HEADER LIPID BINDING PROTEIN 03-SEP-14 4WBK
TITLE THE 1.37 ANGSTROM X-RAY STRUCTURE OF THE HUMAN HEART FATTY ACID-
TITLE 2 BINDING PROTEIN COMPLEXED WITH STEARIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FATTY ACID-BINDING PROTEIN, HEART;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FATTY ACID-BINDING PROTEIN 3,HEART-TYPE FATTY ACID-BINDING
COMPND 5 PROTEIN,H-FABP,MAMMARY-DERIVED GROWTH INHIBITOR,MDGI,MUSCLE FATTY
COMPND 6 ACID-BINDING PROTEIN,M-FABP;
COMPND 7 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: FABP3, FABP11, MDGI;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS LIPID-BINDING PROTEIN, LIPID BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.SUGIYAMA,S.MATSUOKA,E.MIZOHATA,D.MATSUOKA,S.MURAKAMI,T.INOUE,
AUTHOR 2 M.MURATA
REVDAT 3 20-MAR-24 4WBK 1 REMARK
REVDAT 2 29-JAN-20 4WBK 1 SOURCE JRNL REMARK
REVDAT 1 28-JAN-15 4WBK 0
JRNL AUTH D.MATSUOKA,S.SUGIYAMA,M.MURATA,S.MATSUOKA
JRNL TITL MOLECULAR DYNAMICS SIMULATIONS OF HEART-TYPE FATTY ACID
JRNL TITL 2 BINDING PROTEIN IN APO AND HOLO FORMS, AND HYDRATION
JRNL TITL 3 STRUCTURE ANALYSES IN THE BINDING CAVITY
JRNL REF J.PHYS.CHEM.B V. 119 114 2015
JRNL REFN ISSN 1089-5647
JRNL PMID 25489786
JRNL DOI 10.1021/JP510384F
REMARK 2
REMARK 2 RESOLUTION. 1.37 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.37
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.79
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 25382
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 + TEST SET) : 0.154
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.176
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1346
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.37
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.41
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1537
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.56
REMARK 3 BIN R VALUE (WORKING SET) : 0.2670
REMARK 3 BIN FREE R VALUE SET COUNT : 83
REMARK 3 BIN FREE R VALUE : 0.2990
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1044
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 191
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.18000
REMARK 3 B22 (A**2) : 1.10000
REMARK 3 B33 (A**2) : 0.08000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.055
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.056
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.041
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.059
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.964
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1129 ; 0.023 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1134 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1527 ; 2.107 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2627 ; 0.879 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 143 ; 6.504 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 42 ;43.869 ;25.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 215 ;14.251 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 4 ;15.887 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 184 ; 0.120 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1239 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 231 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 560 ; 1.186 ; 1.010
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 559 ; 1.177 ; 1.008
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 707 ; 1.776 ; 1.513
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 708 ; 1.774 ; 1.515
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 569 ; 2.658 ; 1.276
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 570 ; 2.656 ; 1.277
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 821 ; 3.852 ; 1.799
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 1344 ; 5.499 ; 9.939
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 1242 ; 5.080 ; 9.102
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4WBK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-SEP-14.
REMARK 100 THE DEPOSITION ID IS D_1000203536.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-APR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL38B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : FIXED EXIT DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26772
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.370
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.37
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.46900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL, 38% PEG3350, PH 8.0,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 27.32250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 16.81000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.40350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 16.81000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.32250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.40350
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: 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 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 ASP A 18 CB - CG - OD2 ANGL. DEV. = -6.5 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 PHE A 57 -70.30 -107.01
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 STE A 200
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4TJZ RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH CAPRIC ACID.
REMARK 900 RELATED ID: 4TKB RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH LEURIC ACID.
REMARK 900 RELATED ID: 4TKH RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH MYRISTIC ACID.
REMARK 900 RELATED ID: 4TKJ RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH PALMITIC ACID.
REMARK 900 RELATED ID: 3WVM RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH STEARIC ACID (0.88 ANGSTROM
REMARK 900 RESOLUTION).
REMARK 900 RELATED ID: 3WBG RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH 1-ANILINONAPHTALENE-8-SULPHONIC ACID
DBREF 4WBK A 0 132 UNP P05413 FABPH_HUMAN 1 133
SEQRES 1 A 133 MET VAL ASP ALA PHE LEU GLY THR TRP LYS LEU VAL ASP
SEQRES 2 A 133 SER LYS ASN PHE ASP ASP TYR MET LYS SER LEU GLY VAL
SEQRES 3 A 133 GLY PHE ALA THR ARG GLN VAL ALA SER MET THR LYS PRO
SEQRES 4 A 133 THR THR ILE ILE GLU LYS ASN GLY ASP ILE LEU THR LEU
SEQRES 5 A 133 LYS THR HIS SER THR PHE LYS ASN THR GLU ILE SER PHE
SEQRES 6 A 133 LYS LEU GLY VAL GLU PHE ASP GLU THR THR ALA ASP ASP
SEQRES 7 A 133 ARG LYS VAL LYS SER ILE VAL THR LEU ASP GLY GLY LYS
SEQRES 8 A 133 LEU VAL HIS LEU GLN LYS TRP ASP GLY GLN GLU THR THR
SEQRES 9 A 133 LEU VAL ARG GLU LEU ILE ASP GLY LYS LEU ILE LEU THR
SEQRES 10 A 133 LEU THR HIS GLY THR ALA VAL CYS THR ARG THR TYR GLU
SEQRES 11 A 133 LYS GLU ALA
HET STE A 200 20
HETNAM STE STEARIC ACID
FORMUL 2 STE C18 H36 O2
FORMUL 3 HOH *191(H2 O)
HELIX 1 AA1 VAL A 1 LEU A 5 5 5
HELIX 2 AA2 ASN A 15 LEU A 23 1 9
HELIX 3 AA3 GLY A 26 SER A 34 1 9
SHEET 1 AA110 THR A 60 LYS A 65 0
SHEET 2 AA110 ILE A 48 HIS A 54 -1 N LEU A 51 O ILE A 62
SHEET 3 AA110 THR A 39 ASN A 45 -1 N THR A 39 O HIS A 54
SHEET 4 AA110 GLY A 6 LYS A 14 -1 N TRP A 8 O THR A 40
SHEET 5 AA110 ALA A 122 LYS A 130 -1 O THR A 127 N VAL A 11
SHEET 6 AA110 LYS A 112 HIS A 119 -1 N LEU A 115 O ARG A 126
SHEET 7 AA110 GLN A 100 ILE A 109 -1 N VAL A 105 O THR A 116
SHEET 8 AA110 LYS A 90 TRP A 97 -1 N LEU A 91 O ARG A 106
SHEET 9 AA110 LYS A 79 ASP A 87 -1 N THR A 85 O VAL A 92
SHEET 10 AA110 PHE A 70 THR A 73 -1 N PHE A 70 O SER A 82
SITE 1 AC1 7 THR A 53 LYS A 58 LEU A 115 ARG A 126
SITE 2 AC1 7 TYR A 128 HOH A 444 HOH A 446
CRYST1 54.645 68.807 33.620 90.00 90.00 90.00 P 21 21 21 4
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 0.018300 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014533 0.000000 0.00000
SCALE3 0.000000 0.000000 0.029744 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
