HEADER OXIDOREDUCTASE 29-OCT-11 2LL7
TITLE SOLUTION NMR STRUCTURE OF CAM BOUND TO THE ENOS CAM BINDING DOMAIN
TITLE 2 PEPTIDE
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: NITRIC OXIDE SYNTHASE, ENDOTHELIAL;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: CALMODULIN-BINDING REGION RESIDUES 493-509;
COMPND 10 SYNONYM: CONSTITUTIVE NOS, CNOS, EC-NOS, ENDOTHELIAL NOS, ENOS, NOS
COMPND 11 TYPE III, NOSIII;
COMPND 12 EC: 1.14.13.39;
COMPND 13 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 EXPRESSION_SYSTEM_VECTOR: PET9DCAM;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: NOS3;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS OXIDOREDUCTASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.PIAZZA,K.FUTREGA,D.E.SPRATT,J.G.GUILLEMETTE,T.DIECKMANN
REVDAT 2 14-JUN-23 2LL7 1 REMARK
REVDAT 1 16-MAY-12 2LL7 0
JRNL AUTH M.PIAZZA,K.FUTREGA,D.E.SPRATT,T.DIECKMANN,J.G.GUILLEMETTE
JRNL TITL STRUCTURE AND DYNAMICS OF CALMODULIN (CAM) BOUND TO NITRIC
JRNL TITL 2 OXIDE SYNTHASE PEPTIDES: EFFECTS OF A PHOSPHOMIMETIC CAM
JRNL TITL 3 MUTATION.
JRNL REF BIOCHEMISTRY V. 51 3651 2012
JRNL REFN ISSN 0006-2960
JRNL PMID 22486744
JRNL DOI 10.1021/BI300327Z
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNSSOLVE, CNSSOLVE
REMARK 3 AUTHORS : BRUNGER, ADAMS, CLORE, GROS, NILGES AND READ
REMARK 3 (CNSSOLVE), BRUNGER, ADAMS, CLORE, GROS, NILGES
REMARK 3 AND READ (CNSSOLVE)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2LL7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-NOV-11.
REMARK 100 THE DEPOSITION ID IS D_1000102517.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.0 MM [U-99% 13C; U-99% 15N]
REMARK 210 PROTEIN_1, 1.0 MM PROTEIN_2, 100
REMARK 210 MM POTASSIUM CHLORIDE, 10 MM
REMARK 210 CALCIUM CHLORIDE, 0.2 MM SODIUM
REMARK 210 AZIDE, 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D CBCA(CO)NH;
REMARK 210 3D HNCA; 3D HCCH-TOCSY; 3D 1H-
REMARK 210 15N NOESY; 3D 1H-13C NOESY
REMARK 210 ALIPHATIC
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 : NULL
REMARK 210 METHOD USED : DGSA-DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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 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 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 121 H MET A 124 1.58
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 1 ASP A 56 70.00 36.94
REMARK 500 1 THR A 79 -100.26 -149.40
REMARK 500 1 ASP A 80 104.92 -177.03
REMARK 500 1 ASP A 122 -18.65 -43.72
REMARK 500 1 LYS B 150 -41.71 -150.86
REMARK 500 1 THR B 151 -53.99 -153.36
REMARK 500 2 ASP A 56 69.22 28.45
REMARK 500 2 THR A 79 -57.98 56.62
REMARK 500 2 ASP A 118 -16.67 -47.31
REMARK 500 2 ASN A 137 -165.89 -110.00
REMARK 500 2 LYS B 150 50.57 79.29
REMARK 500 2 THR B 151 -62.09 -154.51
REMARK 500 2 PHE B 152 -31.67 -153.88
REMARK 500 2 SER B 164 31.72 -95.50
REMARK 500 3 ASP A 2 126.44 62.97
REMARK 500 3 ASP A 56 70.83 36.80
REMARK 500 3 THR A 79 -106.14 -149.14
REMARK 500 3 ASP A 80 99.22 -160.27
REMARK 500 3 LYS A 115 -136.46 -68.96
REMARK 500 3 LEU A 116 132.91 -31.46
REMARK 500 3 ARG A 126 -14.95 -47.14
REMARK 500 3 ALA A 147 76.18 -105.22
REMARK 500 3 LYS B 150 -39.84 -149.16
REMARK 500 3 THR B 151 -49.54 -157.23
REMARK 500 4 ASP A 2 131.57 63.62
REMARK 500 4 ARG A 37 -19.76 -45.76
REMARK 500 4 GLN A 41 127.14 -175.35
REMARK 500 4 ASN A 42 -53.21 -130.04
REMARK 500 4 ASP A 56 69.82 35.92
REMARK 500 4 THR A 79 -96.67 -147.73
REMARK 500 4 ASP A 80 105.39 -176.69
REMARK 500 4 LYS A 115 -138.34 -54.53
REMARK 500 4 LEU A 116 166.71 -40.30
REMARK 500 4 ASP A 118 -17.75 -40.08
REMARK 500 4 ASP A 129 93.59 -61.63
REMARK 500 4 LYS B 150 -37.33 -156.21
REMARK 500 5 GLU A 6 -17.48 -49.78
REMARK 500 5 THR A 79 -104.50 -142.53
REMARK 500 5 LYS A 115 -137.01 -75.11
REMARK 500 5 LEU A 116 145.39 -33.95
REMARK 500 5 ASP A 118 -16.85 -38.64
REMARK 500 5 ALA A 128 44.18 -149.46
REMARK 500 5 ASP A 129 103.63 -59.62
REMARK 500 5 ALA A 147 74.43 -104.29
REMARK 500 5 THR B 151 -33.29 89.28
REMARK 500 5 PHE B 152 22.44 -173.88
REMARK 500 6 ASP A 56 69.54 26.31
REMARK 500 6 ASP A 64 -162.06 -119.69
REMARK 500 6 THR A 79 -108.61 -157.29
REMARK 500 6 ASP A 80 101.53 -167.59
REMARK 500
REMARK 500 THIS ENTRY HAS 173 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2LL6 RELATED DB: PDB
REMARK 900 RELATED ID: 18028 RELATED DB: BMRB
DBREF 2LL7 A 1 148 UNP P62158 CALM_HUMAN 2 149
DBREF 2LL7 B 149 165 UNP P29474 NOS3_HUMAN 493 509
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 TYR 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 GLN
SEQRES 12 A 148 MET MET THR ALA LYS
SEQRES 1 B 17 LYS LYS THR PHE LYS GLU VAL ALA ASN ALA VAL LYS ILE
SEQRES 2 B 17 SER ALA SER LEU
HELIX 1 1 THR A 5 GLU A 14 1 10
HELIX 2 2 ALA A 15 ASP A 20 1 6
HELIX 3 3 GLU A 31 GLY A 40 1 10
HELIX 4 4 THR A 44 ASP A 50 1 7
HELIX 5 5 ASP A 64 LEU A 69 1 6
HELIX 6 6 LEU A 69 ARG A 74 1 6
HELIX 7 7 SER A 81 ARG A 86 1 6
HELIX 8 8 ARG A 86 ASP A 93 1 8
HELIX 9 9 ALA A 102 THR A 110 1 9
HELIX 10 10 ASN A 111 GLY A 113 5 3
HELIX 11 11 GLU A 119 ALA A 128 5 10
HELIX 12 12 ASN A 137 MET A 145 1 9
HELIX 13 13 PHE B 152 SER B 162 1 11
SHEET 1 A 2 ILE A 100 SER A 101 0
SHEET 2 A 2 GLN A 135 VAL A 136 -1 O VAL A 136 N ILE A 100
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
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END