HEADER TRANSCRIPTION 03-APR-12 2LRI
TITLE NMR STRUCTURE OF THE SECOND PHD FINGER OF AIRE (AIRE-PHD2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AUTOIMMUNE REGULATOR;
COMPND 3 CHAIN: C;
COMPND 4 FRAGMENT: PHD-TYPE 2 ZINC FINGER RESIDUES 423-485;
COMPND 5 SYNONYM: AUTOIMMUNE POLYENDOCRINOPATHY CANDIDIASIS ECTODERMAL
COMPND 6 DYSTROPHY PROTEIN, APECED PROTEIN;
COMPND 7 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: AIRE, APECED;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET-24D
KEYWDS ZN BINDING PROTEIN DOMAIN, APECED, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 50
AUTHOR M.GAETANI,F.CHIGNOLA,L.MOLLICA,G.QUILICI,V.MANNELLA,D.SPILIOTOPOULOS,
AUTHOR 2 G.MUSCO
REVDAT 3 14-JUN-23 2LRI 1 REMARK SEQADV LINK
REVDAT 2 16-JAN-13 2LRI 1 JRNL
REVDAT 1 17-OCT-12 2LRI 0
JRNL AUTH M.GAETANI,V.MATAFORA,M.SAARE,D.SPILIOTOPOULOS,L.MOLLICA,
JRNL AUTH 2 G.QUILICI,F.CHIGNOLA,V.MANNELLA,C.ZUCCHELLI,P.PETERSON,
JRNL AUTH 3 A.BACHI,G.MUSCO
JRNL TITL AIRE-PHD FINGERS ARE STRUCTURAL HUBS TO MAINTAIN THE
JRNL TITL 2 INTEGRITY OF CHROMATIN-ASSOCIATED INTERACTOME.
JRNL REF NUCLEIC ACIDS RES. V. 40 11756 2012
JRNL REFN ISSN 0305-1048
JRNL PMID 23074189
JRNL DOI 10.1093/NAR/GKS933
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA 2.3, ARIA 2.3
REMARK 3 AUTHORS : LINGE, O'DONOGHUE AND NILGES (ARIA), LINGE,
REMARK 3 O'DONOGHUE AND NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2LRI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-APR-12.
REMARK 100 THE DEPOSITION ID IS D_1000102742.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 295
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 0.15
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.4-0.8 MM [U-100% 13C; U-100%
REMARK 210 15N] AIRE-PHD2, 50 UM ZINC ION,
REMARK 210 5 MM DTT, 50 MM SODIUM PHOSPHATE,
REMARK 210 0.15 M SODIUM CHLORIDE, 0.02 %
REMARK 210 SODIUM AZIDE, 90% H2O/10% D2O;
REMARK 210 0.4-0.8 MM [U-100% 13C; U-100%
REMARK 210 15N] AIRE-PHD2, 5 MM DTT, 50 UM
REMARK 210 ZINC ION, 50 MM SODIUM PHOSPHATE,
REMARK 210 0.15 M SODIUM CHLORIDE, 0.02 %
REMARK 210 SODIUM AZIDE, 100% D2O; 0.4-0.8
REMARK 210 MM [U-100% 15N] AIRE-PHD2, 5 MM
REMARK 210 DTT, 50 UM ZINC ION, 50 MM
REMARK 210 SODIUM PHOSPHATE, 0.15 M SODIUM
REMARK 210 CHLORIDE, 0.02 % SODIUM AZIDE,
REMARK 210 90% H2O/10% D2O; 0.4-0.8 MM AIRE-
REMARK 210 PHD2, 5 MM DTT, 50 UM ZINC ION,
REMARK 210 50 MM SODIUM PHOSPHATE, 0.15 M
REMARK 210 SODIUM CHLORIDE, 0.02 % SODIUM
REMARK 210 AZIDE, 90% H2O/10% D2O; 0.4-0.8
REMARK 210 MM AIRE-PHD2, 5 MM DTT, 50 UM
REMARK 210 ZINC ION, 50 MM SODIUM PHOSPHATE,
REMARK 210 0.15 M SODIUM CHLORIDE, 0.02 %
REMARK 210 SODIUM AZIDE, 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 2D 1H-1H TOCSY; 2D 1H-1H NOESY;
REMARK 210 3D CBCA(CO)NH; 3D C(CO)NH; 3D
REMARK 210 HNCO; 3D HNCA; 3D H(CCO)NH; 3D
REMARK 210 HCCH-TOCSY; 3D HNHA; 3D 1H-15N
REMARK 210 NOESY; 3D 1H-13C NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CCPNMR 2.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 50
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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
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 ALA C 2 34.53 -147.42
REMARK 500 1 MET C 3 33.98 -148.43
REMARK 500 1 PHE C 40 79.02 -117.76
REMARK 500 1 PRO C 64 99.69 -58.94
REMARK 500 2 PRO C 11 41.91 -71.91
REMARK 500 3 ALA C 2 -71.17 69.17
REMARK 500 3 PRO C 11 89.64 -60.31
REMARK 500 3 PRO C 64 86.24 -62.88
REMARK 500 5 PRO C 64 98.84 -61.53
REMARK 500 6 LEU C 9 76.93 -101.25
REMARK 500 6 PRO C 11 95.92 -55.20
REMARK 500 6 ASP C 59 42.26 -89.54
REMARK 500 6 PRO C 64 92.78 -68.09
REMARK 500 7 PRO C 11 109.03 -60.00
REMARK 500 7 PRO C 64 23.88 -71.46
REMARK 500 8 MET C 3 40.60 -78.85
REMARK 500 8 PRO C 64 41.65 -81.41
REMARK 500 9 ALA C 2 -86.63 62.81
REMARK 500 9 MET C 3 83.02 -157.68
REMARK 500 9 GLU C 4 65.39 -101.42
REMARK 500 10 ALA C 2 84.79 57.11
REMARK 500 10 GLU C 4 -99.61 59.75
REMARK 500 10 PRO C 11 58.97 -68.98
REMARK 500 10 ALA C 32 141.09 -173.12
REMARK 500 10 VAL C 65 33.57 -95.59
REMARK 500 11 GLN C 6 44.46 -89.87
REMARK 500 11 ALA C 13 73.53 -153.87
REMARK 500 12 GLN C 7 89.99 -171.67
REMARK 500 12 THR C 49 46.60 -89.12
REMARK 500 12 VAL C 60 65.52 -108.89
REMARK 500 13 MET C 3 35.12 -148.34
REMARK 500 14 ALA C 2 56.92 -98.09
REMARK 500 14 GLN C 6 -60.32 -102.97
REMARK 500 14 GLN C 7 56.53 -98.54
REMARK 500 14 PRO C 11 34.04 -72.52
REMARK 500 14 ASP C 59 43.54 -90.11
REMARK 500 15 PRO C 11 47.28 -72.13
REMARK 500 15 PRO C 64 61.11 -69.32
REMARK 500 16 LEU C 9 94.98 57.00
REMARK 500 17 PRO C 11 45.40 -71.51
REMARK 500 17 CYS C 15 107.74 -56.96
REMARK 500 17 ALA C 32 119.86 -163.96
REMARK 500 17 THR C 49 35.52 -94.83
REMARK 500 18 ALA C 2 -159.22 61.35
REMARK 500 18 ALA C 13 74.54 -112.72
REMARK 500 18 THR C 49 70.57 -115.46
REMARK 500 18 VAL C 60 48.02 -89.71
REMARK 500 19 PRO C 11 107.75 -58.20
REMARK 500 20 THR C 49 -75.44 -89.63
REMARK 500 21 ASN C 8 41.49 -83.97
REMARK 500
REMARK 500 THIS ENTRY HAS 118 RAMACHANDRAN OUTLIERS.
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 ZN C 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 15 SG
REMARK 620 2 CYS C 18 SG 110.0
REMARK 620 3 HIS C 35 ND1 109.2 110.5
REMARK 620 4 CYS C 38 SG 108.7 108.7 109.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 102 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 27 SG
REMARK 620 2 CYS C 30 SG 108.0
REMARK 620 3 CYS C 53 SG 109.2 110.9
REMARK 620 4 CYS C 56 SG 107.7 112.0 109.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 102
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 18374 RELATED DB: BMRB
DBREF 2LRI C 4 66 UNP O43918 AIRE_HUMAN 423 485
SEQADV 2LRI GLY C 1 UNP O43918 EXPRESSION TAG
SEQADV 2LRI ALA C 2 UNP O43918 EXPRESSION TAG
SEQADV 2LRI MET C 3 UNP O43918 EXPRESSION TAG
SEQRES 1 C 66 GLY ALA MET GLU GLY GLN GLN ASN LEU ALA PRO GLY ALA
SEQRES 2 C 66 ARG CYS GLY VAL CYS GLY ASP GLY THR ASP VAL LEU ARG
SEQRES 3 C 66 CYS THR HIS CYS ALA ALA ALA PHE HIS TRP ARG CYS HIS
SEQRES 4 C 66 PHE PRO ALA GLY THR SER ARG PRO GLY THR GLY LEU ARG
SEQRES 5 C 66 CYS ARG SER CYS SER GLY ASP VAL THR PRO ALA PRO VAL
SEQRES 6 C 66 GLU
HET ZN C 101 1
HET ZN C 102 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 HIS C 35 PHE C 40 1 6
SHEET 1 A 2 LEU C 25 ARG C 26 0
SHEET 2 A 2 ALA C 33 PHE C 34 -1 O PHE C 34 N LEU C 25
LINK SG CYS C 15 ZN ZN C 101 1555 1555 2.30
LINK SG CYS C 18 ZN ZN C 101 1555 1555 2.30
LINK SG CYS C 27 ZN ZN C 102 1555 1555 2.30
LINK SG CYS C 30 ZN ZN C 102 1555 1555 2.30
LINK ND1 HIS C 35 ZN ZN C 101 1555 1555 2.00
LINK SG CYS C 38 ZN ZN C 101 1555 1555 2.30
LINK SG CYS C 53 ZN ZN C 102 1555 1555 2.30
LINK SG CYS C 56 ZN ZN C 102 1555 1555 2.29
SITE 1 AC1 4 CYS C 15 CYS C 18 HIS C 35 CYS C 38
SITE 1 AC2 4 CYS C 27 CYS C 30 CYS C 53 CYS C 56
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
