HEADER DNA BINDING PROTEIN 13-JUL-17 5OGU
TITLE STRUCTURE OF DNA-BINDING HU PROTEIN FROM MICOPLASMA SPIROPLASMA
TITLE 2 MELLIFERUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-BINDING PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPIROPLASMA MELLIFERUM KC3;
SOURCE 3 ORGANISM_TAXID: 570509;
SOURCE 4 GENE: SPM_000560;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR D.A.ALTUKHOV,A.A.TALYZINA,Y.K.AGAPOVA,A.V.VLASKINA,D.A.KORZHENEVSKIY,
AUTHOR 2 E.V.BOCHAROV,T.V.RAKITINA,V.I.TIMOFEEV
REVDAT 4 14-JUN-23 5OGU 1 REMARK
REVDAT 3 09-NOV-22 5OGU 1 JRNL
REVDAT 2 08-MAY-19 5OGU 1 REMARK
REVDAT 1 23-AUG-17 5OGU 0
JRNL AUTH V.I.TIMOFEEV,D.A.ALTUKHOV,A.A.TALYZINA,Y.K.AGAPOVA,
JRNL AUTH 2 A.V.VLASKINA,D.A.KORZHENEVSKIY,S.Y.KLEYMENOV,E.V.BOCHAROV,
JRNL AUTH 3 T.V.RAKITINA
JRNL TITL STRUCTURAL PLASTICITY AND THERMAL STABILITY OF THE
JRNL TITL 2 HISTONE-LIKE PROTEIN FROM SPIROPLASMA MELLIFERUM ARE DUE TO
JRNL TITL 3 PHENYLALANINE INSERTIONS INTO THE CONSERVATIVE SCAFFOLD.
JRNL REF J.BIOMOL.STRUCT.DYN. V. 36 4392 2018
JRNL REFN ESSN 1538-0254
JRNL PMID 29283021
JRNL DOI 10.1080/07391102.2017.1417162
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : GROMACS
REMARK 3 AUTHORS : HERMAN BERENDSEN'S GROUP, DEPARTMENT OF
REMARK 3 BIOPHYSICAL CHEMISTRY OF GRONINGEN UNIVERSITY
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5OGU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1200005707.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.7
REMARK 210 IONIC STRENGTH : 0.375
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 5 % [U-2H] D2O, 95% H2O/5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : UNIFORM NMR SYSTEM
REMARK 210 SPECTROMETER MANUFACTURER : AGILENT
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : TALOS+
REMARK 210 METHOD USED : MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 5000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 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 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 OE2 GLU A 43 HZ3 LYS A 51 1.52
REMARK 500 OD1 ASP A 90 HZ3 LYS B 35 1.59
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 1 PHE A 14 CB - CG - CD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 1 VAL A 17 CA - CB - CG1 ANGL. DEV. = 9.6 DEGREES
REMARK 500 1 GLU A 43 OE1 - CD - OE2 ANGL. DEV. = -8.6 DEGREES
REMARK 500 1 ILE A 46 CA - CB - CG1 ANGL. DEV. = 11.8 DEGREES
REMARK 500 1 GLY A 48 C - N - CA ANGL. DEV. = 16.2 DEGREES
REMARK 500 1 ARG A 57 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 1 ARG A 63 NE - CZ - NH2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 1 ASP A 90 CB - CG - OD1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 1 ASP A 90 CB - CG - OD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 1 PHE B 29 CB - CG - CD2 ANGL. DEV. = 4.3 DEGREES
REMARK 500 1 PHE B 49 CB - CG - CD1 ANGL. DEV. = -5.3 DEGREES
REMARK 500 1 ARG B 57 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 1 ARG B 57 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 2 PHE A 29 CG - CD2 - CE2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 2 ASP A 32 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 2 ARG A 60 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 2 ARG A 60 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 2 ARG A 63 NE - CZ - NH1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 2 GLU B 5 OE1 - CD - OE2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 2 PHE B 14 CZ - CE2 - CD2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 2 ILE B 46 CA - CB - CG1 ANGL. DEV. = 12.0 DEGREES
REMARK 500 2 ARG B 57 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 2 ARG B 57 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 2 ASP B 61 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 2 ARG B 63 NE - CZ - NH1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 2 ARG B 63 NE - CZ - NH2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 2 PHE B 81 CB - CG - CD1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 3 LYS A 82 N - CA - CB ANGL. DEV. = -12.2 DEGREES
REMARK 500 3 PHE B 31 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 3 PHE B 49 CB - CG - CD2 ANGL. DEV. = 4.4 DEGREES
REMARK 500 3 PHE B 49 CB - CG - CD1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 3 ARG B 60 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 3 ARG B 60 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 3 PHE B 81 CB - CG - CD1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 4 VAL A 17 CA - CB - CG1 ANGL. DEV. = 10.8 DEGREES
REMARK 500 4 PHE A 29 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 4 ALA A 40 CB - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 4 ARG A 63 CD - NE - CZ ANGL. DEV. = 9.4 DEGREES
REMARK 500 4 ARG A 63 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 4 SER B 19 CB - CA - C ANGL. DEV. = 12.7 DEGREES
REMARK 500 4 PHE B 31 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 4 GLU B 56 OE1 - CD - OE2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 4 ARG B 57 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 4 ALA B 58 CB - CA - C ANGL. DEV. = -12.5 DEGREES
REMARK 500 4 ARG B 60 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 5 VAL A 39 CA - CB - CG1 ANGL. DEV. = 9.4 DEGREES
REMARK 500 5 ARG A 57 NE - CZ - NH1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 5 ARG A 57 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 5 ARG A 63 NH1 - CZ - NH2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 5 ARG A 63 NE - CZ - NH2 ANGL. DEV. = -10.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 201 ANGLE DEVIATIONS.
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 PHE A 14 61.70 -113.68
REMARK 500 1 LYS A 88 -107.20 -120.86
REMARK 500 1 THR B 67 -33.93 -138.12
REMARK 500 1 LYS B 72 37.83 -145.53
REMARK 500 1 LYS B 88 -91.33 -136.86
REMARK 500 2 ASP A 16 1.90 -68.08
REMARK 500 2 VAL A 17 -35.71 -146.44
REMARK 500 2 LYS A 20 -70.93 -29.60
REMARK 500 2 ALA A 47 102.95 -34.21
REMARK 500 2 THR A 67 -53.96 -137.64
REMARK 500 2 LYS A 72 34.97 -154.25
REMARK 500 2 LYS A 88 -109.72 -133.81
REMARK 500 2 ASN A 92 89.07 -69.46
REMARK 500 2 LYS B 72 47.52 -143.19
REMARK 500 2 LYS B 82 101.15 -161.42
REMARK 500 2 ALA B 83 156.20 -42.66
REMARK 500 2 LYS B 88 -65.22 -146.02
REMARK 500 3 VAL A 17 -42.19 -139.68
REMARK 500 3 PHE A 29 -9.79 -48.41
REMARK 500 3 VAL A 30 -70.01 -76.65
REMARK 500 3 LYS A 72 58.08 -140.85
REMARK 500 3 LYS A 88 -107.72 -135.63
REMARK 500 3 PHE B 14 57.65 -140.30
REMARK 500 3 VAL B 17 -69.69 -128.54
REMARK 500 3 LYS B 20 -49.39 -29.76
REMARK 500 3 LYS B 72 56.07 -144.86
REMARK 500 3 SER B 78 -146.86 -136.88
REMARK 500 3 LYS B 88 -84.60 -156.48
REMARK 500 4 ALA A 47 100.36 -59.89
REMARK 500 4 THR A 67 -70.01 -131.32
REMARK 500 4 LYS A 88 -110.72 -125.26
REMARK 500 4 VAL B 17 -62.67 -128.39
REMARK 500 4 ALA B 47 108.46 -50.00
REMARK 500 4 LYS B 72 51.35 -156.71
REMARK 500 4 LYS B 88 -71.41 -141.56
REMARK 500 5 VAL A 17 -61.68 -105.40
REMARK 500 5 ALA A 47 100.13 -56.04
REMARK 500 5 THR A 67 -40.24 -137.65
REMARK 500 5 LYS A 72 83.68 -158.29
REMARK 500 5 LYS A 88 -78.53 -141.70
REMARK 500 5 THR B 15 -39.55 -39.37
REMARK 500 5 VAL B 17 -8.03 -142.54
REMARK 500 5 THR B 67 -52.85 -120.09
REMARK 500 5 LYS B 72 64.42 -156.30
REMARK 500 5 ALA B 75 98.68 -59.22
REMARK 500 5 LYS B 88 -80.60 -140.60
REMARK 500 6 PHE A 14 33.70 -141.59
REMARK 500 6 ALA A 47 99.06 -44.87
REMARK 500 6 LYS A 72 51.84 -151.94
REMARK 500 6 LYS A 85 -48.66 -24.81
REMARK 500
REMARK 500 THIS ENTRY HAS 128 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 HIS A 0 MET A 1 6 149.25
REMARK 500 ALA B 75 SER B 76 7 -140.50
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 1 ARG B 63 0.08 SIDE CHAIN
REMARK 500 1 PHE B 81 0.08 SIDE CHAIN
REMARK 500 2 PHE A 14 0.13 SIDE CHAIN
REMARK 500 7 HIS A 33 0.07 SIDE CHAIN
REMARK 500 7 HIS B 22 0.11 SIDE CHAIN
REMARK 500 7 GLU B 69 0.07 SIDE CHAIN
REMARK 500 8 ARG B 60 0.07 SIDE CHAIN
REMARK 500 10 ARG A 57 0.09 SIDE CHAIN
REMARK 500 11 PHE A 49 0.07 SIDE CHAIN
REMARK 500 11 ARG A 63 0.07 SIDE CHAIN
REMARK 500 14 PHE A 14 0.08 SIDE CHAIN
REMARK 500 14 PHE A 81 0.08 SIDE CHAIN
REMARK 500 15 GLU A 12 0.07 SIDE CHAIN
REMARK 500 15 PHE A 14 0.08 SIDE CHAIN
REMARK 500 15 PHE A 81 0.07 SIDE CHAIN
REMARK 500 15 PHE B 31 0.09 SIDE CHAIN
REMARK 500 15 ARG B 63 0.11 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 5 THR B 67 10.02
REMARK 500 9 ILE B 10 -11.99
REMARK 500 15 LEU B 38 -10.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 34163 RELATED DB: BMRB
REMARK 900 STRUCTURE OF DNA-BINDING HU PROTEIN FROM MICOPLASMA SPIROPLASMA
REMARK 900 MELLIFERUM
DBREF1 5OGU A 1 93 UNP A0A037USE5_SPIME
DBREF2 5OGU A A0A037USE5 1 93
DBREF1 5OGU B 1 93 UNP A0A037USE5_SPIME
DBREF2 5OGU B A0A037USE5 1 93
SEQADV 5OGU GLY A -1 UNP A0A037USE EXPRESSION TAG
SEQADV 5OGU HIS A 0 UNP A0A037USE EXPRESSION TAG
SEQADV 5OGU GLY B -1 UNP A0A037USE EXPRESSION TAG
SEQADV 5OGU HIS B 0 UNP A0A037USE EXPRESSION TAG
SEQRES 1 A 95 GLY HIS MET SER LYS LYS GLU LEU ALA ALA GLN ILE ALA
SEQRES 2 A 95 GLU LYS PHE THR ASP VAL LEU SER LYS THR HIS ALA GLU
SEQRES 3 A 95 GLU ILE THR ASN PHE VAL PHE ASP HIS ILE LYS LYS ALA
SEQRES 4 A 95 LEU VAL ALA GLY LYS GLU VAL SER ILE ALA GLY PHE GLY
SEQRES 5 A 95 LYS PHE ALA VAL THR GLU ARG ALA ALA ARG ASP GLY ARG
SEQRES 6 A 95 ASN PRO SER THR GLY GLU THR ILE LYS ILE PRO ALA SER
SEQRES 7 A 95 LYS SER ALA LYS PHE LYS ALA GLY LYS GLN LEU LYS THR
SEQRES 8 A 95 ASP LEU ASN ASN
SEQRES 1 B 95 GLY HIS MET SER LYS LYS GLU LEU ALA ALA GLN ILE ALA
SEQRES 2 B 95 GLU LYS PHE THR ASP VAL LEU SER LYS THR HIS ALA GLU
SEQRES 3 B 95 GLU ILE THR ASN PHE VAL PHE ASP HIS ILE LYS LYS ALA
SEQRES 4 B 95 LEU VAL ALA GLY LYS GLU VAL SER ILE ALA GLY PHE GLY
SEQRES 5 B 95 LYS PHE ALA VAL THR GLU ARG ALA ALA ARG ASP GLY ARG
SEQRES 6 B 95 ASN PRO SER THR GLY GLU THR ILE LYS ILE PRO ALA SER
SEQRES 7 B 95 LYS SER ALA LYS PHE LYS ALA GLY LYS GLN LEU LYS THR
SEQRES 8 B 95 ASP LEU ASN ASN
HELIX 1 AA1 SER A 2 PHE A 14 1 13
HELIX 2 AA2 SER A 19 VAL A 39 1 21
HELIX 3 AA3 LYS A 85 LYS A 88 5 4
HELIX 4 AA4 SER B 2 GLU B 12 1 11
HELIX 5 AA5 THR B 21 GLY B 41 1 21
SHEET 1 AA1 4 HIS A 0 MET A 1 0
SHEET 2 AA1 4 GLU B 43 ILE B 46 1 O SER B 45 N MET A 1
SHEET 3 AA1 4 GLY B 50 GLU B 56 -1 O GLY B 50 N ILE B 46
SHEET 4 AA1 4 LYS B 77 ALA B 83 -1 O LYS B 82 N LYS B 51
SHEET 1 AA2 4 SER A 76 ALA A 83 0
SHEET 2 AA2 4 GLY A 50 ARG A 57 -1 N ARG A 57 O SER A 76
SHEET 3 AA2 4 GLU A 43 ILE A 46 -1 N VAL A 44 O PHE A 52
SHEET 4 AA2 4 HIS B 0 MET B 1 1 O MET B 1 N SER A 45
SHEET 1 AA3 2 ARG A 60 ARG A 63 0
SHEET 2 AA3 2 THR A 70 ILE A 73 -1 O ILE A 73 N ARG A 60
SHEET 1 AA4 2 ARG B 60 ARG B 63 0
SHEET 2 AA4 2 THR B 70 ILE B 73 -1 O ILE B 71 N GLY B 62
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 2
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 0.011217 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011217 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011217 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END