HEADER CALCIUM BINDING PROTEIN/PROTEIN BINDING 04-MAY-16 5JQA
TITLE CAM:RM20 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 FRAGMENT: UNP RESIDUES 1691-1710;
COMPND 10 SYNONYM: SMMLCK, KINASE-RELATED PROTEIN, KRP, TELOKIN;
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 CALMODULIN, CALCIUM SIGNAL TRANSDUCTION, PROTEIN KINASE, MYOSIN LIGHT
KEYWDS 2 CHAIN KINASE, CALCIUM BINDING PROTEIN-PROTEIN BINDING COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR V.L.TOKARS,G.MINASOV,W.F.ANDERSON,D.M.WATTERSON
REVDAT 2 27-SEP-23 5JQA 1 REMARK
REVDAT 1 11-OCT-17 5JQA 0
JRNL AUTH V.L.TOKARS,G.MINASOV,W.F.ANDERSON,D.M.WATTERSON
JRNL TITL CAM:RM20 COMPLEX
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 12699
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) : 0.155
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 910
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.07
REMARK 3 BIN R VALUE (WORKING SET) : 0.2190
REMARK 3 BIN FREE R VALUE SET COUNT : 52
REMARK 3 BIN FREE R VALUE : 0.2560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1323
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 155
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.26000
REMARK 3 B22 (A**2) : -0.24000
REMARK 3 B33 (A**2) : -0.06000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.18000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.142
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.123
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.092
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.796
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
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): 1464 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1380 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1971 ; 1.357 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3195 ; 0.819 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 187 ; 3.161 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 81 ;27.065 ;25.432
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 293 ;10.642 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;15.705 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 209 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1725 ; 0.022 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 327 ; 0.018 ; 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): 725 ; 2.087 ; 1.866
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 723 ; 2.075 ; 1.857
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 919 ; 3.257 ; 2.758
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 920 ; 3.257 ; 2.763
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 739 ; 2.742 ; 2.256
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 740 ; 2.740 ; 2.259
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1053 ; 4.481 ; 3.232
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 1972 ; 7.066 ;15.947
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 1907 ; 7.004 ;15.478
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): -6.9266 1.2518 -7.7556
REMARK 3 T TENSOR
REMARK 3 T11: 0.0164 T22: 0.0519
REMARK 3 T33: 0.0371 T12: 0.0255
REMARK 3 T13: -0.0042 T23: 0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 0.5434 L22: 0.4639
REMARK 3 L33: 1.1206 L12: -0.3393
REMARK 3 L13: 0.7699 L23: -0.4013
REMARK 3 S TENSOR
REMARK 3 S11: -0.0695 S12: -0.0729 S13: -0.0108
REMARK 3 S21: 0.0507 S22: 0.0699 S23: 0.0122
REMARK 3 S31: -0.0978 S32: -0.0919 S33: -0.0003
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): -1.3731 -17.5265 -14.1849
REMARK 3 T TENSOR
REMARK 3 T11: 0.0167 T22: 0.0459
REMARK 3 T33: 0.0337 T12: -0.0057
REMARK 3 T13: -0.0126 T23: -0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 0.9014 L22: 0.5276
REMARK 3 L33: 0.1594 L12: 0.0534
REMARK 3 L13: -0.0700 L23: -0.1296
REMARK 3 S TENSOR
REMARK 3 S11: -0.0088 S12: -0.0368 S13: 0.0725
REMARK 3 S21: -0.0134 S22: -0.0003 S23: -0.0078
REMARK 3 S31: 0.0346 S32: -0.0134 S33: 0.0091
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 1 B 21
REMARK 3 ORIGIN FOR THE GROUP (A): -3.2795 -7.3740 -7.1853
REMARK 3 T TENSOR
REMARK 3 T11: 0.0113 T22: 0.0573
REMARK 3 T33: 0.0402 T12: -0.0048
REMARK 3 T13: -0.0091 T23: -0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 2.8862 L22: 1.4657
REMARK 3 L33: 1.4010 L12: -1.8709
REMARK 3 L13: -1.6074 L23: 0.6855
REMARK 3 S TENSOR
REMARK 3 S11: -0.0578 S12: -0.0137 S13: 0.0596
REMARK 3 S21: -0.0004 S22: 0.0540 S23: -0.0699
REMARK 3 S31: 0.0872 S32: -0.0658 S33: 0.0038
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 5JQA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000220969.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-NOV-14
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-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : DIAMOND(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15660
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.720
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 200 DATA REDUNDANCY : 96.60
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.72
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2O5G
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE, PH 4.6, 25% W/V
REMARK 280 PEG4000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 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 28.52400
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: 3630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 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: 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 NH2 ARG A 37 O HOH A 501 2.03
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 MET A 76 -64.03 -122.32
REMARK 500 LYS A 77 95.83 85.98
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 83.2
REMARK 620 3 ASP A 24 OD1 83.7 81.0
REMARK 620 4 THR A 26 O 83.7 158.5 80.7
REMARK 620 5 GLU A 31 OE1 110.6 126.5 149.2 74.3
REMARK 620 6 GLU A 31 OE2 99.0 74.1 154.4 124.9 53.1
REMARK 620 7 HOH A 565 O 161.3 79.5 86.7 110.5 85.5 83.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 56 OD1
REMARK 620 2 ASP A 58 OD1 79.2
REMARK 620 3 ASN A 60 OD1 84.3 73.4
REMARK 620 4 THR A 62 O 88.9 152.6 81.0
REMARK 620 5 GLU A 67 OE1 104.9 125.0 160.3 81.8
REMARK 620 6 GLU A 67 OE2 91.1 75.5 148.9 129.8 49.9
REMARK 620 7 HOH A 575 O 161.5 82.3 90.8 108.0 85.4 83.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 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 83.0 74.9
REMARK 620 4 TYR A 99 O 90.4 153.9 79.6
REMARK 620 5 GLU A 104 OE1 110.6 130.9 151.2 75.2
REMARK 620 6 GLU A 104 OE2 96.7 78.5 153.2 127.2 53.4
REMARK 620 7 HOH A 541 O 161.1 80.8 86.9 103.5 85.7 85.2
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 81.3
REMARK 620 3 ASP A 133 OD1 81.4 81.5
REMARK 620 4 GLN A 135 O 84.0 156.7 78.5
REMARK 620 5 GLU A 140 OE1 116.5 121.5 151.4 81.4
REMARK 620 6 GLU A 140 OE2 86.3 75.9 155.6 121.1 52.6
REMARK 620 7 HOH A 521 O 156.2 83.5 78.4 103.9 87.0 107.6
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 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 5JQA A 0 148 UNP P62158 CALM_HUMAN 1 149
DBREF 5JQA B 1 20 UNP Q15746 MYLK_HUMAN 1691 1710
SEQADV 5JQA NH2 B 21 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 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 21 ARG ARG LYS TRP GLN LYS THR GLY ASN ALA VAL ARG ALA
SEQRES 2 B 21 ILE GLY ARG LEU SER SER MET NH2
HET NH2 B 21 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 *155(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 LEU A 112 1 12
HELIX 7 AA7 THR A 117 ASP A 129 1 13
HELIX 8 AA8 TYR A 138 THR A 146 1 9
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
SHEET 1 AA2 2 TYR A 99 ILE A 100 0
SHEET 2 AA2 2 VAL A 136 ASN A 137 -1 O VAL A 136 N ILE A 100
LINK C MET B 20 N NH2 B 21 1555 1555 1.34
LINK OD1 ASP A 20 CA CA A 401 1555 1555 2.24
LINK OD1 ASP A 22 CA CA A 401 1555 1555 2.42
LINK OD1 ASP A 24 CA CA A 401 1555 1555 2.36
LINK O THR A 26 CA CA A 401 1555 1555 2.34
LINK OE1 GLU A 31 CA CA A 401 1555 1555 2.42
LINK OE2 GLU A 31 CA CA A 401 1555 1555 2.52
LINK OD1 ASP A 56 CA CA A 402 1555 1555 2.24
LINK OD1 ASP A 58 CA CA A 402 1555 1555 2.48
LINK OD1 ASN A 60 CA CA A 402 1555 1555 2.33
LINK O THR A 62 CA CA A 402 1555 1555 2.33
LINK OE1 GLU A 67 CA CA A 402 1555 1555 2.55
LINK OE2 GLU A 67 CA CA A 402 1555 1555 2.69
LINK OD1 ASP A 93 CA CA A 403 1555 1555 2.28
LINK OD1 ASP A 95 CA CA A 403 1555 1555 2.40
LINK OD1 ASN A 97 CA CA A 403 1555 1555 2.45
LINK O TYR A 99 CA CA A 403 1555 1555 2.26
LINK OE1 GLU A 104 CA CA A 403 1555 1555 2.43
LINK OE2 GLU A 104 CA CA A 403 1555 1555 2.53
LINK OD1 ASP A 129 CA CA A 404 1555 1555 2.35
LINK OD1 ASP A 131 CA CA A 404 1555 1555 2.28
LINK OD1 ASP A 133 CA CA A 404 1555 1555 2.46
LINK O GLN A 135 CA CA A 404 1555 1555 2.29
LINK OE1 GLU A 140 CA CA A 404 1555 1555 2.40
LINK OE2 GLU A 140 CA CA A 404 1555 1555 2.59
LINK CA CA A 401 O HOH A 565 1555 1555 2.30
LINK CA CA A 402 O HOH A 575 1555 1555 2.12
LINK CA CA A 403 O HOH A 541 1555 1555 2.52
LINK CA CA A 404 O HOH A 521 1555 1555 2.35
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 565
SITE 1 AC2 6 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 AC2 6 GLU A 67 HOH A 575
SITE 1 AC3 6 ASP A 93 ASP A 95 ASN A 97 TYR A 99
SITE 2 AC3 6 GLU A 104 HOH A 541
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 521
CRYST1 29.016 57.048 45.068 90.00 98.17 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 0.034464 0.000000 0.004950 0.00000
SCALE2 0.000000 0.017529 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022416 0.00000
(ATOM LINES ARE NOT SHOWN.)
END