HEADER LIPID BINDING PROTEIN 17-NOV-10 2L68
TITLE SOLUTION STRUCTURE OF HUMAN HOLO L-FABP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FATTY ACID-BINDING PROTEIN, LIVER;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FATTY ACID-BINDING PROTEIN 1, LIVER-TYPE FATTY ACID-BINDING
COMPND 5 PROTEIN, L-FABP;
COMPND 6 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: FABP1, FABPL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: MG1655;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PMON
KEYWDS LIPID BINDING PROTEIN, FATTY ACID CARRIER, HOLO FORM
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.CAI,C.LUECKE,Z.CHEN,Y.QIAO,E.S.KLIMTCHUK,J.A.HAMILTON
REVDAT 3 20-FEB-13 2L68 1 JRNL
REVDAT 2 13-JUN-12 2L68 1 JRNL
REVDAT 1 23-NOV-11 2L68 0
JRNL AUTH J.CAI,C.LUCKE,Z.CHEN,Y.QIAO,E.KLIMTCHUK,J.A.HAMILTON
JRNL TITL SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF HUMAN LIVER
JRNL TITL 2 FATTY ACID BINDING PROTEIN: FATTY ACID BINDING REVISITED.
JRNL REF BIOPHYS.J. V. 102 2585 2012
JRNL REFN ISSN 0006-3495
JRNL PMID 22713574
JRNL DOI 10.1016/J.BPJ.2012.04.039
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISCOVER 2000
REMARK 3 AUTHORS : ACCELRYS SOFTWARE INC.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2L68 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-NOV-10.
REMARK 100 THE RCSB ID CODE IS RCSB102008.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 150
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 20 MM POTASSIUM PHOSPHATE, 150
REMARK 210 MM SODIUM CHLORIDE, 0.05 % SODIUM
REMARK 210 AZIDE, 3 MM HUMAN LIVER FATTY
REMARK 210 ACID BINDING PROTEIN, 15 MM [U-
REMARK 210 13C] POTASSIUM OLEATE, 95% H2O/5%
REMARK 210 D2O; 20 MM POTASSIUM PHOSPHATE,
REMARK 210 150 MM SODIUM CHLORIDE, 0.05 %
REMARK 210 SODIUM AZIDE, 2 MM [U-15N] HUMAN
REMARK 210 LIVER FATTY ACID BINDING PROTEIN,
REMARK 210 10 MM POTASSIUM OLEATE, 95% H2O/
REMARK 210 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-1H TOCSY;
REMARK 210 2D 1H-1H NOESY; 3D 1H-15N NOESY;
REMARK 210 3D 1H-15N TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA 2.1, NMRVIEW 8.0, XWINNMR
REMARK 210 3.5, TOPSPIN 1.3
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: 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 6 HIS A 47 CG HIS A 47 CD2 0.059
REMARK 500 9 HIS A 47 CG HIS A 47 CD2 0.054
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 HIS A 47 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 1 ARG A 122 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 2 HIS A 47 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 2 ARG A 122 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 3 HIS A 47 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 3 ARG A 122 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 3 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 4 HIS A 47 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 4 ARG A 122 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 4 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 5 HIS A 47 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 5 ARG A 122 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 5 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 6 HIS A 47 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 6 ARG A 122 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 6 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 7 HIS A 47 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 7 ARG A 122 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 7 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 8 HIS A 47 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 8 ARG A 122 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 8 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 9 HIS A 47 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 9 ARG A 122 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 9 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 10 HIS A 47 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 10 ARG A 122 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 10 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 11 HIS A 47 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 11 ARG A 122 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 11 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 12 HIS A 47 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 12 ARG A 122 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 12 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 13 HIS A 47 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 13 ARG A 122 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 13 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 14 HIS A 47 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 14 ARG A 122 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 14 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 15 HIS A 47 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 15 ARG A 122 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 15 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 16 HIS A 47 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 16 ARG A 122 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 16 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 17 HIS A 47 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 17 ARG A 122 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 60 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 GLN A 10 -65.53 -109.37
REMARK 500 1 GLU A 13 -70.44 -79.51
REMARK 500 1 GLU A 77 -46.07 -166.88
REMARK 500 1 ASN A 89 -44.64 -157.48
REMARK 500 1 PHE A 95 -101.05 -91.30
REMARK 500 1 LYS A 96 78.12 -110.39
REMARK 500 1 ASP A 107 52.63 -118.86
REMARK 500 2 GLN A 10 -64.80 -121.57
REMARK 500 2 GLU A 13 -70.18 -88.52
REMARK 500 2 ASN A 14 68.66 -114.63
REMARK 500 2 THR A 75 -71.39 -164.22
REMARK 500 2 ASN A 89 -43.34 -155.60
REMARK 500 2 PHE A 95 -85.05 -84.64
REMARK 500 2 LYS A 96 -75.28 -121.74
REMARK 500 3 MET A 74 -100.27 68.74
REMARK 500 3 ASN A 89 -38.79 -158.65
REMARK 500 3 THR A 94 -78.42 -80.47
REMARK 500 3 PHE A 95 171.38 65.00
REMARK 500 4 PHE A 3 -35.40 80.39
REMARK 500 4 GLN A 10 -58.22 -126.33
REMARK 500 4 ASN A 89 -32.00 -158.49
REMARK 500 4 PHE A 95 37.43 -83.38
REMARK 500 4 LYS A 96 -81.04 69.99
REMARK 500 4 ASP A 107 50.39 -114.47
REMARK 500 4 LEU A 115 75.43 -117.87
REMARK 500 5 GLN A 10 -65.24 -98.60
REMARK 500 5 LYS A 80 86.32 64.36
REMARK 500 5 VAL A 83 127.24 80.25
REMARK 500 5 ASN A 89 -39.29 -151.51
REMARK 500 5 PHE A 95 -70.74 -84.18
REMARK 500 5 LYS A 96 -77.30 -120.70
REMARK 500 5 ILE A 108 -164.64 -123.62
REMARK 500 6 PHE A 3 -152.52 -87.45
REMARK 500 6 SER A 4 88.19 62.00
REMARK 500 6 LYS A 57 100.18 -163.99
REMARK 500 6 MET A 74 -72.80 -118.10
REMARK 500 6 ASN A 89 -43.55 -158.63
REMARK 500 6 PHE A 95 -76.82 -70.03
REMARK 500 6 LYS A 96 -72.58 -120.97
REMARK 500 6 ILE A 108 -165.44 -126.77
REMARK 500 7 GLN A 10 -64.68 -104.88
REMARK 500 7 THR A 75 -76.71 -151.00
REMARK 500 7 ASN A 89 -18.47 -160.84
REMARK 500 7 PHE A 95 -116.40 -136.03
REMARK 500 7 ASN A 105 -99.77 -94.33
REMARK 500 7 ASP A 107 49.26 -96.39
REMARK 500 8 GLN A 10 -60.63 -100.19
REMARK 500 8 GLU A 77 139.91 76.31
REMARK 500 8 LYS A 80 112.40 76.85
REMARK 500 8 ASP A 88 -10.38 71.92
REMARK 500
REMARK 500 THIS ENTRY HAS 141 RAMACHANDRAN OUTLIERS.
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 4 PHE A 3 23.4 L L OUTSIDE RANGE
REMARK 500 10 PHE A 3 23.6 L L OUTSIDE RANGE
REMARK 500 18 PHE A 3 23.2 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 15429 RELATED DB: BMRB
REMARK 900 RAT APO L-FABP ASSIGNMENT
REMARK 900 RELATED ID: 15433 RELATED DB: BMRB
REMARK 900 RAT HOLO L-FABP ASSIGNMENT
REMARK 900 RELATED ID: 1LFO RELATED DB: PDB
REMARK 900 RAT HOLO L-FABP X-RAY STRUCTURE
REMARK 900 RELATED ID: 2JU3 RELATED DB: PDB
REMARK 900 RAT APO L-FABP SOLUTION STRUCTURE
REMARK 900 RELATED ID: 2JU7 RELATED DB: PDB
REMARK 900 RAT HOLO L-FABP SOLUTION STRUCTURE
REMARK 900 RELATED ID: 2F73 RELATED DB: PDB
REMARK 900 HUMAN L-FABP X-RAY STRUCTURE
REMARK 900 RELATED ID: 2PY1 RELATED DB: PDB
REMARK 900 HUMAN L-FABP SOLUTION STRUCTURE
REMARK 900 RELATED ID: 17303 RELATED DB: BMRB
DBREF 2L68 A 2 127 UNP P07148 FABPL_HUMAN 2 127
SEQRES 1 A 126 SER PHE SER GLY LYS TYR GLN LEU GLN SER GLN GLU ASN
SEQRES 2 A 126 PHE GLU ALA PHE MET LYS ALA ILE GLY LEU PRO GLU GLU
SEQRES 3 A 126 LEU ILE GLN LYS GLY LYS ASP ILE LYS GLY VAL SER GLU
SEQRES 4 A 126 ILE VAL GLN ASN GLY LYS HIS PHE LYS PHE THR ILE THR
SEQRES 5 A 126 ALA GLY SER LYS VAL ILE GLN ASN GLU PHE THR VAL GLY
SEQRES 6 A 126 GLU GLU CYS GLU LEU GLU THR MET THR GLY GLU LYS VAL
SEQRES 7 A 126 LYS THR VAL VAL GLN LEU GLU GLY ASP ASN LYS LEU VAL
SEQRES 8 A 126 THR THR PHE LYS ASN ILE LYS SER VAL THR GLU LEU ASN
SEQRES 9 A 126 GLY ASP ILE ILE THR ASN THR MET THR LEU GLY ASP ILE
SEQRES 10 A 126 VAL PHE LYS ARG ILE SER LYS ARG ILE
HELIX 1 1 PHE A 15 ILE A 22 1 8
HELIX 2 2 GLU A 26 ASP A 34 1 9
SHEET 1 A 9 LYS A 57 THR A 64 0
SHEET 2 A 9 HIS A 47 ALA A 54 -1 N ILE A 52 O ILE A 59
SHEET 3 A 9 VAL A 38 ASN A 44 -1 N GLU A 40 O THR A 51
SHEET 4 A 9 GLY A 5 GLU A 13 -1 N TYR A 7 O SER A 39
SHEET 5 A 9 ILE A 118 ARG A 126 -1 O ILE A 123 N GLN A 10
SHEET 6 A 9 THR A 110 LEU A 115 -1 N MET A 113 O PHE A 120
SHEET 7 A 9 LYS A 99 GLU A 103 -1 N GLU A 103 O THR A 110
SHEET 8 A 9 LYS A 90 THR A 94 -1 N THR A 93 O SER A 100
SHEET 9 A 9 GLN A 84 GLU A 86 -1 N GLU A 86 O LYS A 90
SHEET 1 B 2 GLU A 68 GLU A 72 0
SHEET 2 B 2 VAL A 79 VAL A 82 -1 O VAL A 79 N LEU A 71
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
