HEADER LEUCINE ZIPPER 20-OCT-93 1GCL
TITLE GCN4 LEUCINE ZIPPER CORE MUTANT P-LI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GCN4;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932
KEYWDS HYDROPHOBIC CORE MUTANT, LEUCINE ZIPPER
EXPDTA X-RAY DIFFRACTION
AUTHOR P.B.HARBURY,T.ZHANG,P.S.KIM,T.ALBER
REVDAT 3 24-APR-13 1GCL 1 SEQADV VERSN
REVDAT 2 24-FEB-09 1GCL 1 VERSN
REVDAT 1 03-JUN-95 1GCL 0
JRNL AUTH P.B.HARBURY,T.ZHANG,P.S.KIM,T.ALBER
JRNL TITL A SWITCH BETWEEN TWO-, THREE-, AND FOUR-STRANDED COILED
JRNL TITL 2 COILS IN GCN4 LEUCINE ZIPPER MUTANTS.
JRNL REF SCIENCE V. 262 1401 1993
JRNL REFN ISSN 0036-8075
JRNL PMID 8248779
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.K.SHEA,J.D.KLEMM,P.S.KIM,T.ALBER
REMARK 1 TITL X-RAY STRUCTURE OF THE GCN4 LEUCINE ZIPPER, A TWO-STRANDED,
REMARK 1 TITL 2 PARALLEL COILED COIL
REMARK 1 REF SCIENCE V. 254 539 1991
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 2
REMARK 1 AUTH E.K.SHEA,R.RUTKOWSKI,P.S.KIM
REMARK 1 TITL EVIDENCE THAT THE LEUCINE ZIPPER IS A COILED COIL
REMARK 1 REF SCIENCE V. 243 538 1989
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT, X-PLOR
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS,BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : 5.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 5266
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.152
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1060
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 77
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.018 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 2.900 ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GCL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 1992
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 5643
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 73.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 32.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 23.71600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 25.88250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.31700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 25.88250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.71600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 24.31700
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 GLU A 32
REMARK 465 ARG A 33
REMARK 465 GLU B 32
REMARK 465 ARG B 33
REMARK 465 GLU C 32
REMARK 465 ARG C 33
REMARK 465 GLU D 32
REMARK 465 ARG D 33
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH2 ARG B 1 O LYS C 28 1655 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 6 CD GLU A 6 OE1 0.096
REMARK 500 GLU A 20 CD GLU A 20 OE2 0.084
REMARK 500 GLU B 10 CD GLU B 10 OE2 0.070
REMARK 500 GLU B 20 CD GLU B 20 OE2 0.069
REMARK 500 GLU B 22 CD GLU B 22 OE2 0.079
REMARK 500 GLU C 10 CD GLU C 10 OE2 0.068
REMARK 500 GLU C 20 CD GLU C 20 OE2 0.078
REMARK 500 GLU D 6 CD GLU D 6 OE1 0.093
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 1 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG B 1 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ILE B 5 CA - CB - CG1 ANGL. DEV. = -11.7 DEGREES
REMARK 500 ARG B 25 NE - CZ - NH2 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG C 1 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG C 1 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ASP C 7 CB - CG - OD1 ANGL. DEV. = 7.7 DEGREES
REMARK 500 ASP C 7 CB - CG - OD2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 TYR C 17 CB - CG - CD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG C 25 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ASP D 7 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 TYR D 17 CB - CG - CD1 ANGL. DEV. = 3.9 DEGREES
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 ASP A 7 1.83 -65.24
REMARK 500 GLU B 6 34.39 -86.93
REMARK 500 LYS B 27 -73.38 -73.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 HIS B 18 24.6 L L OUTSIDE RANGE
REMARK 500 LYS B 28 24.5 L L OUTSIDE RANGE
REMARK 500 GLU C 22 24.9 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 42 DISTANCE = 5.38 ANGSTROMS
REMARK 525 HOH B 46 DISTANCE = 6.78 ANGSTROMS
REMARK 525 HOH B 54 DISTANCE = 5.09 ANGSTROMS
REMARK 525 HOH C 43 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH C 44 DISTANCE = 5.18 ANGSTROMS
REMARK 525 HOH D 45 DISTANCE = 5.14 ANGSTROMS
REMARK 525 HOH D 46 DISTANCE = 6.15 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE A 0
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE B 0
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE C 0
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE D 0
DBREF 1GCL A 1 33 UNP P03069 GCN4_YEAST 249 281
DBREF 1GCL B 1 33 UNP P03069 GCN4_YEAST 249 281
DBREF 1GCL C 1 33 UNP P03069 GCN4_YEAST 249 281
DBREF 1GCL D 1 33 UNP P03069 GCN4_YEAST 249 281
SEQADV 1GCL ILE A 5 UNP P03069 LEU 253 ENGINEERED MUTATION
SEQADV 1GCL LEU A 9 UNP P03069 VAL 257 ENGINEERED MUTATION
SEQADV 1GCL ILE A 12 UNP P03069 LEU 260 ENGINEERED MUTATION
SEQADV 1GCL LEU A 16 UNP P03069 ASN 264 ENGINEERED MUTATION
SEQADV 1GCL ILE A 19 UNP P03069 LEU 267 ENGINEERED MUTATION
SEQADV 1GCL LEU A 23 UNP P03069 VAL 271 ENGINEERED MUTATION
SEQADV 1GCL ILE A 26 UNP P03069 LEU 274 ENGINEERED MUTATION
SEQADV 1GCL LEU A 30 UNP P03069 VAL 278 ENGINEERED MUTATION
SEQADV 1GCL ILE B 5 UNP P03069 LEU 253 ENGINEERED MUTATION
SEQADV 1GCL LEU B 9 UNP P03069 VAL 257 ENGINEERED MUTATION
SEQADV 1GCL ILE B 12 UNP P03069 LEU 260 ENGINEERED MUTATION
SEQADV 1GCL LEU B 16 UNP P03069 ASN 264 ENGINEERED MUTATION
SEQADV 1GCL ILE B 19 UNP P03069 LEU 267 ENGINEERED MUTATION
SEQADV 1GCL LEU B 23 UNP P03069 VAL 271 ENGINEERED MUTATION
SEQADV 1GCL ILE B 26 UNP P03069 LEU 274 ENGINEERED MUTATION
SEQADV 1GCL LEU B 30 UNP P03069 VAL 278 ENGINEERED MUTATION
SEQADV 1GCL ILE C 5 UNP P03069 LEU 253 ENGINEERED MUTATION
SEQADV 1GCL LEU C 9 UNP P03069 VAL 257 ENGINEERED MUTATION
SEQADV 1GCL ILE C 12 UNP P03069 LEU 260 ENGINEERED MUTATION
SEQADV 1GCL LEU C 16 UNP P03069 ASN 264 ENGINEERED MUTATION
SEQADV 1GCL ILE C 19 UNP P03069 LEU 267 ENGINEERED MUTATION
SEQADV 1GCL LEU C 23 UNP P03069 VAL 271 ENGINEERED MUTATION
SEQADV 1GCL ILE C 26 UNP P03069 LEU 274 ENGINEERED MUTATION
SEQADV 1GCL LEU C 30 UNP P03069 VAL 278 ENGINEERED MUTATION
SEQADV 1GCL ILE D 5 UNP P03069 LEU 253 ENGINEERED MUTATION
SEQADV 1GCL LEU D 9 UNP P03069 VAL 257 ENGINEERED MUTATION
SEQADV 1GCL ILE D 12 UNP P03069 LEU 260 ENGINEERED MUTATION
SEQADV 1GCL LEU D 16 UNP P03069 ASN 264 ENGINEERED MUTATION
SEQADV 1GCL ILE D 19 UNP P03069 LEU 267 ENGINEERED MUTATION
SEQADV 1GCL LEU D 23 UNP P03069 VAL 271 ENGINEERED MUTATION
SEQADV 1GCL ILE D 26 UNP P03069 LEU 274 ENGINEERED MUTATION
SEQADV 1GCL LEU D 30 UNP P03069 VAL 278 ENGINEERED MUTATION
SEQRES 1 A 34 ACE ARG MET LYS GLN ILE GLU ASP LYS LEU GLU GLU ILE
SEQRES 2 A 34 LEU SER LYS LEU TYR HIS ILE GLU ASN GLU LEU ALA ARG
SEQRES 3 A 34 ILE LYS LYS LEU LEU GLY GLU ARG
SEQRES 1 B 34 ACE ARG MET LYS GLN ILE GLU ASP LYS LEU GLU GLU ILE
SEQRES 2 B 34 LEU SER LYS LEU TYR HIS ILE GLU ASN GLU LEU ALA ARG
SEQRES 3 B 34 ILE LYS LYS LEU LEU GLY GLU ARG
SEQRES 1 C 34 ACE ARG MET LYS GLN ILE GLU ASP LYS LEU GLU GLU ILE
SEQRES 2 C 34 LEU SER LYS LEU TYR HIS ILE GLU ASN GLU LEU ALA ARG
SEQRES 3 C 34 ILE LYS LYS LEU LEU GLY GLU ARG
SEQRES 1 D 34 ACE ARG MET LYS GLN ILE GLU ASP LYS LEU GLU GLU ILE
SEQRES 2 D 34 LEU SER LYS LEU TYR HIS ILE GLU ASN GLU LEU ALA ARG
SEQRES 3 D 34 ILE LYS LYS LEU LEU GLY GLU ARG
HET ACE A 0 3
HET ACE B 0 3
HET ACE C 0 3
HET ACE D 0 3
HETNAM ACE ACETYL GROUP
FORMUL 1 ACE 4(C2 H4 O)
FORMUL 5 HOH *77(H2 O)
HELIX 1 1 ARG A 1 LEU A 29 1 29
HELIX 2 2 ARG B 1 GLU B 6 1 6
HELIX 3 3 LYS B 8 GLY B 31 1 24
HELIX 4 4 ARG C 1 LEU C 30 1 30
HELIX 5 5 MET D 2 GLY D 31 1 30
LINK C ACE A 0 N ARG A 1 1555 1555 1.32
LINK C ACE B 0 N ARG B 1 1555 1555 1.34
LINK C ACE C 0 N ARG C 1 1555 1555 1.35
LINK C ACE D 0 N ARG D 1 1555 1555 1.34
SITE 1 AC1 6 ARG A 1 MET A 2 LYS A 3 LYS B 28
SITE 2 AC1 6 LEU B 29 GLY B 31
SITE 1 AC2 3 ARG B 1 MET B 2 LYS B 3
SITE 1 AC3 5 ARG B 1 ARG C 1 MET C 2 LYS C 3
SITE 2 AC3 5 GLN C 4
SITE 1 AC4 3 LYS A 28 LEU A 29 ARG D 1
CRYST1 47.432 48.634 51.765 90.00 90.00 90.00 P 21 21 21 16
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 0.021083 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020562 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019318 0.00000
HETATM 1 C ACE A 0 33.919 19.079 37.960 1.00 19.62 C
HETATM 2 O ACE A 0 32.845 18.470 38.149 1.00 63.85 O
HETATM 3 CH3 ACE A 0 35.057 18.354 37.267 1.00 99.99 C
(ATOM LINES ARE NOT SHOWN.)
END
