HEADER TRANSCRIPTION 28-MAY-14 4TL1
TITLE GCN4-P1 WITH MUTATION TO 1-AMINOCYCLOHEXANECARBOXYLIC ACID AT RESIDUE
TITLE 2 10
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GENERAL CONTROL PROTEIN GCN4;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 249-281;
COMPND 5 SYNONYM: AMINO ACID BIOSYNTHESIS REGULATORY PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 4 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 5 ORGANISM_TAXID: 559292
KEYWDS COILED COIL, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR N.A.TAVENOR,K.I.SILVA,S.SAXENA,W.S.HORNE
REVDAT 7 27-SEP-23 4TL1 1 REMARK
REVDAT 6 27-NOV-19 4TL1 1 REMARK
REVDAT 5 22-NOV-17 4TL1 1 REMARK
REVDAT 4 13-SEP-17 4TL1 1 SOURCE KEYWDS JRNL REMARK
REVDAT 3 01-OCT-14 4TL1 1 JRNL
REVDAT 2 20-AUG-14 4TL1 1 TITLE
REVDAT 1 06-AUG-14 4TL1 0
JRNL AUTH N.A.TAVENOR,K.I.SILVA,S.SAXENA,W.S.HORNE
JRNL TITL ORIGINS OF STRUCTURAL FLEXIBILITY IN PROTEIN-BASED
JRNL TITL 2 SUPRAMOLECULAR POLYMERS REVEALED BY DEER SPECTROSCOPY.
JRNL REF J.PHYS.CHEM.B V. 118 9881 2014
JRNL REFN ISSN 1089-5647
JRNL PMID 25060334
JRNL DOI 10.1021/JP505643W
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.48
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.460
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 6371
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.680
REMARK 3 FREE R VALUE TEST SET COUNT : 298
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 20.4854 - 2.2676 0.98 3086 153 0.1756 0.2116
REMARK 3 2 2.2676 - 1.8002 0.97 2987 145 0.2161 0.2851
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.960
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.011 582
REMARK 3 ANGLE : 1.106 783
REMARK 3 CHIRALITY : 0.066 86
REMARK 3 PLANARITY : 0.005 99
REMARK 3 DIHEDRAL : 13.981 252
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4TL1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1000201800.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-DEC-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6386
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 20.480
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.17600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CRYSTALCLEAR, PHENIX
REMARK 200 STARTING MODEL: 2ZTA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM CITRATE TRIBASIC, 0.1 M
REMARK 280 SODIUM CACODYLATE PH 6.5, 30% V/V ISOPROPANOL, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
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 41.66100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 15.17500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 41.66100
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 15.17500
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 4830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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 NH2 B 34
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 LYS A 3 CD CE NZ
REMARK 470 GLN A 4 CG CD OE1 NE2
REMARK 470 ARG A 33 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 28 CD CE NZ
REMARK 470 ARG B 33 CA C O CB CG CD NE
REMARK 470 ARG B 33 CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 OH TYR B 17 O HOH B 101 2.14
REMARK 500 O HOH A 215 O HOH A 223 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ACE B 0 and ARG B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide VAL B 9 and 02K B 10
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 02K B 10 and GLU B
REMARK 800 11
DBREF 4TL1 A 1 33 UNP P03069 GCN4_YEAST 249 281
DBREF 4TL1 B 1 33 UNP P03069 GCN4_YEAST 249 281
SEQADV 4TL1 ACE A 0 UNP P03069 INSERTION
SEQADV 4TL1 02K A 10 UNP P03069 GLU 258 ENGINEERED MUTATION
SEQADV 4TL1 NH2 A 34 UNP P03069 INSERTION
SEQADV 4TL1 ACE B 0 UNP P03069 INSERTION
SEQADV 4TL1 02K B 10 UNP P03069 GLU 258 ENGINEERED MUTATION
SEQADV 4TL1 NH2 B 34 UNP P03069 INSERTION
SEQRES 1 A 35 ACE ARG MET LYS GLN LEU GLU ASP LYS VAL 02K GLU LEU
SEQRES 2 A 35 LEU SER LYS ASN TYR HIS LEU GLU ASN GLU VAL ALA ARG
SEQRES 3 A 35 LEU LYS LYS LEU VAL GLY GLU ARG NH2
SEQRES 1 B 35 ACE ARG MET LYS GLN LEU GLU ASP LYS VAL 02K GLU LEU
SEQRES 2 B 35 LEU SER LYS ASN TYR HIS LEU GLU ASN GLU VAL ALA ARG
SEQRES 3 B 35 LEU LYS LYS LEU VAL GLY GLU ARG NH2
HET ACE A 0 3
HET 02K A 10 20
HET NH2 A 34 1
HET ACE B 0 3
HET 02K B 10 20
HET IPA A 101 4
HETNAM ACE ACETYL GROUP
HETNAM 02K 1-AMINOCYCLOHEXANECARBOXYLIC ACID
HETNAM NH2 AMINO GROUP
HETNAM IPA ISOPROPYL ALCOHOL
HETSYN IPA 2-PROPANOL
FORMUL 1 ACE 2(C2 H4 O)
FORMUL 1 02K 2(C7 H13 N O2)
FORMUL 1 NH2 H2 N
FORMUL 3 IPA C3 H8 O
FORMUL 4 HOH *69(H2 O)
HELIX 1 AA1 ARG A 1 ARG A 33 1 33
HELIX 2 AA2 ARG B 1 GLY B 31 1 31
LINK C ACE A 0 N ARG A 1 1555 1555 1.33
LINK C VAL A 9 N 02K A 10 1555 1555 1.33
LINK C 02K A 10 N GLU A 11 1555 1555 1.33
LINK C ARG A 33 N NH2 A 34 1555 1555 1.33
LINK C ACE B 0 N ARG B 1 1555 1555 1.33
LINK C VAL B 9 N 02K B 10 1555 1555 1.34
LINK C 02K B 10 N GLU B 11 1555 1555 1.33
SITE 1 AC1 3 LYS A 8 LEU A 13 LYS B 8
SITE 1 AC2 10 MET A 2 GLU A 6 HOH A 217 MET B 2
SITE 2 AC2 10 LYS B 3 GLN B 4 LEU B 5 TYR B 17
SITE 3 AC2 10 ASN B 21 HOH B 103
SITE 1 AC3 11 02K A 10 TYR A 17 LEU B 5 GLU B 6
SITE 2 AC3 11 ASP B 7 LYS B 8 GLU B 11 LEU B 12
SITE 3 AC3 11 LEU B 13 SER B 14 HOH B 106
SITE 1 AC4 17 02K A 10 ARG A 25 HOH A 212 GLU B 6
SITE 2 AC4 17 ASP B 7 LYS B 8 VAL B 9 LEU B 12
SITE 3 AC4 17 LEU B 13 SER B 14 LYS B 15 GLU B 32
SITE 4 AC4 17 HOH B 106 HOH B 107 HOH B 109 HOH B 110
SITE 5 AC4 17 HOH B 111
CRYST1 83.322 30.350 28.019 90.00 101.68 90.00 C 1 2 1 8
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 0.012002 0.000000 0.002481 0.00000
SCALE2 0.000000 0.032949 0.000000 0.00000
SCALE3 0.000000 0.000000 0.036445 0.00000
HETATM 1 C ACE A 0 -38.816 -0.802 16.882 1.00 60.97 C
HETATM 2 O ACE A 0 -38.178 -1.154 15.884 1.00 55.93 O
HETATM 3 CH3 ACE A 0 -40.288 -1.145 17.027 1.00 48.17 C
(ATOM LINES ARE NOT SHOWN.)
END
