HEADER HYDROLASE 10-JAN-12 4AEF
TITLE THE CRYSTAL STRUCTURE OF THERMOSTABLE AMYLASE FROM THE PYROCOCCUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEOPULLULANASE (ALPHA-AMYLASE II);
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: THERMOSTABLE AMYLASE;
COMPND 5 EC: 3.2.1.135;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;
SOURCE 3 ORGANISM_TAXID: 2261;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PETPFTA-6H;
SOURCE 9 OTHER_DETAILS: DSM3638
KEYWDS HYDROLASE, THERMOSTABILITY, HIGH TEMPERATURE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.-N.SONG,T.-Y.JUNG,S.-M.YOON,S.-J.YANG,K.-H.PARK,E.-J.WOO
REVDAT 3 20-DEC-23 4AEF 1 REMARK
REVDAT 2 16-JAN-13 4AEF 1 JRNL
REVDAT 1 31-OCT-12 4AEF 0
JRNL AUTH J.-T.PARK,H.-N.SONG,T.-Y.JUNG,M.H.LEE,S.G.PARK,E.-J.WOO,
JRNL AUTH 2 K.-H.PARK
JRNL TITL A NOVEL DOMAIN ARRANGEMENT IN A MONOMERIC
JRNL TITL 2 CYCLODEXTRIN-HYDROLYZING ENZYME FROM THE HYPERTHERMOPHILE
JRNL TITL 3 PYROCOCCUS FURIOSUS.
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1834 380 2013
JRNL REFN ISSN 0006-3002
JRNL PMID 22902546
JRNL DOI 10.1016/J.BBAPAP.2012.08.001
REMARK 2
REMARK 2 RESOLUTION. 2.34 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.34
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.43
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 80333.850
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 61332
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 SET) : 0.211
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3095
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.34
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.49
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 9038
REMARK 3 BIN R VALUE (WORKING SET) : 0.2340
REMARK 3 BIN FREE R VALUE : 0.2810
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 462
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.013
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10642
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 240
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.23000
REMARK 3 B22 (A**2) : -2.23000
REMARK 3 B33 (A**2) : 4.47000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.18
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.33
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.25
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.770
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.300 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.130 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.000 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.950 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 38.48
REMARK 3
REMARK 3 NCS MODEL : NONE
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 4AEF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1290050913.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61332
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.340
REMARK 200 RESOLUTION RANGE LOW (A) : 29.430
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.25000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.870
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1J0H
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2% POLYETHYLENE GLYCOL (PEG)400, 2M
REMARK 280 AMMONIUM SULFATE, 0.1M HEPES BUFFER PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.92800
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 16.96400
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 50.89200
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 GLY A 225
REMARK 465 ILE A 226
REMARK 465 ALA A 227
REMARK 465 TYR A 228
REMARK 465 PRO A 229
REMARK 465 LYS A 230
REMARK 465 ASP A 231
REMARK 465 LYS A 232
REMARK 465 TYR A 233
REMARK 465 GLY B 225
REMARK 465 ILE B 226
REMARK 465 ALA B 227
REMARK 465 TYR B 228
REMARK 465 PRO B 229
REMARK 465 LYS B 230
REMARK 465 ASP B 231
REMARK 465 LYS B 232
REMARK 465 TYR B 233
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 O LYS A 324 O GLU A 326 2.19
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 GLU A 49 CB - CA - C ANGL. DEV. = 21.0 DEGREES
REMARK 500 ASN A 327 CB - CA - C ANGL. DEV. = -12.9 DEGREES
REMARK 500 PRO A 340 N - CA - C ANGL. DEV. = -25.2 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 SER A 6 -175.67 -175.03
REMARK 500 ASN A 37 24.15 -142.70
REMARK 500 GLU A 49 -78.34 -90.48
REMARK 500 ARG A 84 147.02 -179.64
REMARK 500 HIS A 94 94.12 -162.89
REMARK 500 LEU A 108 -54.41 -153.58
REMARK 500 LEU A 118 86.55 -162.78
REMARK 500 ASP A 169 -154.91 -108.69
REMARK 500 LYS A 170 -97.57 -146.32
REMARK 500 ASP A 271 73.50 -119.19
REMARK 500 GLU A 326 -174.83 -67.82
REMARK 500 LYS A 344 101.76 -58.70
REMARK 500 GLU A 345 -32.34 63.03
REMARK 500 LYS A 353 46.58 -85.56
REMARK 500 SER A 354 -117.69 54.35
REMARK 500 SER A 355 -11.34 69.71
REMARK 500 GLU A 357 -11.72 82.80
REMARK 500 ASN A 369 40.35 -98.28
REMARK 500 PHE A 374 -132.85 49.26
REMARK 500 ASP A 440 -155.87 -138.58
REMARK 500 PHE A 447 -70.94 69.33
REMARK 500 LYS A 449 -100.16 -124.23
REMARK 500 ASN A 455 74.73 -67.99
REMARK 500 ARG A 552 45.70 -88.05
REMARK 500 LYS A 592 117.18 -166.12
REMARK 500 ARG A 595 -101.16 60.47
REMARK 500 MET A 605 52.23 36.42
REMARK 500 TYR A 615 45.06 -94.96
REMARK 500 TYR A 630 66.62 37.47
REMARK 500 LYS A 639 128.21 -174.11
REMARK 500 SER B 6 -177.01 -172.37
REMARK 500 GLU B 26 53.97 -155.15
REMARK 500 ASN B 37 22.48 -141.71
REMARK 500 ARG B 84 147.96 -171.66
REMARK 500 HIS B 94 93.03 -160.93
REMARK 500 LEU B 108 -47.19 -152.74
REMARK 500 HIS B 111 131.55 -171.48
REMARK 500 LEU B 118 86.01 -159.14
REMARK 500 ASP B 169 -156.79 -116.43
REMARK 500 LYS B 170 -87.78 -141.38
REMARK 500 PHE B 217 -70.19 -69.90
REMARK 500 ASP B 271 75.34 -115.04
REMARK 500 GLU B 326 -170.49 -66.30
REMARK 500 ASN B 327 -20.08 63.18
REMARK 500 SER B 329 2.56 -68.25
REMARK 500 ARG B 335 78.84 -110.21
REMARK 500 VAL B 341 -112.39 59.34
REMARK 500 GLU B 345 -4.82 74.28
REMARK 500 LYS B 353 47.96 -74.94
REMARK 500 SER B 354 -119.91 55.00
REMARK 500
REMARK 500 THIS ENTRY HAS 63 RAMACHANDRAN OUTLIERS.
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 TYR A 534 0.06 SIDE CHAIN
REMARK 500 TYR B 534 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4AEF A 1 645 UNP Q8TZP8 Q8TZP8_PYRFU 1 645
DBREF 4AEF B 1 645 UNP Q8TZP8 Q8TZP8_PYRFU 1 645
SEQRES 1 A 645 MET TYR LYS LEU VAL SER PHE ARG ASP SER GLU ILE PHE
SEQRES 2 A 645 GLY ARG VAL ALA GLU VAL GLU PHE SER LEU ILE ARG GLU
SEQRES 3 A 645 GLY SER TYR ALA TYR LEU LEU GLY ASP PHE ASN ALA PHE
SEQRES 4 A 645 ASN GLU GLY SER PHE ARG MET GLU GLN GLU GLY LYS ASN
SEQRES 5 A 645 TRP LYS ILE LYS ILE ALA LEU PRO GLU GLY VAL TRP HIS
SEQRES 6 A 645 TYR ALA PHE SER ILE ASP GLY LYS PHE VAL LEU ASP PRO
SEQRES 7 A 645 ASP ASN PRO GLU ARG ARG VAL TYR THR ARG LYS GLY TYR
SEQRES 8 A 645 LYS PHE HIS ARG GLU VAL ASN VAL ALA ARG ILE VAL LYS
SEQRES 9 A 645 SER ASP ASP LEU VAL PHE HIS THR PRO SER LEU LEU TYR
SEQRES 10 A 645 LEU TYR GLU ILE PHE GLY ARG VAL HIS VAL LEU LEU ARG
SEQRES 11 A 645 THR GLN LYS GLY VAL ILE LYS GLY ALA THR PHE LEU GLY
SEQRES 12 A 645 GLU LYS HIS VAL PRO MET ARG LYS LYS ALA SER ASP GLU
SEQRES 13 A 645 LEU PHE ASP TYR PHE GLU VAL ILE VAL GLU GLY GLY ASP
SEQRES 14 A 645 LYS ARG LEU ASN TYR SER PHE GLU VAL LEU THR MET GLU
SEQRES 15 A 645 GLY ALA LYS PHE GLU TYR GLY GLN PHE LYS ALA ARG PRO
SEQRES 16 A 645 PHE SER ILE GLU PHE PRO THR TRP VAL ILE ASP ARG VAL
SEQRES 17 A 645 PHE TYR GLN ILE MET PRO ASP LYS PHE ALA ARG SER ARG
SEQRES 18 A 645 LYS ILE GLN GLY ILE ALA TYR PRO LYS ASP LYS TYR TRP
SEQRES 19 A 645 GLY GLY ASP LEU ILE GLY ILE LYS GLU LYS ILE ASP HIS
SEQRES 20 A 645 LEU VAL ASN LEU GLY ILE ASN ALA ILE TYR LEU THR PRO
SEQRES 21 A 645 ILE PHE SER SER LEU THR TYR HIS GLY TYR ASP ILE VAL
SEQRES 22 A 645 ASP TYR PHE HIS VAL ALA ARG ARG LEU GLY GLY ASP ARG
SEQRES 23 A 645 ALA PHE VAL ASP LEU LEU SER GLU LEU LYS ARG PHE ASP
SEQRES 24 A 645 ILE LYS VAL ILE LEU ASP GLY VAL PHE HIS HIS THR SER
SEQRES 25 A 645 PHE PHE HIS PRO TYR PHE GLN ASP VAL VAL ARG LYS GLY
SEQRES 26 A 645 GLU ASN SER SER PHE LYS ASN PHE TYR ARG ILE ILE LYS
SEQRES 27 A 645 PHE PRO VAL VAL SER LYS GLU PHE LEU GLN ILE LEU HIS
SEQRES 28 A 645 SER LYS SER SER TRP GLU GLU LYS TYR LYS LYS ILE LYS
SEQRES 29 A 645 SER LEU GLY TRP ASN TYR GLU SER PHE PHE SER VAL TRP
SEQRES 30 A 645 ILE MET PRO ARG LEU ASN HIS ASP ASN PRO LYS VAL ARG
SEQRES 31 A 645 GLU PHE ILE LYS ASN VAL ILE LEU PHE TRP THR ASN LYS
SEQRES 32 A 645 GLY VAL ASP GLY PHE ARG MET ASP VAL ALA HIS GLY VAL
SEQRES 33 A 645 PRO PRO GLU VAL TRP LYS GLU VAL ARG GLU ALA LEU PRO
SEQRES 34 A 645 LYS GLU LYS TYR LEU ILE GLY GLU VAL MET ASP ASP ALA
SEQRES 35 A 645 ARG LEU TRP LEU PHE ASP LYS PHE HIS GLY VAL MET ASN
SEQRES 36 A 645 TYR ARG LEU TYR ASP ALA ILE LEU ARG PHE PHE GLY TYR
SEQRES 37 A 645 GLU GLU ILE THR ALA GLU GLU PHE LEU ASN GLU LEU GLU
SEQRES 38 A 645 LEU LEU SER SER TYR TYR GLY PRO ALA GLU TYR LEU MET
SEQRES 39 A 645 TYR ASN PHE LEU ASP ASN HIS ASP VAL GLU ARG PHE LEU
SEQRES 40 A 645 ASP ILE VAL GLY ASP LYS ARG LYS TYR VAL CYS ALA LEU
SEQRES 41 A 645 VAL PHE LEU MET THR TYR LYS GLY ILE PRO SER LEU PHE
SEQRES 42 A 645 TYR GLY ASP GLU ILE GLY LEU ARG GLY ILE ASN LEU GLN
SEQRES 43 A 645 GLY MET GLU SER SER ARG ALA PRO MET LEU TRP ASN GLU
SEQRES 44 A 645 GLU GLU TRP ASP GLN ARG ILE LEU GLU ILE THR LYS THR
SEQRES 45 A 645 LEU VAL LYS ILE ARG LYS ASN ASN LYS ALA LEU LEU PHE
SEQRES 46 A 645 GLY ASN PHE VAL PRO VAL LYS PHE LYS ARG LYS PHE MET
SEQRES 47 A 645 VAL TYR LYS ARG GLU HIS MET GLY GLU ARG THR ILE VAL
SEQRES 48 A 645 ALA ILE ASN TYR SER ASN SER ARG VAL LYS GLU LEU GLY
SEQRES 49 A 645 ILE THR ILE PRO GLU TYR SER GLY VAL ILE ILE ASN GLU
SEQRES 50 A 645 ASP LYS VAL LYS LEU ILE LYS TYR
SEQRES 1 B 645 MET TYR LYS LEU VAL SER PHE ARG ASP SER GLU ILE PHE
SEQRES 2 B 645 GLY ARG VAL ALA GLU VAL GLU PHE SER LEU ILE ARG GLU
SEQRES 3 B 645 GLY SER TYR ALA TYR LEU LEU GLY ASP PHE ASN ALA PHE
SEQRES 4 B 645 ASN GLU GLY SER PHE ARG MET GLU GLN GLU GLY LYS ASN
SEQRES 5 B 645 TRP LYS ILE LYS ILE ALA LEU PRO GLU GLY VAL TRP HIS
SEQRES 6 B 645 TYR ALA PHE SER ILE ASP GLY LYS PHE VAL LEU ASP PRO
SEQRES 7 B 645 ASP ASN PRO GLU ARG ARG VAL TYR THR ARG LYS GLY TYR
SEQRES 8 B 645 LYS PHE HIS ARG GLU VAL ASN VAL ALA ARG ILE VAL LYS
SEQRES 9 B 645 SER ASP ASP LEU VAL PHE HIS THR PRO SER LEU LEU TYR
SEQRES 10 B 645 LEU TYR GLU ILE PHE GLY ARG VAL HIS VAL LEU LEU ARG
SEQRES 11 B 645 THR GLN LYS GLY VAL ILE LYS GLY ALA THR PHE LEU GLY
SEQRES 12 B 645 GLU LYS HIS VAL PRO MET ARG LYS LYS ALA SER ASP GLU
SEQRES 13 B 645 LEU PHE ASP TYR PHE GLU VAL ILE VAL GLU GLY GLY ASP
SEQRES 14 B 645 LYS ARG LEU ASN TYR SER PHE GLU VAL LEU THR MET GLU
SEQRES 15 B 645 GLY ALA LYS PHE GLU TYR GLY GLN PHE LYS ALA ARG PRO
SEQRES 16 B 645 PHE SER ILE GLU PHE PRO THR TRP VAL ILE ASP ARG VAL
SEQRES 17 B 645 PHE TYR GLN ILE MET PRO ASP LYS PHE ALA ARG SER ARG
SEQRES 18 B 645 LYS ILE GLN GLY ILE ALA TYR PRO LYS ASP LYS TYR TRP
SEQRES 19 B 645 GLY GLY ASP LEU ILE GLY ILE LYS GLU LYS ILE ASP HIS
SEQRES 20 B 645 LEU VAL ASN LEU GLY ILE ASN ALA ILE TYR LEU THR PRO
SEQRES 21 B 645 ILE PHE SER SER LEU THR TYR HIS GLY TYR ASP ILE VAL
SEQRES 22 B 645 ASP TYR PHE HIS VAL ALA ARG ARG LEU GLY GLY ASP ARG
SEQRES 23 B 645 ALA PHE VAL ASP LEU LEU SER GLU LEU LYS ARG PHE ASP
SEQRES 24 B 645 ILE LYS VAL ILE LEU ASP GLY VAL PHE HIS HIS THR SER
SEQRES 25 B 645 PHE PHE HIS PRO TYR PHE GLN ASP VAL VAL ARG LYS GLY
SEQRES 26 B 645 GLU ASN SER SER PHE LYS ASN PHE TYR ARG ILE ILE LYS
SEQRES 27 B 645 PHE PRO VAL VAL SER LYS GLU PHE LEU GLN ILE LEU HIS
SEQRES 28 B 645 SER LYS SER SER TRP GLU GLU LYS TYR LYS LYS ILE LYS
SEQRES 29 B 645 SER LEU GLY TRP ASN TYR GLU SER PHE PHE SER VAL TRP
SEQRES 30 B 645 ILE MET PRO ARG LEU ASN HIS ASP ASN PRO LYS VAL ARG
SEQRES 31 B 645 GLU PHE ILE LYS ASN VAL ILE LEU PHE TRP THR ASN LYS
SEQRES 32 B 645 GLY VAL ASP GLY PHE ARG MET ASP VAL ALA HIS GLY VAL
SEQRES 33 B 645 PRO PRO GLU VAL TRP LYS GLU VAL ARG GLU ALA LEU PRO
SEQRES 34 B 645 LYS GLU LYS TYR LEU ILE GLY GLU VAL MET ASP ASP ALA
SEQRES 35 B 645 ARG LEU TRP LEU PHE ASP LYS PHE HIS GLY VAL MET ASN
SEQRES 36 B 645 TYR ARG LEU TYR ASP ALA ILE LEU ARG PHE PHE GLY TYR
SEQRES 37 B 645 GLU GLU ILE THR ALA GLU GLU PHE LEU ASN GLU LEU GLU
SEQRES 38 B 645 LEU LEU SER SER TYR TYR GLY PRO ALA GLU TYR LEU MET
SEQRES 39 B 645 TYR ASN PHE LEU ASP ASN HIS ASP VAL GLU ARG PHE LEU
SEQRES 40 B 645 ASP ILE VAL GLY ASP LYS ARG LYS TYR VAL CYS ALA LEU
SEQRES 41 B 645 VAL PHE LEU MET THR TYR LYS GLY ILE PRO SER LEU PHE
SEQRES 42 B 645 TYR GLY ASP GLU ILE GLY LEU ARG GLY ILE ASN LEU GLN
SEQRES 43 B 645 GLY MET GLU SER SER ARG ALA PRO MET LEU TRP ASN GLU
SEQRES 44 B 645 GLU GLU TRP ASP GLN ARG ILE LEU GLU ILE THR LYS THR
SEQRES 45 B 645 LEU VAL LYS ILE ARG LYS ASN ASN LYS ALA LEU LEU PHE
SEQRES 46 B 645 GLY ASN PHE VAL PRO VAL LYS PHE LYS ARG LYS PHE MET
SEQRES 47 B 645 VAL TYR LYS ARG GLU HIS MET GLY GLU ARG THR ILE VAL
SEQRES 48 B 645 ALA ILE ASN TYR SER ASN SER ARG VAL LYS GLU LEU GLY
SEQRES 49 B 645 ILE THR ILE PRO GLU TYR SER GLY VAL ILE ILE ASN GLU
SEQRES 50 B 645 ASP LYS VAL LYS LEU ILE LYS TYR
FORMUL 3 HOH *240(H2 O)
HELIX 1 1 LYS A 89 LYS A 92 5 4
HELIX 2 2 PRO A 201 ARG A 207 5 7
HELIX 3 3 MET A 213 ALA A 218 1 6
HELIX 4 4 ASP A 237 LYS A 244 1 8
HELIX 5 5 LYS A 244 GLY A 252 1 9
HELIX 6 6 ARG A 280 GLY A 283 5 4
HELIX 7 7 GLY A 284 PHE A 298 1 15
HELIX 8 8 HIS A 315 GLY A 325 1 11
HELIX 9 9 PHE A 330 PHE A 333 5 4
HELIX 10 10 GLU A 345 LYS A 353 1 9
HELIX 11 11 SER A 354 GLU A 358 5 5
HELIX 12 12 LYS A 359 GLY A 367 1 9
HELIX 13 13 ASN A 386 LYS A 403 1 18
HELIX 14 14 VAL A 412 VAL A 416 5 5
HELIX 15 15 PRO A 417 LEU A 428 1 12
HELIX 16 16 ALA A 442 LEU A 446 5 5
HELIX 17 17 ASN A 455 PHE A 466 1 12
HELIX 18 18 THR A 472 GLY A 488 1 17
HELIX 19 19 PRO A 489 MET A 494 5 6
HELIX 20 20 ARG A 505 GLY A 511 1 7
HELIX 21 21 ASP A 512 TYR A 526 1 15
HELIX 22 22 GLY A 535 GLY A 539 5 5
HELIX 23 23 ASN A 558 TRP A 562 5 5
HELIX 24 24 ASP A 563 ASN A 579 1 17
HELIX 25 25 ASN A 580 GLY A 586 1 7
HELIX 26 26 LYS B 89 LYS B 92 5 4
HELIX 27 27 PRO B 201 ILE B 205 5 5
HELIX 28 28 MET B 213 ALA B 218 1 6
HELIX 29 29 ASP B 237 LYS B 244 1 8
HELIX 30 30 LYS B 244 GLY B 252 1 9
HELIX 31 31 ARG B 280 GLY B 283 5 4
HELIX 32 32 GLY B 284 PHE B 298 1 15
HELIX 33 33 HIS B 315 GLY B 325 1 11
HELIX 34 34 PHE B 330 PHE B 333 5 4
HELIX 35 35 PHE B 346 HIS B 351 1 6
HELIX 36 36 SER B 354 GLU B 357 5 4
HELIX 37 37 GLU B 358 GLY B 367 1 10
HELIX 38 38 ASN B 386 LYS B 403 1 18
HELIX 39 39 VAL B 412 VAL B 416 5 5
HELIX 40 40 PRO B 417 LEU B 428 1 12
HELIX 41 41 ALA B 442 LEU B 446 5 5
HELIX 42 42 ASN B 455 PHE B 466 1 12
HELIX 43 43 THR B 472 GLY B 488 1 17
HELIX 44 44 PRO B 489 MET B 494 5 6
HELIX 45 45 ARG B 505 GLY B 511 1 7
HELIX 46 46 ASP B 512 TYR B 526 1 15
HELIX 47 47 GLY B 535 GLY B 539 5 5
HELIX 48 48 ASN B 558 TRP B 562 5 5
HELIX 49 49 ASP B 563 ASN B 579 1 17
HELIX 50 50 ASN B 580 GLY B 586 1 7
SHEET 1 AA 7 TYR A 2 SER A 10 0
SHEET 2 AA 7 GLY A 14 ILE A 24 -1 O GLY A 14 N SER A 10
SHEET 3 AA 7 ASN A 52 LEU A 59 -1 O TRP A 53 N LEU A 23
SHEET 4 AA 7 ARG A 45 GLN A 48 -1 O GLU A 47 N LYS A 54
SHEET 5 AA 7 ALA A 30 GLY A 34 -1 O ALA A 30 N MET A 46
SHEET 6 AA 7 GLY A 62 ILE A 70 -1 O ALA A 67 N LEU A 33
SHEET 7 AA 7 LYS A 73 VAL A 75 1 O LYS A 73 N ILE A 70
SHEET 1 AB 8 TYR A 2 SER A 10 0
SHEET 2 AB 8 GLY A 14 ILE A 24 -1 O GLY A 14 N SER A 10
SHEET 3 AB 8 ASN A 52 LEU A 59 -1 O TRP A 53 N LEU A 23
SHEET 4 AB 8 ARG A 45 GLN A 48 -1 O GLU A 47 N LYS A 54
SHEET 5 AB 8 ALA A 30 GLY A 34 -1 O ALA A 30 N MET A 46
SHEET 6 AB 8 GLY A 62 ILE A 70 -1 O ALA A 67 N LEU A 33
SHEET 7 AB 8 PHE A 93 ILE A 102 -1 O ASN A 98 N TYR A 66
SHEET 8 AB 8 ARG A 83 ARG A 88 -1 O ARG A 84 N VAL A 97
SHEET 1 AC 2 LYS A 73 VAL A 75 0
SHEET 2 AC 2 GLY A 62 ILE A 70 1 O PHE A 68 N VAL A 75
SHEET 1 AD 2 VAL A 109 PHE A 110 0
SHEET 2 AD 2 ARG A 124 GLN A 132 -1 O ARG A 130 N PHE A 110
SHEET 1 AE 2 LEU A 118 ILE A 121 0
SHEET 2 AE 2 ARG A 124 GLN A 132 -1 O ARG A 124 N ILE A 121
SHEET 1 AF 4 ARG A 150 SER A 154 0
SHEET 2 AF 4 PHE A 158 GLU A 166 -1 O TYR A 160 N LYS A 152
SHEET 3 AF 4 ARG A 124 GLN A 132 -1 O VAL A 125 N VAL A 165
SHEET 4 AF 4 LEU A 118 ILE A 121 -1 O TYR A 119 N HIS A 126
SHEET 1 AG 4 ARG A 150 SER A 154 0
SHEET 2 AG 4 PHE A 158 GLU A 166 -1 O TYR A 160 N LYS A 152
SHEET 3 AG 4 ARG A 124 GLN A 132 -1 O VAL A 125 N VAL A 165
SHEET 4 AG 4 VAL A 109 PHE A 110 -1 O PHE A 110 N ARG A 130
SHEET 1 AH 4 HIS A 146 PRO A 148 0
SHEET 2 AH 4 ILE A 136 LEU A 142 -1 O PHE A 141 N VAL A 147
SHEET 3 AH 4 LEU A 172 THR A 180 -1 O SER A 175 N LEU A 142
SHEET 4 AH 4 LYS A 185 ALA A 193 -1 O PHE A 186 N VAL A 178
SHEET 1 AI 7 GLY A 452 VAL A 453 0
SHEET 2 AI 7 TYR A 433 GLY A 436 1 N GLY A 436 O GLY A 452
SHEET 3 AI 7 GLY A 407 MET A 410 1 O PHE A 408 N ILE A 435
SHEET 4 AI 7 LYS A 301 GLY A 306 1 O LEU A 304 N ARG A 409
SHEET 5 AI 7 ALA A 255 LEU A 258 1 O ILE A 256 N ILE A 303
SHEET 6 AI 7 PHE A 209 ILE A 212 1 O TYR A 210 N TYR A 257
SHEET 7 AI 7 SER A 531 PHE A 533 1 O LEU A 532 N GLN A 211
SHEET 1 AJ 2 PHE A 262 SER A 264 0
SHEET 2 AJ 2 ILE A 272 VAL A 278 -1 N VAL A 273 O SER A 263
SHEET 1 AK 2 SER A 372 PHE A 373 0
SHEET 2 AK 2 VAL A 376 PRO A 380 -1 N VAL A 376 O PHE A 373
SHEET 1 AL 2 ILE A 543 LEU A 545 0
SHEET 2 AL 2 MET A 548 SER A 550 -1 O MET A 548 N LEU A 545
SHEET 1 AM 5 ASN A 587 LYS A 594 0
SHEET 2 AM 5 PHE A 597 HIS A 604 -1 O PHE A 597 N LYS A 594
SHEET 3 AM 5 GLU A 607 ASN A 614 -1 O GLU A 607 N HIS A 604
SHEET 4 AM 5 SER A 631 ASN A 636 -1 O SER A 631 N ASN A 614
SHEET 5 AM 5 LYS A 639 ILE A 643 -1 O LYS A 639 N ASN A 636
SHEET 1 AN 2 VAL A 620 GLU A 622 0
SHEET 2 AN 2 ILE A 625 ILE A 627 -1 O ILE A 625 N GLU A 622
SHEET 1 BA 7 TYR B 2 SER B 10 0
SHEET 2 BA 7 GLY B 14 ILE B 24 -1 O GLY B 14 N SER B 10
SHEET 3 BA 7 ASN B 52 LEU B 59 -1 O TRP B 53 N LEU B 23
SHEET 4 BA 7 ARG B 45 GLN B 48 -1 O GLU B 47 N LYS B 54
SHEET 5 BA 7 ALA B 30 GLY B 34 -1 O ALA B 30 N MET B 46
SHEET 6 BA 7 GLY B 62 ILE B 70 -1 O ALA B 67 N LEU B 33
SHEET 7 BA 7 LYS B 73 VAL B 75 1 O LYS B 73 N ILE B 70
SHEET 1 BB 8 TYR B 2 SER B 10 0
SHEET 2 BB 8 GLY B 14 ILE B 24 -1 O GLY B 14 N SER B 10
SHEET 3 BB 8 ASN B 52 LEU B 59 -1 O TRP B 53 N LEU B 23
SHEET 4 BB 8 ARG B 45 GLN B 48 -1 O GLU B 47 N LYS B 54
SHEET 5 BB 8 ALA B 30 GLY B 34 -1 O ALA B 30 N MET B 46
SHEET 6 BB 8 GLY B 62 ILE B 70 -1 O ALA B 67 N LEU B 33
SHEET 7 BB 8 PHE B 93 ILE B 102 -1 O ASN B 98 N TYR B 66
SHEET 8 BB 8 ARG B 83 ARG B 88 -1 O ARG B 84 N VAL B 97
SHEET 1 BC 2 LYS B 73 VAL B 75 0
SHEET 2 BC 2 GLY B 62 ILE B 70 1 O PHE B 68 N VAL B 75
SHEET 1 BD 2 VAL B 109 PHE B 110 0
SHEET 2 BD 2 ARG B 124 GLN B 132 -1 O ARG B 130 N PHE B 110
SHEET 1 BE 2 LEU B 118 ILE B 121 0
SHEET 2 BE 2 ARG B 124 GLN B 132 -1 O ARG B 124 N ILE B 121
SHEET 1 BF 4 ARG B 150 SER B 154 0
SHEET 2 BF 4 PHE B 158 GLU B 166 -1 O TYR B 160 N LYS B 152
SHEET 3 BF 4 ARG B 124 GLN B 132 -1 O VAL B 125 N VAL B 165
SHEET 4 BF 4 LEU B 118 ILE B 121 -1 O TYR B 119 N HIS B 126
SHEET 1 BG 4 ARG B 150 SER B 154 0
SHEET 2 BG 4 PHE B 158 GLU B 166 -1 O TYR B 160 N LYS B 152
SHEET 3 BG 4 ARG B 124 GLN B 132 -1 O VAL B 125 N VAL B 165
SHEET 4 BG 4 VAL B 109 PHE B 110 -1 O PHE B 110 N ARG B 130
SHEET 1 BH 4 HIS B 146 PRO B 148 0
SHEET 2 BH 4 ILE B 136 LEU B 142 -1 O PHE B 141 N VAL B 147
SHEET 3 BH 4 LEU B 172 THR B 180 -1 O SER B 175 N LEU B 142
SHEET 4 BH 4 LYS B 185 ALA B 193 -1 O PHE B 186 N VAL B 178
SHEET 1 BI 7 GLY B 452 VAL B 453 0
SHEET 2 BI 7 TYR B 433 GLY B 436 1 N GLY B 436 O GLY B 452
SHEET 3 BI 7 GLY B 407 MET B 410 1 O PHE B 408 N ILE B 435
SHEET 4 BI 7 LYS B 301 GLY B 306 1 O LEU B 304 N ARG B 409
SHEET 5 BI 7 ALA B 255 LEU B 258 1 O ILE B 256 N ILE B 303
SHEET 6 BI 7 PHE B 209 ILE B 212 1 O TYR B 210 N TYR B 257
SHEET 7 BI 7 SER B 531 PHE B 533 1 O LEU B 532 N GLN B 211
SHEET 1 BJ 2 PHE B 262 SER B 264 0
SHEET 2 BJ 2 ILE B 272 VAL B 278 -1 N VAL B 273 O SER B 263
SHEET 1 BK 2 ILE B 543 LEU B 545 0
SHEET 2 BK 2 MET B 548 SER B 550 -1 O MET B 548 N LEU B 545
SHEET 1 BL 5 ASN B 587 LYS B 594 0
SHEET 2 BL 5 PHE B 597 HIS B 604 -1 O PHE B 597 N LYS B 594
SHEET 3 BL 5 GLU B 607 ASN B 614 -1 O GLU B 607 N HIS B 604
SHEET 4 BL 5 SER B 631 ASN B 636 -1 O SER B 631 N ASN B 614
SHEET 5 BL 5 LYS B 639 ILE B 643 -1 O LYS B 639 N ASN B 636
SHEET 1 BM 2 VAL B 620 GLU B 622 0
SHEET 2 BM 2 ILE B 625 ILE B 627 -1 O ILE B 625 N GLU B 622
CRYST1 150.065 150.065 67.856 90.00 90.00 90.00 P 41 8
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 0.006664 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006664 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014737 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
