNS
JRNL TITL THE MODE OF BINDING OF CALMODULIN TO DEATH-ASSOCIATED
JRNL TITL 2 PROTEIN KINASES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0000
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : -3.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 10396
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) : 0.227
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 520
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 743
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE SET COUNT : 39
REMARK 3 BIN FREE R VALUE : 0.3070
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1328
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 90
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 28.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.59000
REMARK 3 B22 (A**2) : 0.08000
REMARK 3 B33 (A**2) : -0.41000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.37000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.277
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.219
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.200
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.594
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.870
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1392 ; 0.009 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1228 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1867 ; 0.988 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2872 ; 0.773 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 174 ; 5.579 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 77 ;29.804 ;25.325
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 266 ;16.988 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;17.530 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 202 ; 0.059 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1592 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 278 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 446 ; 0.194 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1550 ; 0.202 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 831 ; 0.084 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 64 ; 0.177 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 15 ; 0.148 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 23 ; 0.181 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 73 ; 0.195 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.222 ; 0.200
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): 898 ; 0.682 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 355 ; 0.111 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1372 ; 1.050 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 568 ; 1.121 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 495 ; 1.466 ; 5.000
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 : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 81 A 148
REMARK 3 RESIDUE RANGE : A 153 A 154
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5656 -0.0273 9.1508
REMARK 3 T TENSOR
REMARK 3 T11: 0.2482 T22: -0.0252
REMARK 3 T33: -0.2193 T12: 0.0416
REMARK 3 T13: -0.0510 T23: 0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 3.4776 L22: 12.6509
REMARK 3 L33: 20.1772 L12: -3.5799
REMARK 3 L13: -3.9439 L23: 2.6607
REMARK 3 S TENSOR
REMARK 3 S11: -0.1280 S12: -0.2370 S13: -0.0509
REMARK 3 S21: -0.3258 S22: 0.0702 S23: -0.2436
REMARK 3 S31: 0.6635 S32: -0.0062 S33: 0.0578
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 80
REMARK 3 RESIDUE RANGE : A 151 A 152
REMARK 3 ORIGIN FOR THE GROUP (A): 12.2505 11.6484 27.4472
REMARK 3 T TENSOR
REMARK 3 T11: -0.2450 T22: -0.2278
REMARK 3 T33: -0.1566 T12: 0.0308
REMARK 3 T13: -0.0016 T23: -0.0227
REMARK 3 L TENSOR
REMARK 3 L11: 7.4375 L22: 2.5046
REMARK 3 L33: 3.7182 L12: -2.5041
REMARK 3 L13: -0.3317 L23: -0.3655
REMARK 3 S TENSOR
REMARK 3 S11: 0.1041 S12: 0.4184 S13: -0.2425
REMARK 3 S21: -0.1133 S22: -0.0885 S23: 0.1808
REMARK 3 S31: 0.2038 S32: 0.0178 S33: -0.0156
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 302 B 320
REMARK 3 ORIGIN FOR THE GROUP (A): 13.3257 3.4566 19.6406
REMARK 3 T TENSOR
REMARK 3 T11: 0.0496 T22: -0.0497
REMARK 3 T33: -0.1818 T12: 0.0756
REMARK 3 T13: -0.0444 T23: -0.0308
REMARK 3 L TENSOR
REMARK 3 L11: 16.2638 L22: 14.5867
REMARK 3 L33: 22.9594 L12: -8.4429
REMARK 3 L13: -12.0702 L23: 4.5706
REMARK 3 S TENSOR
REMARK 3 S11: -0.5607 S12: -0.6563 S13: -0.5514
REMARK 3 S21: 0.0689 S22: 0.5667 S23: 0.0069
REMARK 3 S31: 1.4941 S32: 1.2367 S33: -0.0060
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 DURING REFINEMENT
REMARK 4
REMARK 4 1WRZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-NOV-04.
REMARK 100 THE DEPOSITION ID IS D_1000023929.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUL-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X13
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8043
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10397
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.36400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM ACETATE, PEG 1500, CALCIUM
REMARK 280 CHLORIDE, PH 4.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 33.03500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 16.88000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 33.03500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 16.88000
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 MET A 0
REMARK 465 ALA A 1
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 ASP A 22 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 93 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 131 CB - CG - OD2 ANGL. DEV. = 6.2 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 3 -78.34 149.35
REMARK 500 LEU A 4 121.19 73.12
REMARK 500 MET A 76 21.07 -79.56
REMARK 500 LYS A 77 100.76 -174.32
REMARK 500 ASP A 78 -56.83 -169.77
REMARK 500 ASP A 80 98.09 96.60
REMARK 500 SER A 81 -59.55 -148.28
REMARK 500 GLU A 83 -1.25 65.56
REMARK 500 LYS A 115 56.74 -96.95
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 CA A 151 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 20 OD2
REMARK 620 2 ASP A 22 OD2 79.8
REMARK 620 3 ASP A 24 OD1 80.3 78.1
REMARK 620 4 THR A 26 O 84.8 154.7 79.7
REMARK 620 5 GLU A 31 OE1 109.0 129.5 151.4 74.5
REMARK 620 6 GLU A 31 OE2 98.7 77.0 154.8 125.4 52.7
REMARK 620 7 HOH A5011 O 157.7 82.3 83.1 106.7 92.7 90.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 152 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 56 OD1
REMARK 620 2 ASP A 58 OD1 81.6
REMARK 620 3 ASN A 60 OD1 85.7 76.8
REMARK 620 4 THR A 62 O 84.4 158.4 86.0
REMARK 620 5 GLU A 67 OE1 92.9 72.3 148.9 124.9
REMARK 620 6 GLU A 67 OE2 108.2 122.9 156.6 77.1 51.6
REMARK 620 7 HOH A5012 O 157.6 77.1 82.8 113.8 87.2 89.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 153 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 93 OD2
REMARK 620 2 ASP A 95 OD1 90.0
REMARK 620 3 ASN A 97 OD1 81.9 77.9
REMARK 620 4 TYR A 99 O 85.2 155.7 77.9
REMARK 620 5 GLU A 104 OE1 112.6 69.3 143.6 134.3
REMARK 620 6 GLU A 104 OE2 118.7 119.5 150.9 83.3 51.0
REMARK 620 7 HOH A5013 O 157.7 83.0 75.9 92.5 84.7 82.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 154 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 129 OD1
REMARK 620 2 ASP A 131 OD2 101.1
REMARK 620 3 ASP A 133 OD2 93.9 91.5
REMARK 620 4 GLN A 135 O 75.3 175.8 86.7
REMARK 620 5 GLU A 140 OE1 95.2 74.0 164.2 108.2
REMARK 620 6 GLU A 140 OE2 103.0 114.3 145.2 69.0 43.8
REMARK 620 7 HOH A5014 O 175.3 83.6 86.3 100.1 85.8 74.5
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 151
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 152
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 153
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 154
DBREF 1WRZ A 0 148 GB 30584053 AAP36275 1 149
DBREF 1WRZ B 302 320 UNP Q9UIK4 DAK2_HUMAN 312 330
SEQRES 1 A 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 A 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 A 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 A 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 A 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 A 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 A 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 A 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 A 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 A 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 A 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 A 149 GLN MET MET THR ALA LYS
SEQRES 1 B 19 ARG ARG ARG TRP LYS LEU SER PHE SER ILE VAL SER LEU
SEQRES 2 B 19 CYS ASN HIS LEU THR ARG
HET CA A 151 1
HET CA A 152 1
HET CA A 153 1
HET CA A 154 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 4(CA 2+)
FORMUL 7 HOH *90(H2 O)
HELIX 1 1 THR A 5 ASP A 20 1 16
HELIX 2 2 THR A 28 LEU A 39 1 12
HELIX 3 3 THR A 44 ASP A 56 1 13
HELIX 4 4 ASP A 64 LYS A 75 1 12
HELIX 5 5 GLU A 84 ASP A 93 1 10
HELIX 6 6 SER A 101 GLY A 113 1 13
HELIX 7 7 THR A 117 ASP A 129 1 13
HELIX 8 8 TYR A 138 MET A 145 1 8
HELIX 9 9 ARG B 303 THR B 319 1 17
SHEET 1 A 2 TYR A 99 ILE A 100 0
SHEET 2 A 2 VAL A 136 ASN A 137 -1 O VAL A 136 N ILE A 100
LINK OD2 ASP A 20 CA CA A 151 1555 1555 2.29
LINK OD2 ASP A 22 CA CA A 151 1555 1555 2.36
LINK OD1 ASP A 24 CA CA A 151 1555 1555 2.43
LINK O THR A 26 CA CA A 151 1555 1555 2.27
LINK OE1 GLU A 31 CA CA A 151 1555 1555 2.46
LINK OE2 GLU A 31 CA CA A 151 1555 1555 2.43
LINK OD1 ASP A 56 CA CA A 152 1555 1555 2.16
LINK OD1 ASP A 58 CA CA A 152 1555 1555 2.44
LINK OD1 ASN A 60 CA CA A 152 1555 1555 2.33
LINK O THR A 62 CA CA A 152 1555 1555 2.38
LINK OE1 GLU A 67 CA CA A 152 1555 1555 2.63
LINK OE2 GLU A 67 CA CA A 152 1555 1555 2.30
LINK OD2 ASP A 93 CA CA A 153 1555 1555 2.32
LINK OD1 ASP A 95 CA CA A 153 1555 1555 2.53
LINK OD1 ASN A 97 CA CA A 153 1555 1555 2.39
LINK O TYR A 99 CA CA A 153 1555 1555 2.32
LINK OE1 GLU A 104 CA CA A 153 1555 1555 2.74
LINK OE2 GLU A 104 CA CA A 153 1555 1555 2.25
LINK OD1 ASP A 129 CA CA A 154 1555 1555 2.36
LINK OD2 ASP A 131 CA CA A 154 1555 1555 2.10
LINK OD2 ASP A 133 CA CA A 154 1555 1555 2.24
LINK O GLN A 135 CA CA A 154 1555 1555 2.41
LINK OE1 GLU A 140 CA CA A 154 1555 1555 2.96
LINK OE2 GLU A 140 CA CA A 154 1555 1555 2.87
LINK CA CA A 151 O HOH A5011 1555 1555 2.32
LINK CA CA A 152 O HOH A5012 1555 1555 2.31
LINK CA CA A 153 O HOH A5013 1555 1555 2.33
LINK CA CA A 154 O HOH A5014 1555 1555 2.41
SITE 1 AC1 6 ASP A 20 ASP A 22 ASP A 24 THR A 26
SITE 2 AC1 6 GLU A 31 HOH A5011
SITE 1 AC2 6 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 AC2 6 GLU A 67 HOH A5012
SITE 1 AC3 6 ASP A 93 ASP A 95 ASN A 97 TYR A 99
SITE 2 AC3 6 GLU A 104 HOH A5013
SITE 1 AC4 6 ASP A 129 ASP A 131 ASP A 133 GLN A 135
SITE 2 AC4 6 GLU A 140 HOH A5014
CRYST1 66.070 33.760 73.870 90.00 110.04 90.00 C 1 2 1 4
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 0.015135 0.000000 0.005521 0.00000
SCALE2 0.000000 0.029621 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014410 0.00000
(ATOM LINES ARE NOT SHOWN.)
END