HEADER METAL BINDING PROTEIN/TRANSFERASE 29-JUN-12 2LV6
TITLE THE COMPLEX BETWEEN CA-CALMODULIN AND SKELETAL MUSCLE MYOSIN LIGHT
TITLE 2 CHAIN KINASE FROM COMBINATION OF NMR AND AQUEOUS AND CONTRAST-MATCHED
TITLE 3 SAXS DATA
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 2, SKELETAL/CARDIAC MUSCLE;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: CALMODULIN-BINDING RESIDUES 566-591;
COMPND 10 SYNONYM: MLCK2;
COMPND 11 EC: 2.7.11.18;
COMPND 12 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: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 10 EXPRESSION_SYSTEM_VARIANT: CODON-PLUS (DE3) RIPL;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR: PET21A;
SOURCE 12 MOL_ID: 2;
SOURCE 13 SYNTHETIC: YES;
SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 15 ORGANISM_COMMON: HUMAN;
SOURCE 16 ORGANISM_TAXID: 9606
KEYWDS PB-SUBSTITUTED, PROTEIN COMPLEX, METAL BINDING PROTEIN-TRANSFERASE
KEYWDS 2 COMPLEX
EXPDTA SOLUTION SCATTERING; SOLUTION NMR
AUTHOR A.V.GRISHAEV,N.J.ANTHIS,G.M.CLORE
REVDAT 2 27-MAR-13 2LV6 1 REMARK
REVDAT 1 20-FEB-13 2LV6 0
JRNL AUTH A.GRISHAEV,N.J.ANTHIS,G.M.CLORE
JRNL TITL CONTRAST-MATCHED SMALL-ANGLE X-RAY SCATTERING FROM A
JRNL TITL 2 HEAVY-ATOM-LABELED PROTEIN IN STRUCTURE DETERMINATION:
JRNL TITL 3 APPLICATION TO A LEAD-SUBSTITUTED CALMODULIN-PEPTIDE
JRNL TITL 4 COMPLEX.
JRNL REF J.AM.CHEM.SOC. V. 134 14686 2012
JRNL REFN ISSN 0002-7863
JRNL PMID 22908850
JRNL DOI 10.1021/JA306359Z
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0, CUSTOM
REMARK 3 AUTHORS : BRUNGER, ADAMS, CLORE, GROS, NILGES AND READ (CNS)
REMARK 3 , GRISHAEV (CUSTOM)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RELATIVE POSITIONS OF THE N- AND C-
REMARK 3 TERMINAL DOMAINS OF CALMODULIN, RIGIDLY HELD AT THOSE OF THE 1MXE
REMARK 3 STRUCTURE, CHAIN A, WERE OPTIMIZED VIA A ROTATIONAL/TRANSLATIONAL
REMARK 3 GRID SEARCH WITH STEPS OF 2DEG AND 1A, RESPECTIVELY WITH THE BEST
REMARK 3 MODEL FITTED AGAINST RDC AND SCATTERING INTENSITY DATA.
REMARK 3 COORDINATES OF THE CALMODULIN LINKER RESIDUES (76-81) AND THE
REMARK 3 INTERFACIAL SIDE CHAINS WERE REGULARIZED VIA A MOLECULAR
REMARK 3 DYNAMICS/SIMULATED ANNEALING PROTOCOL WITH THE BACKBONE ATOMS AND
REMARK 3 THE REMAINING SIDE CHAINS HELD FIXED AT THE GEOMETRY RESULTING
REMARK 3 FROM THE RIGID-BODY GRID SEARCH OF THE PREVIOUS STEP.
REMARK 4
REMARK 4 2LV6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JAN-13.
REMARK 100 THE RCSB ID CODE IS RCSB102873.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 300
REMARK 210 PH : 6.5; 6.5
REMARK 210 IONIC STRENGTH : 0.1; 0.15
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.3 MM [U-13C; U-15N; U-2H]
REMARK 210 CALMODULIN, 0.3 MM SSMLCK, 95%
REMARK 210 H2O/5% D2O; 0.06-0.25 MM [U-13C;
REMARK 210 U-15N; U-2H] CALMODULIN, 0.06-
REMARK 210 0.25 MM SSMLCK, 65% W/V SUCROSE/
REMARK 210 H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, SPARKY, CUSTOM
REMARK 210 METHOD USED : RIGID-BODY OPTIMIZATION,
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 265
REMARK 265 EXPERIMENTAL DETAILS
REMARK 265
REMARK 265 EXPERIMENT TYPE : SMALL ANGLE X-RAY SCATTERING
REMARK 265 DATA ACQUISITION
REMARK 265 RADIATION/NEUTRON SOURCE : ADVANCED PHOTON SOURCE
REMARK 265 SYNCHROTRON (Y/N) : Y
REMARK 265 BEAMLINE TYPE : 12-IDB
REMARK 265 BEAMLINE INSTRUMENT : NULL
REMARK 265 DETECTOR TYPE : PILATUS 2M
REMARK 265 DETECTOR MANUFACTURER DETAILS : DECTRIS
REMARK 265 TEMPERATURE (KELVIN) : 298
REMARK 265 PH : 6.5
REMARK 265 NUMBER OF TIME FRAMES USED : 20
REMARK 265 PROTEIN CONCENTRATION RANGE (MG/ML) : 1.2-5.0
REMARK 265 SAMPLE BUFFER : 25MM HEPES, 150 MM
REMARK 265 KCL, 3 MM CACL2, 1 MM
REMARK 265 TCEP, H2O
REMARK 265 DATA REDUCTION SOFTWARE : MARDETECTOR, IGOR
REMARK 265 GUINIER MEAN RADIUS OF GYRATION (NM) : 1.78
REMARK 265 SIGMA MEAN RADIUS OF GYRATION : 0.04
REMARK 265 R(XS-1) MEAN CROSS SECTIONAL RADII (NM) : NULL
REMARK 265 R(XS-1) SIGMA MEAN CROSS SECTIONAL RADII : NULL
REMARK 265 R(XS-2) MEAN CROSS SECTIONAL RADII (NM) : NULL
REMARK 265 R(XS-2) SIGMA MEAN CROSS SECTIONAL RADII : NULL
REMARK 265 P(R) PROTEIN LENGTH (NM) : 6.0
REMARK 265
REMARK 265 EXPERIMENT TYPE : SMALL ANGLE X-RAY SCATTERING
REMARK 265 DATA ACQUISITION
REMARK 265 RADIATION/NEUTRON SOURCE : ADVANCED PHOTON SOURCE
REMARK 265 SYNCHROTRON (Y/N) : Y
REMARK 265 BEAMLINE TYPE : 12-IDC
REMARK 265 BEAMLINE INSTRUMENT : NULL
REMARK 265 DETECTOR TYPE : GOLD CCD
REMARK 265 DETECTOR MANUFACTURER DETAILS : NULL
REMARK 265 TEMPERATURE (KELVIN) : 298
REMARK 265 PH : 6.5
REMARK 265 NUMBER OF TIME FRAMES USED : 20
REMARK 265 PROTEIN CONCENTRATION RANGE (MG/ML) : 5.0 - 9.5
REMARK 265 SAMPLE BUFFER : 25MM HEPES, 150 MM
REMARK 265 KCL, 1 MM TCEP, 3
REMARK 265 MICROMOL PBCL2, 65%
REMARK 265 SUCROSE, H2O
REMARK 265 DATA REDUCTION SOFTWARE : MARDETECTOR, IGOR
REMARK 265 GUINIER MEAN RADIUS OF GYRATION (NM) : 1.8
REMARK 265 SIGMA MEAN RADIUS OF GYRATION : 0.2
REMARK 265 R(XS-1) MEAN CROSS SECTIONAL RADII (NM) : NULL
REMARK 265 R(XS-1) SIGMA MEAN CROSS SECTIONAL RADII : NULL
REMARK 265 R(XS-2) MEAN CROSS SECTIONAL RADII (NM) : NULL
REMARK 265 R(XS-2) SIGMA MEAN CROSS SECTIONAL RADII : NULL
REMARK 265 P(R) PROTEIN LENGTH (NM) : NULL
REMARK 265
REMARK 265 DATA ANALYSIS AND MODEL FITTING:
REMARK 265 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 265 SOFTWARE USED : PRIMUS, GNOM
REMARK 265 SOFTWARE AUTHORS : NULL
REMARK 265 STARTING MODEL : NULL
REMARK 265
REMARK 265 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 265 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 265 CONFORMERS, SELECTION CRITERIA : BEST-FITTING CONFORMER BASED ON
REMARK 265 THE FIT OF AQUEOUS SAXS DATA FOR CA-CAM/MLCK, CONTRAST-MATCHED
REMARK 265 (65% SUCROSE) SAXS DATA FOR PB-CAM/MLCK, AND BACKBONE 1H-15N
REMARK 265 RESIDUAL DIPOLAR COUPLINGS FOR CAM IN THE CA-CAM/MLCK COMPLEX
REMARK 265
REMARK 265 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 265
REMARK 265 OTHER DETAILS: 4000000000000 STARTING RELATIVE POSITIONS OF THE N
REMARK 265 -TERM (1-75) AND C-TERM (82-148) DOMAINS OF CAM WERE BUILT USING
REMARK 265 COORDINATES IN THE PDB DEPOSITION 1MXE:A. TAIL RESIDUES 1-4 AND
REMARK 265 144-148 WERE BEST-FITTED TO 1MXE USING MODELS 1J7O AND 1J7P.
REMARK 265 THESE 4*1011 MODELS SAMPLE IN AN EXHAUSTIVE FASHION ALL POSSIBLE
REMARK 265 RELATIVE DOMAIN POSITIONS WHICH DIFFER BY NO MORE THAN 1A IN
REMARK 265 TERMS OF C-TERM DOMAIN PLACEMENT WHEN N-TERM DOMAIN IS FIXED.
REMARK 265 ROTATIONAL AND TRANSLATIONAL GRIDS OF 2DEG AND 1A WERE USED. THE
REMARK 265 MODELS WERE THEN FILTERED TO EXHIBIT FIT TO THE RDC DATA NO WORSE
REMARK 265 THAN 10% HIGHER THAN GLOBAL MINIMUM FOUND BY NLS OPTIMIZATION OF
REMARK 265 ORIENTATION OF THE C-TERM RELATIVE TO THE N-TERM DOMAIN.
REMARK 265 ADDITIONAL FILTERS WERE THEN APPLIED INCLUDING ABSENCE OF CLASHES
REMARK 265 <2.5 A BETWEEN HEAVY BACKBONE AND CB ATOMS, AND RGYR OF 13-19A.
REMARK 265 FOR THE GEOMETRIES THAT PASSED ABOVE REQUIREMENTS, POSITION OF
REMARK 265 MLCK FROM 2BBM DEPOSITION WAS BEST-FITTED IN A RIGID-BODY MANNER
REMARK 265 AGAINST NOE DISTANCE RESTRAINTS FROM 2BBM DEPOSITION AND CLASH
REMARK 265 AVOIDANCE FUNCTION INCLUDING HEAVY BACKBONE AND CB ATOMS. CAM
REMARK 265 CONFORMATIONS WHICH EXHIBITED AT LEAST 1 NOE VIOLATION EXCEEDING
REMARK 265 3A FOR THE BEST-FITTED MLCK WERE REJECTED. LINKER COORDINATES
REMARK 265 WERE THEN BUILT FOR RESIDUES 76-81 USING 8-RESIDUE BACKBONE AND
REMARK 265 CB-CONTAINING SEGMENTS FROM A PDB-BASED DATABASE INCLUDING 2.2
REMARK 265 MILLION RESIDUES IN TOTAL. LINKERS WHICH CLASHED WITH CAM DOMAINS
REMARK 265 OR MLCK OR EXHIBITED RMSD ABOVE 1.2 A FOR RESIDUES 1 AND 8 VS
REMARK 265 RESIDUES 75 AND 82 OF CAM WERE REJECTED. CAM CONFORMATION FOR
REMARK 265 WHICH SUCH LINKERS COULD NOT BE BUILT WERE REJECTED LEADING TO A
REMARK 265 TOTAL OF APPROXIMATELY 75000 STRUCTURES. THESE STRUCTURES WERE
REMARK 265 FITTED TO THE SAXS AND RDC DATA WITH THE OVERALL BEST-FITTING
REMARK 265 MODEL RETAINED FOR DEPOSITION. THE COORDINATES OF THE LINKER
REMARK 265 RESIDUES 76-81 AND SIDECHAINS WERE REGULARIZED BY ENERGY
REMARK 265 MINIMIZATION VIA XPLOR-NIH PRIOR TO THE DEPOSITION WITH THE
REMARK 265 ACTIVE ENERGY TERMS INCLUDING BONDS, ANGLES, IMPROPERS, NON-
REMARK 265 BONDED, AND CONFORMATIONAL DATABASE POTENTIALS OF MEAN FORCE.
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: 1442 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 2977 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.7 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 VAL A 142 H THR A 146 1.51
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 THR A 79 -89.12 59.96
REMARK 500 ASP A 80 37.00 170.10
REMARK 500 SER A 81 -145.66 51.74
REMARK 500 GLU A 82 -46.25 112.85
REMARK 500 ALA A 147 169.99 59.61
REMARK 500 SER B 221 91.37 -54.72
REMARK 500 SER B 222 88.60 -55.37
REMARK 500 SER B 223 102.93 25.31
REMARK 500 ALA B 225 -38.60 -35.63
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 204 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 129 OD1
REMARK 620 2 GLN A 135 O 84.8
REMARK 620 3 ASP A 133 OD1 86.8 78.8
REMARK 620 4 GLU A 140 OE1 108.7 78.7 151.2
REMARK 620 5 ASP A 131 OD1 89.4 154.0 75.7 126.9
REMARK 620 6 GLU A 140 OE2 91.4 125.5 155.5 51.3 79.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 203 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 93 OD1
REMARK 620 2 PHE A 99 O 84.2
REMARK 620 3 ASP A 95 OD1 82.8 153.5
REMARK 620 4 GLU A 104 OE1 103.4 77.3 128.2
REMARK 620 5 ASN A 97 OD1 87.0 77.7 78.7 151.7
REMARK 620 6 GLU A 104 OE2 99.4 128.4 76.5 51.6 153.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 56 OD1
REMARK 620 2 ASP A 58 OD1 81.3
REMARK 620 3 ASN A 60 OD1 84.8 77.8
REMARK 620 4 THR A 62 O 87.2 155.3 79.5
REMARK 620 5 GLU A 67 OE1 106.0 124.2 156.2 79.9
REMARK 620 6 GLU A 67 OE2 89.2 74.8 152.6 127.0 50.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 26 O
REMARK 620 2 ASP A 24 OD1 85.7
REMARK 620 3 ASP A 22 OD1 157.4 82.6
REMARK 620 4 ASP A 20 OD1 82.3 90.2 78.5
REMARK 620 5 GLU A 31 OE2 116.6 157.7 76.5 93.1
REMARK 620 6 GLU A 31 OE1 72.4 145.4 126.2 112.4 51.3
REMARK 620 N 1 2 3 4 5
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 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 204
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MXE RELATED DB: PDB
REMARK 900 BACKBONE COORDINATES OF THE N- AND C-TERMINAL DOMAINS FROM
REMARK 900 THIS ENTRY (RESIDUES 5-75 AND 82-146, RESPECTIVELY) WERE
REMARK 900 USED DURING RIGID-BODY OPTIMIZATION OF THE GEOMETRY OF THE
REMARK 900 CAM/MLCK COMPLEX.
REMARK 900 RELATED ID: 2BBM RELATED DB: PDB
REMARK 900 SKMLCK PEPTIDE COORDINATES AND DISTANCE RESTRAINTS FROM
REMARK 900 THIS ENTRY WERE USED DURING RIGID-BODY OPTIMIZATION OF THE
REMARK 900 GEOMETRY OF THE CAM/MLCK COMPLEX.
REMARK 900 RELATED ID: 18556 RELATED DB: BMRB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS DEPOSITED STRUCTURE OF HUMAN CALMODULIN WAS REFINED USING
REMARK 999 INDIVIDUAL DOMAIN COORDINATES OF DEPOSITION 1MXE, WHICH CORRESPONDS
REMARK 999 TO THE CHICKEN CALMODULIN. THE SEQUENCES OF HUMAN AND CHICKEN
REMARK 999 CALMODULIN DIFFER IN TWO POSITIONS, 99 (TYR FOR HUMAN AND PHE FOR
REMARK 999 CHICKEN) AND 143 (GLN FOR HUMAN AND THR FOR CHICKEN). THEREFORE,
REMARK 999 THE SIDECHAIN COORDINATES OF RESIDUES 99 AND 143 IN THIS DEPOSITION
REMARK 999 DO NOT REPRESENT COMPOSITION OF THE SAMPLES USED FOR EXPERIMENTAL
REMARK 999 DATA COLLECTION. THIS DISCREPANCIES DO NOT PRODUCE ANY DIFFERENCES
REMARK 999 WHEN EXPERIMENTAL DATA ARE FITTED SINCE BACKBONE N-HN RDC AND
REMARK 999 CONTRAST-MATCHED SAXS DATA DO NOT INVOLVE THE SIDECHAIN COORDINATES
REMARK 999 AND THEIR IMPACT ON THE AQUEOUS SAXS DATA IS NEGLIGIBLE.
DBREF 2LV6 A 1 148 UNP P62158 CALM_HUMAN 2 149
DBREF 2LV6 B 201 226 UNP Q9H1R3 MYLK2_HUMAN 566 591
SEQADV 2LV6 PHE A 99 UNP P62158 TYR 100 SEE REMARK 999
SEQADV 2LV6 THR A 143 UNP P62158 GLN 144 SEE REMARK 999
SEQRES 1 A 148 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES 2 A 148 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR
SEQRES 3 A 148 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU
SEQRES 4 A 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE
SEQRES 5 A 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE
SEQRES 6 A 148 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP
SEQRES 7 A 148 THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL
SEQRES 8 A 148 PHE ASP LYS ASP GLY ASN GLY PHE ILE SER ALA ALA GLU
SEQRES 9 A 148 LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR
SEQRES 10 A 148 ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE
SEQRES 11 A 148 ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL THR
SEQRES 12 A 148 MET MET THR ALA LYS
SEQRES 1 B 26 LYS ARG ARG TRP LYS LYS ASN PHE ILE ALA VAL SER ALA
SEQRES 2 B 26 ALA ASN ARG PHE LYS LYS ILE SER SER SER GLY ALA LEU
HET CA A 201 1
HET CA A 202 1
HET CA A 203 1
HET CA A 204 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 4(CA 2+)
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 PHE A 65 ASP A 78 1 14
HELIX 5 5 GLU A 82 ASP A 93 1 12
HELIX 6 6 SER A 101 LEU A 112 1 12
HELIX 7 7 THR A 117 ASP A 129 1 13
HELIX 8 8 TYR A 138 ALA A 147 1 10
HELIX 9 9 ARG B 203 ILE B 220 1 18
SHEET 1 A 2 THR A 26 ILE A 27 0
SHEET 2 A 2 ILE A 63 ASP A 64 -1 O ILE A 63 N ILE A 27
SHEET 1 B 2 PHE A 99 ILE A 100 0
SHEET 2 B 2 VAL A 136 ASN A 137 -1 O VAL A 136 N ILE A 100
LINK OD1 ASP A 129 CA CA A 204 1555 1555 2.26
LINK OD1 ASP A 93 CA CA A 203 1555 1555 2.26
LINK OD1 ASP A 56 CA CA A 201 1555 1555 2.28
LINK O PHE A 99 CA CA A 203 1555 1555 2.30
LINK O THR A 26 CA CA A 202 1555 1555 2.33
LINK OD1 ASP A 95 CA CA A 203 1555 1555 2.34
LINK OD1 ASP A 24 CA CA A 202 1555 1555 2.35
LINK O GLN A 135 CA CA A 204 1555 1555 2.37
LINK OD1 ASP A 58 CA CA A 201 1555 1555 2.37
LINK OD1 ASN A 60 CA CA A 201 1555 1555 2.38
LINK OD1 ASP A 22 CA CA A 202 1555 1555 2.38
LINK OD1 ASP A 20 CA CA A 202 1555 1555 2.38
LINK O THR A 62 CA CA A 201 1555 1555 2.42
LINK OD1 ASP A 133 CA CA A 204 1555 1555 2.43
LINK OE1 GLU A 104 CA CA A 203 1555 1555 2.48
LINK OE1 GLU A 140 CA CA A 204 1555 1555 2.48
LINK OE1 GLU A 67 CA CA A 201 1555 1555 2.49
LINK OD1 ASN A 97 CA CA A 203 1555 1555 2.50
LINK OE2 GLU A 104 CA CA A 203 1555 1555 2.51
LINK OE2 GLU A 31 CA CA A 202 1555 1555 2.52
LINK OE1 GLU A 31 CA CA A 202 1555 1555 2.56
LINK OE2 GLU A 67 CA CA A 201 1555 1555 2.58
LINK OD1 ASP A 131 CA CA A 204 1555 1555 2.58
LINK OE2 GLU A 140 CA CA A 204 1555 1555 2.60
SITE 1 AC1 5 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 AC1 5 GLU A 67
SITE 1 AC2 5 ASP A 20 ASP A 22 ASP A 24 THR A 26
SITE 2 AC2 5 GLU A 31
SITE 1 AC3 5 ASP A 93 ASP A 95 ASN A 97 PHE A 99
SITE 2 AC3 5 GLU A 104
SITE 1 AC4 5 ASP A 129 ASP A 131 ASP A 133 GLN A 135
SITE 2 AC4 5 GLU A 140
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END