HEADER STRUCTURAL PROTEIN 22-APR-03 1UCU
TITLE R-TYPE STRAIGHT FLAGELLAR FILAMENT MADE OF FULL-LENGTH FLAGELLIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHASE 1 FLAGELLIN;
COMPND 3 CHAIN: A;
COMPND 4 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 3 ORGANISM_TAXID: 602;
SOURCE 4 STRAIN: SJW 1665
KEYWDS FLAGELLIN, FLAGELLAR FILAMENT, HELICAL RECONSTRUCTION, STRUCTURAL
KEYWDS 2 PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR K.YONEKURA,S.MAKI-YONEKURA,K.NAMBA
REVDAT 3 13-MAR-24 1UCU 1 HEADER REMARK
REVDAT 2 24-FEB-09 1UCU 1 VERSN
REVDAT 1 12-AUG-03 1UCU 0
JRNL AUTH K.YONEKURA,S.MAKI-YONEKURA,K.NAMBA
JRNL TITL COMPLETE ATOMIC MODEL OF THE BACTERIAL FLAGELLAR FILAMENT BY
JRNL TITL 2 ELECTRON CRYOMICROSCOPY
JRNL REF NATURE V. 424 643 2003
JRNL REFN ISSN 0028-0836
JRNL PMID 12904785
JRNL DOI 10.1038/NATURE01830
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.A.SAMATEY,K.IMADA,S.NAGASHIMA,F.VONDERVISZT,T.KUMASAKA,
REMARK 1 AUTH 2 M.YAMAMOTO,K.NAMBA
REMARK 1 TITL STRUCTURE OF THE BACTERIAL FLAGELLAR PROTOFILAMENT AND
REMARK 1 TITL 2 IMPLICATIONS FOR A SWITCH FOR SUPERCOILING
REMARK 1 REF NATURE V. 410 331 2001
REMARK 1 REFN ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. 4.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : X-PLOR
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : 1IO1
REMARK 3 REFINEMENT SPACE : RECIPROCAL
REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT
REMARK 3 REFINEMENT TARGET : AMPLITUDE-WEIGHTED PHASE RESIDUAL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : REFINEMENT PROTOCOL--POSITIONAL AND SIMULATED
REMARK 3 ANNEALING
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : 1.000
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 4.000
REMARK 3 NUMBER OF PARTICLES : 102
REMARK 3 CTF CORRECTION METHOD : NULL
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: R-TYPE STRAIGHT
REMARK 3 FLAGELLAR FILAMENT
REMARK 3
REMARK 3 OTHER DETAILS: THE ATOMIC MODEL OF A FLAGELLIN FRAGMENT F41 FROM
REMARK 3 SAMATEY ET AL (2001) NATURE 410 331-337 (PDB ENTRY 1IO1) WAS
REMARK 3 FITTED TO THE DENSITY MAP USING O. THEN, INITIAL MODEL OF FULL-
REMARK 3 LENGTH FLAGELLIN WAS BUILT BY TRACING MISSING TERMINAL CHAINS.
REMARK 3 THE MODEL WAS REFINED USING BOTH POSITIONAL AND SIMULATED
REMARK 3 ANNEALING REFINEMENTS, BY A MOLECULAR DYNAMICS REFINEMENT
REMARK 3 PROGRAM, FEX-PLOR, WHICH WE DEVELOPED BASED ON FX-PLOR FOR EM
REMARK 3 IMAGE ANALYSIS OF THE HELICAL ASSEMBLY. THE AMPLITUDE-WEIGHTED
REMARK 3 PHASE-RESIDUAL WAS IMPLEMENTED AS AN EFFECTIVE POTENTIAL ENERGY.
REMARK 3 THE LAYER-LINE AMPLITUDE DISTRIBUTIONS OF THE EM DATA WERE THEN
REMARK 3 SCALED TO THE STRUCTURE FACTORS CALCULATED FROM THE MODEL BASED
REMARK 3 ON THEIR RADIAL AMPLITUDE PROFILES OBTAINED BY AVERAGING THE
REMARK 3 AMPLITUDES WITHIN EACH RESOLUTION SHELL. THE DENSITY MAP WAS
REMARK 3 CALCULATED AGAIN, AND MODEL BUILDING AND REFINEMENT WERE
REMARK 3 ITERATED.
REMARK 4
REMARK 4 1UCU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.
REMARK 100 THE DEPOSITION ID IS D_1000005686.
REMARK 244
REMARK 244 OTHER_DETAILS:
REMARK 244 REPEAT DISTANCE (ANGSTROMS) : 1698.8
REMARK 244 BASIC HELIX INDEX (N10, L10) : ( 11, 4)
REMARK 244 (N01, L01) : ( -5, 31)
REMARK 244 SELECTION RULE : L = 66 N + 361 M
REMARK 244 MAXIMUM BESSEL ORDER : 170
REMARK 244 NUMBER OF LAYER-LINES : 298
REMARK 244 NUMBER OF FILAMENT IMAGES : 102
REMARK 244 NUMBER OF MOLECULAR IMAGES : 41,469
REMARK 244 EFFECTIVE RESOLUTION (ANGSTROMS) : 4.000 ALONG THE
REMARK 244 MERIDIAN
REMARK 244 EFFECTIVE RESOLUTION (ANGSTROMS) : 5.000 ALONG THE
REMARK 244 EQUATOR
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : HELICAL
REMARK 245 SPECIMEN TYPE : VITREOUS ICE (CRYO EM)
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : FILAMENT
REMARK 245 PARTICLE TYPE : HELICAL
REMARK 245 NAME OF SAMPLE : R-TYPE STRAIGHT FLAGELLAR
REMARK 245 FILAMENT
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.10
REMARK 245 SAMPLE SUPPORT DETAILS : QUANTIFOIL R1.2/1.3 (25 NM
REMARK 245 THICK)
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : 150MM NACL, 2MM MGCL2, 20MM
REMARK 245 TRIS-HCL, 2-5% GLYCEROL
REMARK 245 PH : 7.80
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : 4.00
REMARK 245 MICROSCOPE MODEL : JEOL 3000SFF
REMARK 245 DETECTOR TYPE : KODAK SO-163 FILM
REMARK 245 MINIMUM DEFOCUS (NM) : 1100.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 2200.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : 0.00
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : 0.00
REMARK 245 NOMINAL CS : 1.60
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 2000.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 50000
REMARK 245 CALIBRATED MAGNIFICATION : 47600
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
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 THR A 212 CB THR A 212 CG2 0.302
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 ASP A 42 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 THR A 54 CA - CB - CG2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 ASN A 66 CB - CG - OD1 ANGL. DEV. = -17.3 DEGREES
REMARK 500 ARG A 90 NE - CZ - NH2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG A 118 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 GLY A 211 N - CA - C ANGL. DEV. = -17.5 DEGREES
REMARK 500 TYR A 458 CB - CA - C ANGL. DEV. = 15.1 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 ASN A 38 37.86 -84.45
REMARK 500 ASP A 43 58.07 -68.35
REMARK 500 ALA A 99 -8.44 -57.15
REMARK 500 THR A 193 -160.01 -103.74
REMARK 500 LEU A 197 105.99 -56.33
REMARK 500 LYS A 251 2.67 -65.80
REMARK 500 THR A 252 -62.68 -106.39
REMARK 500 ASN A 285 -38.27 -34.78
REMARK 500 ALA A 286 -22.44 -30.23
REMARK 500 LYS A 348 107.17 72.42
REMARK 500 ALA A 351 -167.34 53.23
REMARK 500 ASP A 352 -47.07 167.23
REMARK 500 ASP A 353 44.66 -161.61
REMARK 500 THR A 355 160.78 87.11
REMARK 500 GLN A 393 78.22 -150.69
REMARK 500 PRO A 394 -135.95 -76.14
REMARK 500 ASP A 395 104.61 28.05
REMARK 500 GLU A 398 -168.43 -70.43
REMARK 500 GLN A 429 -71.51 -36.38
REMARK 500 SER A 456 170.07 170.57
REMARK 500 TYR A 458 -148.98 -156.50
REMARK 500 ALA A 459 -91.25 -36.96
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 ASN A 66 0.08 SIDE CHAIN
REMARK 500 ARG A 90 0.28 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED
DBREF 1UCU A 1 494 UNP P06179 FLIC_SALTY 1 494
SEQADV 1UCU VAL A 449 UNP P06179 ALA 449 SEE REMARK 999
SEQRES 1 A 494 ALA GLN VAL ILE ASN THR ASN SER LEU SER LEU LEU THR
SEQRES 2 A 494 GLN ASN ASN LEU ASN LYS SER GLN SER ALA LEU GLY THR
SEQRES 3 A 494 ALA ILE GLU ARG LEU SER SER GLY LEU ARG ILE ASN SER
SEQRES 4 A 494 ALA LYS ASP ASP ALA ALA GLY GLN ALA ILE ALA ASN ARG
SEQRES 5 A 494 PHE THR ALA ASN ILE LYS GLY LEU THR GLN ALA SER ARG
SEQRES 6 A 494 ASN ALA ASN ASP GLY ILE SER ILE ALA GLN THR THR GLU
SEQRES 7 A 494 GLY ALA LEU ASN GLU ILE ASN ASN ASN LEU GLN ARG VAL
SEQRES 8 A 494 ARG GLU LEU ALA VAL GLN SER ALA ASN SER THR ASN SER
SEQRES 9 A 494 GLN SER ASP LEU ASP SER ILE GLN ALA GLU ILE THR GLN
SEQRES 10 A 494 ARG LEU ASN GLU ILE ASP ARG VAL SER GLY GLN THR GLN
SEQRES 11 A 494 PHE ASN GLY VAL LYS VAL LEU ALA GLN ASP ASN THR LEU
SEQRES 12 A 494 THR ILE GLN VAL GLY ALA ASN ASP GLY GLU THR ILE ASP
SEQRES 13 A 494 ILE ASP LEU LYS GLN ILE ASN SER GLN THR LEU GLY LEU
SEQRES 14 A 494 ASP THR LEU ASN VAL GLN GLN LYS TYR LYS VAL SER ASP
SEQRES 15 A 494 THR ALA ALA THR VAL THR GLY TYR ALA ASP THR THR ILE
SEQRES 16 A 494 ALA LEU ASP ASN SER THR PHE LYS ALA SER ALA THR GLY
SEQRES 17 A 494 LEU GLY GLY THR ASP GLN LYS ILE ASP GLY ASP LEU LYS
SEQRES 18 A 494 PHE ASP ASP THR THR GLY LYS TYR TYR ALA LYS VAL THR
SEQRES 19 A 494 VAL THR GLY GLY THR GLY LYS ASP GLY TYR TYR GLU VAL
SEQRES 20 A 494 SER VAL ASP LYS THR ASN GLY GLU VAL THR LEU ALA GLY
SEQRES 21 A 494 GLY ALA THR SER PRO LEU THR GLY GLY LEU PRO ALA THR
SEQRES 22 A 494 ALA THR GLU ASP VAL LYS ASN VAL GLN VAL ALA ASN ALA
SEQRES 23 A 494 ASP LEU THR GLU ALA LYS ALA ALA LEU THR ALA ALA GLY
SEQRES 24 A 494 VAL THR GLY THR ALA SER VAL VAL LYS MET SER TYR THR
SEQRES 25 A 494 ASP ASN ASN GLY LYS THR ILE ASP GLY GLY LEU ALA VAL
SEQRES 26 A 494 LYS VAL GLY ASP ASP TYR TYR SER ALA THR GLN ASN LYS
SEQRES 27 A 494 ASP GLY SER ILE SER ILE ASN THR THR LYS TYR THR ALA
SEQRES 28 A 494 ASP ASP GLY THR SER LYS THR ALA LEU ASN LYS LEU GLY
SEQRES 29 A 494 GLY ALA ASP GLY LYS THR GLU VAL VAL SER ILE GLY GLY
SEQRES 30 A 494 LYS THR TYR ALA ALA SER LYS ALA GLU GLY HIS ASN PHE
SEQRES 31 A 494 LYS ALA GLN PRO ASP LEU ALA GLU ALA ALA ALA THR THR
SEQRES 32 A 494 THR GLU ASN PRO LEU GLN LYS ILE ASP ALA ALA LEU ALA
SEQRES 33 A 494 GLN VAL ASP THR LEU ARG SER ASP LEU GLY ALA VAL GLN
SEQRES 34 A 494 ASN ARG PHE ASN SER ALA ILE THR ASN LEU GLY ASN THR
SEQRES 35 A 494 VAL ASN ASN LEU THR SER VAL ARG SER ARG ILE GLU ASP
SEQRES 36 A 494 SER ASP TYR ALA THR GLU VAL SER ASN MET SER ARG ALA
SEQRES 37 A 494 GLN ILE LEU GLN GLN ALA GLY THR SER VAL LEU ALA GLN
SEQRES 38 A 494 ALA ASN GLN VAL PRO GLN ASN VAL LEU SER LEU LEU ARG
HELIX 1 1 GLN A 2 SER A 32 1 31
HELIX 2 2 ALA A 44 ALA A 99 1 56
HELIX 3 3 SER A 104 THR A 129 1 26
HELIX 4 4 ASN A 199 PHE A 202 5 4
HELIX 5 5 ALA A 206 GLY A 210 5 5
HELIX 6 6 LEU A 288 ALA A 298 1 11
HELIX 7 7 ALA A 382 GLU A 386 1 5
HELIX 8 8 ASN A 406 GLU A 454 1 49
HELIX 9 9 ALA A 459 SER A 491 1 33
SHEET 1 A 2 ASN A 141 GLN A 146 0
SHEET 2 A 2 THR A 154 LEU A 159 -1 O ILE A 155 N ILE A 145
SHEET 1 B 5 LYS A 179 ALA A 184 0
SHEET 2 B 5 ALA A 304 THR A 312 -1 N LYS A 308 O THR A 183
SHEET 3 B 5 THR A 318 VAL A 327 -1 O ILE A 319 N TYR A 311
SHEET 4 B 5 ASP A 330 GLN A 336 -1 O ASP A 330 N VAL A 327
SHEET 5 B 5 ILE A 342 ILE A 344 -1 N SER A 343 O THR A 335
SHEET 1 C 2 TYR A 190 ALA A 196 0
SHEET 2 C 2 ASN A 280 ALA A 284 -1 N VAL A 281 O ILE A 195
SHEET 1 D 4 VAL A 256 LEU A 258 0
SHEET 2 D 4 GLY A 243 VAL A 249 -1 N SER A 248 O THR A 257
SHEET 3 D 4 TYR A 229 THR A 236 -1 O TYR A 229 N VAL A 247
SHEET 4 D 4 ASP A 213 ILE A 216 -1 O ASP A 213 N THR A 236
SHEET 1 E 5 VAL A 256 LEU A 258 0
SHEET 2 E 5 GLY A 243 VAL A 249 -1 N SER A 248 O THR A 257
SHEET 3 E 5 TYR A 229 THR A 236 -1 O TYR A 229 N VAL A 247
SHEET 4 E 5 LEU A 220 PHE A 222 -1 O LYS A 221 N TYR A 230
SHEET 5 E 5 GLU A 276 VAL A 278 -1 O GLU A 276 N PHE A 222
SHEET 1 F 3 ASN A 361 GLY A 364 0
SHEET 2 F 3 THR A 370 ILE A 375 -1 O THR A 370 N GLY A 364
SHEET 3 F 3 LYS A 378 ALA A 381 -1 N LYS A 378 O ILE A 375
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
(ATOM LINES ARE NOT SHOWN.)
END