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HEADER HYDROLASE 23-JUN-00 1F6W
TITLE STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT
TITLE 2 ACTIVATED LIPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BILE SALT ACTIVATED LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 TISSUE: PANCREAS;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS BILE SALT ACTIVATED LIPASE, ESTERASE, CATALYTIC DOMAIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.TERZYAN,X.ZHANG
REVDAT 1 18-OCT-00 1F6W 0
JRNL AUTH S.TERZYAN,C.-S.WANG,D.DOWNS,B.HUNTER,X.ZHANG
JRNL TITL CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN
JRNL TITL 2 BILE SALT ACTIVATED LIPASE
JRNL REF PROTEIN SCI. V. 9 1783 2000
JRNL REFN ASTM PRCIEI US ISSN 0961-8368
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 85.6
REMARK 3 NUMBER OF REFLECTIONS : 23474
REMARK 3
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) : 0.212
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1171
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 75.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3232
REMARK 3 BIN R VALUE (WORKING SET) : 0.3600
REMARK 3 BIN FREE R VALUE : 0.4100
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 160
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.032
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4151
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 163
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.57000
REMARK 3 B22 (A**2) : -17.67000
REMARK 3 B33 (A**2) : 20.24000
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) : 0.32
REMARK 3 ESD FROM SIGMAA (A) : 0.420
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) : 0.40
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.49
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.60
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.02
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) : 1.89 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.12 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.45 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.51 ; 2.500
REMARK 3
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.28
REMARK 3 BSOL : 31.29
REMARK 3
REMARK 3 NCS MODEL : NULL
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 2 : WATER_REP.PARAM
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 1F6W COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUN-2000.
REMARK 100 THE RCSB ID CODE IS RCSB011317.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-OCT-1999
REMARK 200 TEMPERATURE (KELVIN) : 93.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRANDEIS Q4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25287
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.2
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.44300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1AKN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.0
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, NACL, N-(2-
REMARK 280 ACETAMIDO) IMINODIACETIC ACID
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 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-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 32.35000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.15000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.48500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.15000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.35000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.48500
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 THR A 140 N - CA - C ANGL. DEV. =-10.8 DEGREES
REMARK 500 LEU A 277 N - CA - C ANGL. DEV. = 10.6 DEGREES
REMARK 500 TYR A 284 N - CA - C ANGL. DEV. = 9.7 DEGREES
REMARK 500 ILE A 296 N - CA - C ANGL. DEV. =-11.3 DEGREES
REMARK 500 LYS A 409 N - CA - C ANGL. DEV. =-13.8 DEGREES
REMARK 500 LEU A 417 N - CA - C ANGL. DEV. =-10.0 DEGREES
REMARK 500 ASN A 470 N - CA - C ANGL. DEV. = -9.9 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 SER A 194 56.19 -115.84
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 0 HOH 74 DISTANCE = 6.18 ANGSTROMS
REMARK 525 0 HOH 136 DISTANCE = 5.55 ANGSTROMS
REMARK 525 0 HOH 165 DISTANCE = 7.21 ANGSTROMS
REMARK 525 0 HOH 168 DISTANCE = 6.16 ANGSTROMS
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: 1AKN RELATED DB: PDB
REMARK 900 1AKN CONTAINS THE STRUCTURE OF BOVINE BILE SALT ACTIVATED
REMARK 900 LIPASE
DBREF 1F6W A 1 533 SWS P19835 BAL_HUMAN 21 553
SEQADV 1F6W ASP A 186 SWS P19835 ASN 206 ENGINEERED
SEQADV 1F6W ASP A 298 SWS P19835 ALA 318 ENGINEERED
SEQRES 1 A 533 ALA LYS LEU GLY ALA VAL TYR THR GLU GLY GLY PHE VAL
SEQRES 2 A 533 GLU GLY VAL ASN LYS LYS LEU GLY LEU LEU GLY ASP SER
SEQRES 3 A 533 VAL ASP ILE PHE LYS GLY ILE PRO PHE ALA ALA PRO THR
SEQRES 4 A 533 LYS ALA LEU GLU ASN PRO GLN PRO HIS PRO GLY TRP GLN
SEQRES 5 A 533 GLY THR LEU LYS ALA LYS ASN PHE LYS LYS ARG CYS LEU
SEQRES 6 A 533 GLN ALA THR ILE THR GLN ASP SER THR TYR GLY ASP GLU
SEQRES 7 A 533 ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO GLN GLY ARG
SEQRES 8 A 533 LYS GLN VAL SER ARG ASP LEU PRO VAL MET ILE TRP ILE
SEQRES 9 A 533 TYR GLY GLY ALA PHE LEU MET GLY SER GLY HIS GLY ALA
SEQRES 10 A 533 ASN PHE LEU ASN ASN TYR LEU TYR ASP GLY GLU GLU ILE
SEQRES 11 A 533 ALA THR ARG GLY ASN VAL ILE VAL VAL THR PHE ASN TYR
SEQRES 12 A 533 ARG VAL GLY PRO LEU GLY PHE LEU SER THR GLY ASP ALA
SEQRES 13 A 533 ASN LEU PRO GLY ASN TYR GLY LEU ARG ASP GLN HIS MET
SEQRES 14 A 533 ALA ILE ALA TRP VAL LYS ARG ASN ILE ALA ALA PHE GLY
SEQRES 15 A 533 GLY ASP PRO ASP ASN ILE THR LEU PHE GLY GLU SER ALA
SEQRES 16 A 533 GLY GLY ALA SER VAL SER LEU GLN THR LEU SER PRO TYR
SEQRES 17 A 533 ASN LYS GLY LEU ILE ARG ARG ALA ILE SER GLN SER GLY
SEQRES 18 A 533 VAL ALA LEU SER PRO TRP VAL ILE GLN LYS ASN PRO LEU
SEQRES 19 A 533 PHE TRP ALA LYS LYS VAL ALA GLU LYS VAL GLY CYS PRO
SEQRES 20 A 533 VAL GLY ASP ALA ALA ARG MET ALA GLN CYS LEU LYS VAL
SEQRES 21 A 533 THR ASP PRO ARG ALA LEU THR LEU ALA TYR LYS VAL PRO
SEQRES 22 A 533 LEU ALA GLY LEU GLU TYR PRO MET LEU HIS TYR VAL GLY
SEQRES 23 A 533 PHE VAL PRO VAL ILE ASP GLY ASP PHE ILE PRO ASP ASP
SEQRES 24 A 533 PRO ILE ASN LEU TYR ALA ASN ALA ALA ASP ILE ASP TYR
SEQRES 25 A 533 ILE ALA GLY THR ASN ASN MET ASP GLY HIS ILE PHE ALA
SEQRES 26 A 533 SER ILE ASP MET PRO ALA ILE ASN LYS GLY ASN LYS LYS
SEQRES 27 A 533 VAL THR GLU GLU ASP PHE TYR LYS LEU VAL SER GLU PHE
SEQRES 28 A 533 THR ILE THR LYS GLY LEU ARG GLY ALA LYS THR THR PHE
SEQRES 29 A 533 ASP VAL TYR THR GLU SER TRP ALA GLN ASP PRO SER GLN
SEQRES 30 A 533 GLU ASN LYS LYS LYS THR VAL VAL ASP PHE GLU THR ASP
SEQRES 31 A 533 VAL LEU PHE LEU VAL PRO THR GLU ILE ALA LEU ALA GLN
SEQRES 32 A 533 HIS ARG ALA ASN ALA LYS SER ALA LYS THR TYR ALA TYR
SEQRES 33 A 533 LEU PHE SER HIS PRO SER ARG MET PRO VAL TYR PRO LYS
SEQRES 34 A 533 TRP VAL GLY ALA ASP HIS ALA ASP ASP ILE GLN TYR VAL
SEQRES 35 A 533 PHE GLY LYS PRO PHE ALA THR PRO THR GLY TYR ARG PRO
SEQRES 36 A 533 GLN ASP ARG THR VAL SER LYS ALA MET ILE ALA TYR TRP
SEQRES 37 A 533 THR ASN PHE ALA LYS THR GLY ASP PRO ASN MET GLY ASP
SEQRES 38 A 533 SER ALA VAL PRO THR HIS TRP GLU PRO TYR THR THR GLU
SEQRES 39 A 533 ASN SER GLY TYR LEU GLU ILE THR LYS LYS MET GLY SER
SEQRES 40 A 533 SER SER MET LYS ARG SER LEU ARG THR ASN PHE LEU ARG
SEQRES 41 A 533 TYR TRP THR LEU THR TYR LEU ALA LEU PRO THR VAL THR
FORMUL 2 HOH *163(H2 O1)
HELIX 1 1 GLY A 127 ASN A 135 1 9
HELIX 2 2 GLY A 146 LEU A 151 1 6
HELIX 3 3 ASN A 161 ILE A 178 1 18
HELIX 4 4 SER A 194 LEU A 205 1 12
HELIX 5 5 PRO A 233 VAL A 244 1 12
HELIX 6 6 ALA A 251 THR A 261 1 11
HELIX 7 7 ASP A 262 ALA A 269 1 8
HELIX 8 8 GLY A 321 MET A 329 1 9
HELIX 9 9 THR A 340 THR A 352 1 13
HELIX 10 10 GLY A 356 THR A 368 1 13
HELIX 11 12 ASP A 438 GLY A 444 1 7
HELIX 12 13 PRO A 455 GLY A 475 5 21
HELIX 13 14 ARG A 515 LEU A 527 1 13
SHEET 1 A 3 GLY A 4 THR A 8 0
SHEET 2 A 3 GLY A 11 GLY A 15 -1 N GLY A 11 O THR A 8
SHEET 3 A 3 THR A 54 LYS A 56 1 O LEU A 55 N GLU A 14
SHEET 1 B11 VAL A 16 LEU A 20 0
SHEET 2 B11 ASP A 25 PRO A 34 -1 O VAL A 27 N LYS A 18
SHEET 3 B11 LEU A 81 GLY A 90 -1 N LEU A 83 O ILE A 33
SHEET 4 B11 ILE A 137 ASN A 142 -1 N VAL A 138 O TRP A 86
SHEET 5 B11 LEU A 98 ILE A 104 1 O PRO A 99 N ILE A 137
SHEET 6 B11 GLY A 183 GLU A 193 1 N ASP A 184 O LEU A 98
SHEET 7 B11 ARG A 215 SER A 220 1 O ARG A 215 N LEU A 190
SHEET 8 B11 ASP A 311 ASN A 318 1 O ASP A 311 N ALA A 216
SHEET 9 B11 LYS A 412 SER A 419 1 N TYR A 414 O TYR A 312
SHEET 10 B11 TYR A 498 ILE A 501 1 O LEU A 499 N LEU A 417
SHEET 11 B11 SER A 509 LYS A 511 -1 N LYS A 511 O TYR A 498
SSBOND 1 CYS A 64 CYS A 80
SSBOND 2 CYS A 246 CYS A 257
CRYST1 64.700 88.970 104.300 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 0.015458 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011240 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009587 0.00000
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