HEADER TRANSFERASE 09-MAY-16 5JTH
TITLE CRYSTAL STRUCTURE OF E67A CALMODULIN - CAM:RM20 ANALOG COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CAM;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: MYOSIN LIGHT CHAIN KINASE, SMOOTH MUSCLE;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: SMMLCK,KINASE-RELATED PROTEIN,KRP,TELOKIN;
COMPND 10 EC: 2.7.11.18;
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 GENE: CALM1, CALM, CAM, CAM1, CALM2, CAM2, CAMB, CALM3, CALML2,
SOURCE 6 CAM3, CAMC, CAMIII;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606
KEYWDS E67A CALMODULIN, CALCIUM SIGNAL TRANSDUCTION, PROTEIN KINASE, MYOSIN
KEYWDS 2 LIGHT CHAIN KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.L.GRUM-TOKARS,G.MINASOV,W.F.ANDERSON,D.M.WATTERSON
REVDAT 2 06-MAR-24 5JTH 1 TITLE JRNL LINK
REVDAT 1 19-JUL-17 5JTH 0
JRNL AUTH V.L.GRUM-TOKARS,G.MINASOV,W.F.ANDERSON,D.M.WATTERSON
JRNL TITL CRYSTAL STRUCTURE OF E67A CALMODULIN - CAM:RM20 ANALOG
JRNL TITL 2 COMPLEX
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.84 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
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) : 1.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 12001
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 614
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) : 1.84
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.89
REMARK 3 REFLECTION IN BIN (WORKING SET) : 787
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.63
REMARK 3 BIN R VALUE (WORKING SET) : 0.2270
REMARK 3 BIN FREE R VALUE SET COUNT : 43
REMARK 3 BIN FREE R VALUE : 0.2850
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1318
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 122
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.85000
REMARK 3 B22 (A**2) : -1.19000
REMARK 3 B33 (A**2) : 2.47000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.02000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.153
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.133
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.103
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.958
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1449 ; 0.020 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1369 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1949 ; 1.759 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3177 ; 1.022 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 185 ; 3.918 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 79 ;28.252 ;25.570
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 294 ;13.129 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;15.110 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 207 ; 0.135 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1698 ; 0.025 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 321 ; 0.020 ; 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): 717 ; 2.093 ; 2.047
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 715 ; 2.075 ; 2.041
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 909 ; 3.246 ; 3.034
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 910 ; 3.244 ; 3.038
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 732 ; 3.194 ; 2.461
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 733 ; 3.192 ; 2.463
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1041 ; 5.090 ; 3.537
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 1891 ; 7.882 ;17.194
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 1852 ; 7.797 ;16.830
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 2 A 77
REMARK 3 RESIDUE RANGE : A 401 A 402
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1989 1.0428 -7.5408
REMARK 3 T TENSOR
REMARK 3 T11: 0.0407 T22: 0.0994
REMARK 3 T33: 0.0430 T12: 0.0324
REMARK 3 T13: 0.0270 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 2.4328 L22: 1.4996
REMARK 3 L33: 2.3670 L12: -0.7063
REMARK 3 L13: 1.5463 L23: -0.8110
REMARK 3 S TENSOR
REMARK 3 S11: -0.1354 S12: -0.2860 S13: 0.0352
REMARK 3 S21: 0.1822 S22: 0.1244 S23: 0.0536
REMARK 3 S31: -0.1871 S32: -0.1840 S33: 0.0111
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 78 A 148
REMARK 3 RESIDUE RANGE : A 403 A 404
REMARK 3 ORIGIN FOR THE GROUP (A): -1.7482 -17.8031 -14.1812
REMARK 3 T TENSOR
REMARK 3 T11: 0.0030 T22: 0.0762
REMARK 3 T33: 0.0173 T12: -0.0042
REMARK 3 T13: 0.0016 T23: -0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 2.8085 L22: 2.6707
REMARK 3 L33: 1.2301 L12: -0.2046
REMARK 3 L13: -0.2351 L23: -0.2558
REMARK 3 S TENSOR
REMARK 3 S11: -0.0312 S12: -0.1015 S13: 0.1450
REMARK 3 S21: 0.0427 S22: 0.0388 S23: -0.0199
REMARK 3 S31: -0.0310 S32: -0.0127 S33: -0.0075
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 2 B 22
REMARK 3 ORIGIN FOR THE GROUP (A): -3.5957 -7.8235 -6.8627
REMARK 3 T TENSOR
REMARK 3 T11: 0.0284 T22: 0.0575
REMARK 3 T33: 0.0259 T12: -0.0063
REMARK 3 T13: -0.0114 T23: -0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 8.2298 L22: 4.5771
REMARK 3 L33: 3.4563 L12: -4.3419
REMARK 3 L13: -3.0450 L23: 1.7638
REMARK 3 S TENSOR
REMARK 3 S11: 0.0150 S12: -0.2336 S13: 0.1455
REMARK 3 S21: 0.2326 S22: 0.1570 S23: -0.2270
REMARK 3 S31: 0.0272 S32: -0.0231 S33: -0.1719
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: NULL
REMARK 4
REMARK 4 5JTH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000221087.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-FEB-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97857
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12634
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.840
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM ACETATE PH 4.6, 25%(W/V)
REMARK 280 PEG 4000, 20MM CACL2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 28.52650
REMARK 290 SMTRY3 2 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: 3480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9130 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 465 ACE B 0
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 140 CD GLU A 140 OE1 0.077
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 ASP A 95 CB - CG - OD1 ANGL. DEV. = 5.7 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 VAL A 55 36.94 -144.03
REMARK 500 LYS A 77 -75.61 -108.11
REMARK 500 ASP A 80 47.36 -86.34
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 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 20 OD1
REMARK 620 2 ASP A 22 OD1 81.0
REMARK 620 3 ASP A 24 OD1 84.7 78.5
REMARK 620 4 THR A 26 O 83.2 154.7 80.5
REMARK 620 5 GLU A 31 OE1 107.7 129.4 150.2 74.4
REMARK 620 6 GLU A 31 OE2 97.0 74.6 152.4 127.1 55.1
REMARK 620 7 HOH A 529 O 159.4 78.8 87.4 114.2 88.4 81.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 56 OD1
REMARK 620 2 ASP A 58 OD1 71.7
REMARK 620 3 ASP A 58 OD2 89.0 48.2
REMARK 620 4 ASN A 60 OD1 73.7 68.3 116.3
REMARK 620 5 THR A 62 O 77.0 142.1 152.2 83.0
REMARK 620 6 HOH A 519 O 153.8 114.2 114.3 84.7 85.9
REMARK 620 7 HOH A 601 O 92.4 125.5 81.0 156.9 75.8 102.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 93 OD1
REMARK 620 2 ASP A 95 OD1 81.2
REMARK 620 3 ASN A 97 OD1 83.9 77.1
REMARK 620 4 TYR A 99 O 88.0 153.0 77.2
REMARK 620 5 GLU A 104 OE1 110.8 126.4 152.9 80.6
REMARK 620 6 GLU A 104 OE2 94.5 76.7 153.7 129.1 51.1
REMARK 620 7 HOH A 511 O 163.1 82.2 89.1 105.5 82.0 85.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 404 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 129 OD1
REMARK 620 2 ASP A 131 OD1 80.5
REMARK 620 3 ASP A 133 OD1 82.1 80.4
REMARK 620 4 GLN A 135 O 92.8 153.2 72.9
REMARK 620 5 GLN A 135 O 84.1 154.9 77.9 10.7
REMARK 620 6 GLU A 140 OE1 117.8 125.0 148.2 81.1 79.8
REMARK 620 7 GLU A 140 OE2 89.4 75.9 155.9 130.3 123.8 54.8
REMARK 620 8 HOH A 522 O 157.9 81.9 81.9 97.0 107.3 83.4 99.1
REMARK 620 N 1 2 3 4 5 6 7
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 404
DBREF 5JTH A 0 148 UNP P62158 CALM_HUMAN 1 149
DBREF 5JTH B 1 20 UNP Q15746 MYLK_HUMAN 1691 1710
SEQADV 5JTH ALA A 67 UNP P62158 GLU 68 ENGINEERED MUTATION
SEQADV 5JTH ACE B 0 UNP Q15746 ACETYLATION
SEQADV 5JTH NH2 B 22 UNP Q15746 AMIDATION
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 ALA 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 22 ACE ARG ARG LYS TRP GLN LYS THR GLY ASN ALA VAL ARG
SEQRES 2 B 22 ALA ILE GLY ARG LEU SER SER MET NH2
HET NH2 B 22 1
HET CA A 401 1
HET CA A 402 1
HET CA A 403 1
HET CA A 404 1
HETNAM NH2 AMINO GROUP
HETNAM CA CALCIUM ION
FORMUL 2 NH2 H2 N
FORMUL 3 CA 4(CA 2+)
FORMUL 7 HOH *122(H2 O)
HELIX 1 AA1 THR A 5 ASP A 20 1 16
HELIX 2 AA2 THR A 28 LEU A 39 1 12
HELIX 3 AA3 THR A 44 GLU A 54 1 11
HELIX 4 AA4 PHE A 65 ARG A 74 1 10
HELIX 5 AA5 ASP A 80 ASP A 93 1 14
HELIX 6 AA6 SER A 101 GLY A 113 1 13
HELIX 7 AA7 THR A 117 ASP A 129 1 13
HELIX 8 AA8 ASN A 137 THR A 146 1 10
HELIX 9 AA9 ARG B 2 MET B 20 1 19
SHEET 1 AA1 2 THR A 26 ILE A 27 0
SHEET 2 AA1 2 ILE A 63 ASP A 64 -1 O ILE A 63 N ILE A 27
LINK C MET B 20 N NH2 B 22 1555 1555 1.35
LINK OD1 ASP A 20 CA CA A 401 1555 1555 2.29
LINK OD1 ASP A 22 CA CA A 401 1555 1555 2.38
LINK OD1 ASP A 24 CA CA A 401 1555 1555 2.33
LINK O THR A 26 CA CA A 401 1555 1555 2.26
LINK OE1 GLU A 31 CA CA A 401 1555 1555 2.36
LINK OE2 GLU A 31 CA CA A 401 1555 1555 2.42
LINK OD1 ASP A 56 CA CA A 402 1555 1555 2.51
LINK OD1 ASP A 58 CA CA A 402 1555 1555 2.79
LINK OD2 ASP A 58 CA CA A 402 1555 1555 2.58
LINK OD1 ASN A 60 CA CA A 402 1555 1555 2.27
LINK O THR A 62 CA CA A 402 1555 1555 2.65
LINK OD1 ASP A 93 CA CA A 403 1555 1555 2.26
LINK OD1 ASP A 95 CA CA A 403 1555 1555 2.43
LINK OD1 ASN A 97 CA CA A 403 1555 1555 2.39
LINK O TYR A 99 CA CA A 403 1555 1555 2.25
LINK OE1 GLU A 104 CA CA A 403 1555 1555 2.42
LINK OE2 GLU A 104 CA CA A 403 1555 1555 2.63
LINK OD1 ASP A 129 CA CA A 404 1555 1555 2.34
LINK OD1 ASP A 131 CA CA A 404 1555 1555 2.30
LINK OD1 ASP A 133 CA CA A 404 1555 1555 2.40
LINK O AGLN A 135 CA CA A 404 1555 1555 2.28
LINK O BGLN A 135 CA CA A 404 1555 1555 2.35
LINK OE1 GLU A 140 CA CA A 404 1555 1555 2.38
LINK OE2 GLU A 140 CA CA A 404 1555 1555 2.59
LINK CA CA A 401 O HOH A 529 1555 1555 2.41
LINK CA CA A 402 O HOH A 519 1555 1555 2.59
LINK CA CA A 402 O HOH A 601 1555 1555 2.61
LINK CA CA A 403 O HOH A 511 1555 2444 2.43
LINK CA CA A 404 O HOH A 522 1555 1555 2.38
SITE 1 AC1 6 ASP A 20 ASP A 22 ASP A 24 THR A 26
SITE 2 AC1 6 GLU A 31 HOH A 529
SITE 1 AC2 6 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 AC2 6 HOH A 519 HOH A 601
SITE 1 AC3 5 ASP A 93 ASP A 95 ASN A 97 TYR A 99
SITE 2 AC3 5 GLU A 104
SITE 1 AC4 6 ASP A 129 ASP A 131 ASP A 133 GLN A 135
SITE 2 AC4 6 GLU A 140 HOH A 522
CRYST1 29.094 57.053 44.871 90.00 97.18 90.00 P 1 21 1 2
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 0.034371 0.000000 0.004330 0.00000
SCALE2 0.000000 0.017528 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022462 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
