HEADER TRANSCRIPTION/DNA 13-JAN-00 1DU0
TITLE ENGRAILED HOMEODOMAIN Q50A VARIANT DNA COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-
COMPND 3 D(*TP*TP*TP*TP*GP*CP*CP*AP*TP*GP*TP*AP*AP*TP*TP*AP*CP*CP*TP*AP*A)-
COMPND 4 3');
COMPND 5 CHAIN: C;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA (5'-
COMPND 9 D(*AP*TP*TP*AP*GP*GP*TP*AP*AP*TP*TP*AP*CP*AP*TP*GP*GP*CP*AP*AP*A)-
COMPND 10 3');
COMPND 11 CHAIN: D;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: ENGRAILED HOMEODOMAIN;
COMPND 15 CHAIN: A, B;
COMPND 16 SYNONYM: HOMEOTIC PROTEIN ENGRAILED, SEGMENTATION POLARITY HOMEOBOX
COMPND 17 PROTEIN ENGRAILED;
COMPND 18 ENGINEERED: YES;
COMPND 19 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 7 ORGANISM_COMMON: FRUIT FLY;
SOURCE 8 ORGANISM_TAXID: 7227;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HOMEODOMAIN, DNA-BINDING PROTEIN, PROTEIN-DNA COMPLEX, TRANSCRIPTION-
KEYWDS 2 DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.A.GRANT,M.A.ROULD,J.D.KLEMM,C.O.PABO
REVDAT 5 07-FEB-24 1DU0 1 REMARK
REVDAT 4 03-NOV-21 1DU0 1 SEQADV
REVDAT 3 24-FEB-09 1DU0 1 VERSN
REVDAT 2 07-AUG-00 1DU0 3 HETATM REMARK
REVDAT 1 31-JUL-00 1DU0 0
JRNL AUTH R.A.GRANT,M.A.ROULD,J.D.KLEMM,C.O.PABO
JRNL TITL EXPLORING THE ROLE OF GLUTAMINE 50 IN THE HOMEODOMAIN-DNA
JRNL TITL 2 INTERFACE: CRYSTAL STRUCTURE OF ENGRAILED (GLN50 --> ALA)
JRNL TITL 3 COMPLEX AT 2.0 A.
JRNL REF BIOCHEMISTRY V. 39 8187 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 10889025
JRNL DOI 10.1021/BI000071A
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.FRAENKEL,M.A.ROULD,K.A.CHAMBERS,C.O.PABO
REMARK 1 TITL ENGRAILED HOMEODOMAIN-DNA COMPLEX AT 2.2 ANGSTROMS
REMARK 1 TITL 2 RESOLUTION: A DETAILED VIEW OF THE INTERFACE AND COMPARISON
REMARK 1 TITL 3 WITH OTHER ENGRAILED STRUCTURES
REMARK 1 REF J.MOL.BIOL. V. 284 351 1998
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1998.2147
REMARK 1 REFERENCE 2
REMARK 1 AUTH L.TUCKER-KELLOGG,M.A.ROULD,K.A.CHAMBERS,S.E.ADES,R.T.SAUER
REMARK 1 TITL ENGRAILED (GLN50->LYS) HOMEODOMAIN-DNA COMPLEX AT 1.9
REMARK 1 TITL 2 ANGSTROMS RESOLUTION: STRUCTURAL BASIS FOR ENHANCED AFFINITY
REMARK 1 TITL 3 AND ALTERED SPECIFICITY
REMARK 1 REF STRUCTURE V. 5 1047 1997
REMARK 1 REFN ISSN 0969-2126
REMARK 1 DOI 10.1016/S0969-2126(97)00256-6
REMARK 1 REFERENCE 3
REMARK 1 AUTH S.E.ADES,R.T.SAUER
REMARK 1 TITL DIFFERENTIAL DNA-BINDING SPECIFICITY OF THE ENGRAILED
REMARK 1 TITL 2 HOMEODOMAIN: THE ROLE OF RESIDUE 50
REMARK 1 REF BIOCHEMISTRY V. 33 9187 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 4
REMARK 1 AUTH C.A.KISSINGER,B.LIU,E.MARTIN-BLANCO,T.B.KORNBERG,C.O.PABO
REMARK 1 TITL CRYSTAL STRUCTURE OF AN ENGRAILED HOMEODOMAIN-DNA COMPLES AT
REMARK 1 TITL 2 2.8 ANGSTROMS RESOLUTION: A FRAMEWORK FOR UNDERSTANDING
REMARK 1 TITL 3 HOMEODOMAIN-DNA INTERACTIONS
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 63 579 1990
REMARK 1 REFN ISSN 0092-8674
REMARK 1 DOI 10.1016/0092-8674(90)90453-L
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.0
REMARK 3 NUMBER OF REFLECTIONS : 21566
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 SET) : 0.234
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2168
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 56.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2044
REMARK 3 BIN R VALUE (WORKING SET) : 0.3630
REMARK 3 BIN FREE R VALUE : 0.3510
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 203
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.025
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 930
REMARK 3 NUCLEIC ACID ATOMS : 855
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 103
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.70
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.33
REMARK 3 ESD FROM SIGMAA (A) : 0.41
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.36
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.39
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 18.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.440
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.710 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.070 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.800 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 7.330 ; 2.500
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : DNA-RNA.PARAM
REMARK 3 PARAMETER FILE 3 : PARAM19.SOL
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH19.SOL
REMARK 3 TOPOLOGY FILE 3 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DU0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JAN-00.
REMARK 100 THE DEPOSITION ID IS D_1000010365.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JAN-96
REMARK 200 TEMPERATURE (KELVIN) : 128
REMARK 200 PH : 7.0
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 RU200
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 IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23204
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.03900
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) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 70.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.35100
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: 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 (%): 62.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: BIS-TRIS-PROPANE, PEG 400, AMMONIUM
REMARK 280 ACETATE, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
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 63.45000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.77500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 63.45000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.77500
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 APPLY THE FOLLOWING TO CHAINS: C, D, 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 ARG A 3
REMARK 465 PRO A 4
REMARK 465 ARG A 5
REMARK 465 THR A 6
REMARK 465 SER B 159
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 DG D 305 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 DC C 217 0.07 SIDE CHAIN
REMARK 500 DA D 301 0.06 SIDE CHAIN
REMARK 500 DG D 305 0.08 SIDE CHAIN
REMARK 500 DG D 306 0.07 SIDE CHAIN
REMARK 500 DT D 311 0.06 SIDE CHAIN
REMARK 500 DA D 314 0.06 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HDD RELATED DB: PDB
REMARK 900 WILD TYPE ENGRAILED-DNA CO-CRYSTAL 2.8 ANGSTROMS
REMARK 900 RELATED ID: 2HDD RELATED DB: PDB
REMARK 900 Q50K VARIANT ENGRAILED-DNA CO-CRYSTAL
REMARK 900 RELATED ID: 3HDD RELATED DB: PDB
REMARK 900 WILD TYPE ENGRAILED-DNA CO-CRYSTAL 2.2 ANGSTROMS
DBREF 1DU0 A 3 59 UNP P02836 HMEN_DROME 456 512
DBREF 1DU0 B 103 159 UNP P02836 HMEN_DROME 456 512
DBREF 1DU0 C 201 221 PDB 1DU0 1DU0 201 221
DBREF 1DU0 D 301 321 PDB 1DU0 1DU0 301 321
SEQADV 1DU0 ALA A 50 UNP P02836 GLN 503 ENGINEERED MUTATION
SEQADV 1DU0 ALA B 150 UNP P02836 GLN 503 ENGINEERED MUTATION
SEQRES 1 C 21 DT DT DT DT DG DC DC DA DT DG DT DA DA
SEQRES 2 C 21 DT DT DA DC DC DT DA DA
SEQRES 1 D 21 DA DT DT DA DG DG DT DA DA DT DT DA DC
SEQRES 2 D 21 DA DT DG DG DC DA DA DA
SEQRES 1 A 57 ARG PRO ARG THR ALA PHE SER SER GLU GLN LEU ALA ARG
SEQRES 2 A 57 LEU LYS ARG GLU PHE ASN GLU ASN ARG TYR LEU THR GLU
SEQRES 3 A 57 ARG ARG ARG GLN GLN LEU SER SER GLU LEU GLY LEU ASN
SEQRES 4 A 57 GLU ALA GLN ILE LYS ILE TRP PHE ALA ASN LYS ARG ALA
SEQRES 5 A 57 LYS ILE LYS LYS SER
SEQRES 1 B 57 ARG PRO ARG THR ALA PHE SER SER GLU GLN LEU ALA ARG
SEQRES 2 B 57 LEU LYS ARG GLU PHE ASN GLU ASN ARG TYR LEU THR GLU
SEQRES 3 B 57 ARG ARG ARG GLN GLN LEU SER SER GLU LEU GLY LEU ASN
SEQRES 4 B 57 GLU ALA GLN ILE LYS ILE TRP PHE ALA ASN LYS ARG ALA
SEQRES 5 B 57 LYS ILE LYS LYS SER
FORMUL 5 HOH *103(H2 O)
HELIX 1 1 SER A 9 ASN A 23 1 15
HELIX 2 2 THR A 27 GLY A 39 1 13
HELIX 3 3 ASN A 41 LYS A 57 1 17
HELIX 4 4 SER B 109 ASN B 123 1 15
HELIX 5 5 THR B 127 GLY B 139 1 13
HELIX 6 6 ASN B 141 LYS B 157 1 17
CRYST1 126.900 45.550 71.620 90.00 119.90 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 0.007880 0.000000 0.004531 0.00000
SCALE2 0.000000 0.021954 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016106 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
