HEADER TRANSCRIPTION 31-MAR-10 3MEA
TITLE CRYSTAL STRUCTURE OF THE SGF29 IN COMPLEX WITH H3K4ME3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SAGA-ASSOCIATED FACTOR 29 HOMOLOG;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 129-291;
COMPND 5 SYNONYM: COILED-COIL DOMAIN-CONTAINING PROTEIN 101;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: HISTONE H3;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: UNP RESIDUES 2-4;
COMPND 11 SYNONYM: H3K4ME3;
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: CCDC101, SGF29;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-V2R-PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28-MHL;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 14 ORGANISM_COMMON: CLAWED FROG,COMMON PLATANNA,PLATANNA;
SOURCE 15 ORGANISM_TAXID: 8355;
SOURCE 16 OTHER_DETAILS: H3K4ME3 3MER
KEYWDS STRUCTURAL GENOMICS CONSORTIUM, SGC, NUCLEUS, TRANSCRIPTION,
KEYWDS 2 TRANSCRIPTION REGULATION, CHROMOSOMAL PROTEIN, DNA-BINDING,
KEYWDS 3 NUCLEOSOME CORE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.BIAN,C.XU,W.TEMPEL,F.MACKENZIE,C.BOUNTRA,J.WEIGELT,C.H.ARROWSMITH,
AUTHOR 2 A.M.EDWARDS,A.BOCHKAREV,J.MIN,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 5 06-SEP-23 3MEA 1 SEQADV LINK
REVDAT 4 08-NOV-17 3MEA 1 REMARK
REVDAT 3 03-AUG-11 3MEA 1 JRNL
REVDAT 2 29-JUN-11 3MEA 1 JRNL
REVDAT 1 28-APR-10 3MEA 0
JRNL AUTH C.BIAN,C.XU,J.RUAN,K.K.LEE,T.L.BURKE,W.TEMPEL,D.BARSYTE,
JRNL AUTH 2 J.LI,M.WU,B.O.ZHOU,B.E.FLEHARTY,A.PAULSON,A.ALLALI-HASSANI,
JRNL AUTH 3 J.Q.ZHOU,G.MER,P.A.GRANT,J.L.WORKMAN,J.ZANG,J.MIN
JRNL TITL SGF29 BINDS HISTONE H3K4ME2/3 AND IS REQUIRED FOR SAGA
JRNL TITL 2 COMPLEX RECRUITMENT AND HISTONE H3 ACETYLATION.
JRNL REF EMBO J. V. 30 2829 2011
JRNL REFN ISSN 0261-4189
JRNL PMID 21685874
JRNL DOI 10.1038/EMBOJ.2011.193
REMARK 2
REMARK 2 RESOLUTION. 1.26 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.26
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 46365
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) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.117
REMARK 3 FREE R VALUE TEST SET COUNT : 1445
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) : 1.26
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.29
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3303
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.10
REMARK 3 BIN R VALUE (WORKING SET) : 0.3030
REMARK 3 BIN FREE R VALUE SET COUNT : 93
REMARK 3 BIN FREE R VALUE : 0.3220
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1294
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 156
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 10.38
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.22100
REMARK 3 B22 (A**2) : 0.12900
REMARK 3 B33 (A**2) : -0.04700
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.13300
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.049
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.046
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.029
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.476
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.960
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1359 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 912 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1871 ; 1.537 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2230 ; 0.919 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 173 ; 7.329 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 62 ;27.965 ;23.871
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 194 ;11.264 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;14.630 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 205 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1526 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 268 ; 0.001 ; 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): 851 ; 1.556 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 326 ; 0.437 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1379 ; 2.447 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 508 ; 3.189 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 487 ; 4.510 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 2271 ; 1.246 ; 3.000
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES: REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3MEA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-APR-10.
REMARK 100 THE DEPOSITION ID IS D_1000058437.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97927
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46388
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.260
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.26
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.97300
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 3ME9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG3350, 0.1M HEPES. 0.004M
REMARK 280 TRIMETHYLATED H3K3 PEPTIDE WAS PRESENT IN THE PROTEIN STOCK
REMARK 280 SOLUTION, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 46.69250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.71250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 46.69250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 20.71250
REMARK 290 SMTRY3 4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 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 112
REMARK 465 HIS A 113
REMARK 465 HIS A 114
REMARK 465 HIS A 115
REMARK 465 HIS A 116
REMARK 465 HIS A 117
REMARK 465 HIS A 118
REMARK 465 SER A 119
REMARK 465 SER A 120
REMARK 465 ARG A 121
REMARK 465 GLU A 122
REMARK 465 ASN A 123
REMARK 465 ASP A 170
REMARK 465 GLY A 171
REMARK 465 LYS A 288
REMARK 465 GLU A 289
REMARK 465 PRO A 290
REMARK 465 LYS A 291
REMARK 465 GLN B 5
REMARK 465 THR B 6
REMARK 465 ALA B 7
REMARK 465 ARG B 8
REMARK 465 LYS B 9
REMARK 465 SER B 10
REMARK 465 THR B 11
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 127 CG CD OE1 NE2
REMARK 470 LYS A 136 CG CD CE NZ
REMARK 470 LYS A 167 CG CD CE NZ
REMARK 470 GLU A 197 CG CD OE1 OE2
REMARK 470 GLU A 198 CG CD OE1 OE2
REMARK 470 LYS A 200 CG CD CE NZ
REMARK 470 ARG A 208 CG CD NE CZ NH1 NH2
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 ALA A 168 -142.02 -109.42
REMARK 500 GLU A 231 -4.34 81.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ME9 RELATED DB: PDB
REMARK 900 RELATED ID: 3MET RELATED DB: PDB
REMARK 900 RELATED ID: 3MEU RELATED DB: PDB
REMARK 900 RELATED ID: 3MEV RELATED DB: PDB
REMARK 900 RELATED ID: 3MEW RELATED DB: PDB
DBREF 3MEA A 129 291 UNP Q96ES7 SGF29_HUMAN 129 291
DBREF 3MEA B 1 11 UNP Q92133 Q92133_XENLA 2 12
SEQADV 3MEA MET A 112 UNP Q96ES7 EXPRESSION TAG
SEQADV 3MEA HIS A 113 UNP Q96ES7 EXPRESSION TAG
SEQADV 3MEA HIS A 114 UNP Q96ES7 EXPRESSION TAG
SEQADV 3MEA HIS A 115 UNP Q96ES7 EXPRESSION TAG
SEQADV 3MEA HIS A 116 UNP Q96ES7 EXPRESSION TAG
SEQADV 3MEA HIS A 117 UNP Q96ES7 EXPRESSION TAG
SEQADV 3MEA HIS A 118 UNP Q96ES7 EXPRESSION TAG
SEQADV 3MEA SER A 119 UNP Q96ES7 EXPRESSION TAG
SEQADV 3MEA SER A 120 UNP Q96ES7 EXPRESSION TAG
SEQADV 3MEA ARG A 121 UNP Q96ES7 EXPRESSION TAG
SEQADV 3MEA GLU A 122 UNP Q96ES7 EXPRESSION TAG
SEQADV 3MEA ASN A 123 UNP Q96ES7 EXPRESSION TAG
SEQADV 3MEA LEU A 124 UNP Q96ES7 EXPRESSION TAG
SEQADV 3MEA TYR A 125 UNP Q96ES7 EXPRESSION TAG
SEQADV 3MEA PHE A 126 UNP Q96ES7 EXPRESSION TAG
SEQADV 3MEA GLN A 127 UNP Q96ES7 EXPRESSION TAG
SEQADV 3MEA GLY A 128 UNP Q96ES7 EXPRESSION TAG
SEQRES 1 A 180 MET HIS HIS HIS HIS HIS HIS SER SER ARG GLU ASN LEU
SEQRES 2 A 180 TYR PHE GLN GLY THR LEU PRO LEU TRP ILE GLY LYS PRO
SEQRES 3 A 180 GLY ASP LYS PRO PRO PRO LEU CYS GLY ALA ILE PRO ALA
SEQRES 4 A 180 SER GLY ASP TYR VAL ALA ARG PRO GLY ASP LYS VAL ALA
SEQRES 5 A 180 ALA ARG VAL LYS ALA VAL ASP GLY ASP GLU GLN TRP ILE
SEQRES 6 A 180 LEU ALA GLU VAL VAL SER TYR SER HIS ALA THR ASN LYS
SEQRES 7 A 180 TYR GLU VAL ASP ASP ILE ASP GLU GLU GLY LYS GLU ARG
SEQRES 8 A 180 HIS THR LEU SER ARG ARG ARG VAL ILE PRO LEU PRO GLN
SEQRES 9 A 180 TRP LYS ALA ASN PRO GLU THR ASP PRO GLU ALA LEU PHE
SEQRES 10 A 180 GLN LYS GLU GLN LEU VAL LEU ALA LEU TYR PRO GLN THR
SEQRES 11 A 180 THR CYS PHE TYR ARG ALA LEU ILE HIS ALA PRO PRO GLN
SEQRES 12 A 180 ARG PRO GLN ASP ASP TYR SER VAL LEU PHE GLU ASP THR
SEQRES 13 A 180 SER TYR ALA ASP GLY TYR SER PRO PRO LEU ASN VAL ALA
SEQRES 14 A 180 GLN ARG TYR VAL VAL ALA CYS LYS GLU PRO LYS
SEQRES 1 B 11 ALA ARG THR M3L GLN THR ALA ARG LYS SER THR
MODRES 3MEA M3L B 4 LYS N-TRIMETHYLLYSINE
HET M3L B 4 12
HETNAM M3L N-TRIMETHYLLYSINE
FORMUL 2 M3L C9 H21 N2 O2 1+
FORMUL 3 HOH *156(H2 O)
HELIX 1 1 ASP A 223 LEU A 227 5 5
HELIX 2 2 ALA A 280 ARG A 282 5 3
SHEET 1 A 6 GLU A 201 SER A 206 0
SHEET 2 A 6 LYS A 189 ASP A 194 -1 N ASP A 194 O GLU A 201
SHEET 3 A 6 GLU A 173 SER A 184 -1 N VAL A 181 O GLU A 191
SHEET 4 A 6 CYS A 243 ALA A 251 -1 O PHE A 244 N TRP A 175
SHEET 5 A 6 TYR A 260 PHE A 264 -1 O LEU A 263 N LEU A 248
SHEET 6 A 6 LEU A 277 VAL A 279 -1 O LEU A 277 N VAL A 262
SHEET 1 B 6 VAL A 210 PRO A 212 0
SHEET 2 B 6 LYS A 161 LYS A 167 -1 N ALA A 163 O ILE A 211
SHEET 3 B 6 GLU A 173 SER A 184 -1 O ILE A 176 N ALA A 164
SHEET 4 B 6 CYS A 243 ALA A 251 -1 O PHE A 244 N TRP A 175
SHEET 5 B 6 LEU A 233 LEU A 237 -1 N VAL A 234 O ALA A 247
SHEET 6 B 6 VAL A 284 ALA A 286 -1 O VAL A 285 N LEU A 235
LINK C THR B 3 N M3L B 4 1555 1555 1.33
CRYST1 93.385 41.425 52.527 90.00 121.39 90.00 C 1 2 1 4
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 0.010708 0.000000 0.006533 0.00000
SCALE2 0.000000 0.024140 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022301 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
