HEADER CELL CYCLE 06-JUL-15 5CE4
TITLE HIGH RESOLUTION X-RAY AND NEUTRON DIFFRACTION STRUCTURE OF H-FABP
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;
COMPND 8 OTHER_DETAILS: H-FABP
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;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FABP LIPOCALIN, CELL CYCLE
EXPDTA X-RAY DIFFRACTION; NEUTRON DIFFRACTION
AUTHOR A.D.PODJARNY,E.I.HOWARD,M.P.BLAKELEY,B.GUILLOT
REVDAT 4 14-NOV-18 5CE4 1 REMARK
REVDAT 3 06-APR-16 5CE4 1 JRNL
REVDAT 2 16-MAR-16 5CE4 1
REVDAT 1 09-MAR-16 5CE4 0
JRNL AUTH E.I.HOWARD,B.GUILLOT,M.P.BLAKELEY,M.HAERTLEIN,M.MOULIN,
JRNL AUTH 2 A.MITSCHLER,A.COUSIDO-SIAH,F.FADEL,W.M.VALSECCHI,T.TOMIZAKI,
JRNL AUTH 3 T.PETROVA,J.CLAUDOT,A.PODJARNY
JRNL TITL HIGH-RESOLUTION NEUTRON AND X-RAY DIFFRACTION
JRNL TITL 2 ROOM-TEMPERATURE STUDIES OF AN H-FABP-OLEIC ACID COMPLEX:
JRNL TITL 3 STUDY OF THE INTERNAL WATER CLUSTER AND LIGAND BINDING BY A
JRNL TITL 4 TRANSFERRED MULTIPOLAR ELECTRON-DENSITY DISTRIBUTION.
JRNL REF IUCRJ V. 3 115 2016
JRNL REFN ESSN 2052-2525
JRNL PMID 27006775
JRNL DOI 10.1107/S2052252515024161
REMARK 2
REMARK 2 RESOLUTION. 0.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1796)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 0.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.11
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 73652
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.140
REMARK 3 R VALUE (WORKING SET) : 0.139
REMARK 3 FREE R VALUE : 0.159
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 3772
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 31.1257 - 2.9392 0.94 2827 163 0.1458 0.1832
REMARK 3 2 29.9340 - 2.7399 0.90 3297 184 0.1718 0.2231
REMARK 3 3 2.9392 - 2.3332 0.97 2778 145 0.1524 0.1773
REMARK 3 4 2.7399 - 2.1750 0.75 2645 121 0.2257 0.2551
REMARK 3 5 2.3332 - 2.0383 0.97 2772 137 0.1310 0.1234
REMARK 3 6 2.1750 - 1.9001 0.67 2342 121 0.2876 0.2937
REMARK 3 7 2.0383 - 1.8520 0.91 2587 127 0.1188 0.1257
REMARK 3 8 1.8520 - 1.7192 0.93 2573 166 0.1226 0.1258
REMARK 3 9 1.7192 - 1.6179 0.94 2650 138 0.1184 0.1429
REMARK 3 10 1.6179 - 1.5369 0.95 2658 150 0.1094 0.1239
REMARK 3 11 1.5369 - 1.4700 0.96 2660 142 0.1149 0.1378
REMARK 3 12 1.4700 - 1.4134 0.96 2658 130 0.1152 0.1376
REMARK 3 13 1.4134 - 1.3646 0.95 2649 145 0.1139 0.1257
REMARK 3 14 1.3646 - 1.3219 0.88 2421 138 0.1135 0.1286
REMARK 3 15 1.3219 - 1.2842 0.92 2536 153 0.1230 0.1409
REMARK 3 16 1.2842 - 1.2503 0.93 2570 135 0.1223 0.1383
REMARK 3 17 1.2503 - 1.2198 0.94 2627 150 0.1257 0.1399
REMARK 3 18 1.2198 - 1.1921 0.94 2575 123 0.1336 0.1518
REMARK 3 19 1.1921 - 1.1667 0.94 2600 141 0.1348 0.1523
REMARK 3 20 1.1667 - 1.1434 0.93 2561 152 0.1373 0.1583
REMARK 3 21 1.1434 - 1.1218 0.94 2585 128 0.1403 0.1635
REMARK 3 22 1.1218 - 1.1018 0.94 2589 139 0.1536 0.1919
REMARK 3 23 1.1018 - 1.0831 0.90 2468 119 0.1632 0.1754
REMARK 3 24 1.0831 - 1.0656 0.87 2423 132 0.1889 0.2266
REMARK 3 25 1.0656 - 1.0492 0.90 2464 138 0.2069 0.2048
REMARK 3 26 1.0492 - 1.0338 0.92 2548 137 0.2302 0.2503
REMARK 3 27 1.0338 - 1.0192 0.92 2517 135 0.2577 0.2832
REMARK 3 28 1.0192 - 1.0055 0.93 2534 139 0.2792 0.2644
REMARK 3 29 1.0055 - 0.9924 0.91 2495 156 0.3111 0.3285
REMARK 3 30 0.9924 - 0.9800 0.91 2555 114 0.3302 0.3753
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.910
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.049 2523
REMARK 3 ANGLE : 0.967 4110
REMARK 3 CHIRALITY : 0.088 173
REMARK 3 PLANARITY : 0.005 309
REMARK 3 DIHEDRAL : 12.348 608
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5CE4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000205174.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.7085
REMARK 200 MONOCHROMATOR : BARTELS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73795
REMARK 200 RESOLUTION RANGE HIGH (A) : 0.980
REMARK 200 RESOLUTION RANGE LOW (A) : 43.670
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.5
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.6
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 230
REMARK 230 EXPERIMENTAL DETAILS
REMARK 230 EXPERIMENT TYPE : NEUTRON DIFFRACTION
REMARK 230 DATE OF DATA COLLECTION : 01-SEP-12
REMARK 230 TEMPERATURE (KELVIN) : 293.0
REMARK 230 PH : 7.50
REMARK 230 NUMBER OF CRYSTALS USED : NULL
REMARK 230
REMARK 230 NEUTRON SOURCE : NUCLEAR REACTOR
REMARK 230 BEAMLINE : LADI III
REMARK 230 WAVELENGTH OR RANGE (A) : 3-4
REMARK 230 MONOCHROMATOR : NI/TI MULTILAYER FILTER
REMARK 230 OPTICS : LADI-III
REMARK 230
REMARK 230 DETECTOR TYPE : IMAGE PLATE
REMARK 230 DETECTOR MANUFACTURER : FUJI
REMARK 230 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 230 DATA SCALING SOFTWARE : HKL-2000
REMARK 230
REMARK 230 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 230 RESOLUTION RANGE HIGH (A) : NULL
REMARK 230 RESOLUTION RANGE LOW (A) : NULL
REMARK 230 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 230
REMARK 230 OVERALL.
REMARK 230 COMPLETENESS FOR RANGE (%) : NULL
REMARK 230 DATA REDUNDANCY : NULL
REMARK 230 R MERGE (I) : NULL
REMARK 230 R SYM (I) : NULL
REMARK 230 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 230
REMARK 230 IN THE HIGHEST RESOLUTION SHELL.
REMARK 230 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 230 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 230 COMPLETENESS FOR SHELL (%) : NULL
REMARK 230 DATA REDUNDANCY IN SHELL : NULL
REMARK 230 R MERGE FOR SHELL (I) : NULL
REMARK 230 R SYM FOR SHELL (I) : NULL
REMARK 230 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 230
REMARK 230 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 230 SOFTWARE USED : AMORE
REMARK 230 STARTING MODEL: NULL
REMARK 230
REMARK 230 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20MM TRIS 22% PEG 4000 HEAVY WATER, PH
REMARK 280 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
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 17.29400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.59250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.65350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 35.59250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 17.29400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.65350
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 KCAL/MOL
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 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 MET A 0
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 -62.13 -102.80
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 OLA A 201
DBREF 5CE4 A 0 131 UNP P05413 FABPH_HUMAN 1 132
SEQRES 1 A 132 MET VAL ASP ALA PHE LEU GLY THR TRP LYS LEU VAL ASP
SEQRES 2 A 132 SER LYS ASN PHE ASP ASP TYR MET LYS SER LEU GLY VAL
SEQRES 3 A 132 GLY PHE ALA THR ARG GLN VAL ALA SER MET THR LYS PRO
SEQRES 4 A 132 THR THR ILE ILE GLU LYS ASN GLY ASP ILE LEU THR LEU
SEQRES 5 A 132 LYS THR HIS SER THR PHE LYS ASN THR GLU ILE SER PHE
SEQRES 6 A 132 LYS LEU GLY VAL GLU PHE ASP GLU THR THR ALA ASP ASP
SEQRES 7 A 132 ARG LYS VAL LYS SER ILE VAL THR LEU ASP GLY GLY LYS
SEQRES 8 A 132 LEU VAL HIS LEU GLN LYS TRP ASP GLY GLN GLU THR THR
SEQRES 9 A 132 LEU VAL ARG GLU LEU ILE ASP GLY LYS LEU ILE LEU THR
SEQRES 10 A 132 LEU THR HIS GLY THR ALA VAL CYS THR ARG THR TYR GLU
SEQRES 11 A 132 LYS GLU
HET OLA A 201 53
HETNAM OLA OLEIC ACID
FORMUL 2 OLA C18 H34 O2
FORMUL 3 HOH *179(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 MET A 35 1 10
SHEET 1 AA110 THR A 60 PHE A 64 0
SHEET 2 AA110 ILE A 48 HIS A 54 -1 N LEU A 49 O PHE A 64
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 GLU A 107 O ILE A 114
SHEET 8 AA110 LYS A 90 TRP A 97 -1 N TRP A 97 O GLN A 100
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 323 HOH A 350
CRYST1 34.588 55.307 71.185 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 0.028912 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018081 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014048 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
