HEADER METAL BINDING PROTEIN/HORMONE RECEPTOR 15-NOV-11 2LLQ
TITLE SOLUTION NMR-DERIVED STRUCTURE OF CALMODULIN C-LOBE BOUND WITH ER
TITLE 2 ALPHA PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: EF-HAND DOMAINS 3 AND 4, RESIDUES 83-149;
COMPND 5 SYNONYM: CAM;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ESTROGEN RECEPTOR;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: UNP RESIDUES 287-305;
COMPND 11 SYNONYM: ER, ER-ALPHA, ESTRADIOL RECEPTOR, NUCLEAR RECEPTOR SUBFAMILY
COMPND 12 3 GROUP A MEMBER 1;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 3 ORGANISM_COMMON: CLAWED FROG,COMMON PLATANNA,PLATANNA;
SOURCE 4 ORGANISM_TAXID: 8355;
SOURCE 5 GENE: CALM1, CALM2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET3A;
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 METAL BINDING PROTEIN-HORMONE RECEPTOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR Y.ZHANG
REVDAT 2 28-AUG-13 2LLQ 1 JRNL
REVDAT 1 01-FEB-12 2LLQ 0
JRNL AUTH Y.ZHANG,Z.LI,D.B.SACKS,J.B.AMES
JRNL TITL STRUCTURAL BASIS FOR CA2+-INDUCED ACTIVATION AND
JRNL TITL 2 DIMERIZATION OF ESTROGEN RECEPTOR ALPHA BY CALMODULIN.
JRNL REF J.BIOL.CHEM. V. 287 9336 2012
JRNL REFN ISSN 0021-9258
JRNL PMID 22275375
JRNL DOI 10.1074/JBC.M111.334797
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER, ADAMS, CLORE, GROS, NILGES AND READ
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2LLQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-NOV-11.
REMARK 100 THE RCSB ID CODE IS RCSB102536.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 0.02
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM [U-100% 13C; U-100% 15N]
REMARK 210 PROTEIN, 93% H2O/7% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D CBCA(CO)NH;
REMARK 210 3D HNCACB
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, SPARKY
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST 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 OE2 GLU A 84 HZ2 LYS B 299 1.58
REMARK 500 O ARG A 106 HG1 THR A 110 1.60
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 THR A 146 77.88 -102.43
REMARK 500 2 GLU A 83 -71.08 -52.82
REMARK 500 3 THR A 146 55.92 -97.70
REMARK 500 4 VAL A 108 -54.92 -120.04
REMARK 500 5 THR A 146 50.47 -90.01
REMARK 500 6 VAL A 108 -66.87 -120.59
REMARK 500 6 THR A 146 47.62 -86.79
REMARK 500 8 THR A 146 48.68 -97.64
REMARK 500 9 ALA B 289 -29.88 -39.39
REMARK 500 10 THR A 146 31.14 -96.32
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 1 CA A1000 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 104 OE1
REMARK 620 2 ASN A 97 OD1 123.8
REMARK 620 3 TYR A 99 O 77.2 70.3
REMARK 620 4 GLU A 104 OE2 68.5 166.1 121.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 1 CA A1001 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 135 O
REMARK 620 2 GLU A 140 OE2 111.2
REMARK 620 N 1
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 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 18084 RELATED DB: BMRB
REMARK 900 RELATED ID: 2LLO RELATED DB: PDB
DBREF 2LLQ A 82 148 UNP P62155 CALM_XENLA 83 149
DBREF 2LLQ B 287 305 UNP P03372 ESR1_HUMAN 287 305
SEQRES 1 A 67 GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL PHE ASP LYS
SEQRES 2 A 67 ASP GLY ASN GLY TYR ILE SER ALA ALA GLU LEU ARG HIS
SEQRES 3 A 67 VAL MET THR ASN LEU GLY GLU LYS LEU THR ASP GLU GLU
SEQRES 4 A 67 VAL ASP GLU MET ILE ARG GLU ALA ASP ILE ASP GLY ASP
SEQRES 5 A 67 GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN MET MET THR
SEQRES 6 A 67 ALA LYS
SEQRES 1 B 19 ARG ALA ALA ASN LEU TRP PRO SER PRO LEU MET ILE LYS
SEQRES 2 B 19 ARG SER LYS LYS ASN SER
HET CA A1000 1
HET CA A1001 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 2(CA 2+)
HELIX 1 1 GLU A 82 ASP A 93 1 12
HELIX 2 2 SER A 101 GLY A 113 1 13
HELIX 3 3 THR A 117 GLU A 127 1 11
HELIX 4 4 ASN A 137 THR A 146 1 10
HELIX 5 5 ALA B 288 LEU B 291 5 4
HELIX 6 6 TRP B 292 SER B 305 1 14
LINK OE1 GLU A 104 CA CA A1000 1555 1555 1.80
LINK O GLN A 135 CA CA A1001 1555 1555 2.40
LINK OD1 ASN A 97 CA CA A1000 1555 1555 2.48
LINK O TYR A 99 CA CA A1000 1555 1555 2.50
LINK OE2 GLU A 140 CA CA A1001 1555 1555 2.55
LINK OE2 GLU A 104 CA CA A1000 1555 1555 2.01
SITE 1 AC1 5 ASP A 93 ASP A 95 ASN A 97 TYR A 99
SITE 2 AC1 5 GLU A 104
SITE 1 AC2 5 ASP A 129 ASP A 131 ASP A 133 GLN A 135
SITE 2 AC2 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
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
