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HEADER HYDROLASE 20-JUL-01 1JMY
TITLE TRUNCATED RECOMBINANT HUMAN BILE SALT STIMULATED LIPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BILE-SALT-ACTIVATED LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: 1-518;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: KIDNEY CELLS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PNUT
KEYWDS BSSL, BSDL, BILE SALT DEPENDENT LIPASE, BILE SALT
KEYWDS 2 STIMULATED LIPASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.A.MOORE,R.L.KINGSTON,K.M.LOOMES,O.HERNELL,L.BLACKBERG,
AUTHOR 2 H.M.BAKER,E.N.BAKER
REVDAT 2 26-SEP-01 1JMY 1 JRNL
REVDAT 1 08-AUG-01 1JMY 0
JRNL AUTH S.A.MOORE,R.L.KINGSTON,K.M.LOOMES,O.HERNELL,
JRNL AUTH 2 L.BLACKBERG,H.M.BAKER,E.N.BAKER
JRNL TITL THE STRUCTURE OF TRUNCATED RECOMBINANT HUMAN BILE
JRNL TITL 2 SALT-STIMULATED LIPASE REVEALS BILE
JRNL TITL 3 SALT-INDEPENDENT CONFORMATIONAL FLEXIBILITY AT THE
JRNL TITL 4 ACTIVE-SITE LOOP AND PROVIDES INSIGHTS INTO
JRNL TITL 5 HEPARIN BINDING
JRNL REF J.MOL.BIOL. V. 312 511 2001
JRNL REFN ASTM JMOBAK UK ISSN 0022-2836
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF
REMARK 1 TITL 2 NATIVE AND RECOMBINANT HUMAN BILE-SALT DEPENDENT
REMARK 1 TITL 3 LIPASE: STRATEGIES FOR IMPROVEMENT OF DIFFRACTION
REMARK 1 TITL 4 QUALITY
REMARK 1 REF ACTA CRYSTALLOGR., SECT.D V. 56 478 2000
REMARK 1 REFN ASTM ABCRE6 DK ISSN 0907-4449
REMARK 2
REMARK 2 RESOLUTION. 2.60 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 AND HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.6
REMARK 3 NUMBER OF REFLECTIONS : 15613
REMARK 3
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREER
REMARK 3 FREE R VALUE TEST SET SELECTION : 10% OF THE REFLECTION
REMARK 3 SET, RANDOMLY CHOSEN
REMARK 3 R VALUE (WORKING SET) : 0.236
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1570
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3990
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 63
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 11.33000
REMARK 3 B22 (A**2) : 16.34600
REMARK 3 B33 (A**2) : -27.68200
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : TIGHTLY RESTRAINED INDIVIDUAL
REMARK 3 B'S
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JMY COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JUL-2001.
REMARK 100 THE RCSB ID CODE IS RCSB013953.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 1996
REMARK 200 TEMPERATURE (KELVIN) : 113.0
REMARK 200 PH : 6.70
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU 200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE PLUS 0.1 MM
REMARK 200 COLLIMATOR
REMARK 200 OPTICS : GRAPHITE MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15613
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.6
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : 0.10000
REMARK 200 FOR THE DATA SET : 6.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.35000
REMARK 200 R SYM FOR SHELL (I) : 0.35000
REMARK 200 FOR SHELL : 2.000
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: TRUNCATED CORE OF ACETYLCHOLINESTERASE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG-6000, PIPES/KOH, GLYCEROL
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 29.32000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.63000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.04000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.63000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.32000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.04000
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 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 PRO A 273
REMARK 465 LEU A 274
REMARK 465 ALA A 275
REMARK 465 GLY A 276
REMARK 465 LEU A 277
REMARK 465 GLU A 278
REMARK 465 TYR A 279
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 19 CG CD CE NZ
REMARK 470 TYR A 123 CG CD1 CD2 CE1 CE2 CZ OH
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
REMARK 500 CG2 THR A 316 O HOH 867 1.90
REMARK 500 N ARG A 91 O HOH 862 1.97
REMARK 500 O HOH 833 O HOH 860 2.19
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASP A 97 OD2 ASP A 97 CG 0.079
REMARK 500 LEU A 282 C LEU A 282 CA -0.040
REMARK 500 THR A 316 CG2 THR A 316 CB -0.128
REMARK 500 THR A 449 CB THR A 449 CA -0.050
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 GLY A 21 N - CA - C ANGL. DEV. = 13.7 DEGREES
REMARK 500 LEU A 23 CA - CB - CG ANGL. DEV. =-22.3 DEGREES
REMARK 500 LEU A 23 N - CA - C ANGL. DEV. = 14.7 DEGREES
REMARK 500 LEU A 23 C - N - CA ANGL. DEV. = 13.1 DEGREES
REMARK 500 ASN A 121 N - CA - C ANGL. DEV. = 13.9 DEGREES
REMARK 500 LYS A 271 N - CA - C ANGL. DEV. = 10.5 DEGREES
REMARK 500 TYR A 284 N - CA - C ANGL. DEV. = 14.8 DEGREES
REMARK 500 MET A 424 N - CA - C ANGL. DEV. =-10.8 DEGREES
REMARK 500 TRP A 430 N - CA - C ANGL. DEV. =-15.2 DEGREES
REMARK 500 ILE A 521 N - CA - C ANGL. DEV. = 13.8 DEGREES
DBREF 1JMY A 1 518 GB 14734910 XP_035051.1 21 538
SEQADV 1JMY ARG A 331 GB 14734910 ALA 351 CONFLICT
SEQADV 1JMY PRO A 519 GB 14734910 CLONING ARTIFACT
SEQADV 1JMY GLY A 520 GB 14734910 CLONING ARTIFACT
SEQADV 1JMY ILE A 521 GB 14734910 CLONING ARTIFACT
SEQADV 1JMY HIS A 522 GB 14734910 CLONING ARTIFACT
SEQRES 1 A 522 ALA LYS LEU GLY ALA VAL TYR THR GLU GLY GLY PHE VAL
SEQRES 2 A 522 GLU GLY VAL ASN LYS LYS LEU GLY LEU LEU GLY ASP SER
SEQRES 3 A 522 VAL ASP ILE PHE LYS GLY ILE PRO PHE ALA ALA PRO THR
SEQRES 4 A 522 LYS ALA LEU GLU ASN PRO GLN PRO HIS PRO GLY TRP GLN
SEQRES 5 A 522 GLY THR LEU LYS ALA LYS ASN PHE LYS LYS ARG CYS LEU
SEQRES 6 A 522 GLN ALA THR ILE THR GLN ASP SER THR TYR GLY ASP GLU
SEQRES 7 A 522 ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO GLN GLY ARG
SEQRES 8 A 522 LYS GLN VAL SER ARG ASP LEU PRO VAL MET ILE TRP ILE
SEQRES 9 A 522 TYR GLY GLY ALA PHE LEU MET GLY SER GLY HIS GLY ALA
SEQRES 10 A 522 ASN PHE LEU ASN ASN TYR LEU TYR ASP GLY GLU GLU ILE
SEQRES 11 A 522 ALA THR ARG GLY ASN VAL ILE VAL VAL THR PHE ASN TYR
SEQRES 12 A 522 ARG VAL GLY PRO LEU GLY PHE LEU SER THR GLY ASP ALA
SEQRES 13 A 522 ASN LEU PRO GLY ASN TYR GLY LEU ARG ASP GLN HIS MET
SEQRES 14 A 522 ALA ILE ALA TRP VAL LYS ARG ASN ILE ALA ALA PHE GLY
SEQRES 15 A 522 GLY ASP PRO ASN ASN ILE THR LEU PHE GLY GLU SER ALA
SEQRES 16 A 522 GLY GLY ALA SER VAL SER LEU GLN THR LEU SER PRO TYR
SEQRES 17 A 522 ASN LYS GLY LEU ILE ARG ARG ALA ILE SER GLN SER GLY
SEQRES 18 A 522 VAL ALA LEU SER PRO TRP VAL ILE GLN LYS ASN PRO LEU
SEQRES 19 A 522 PHE TRP ALA LYS LYS VAL ALA GLU LYS VAL GLY CYS PRO
SEQRES 20 A 522 VAL GLY ASP ALA ALA ARG MET ALA GLN CYS LEU LYS VAL
SEQRES 21 A 522 THR ASP PRO ARG ALA LEU THR LEU ALA TYR LYS VAL PRO
SEQRES 22 A 522 LEU ALA GLY LEU GLU TYR PRO MET LEU HIS TYR VAL GLY
SEQRES 23 A 522 PHE VAL PRO VAL ILE ASP GLY ASP PHE ILE PRO ALA ASP
SEQRES 24 A 522 PRO ILE ASN LEU TYR ALA ASN ALA ALA ASP ILE ASP TYR
SEQRES 25 A 522 ILE ALA GLY THR ASN ASN MET ASP GLY HIS ILE PHE ALA
SEQRES 26 A 522 SER ILE ASP MET PRO ARG ILE ASN LYS GLY ASN LYS LYS
SEQRES 27 A 522 VAL THR GLU GLU ASP PHE TYR LYS LEU VAL SER GLU PHE
SEQRES 28 A 522 THR ILE THR LYS GLY LEU ARG GLY ALA LYS THR THR PHE
SEQRES 29 A 522 ASP VAL TYR THR GLU SER TRP ALA GLN ASP PRO SER GLN
SEQRES 30 A 522 GLU ASN LYS LYS LYS THR VAL VAL ASP PHE GLU THR ASP
SEQRES 31 A 522 VAL LEU PHE LEU VAL PRO THR GLU ILE ALA LEU ALA GLN
SEQRES 32 A 522 HIS ARG ALA ASN ALA LYS SER ALA LYS THR TYR ALA TYR
SEQRES 33 A 522 LEU PHE SER HIS PRO SER ARG MET PRO VAL TYR PRO LYS
SEQRES 34 A 522 TRP VAL GLY ALA ASP HIS ALA ASP ASP ILE GLN TYR VAL
SEQRES 35 A 522 PHE GLY LYS PRO PHE ALA THR PRO THR GLY TYR ARG PRO
SEQRES 36 A 522 GLN ASP ARG THR VAL SER LYS ALA MET ILE ALA TYR TRP
SEQRES 37 A 522 THR ASN PHE ALA LYS THR GLY ASP PRO ASN MET GLY ASP
SEQRES 38 A 522 SER ALA VAL PRO THR HIS TRP GLU PRO TYR THR THR GLU
SEQRES 39 A 522 ASN SER GLY TYR LEU GLU ILE THR LYS LYS MET GLY SER
SEQRES 40 A 522 SER SER MET LYS ARG SER LEU ARG THR ASN PHE PRO GLY
SEQRES 41 A 522 ILE HIS
HET SO4 600 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 O4 S1 2-
FORMUL 3 HOH *63(H2 O1)
HELIX 1 1 GLY A 127 GLY A 134 1 8
HELIX 2 2 VAL A 145 LEU A 151 1 7
HELIX 3 3 ASN A 161 ILE A 178 1 18
HELIX 4 4 ALA A 179 PHE A 181 5 3
HELIX 5 5 SER A 194 SER A 206 1 13
HELIX 6 6 PRO A 207 LYS A 210 5 4
HELIX 7 7 ASN A 232 GLY A 245 1 14
HELIX 8 8 ASP A 250 THR A 261 1 12
HELIX 9 9 ASP A 262 LEU A 268 1 7
HELIX 10 10 MET A 281 VAL A 285 5 5
HELIX 11 11 ASP A 299 LEU A 303 5 5
HELIX 12 12 LEU A 303 ALA A 308 5 6
HELIX 13 13 GLY A 321 MET A 329 1 9
HELIX 14 14 PRO A 330 ASN A 333 5 4
HELIX 15 15 GLU A 341 SER A 349 1 9
HELIX 16 16 GLY A 356 TYR A 367 1 12
HELIX 17 17 SER A 376 PHE A 393 1 18
HELIX 18 18 PHE A 393 ALA A 406 1 14
HELIX 19 19 ASP A 438 PHE A 443 1 6
HELIX 20 20 GLY A 444 THR A 449 1 6
HELIX 21 21 PRO A 450 TYR A 453 5 4
HELIX 22 22 ARG A 454 GLY A 475 1 22
HELIX 23 23 GLY A 506 SER A 508 5 3
SHEET 1 A 3 VAL A 6 THR A 8 0
SHEET 2 A 3 GLY A 11 GLU A 14 -1 N GLY A 11 O THR A 8
SHEET 3 A 3 THR A 54 LYS A 56 1 N LEU A 55 O PHE A 12
SHEET 1 B11 VAL A 16 LYS A 19 0
SHEET 2 B11 SER A 26 PRO A 34 -1 O VAL A 27 N LYS A 18
SHEET 3 B11 TYR A 82 GLN A 89 -1 N LEU A 83 O ILE A 33
SHEET 4 B11 ILE A 137 PHE A 141 -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 GLN A 219 1 N ARG A 215 O ILE A 188
SHEET 8 B11 ASP A 311 ASN A 317 1 O ASP A 311 N ALA A 216
SHEET 9 B11 THR A 413 PHE A 418 1 O TYR A 414 N ALA A 314
SHEET 10 B11 TYR A 498 ILE A 501 1 O LEU A 499 N LEU A 417
SHEET 11 B11 MET A 510 LYS A 511 -1 N LYS A 511 O TYR A 498
SHEET 1 C 2 GLN A 66 ALA A 67 0
SHEET 2 C 2 THR A 74 TYR A 75 -1 O TYR A 75 N GLN A 66
SHEET 1 D 2 ASN A 118 PHE A 119 0
SHEET 2 D 2 ASN A 122 TYR A 123 -1 O ASN A 122 N PHE A 119
SSBOND 1 CYS A 64 CYS A 80
SSBOND 2 CYS A 246 CYS A 257
CRYST1 58.640 90.080 103.260 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 0.017053 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011101 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009684 0.00000 |