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HEADER HYDROLASE 28-JAN-98 2BCE
TITLE CHOLESTEROL ESTERASE FROM BOS TAURUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLESTEROL ESTERASE;
COMPND 3 CHAIN: NULL;
COMPND 4 SYNONYM: BILE SALT ACTIVATED LIPASE, BILE SALT STIMULATED
COMPND 5 LIPASE;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: N 187 Q, N 361 Q
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGAN: PANCREAS;
SOURCE 5 CELLULAR_LOCATION: EXTRACELLULAR;
SOURCE 6 EXPRESSION_SYSTEM_CELL: HEK 293;
SOURCE 7 EXPRESSION_SYSTEM_CELLULAR_LOCATION: EXTRACELLULAR
KEYWDS HYDROLASE, ESTERASE, LIPASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.C.-H.CHEN,L.J.W.MIERCKE,J.KRUCINSKI,J.R.STARR,G.SAENZ,
AUTHOR 2 X.WANG,C.A.SPILBURG,L.G.LANGE,J.L.ELLSWORTH,R.M.STROUD
REVDAT 2 23-FEB-99 2BCEA 1 REMARK SPRSDE
REVDAT 1 02-FEB-99 2BCE 0
SPRSDE 23-FEB-99 2BCE 1BCN
JRNL AUTH J.C.-H.CHEN,L.J.W.MIERCKE,J.KRUCINSKI,J.R.STARR,
JRNL AUTH 2 G.SAENZ,X.WANG,C.A.SPILBURG,L.G.LANGE,
JRNL AUTH 3 J.L.ELLSWORTH,R.M.STROUD
JRNL TITL STRUCTURE OF BOVINE PANCREATIC CHOLESTEROL ESTERASE
JRNL TITL 2 AT 1.6 A: NOVEL STRUCTURAL FEATURES INVOLVED IN
JRNL TITL 3 LIPASE ACTIVATION
JRNL REF BIOCHEMISTRY V. 15 5107 1998
JRNL REFN ASTM BICHAW US ISSN 0006-2960 0033
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.843
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.001
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.1
REMARK 3 NUMBER OF REFLECTIONS : 41183
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 : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.0
REMARK 3 FREE R VALUE TEST SET COUNT : 2768
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 : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.67
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 68.1
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1644
REMARK 3 BIN R VALUE (WORKING SET) : 0.2831
REMARK 3 BIN FREE R VALUE : 0.2964
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.0
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 117
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 : 532
REMARK 3 NUCLEIC ACID ATOMS : NULL
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 199
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 8.76
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.044
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.2159
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : 40.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.2548
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.377
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 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 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2BCE COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 5
REMARK 5 WARNING
REMARK 5 2BCE: THIS IS LAYER 1 RELEASE.
REMARK 5
REMARK 5 PLEASE NOTE THAT THIS ENTRY WAS RELEASED AFTER DEPOSITOR
REMARK 5 CHECKING AND APPROVAL AND AFTER INITIAL PROCESSING AND
REMARK 5 REVIEW BY PDB STAFF. HOWEVER, FINAL QUALITY CHECKS HAVE
REMARK 5 NOT BEEN DONE.
REMARK 5
REMARK 5 AN AUXILIARY FILE, AUX2BCE.RPT, IS AVAILABLE FROM THE
REMARK 5 PDB FTP SERVER AND IS ACCESSIBLE THROUGH THE 3DB BROWSER.
REMARK 5 THE FILE CONTAINS THE OUTPUT OF THE PROGRAM WHAT_CHECK AND
REMARK 5 OTHER DIAGNOSTICS.
REMARK 5
REMARK 5 NOMENCLATURE IN THIS ENTRY, INCLUDING HET RESIDUE NAMES
REMARK 5 AND HET ATOM NAMES, HAS NOT BEEN STANDARDIZED BY THE PDB
REMARK 5 PROCESSING STAFF. A LAYER 2 ENTRY WILL BE RELEASED SHORTLY
REMARK 5 AFTER THIS STANDARDIZATION IS COMPLETED AND APPROVED BY THE
REMARK 5 DEPOSITOR. THE LAYER 2 ENTRY WILL BE TREATED AS A
REMARK 5 CORRECTION TO THIS ONE, WITH THE APPROPRIATE REVDAT RECORD.
REMARK 5
REMARK 5 FURTHER INFORMATION INCLUDING VALIDATION CRITERIA USED IN
REMARK 5 CHECKING THIS ENTRY AND A LIST OF MANDATORY DATA FIELDS
REMARK 5 ARE AVAILABLE FROM THE PDB WEB SITE AT
REMARK 5 HTTP://WWW.PDB.BNL.GOV/.
REMARK 6
REMARK 6 THE SIDE-CHAIN ATOMS OF THE RESIDUES AS LISTED IN REMARK 470
REMARK 6 ARE DUE TO THE LACK OF INTERPRETABLE DENSITY BEYOND THE
REMARK 6 BETA CARBON OF THE AMINO ACID.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : MAR-1996
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : 7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.08
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66076
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.60
REMARK 200 RESOLUTION RANGE LOW (A) : INFINITY
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.1
REMARK 200 DATA REDUNDANCY : 2.3
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.087
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.5
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 68.1
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 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 2ACE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.0
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 1/2+X,1/2+Y,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 50.21089
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.12526
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 50.21089
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 27.12526
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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 56 CG CD CE NZ
REMARK 470 LYS 253 CG CD CE NZ
REMARK 470 LYS 271 CG CD CE NZ
REMARK 470 ASN 335 CG OD1 ND2
REMARK 470 GLN 337 CG CD OE1 NE2
REMARK 470 LYS 346 CG CD CE NZ
REMARK 470 ARG 358 CG CD NE CZ NH1 NH2
REMARK 470 LYS 429 CG CD CE NZ
REMARK 470 LEU 451 CG CD1 CD2
REMARK 470 THR 533 OG1 CG2
REMARK 850
REMARK 850 CORRECTION BEFORE RELEASE
REMARK 850 ORIGINAL DEPOSITION REVISED PRIOR TO RELEASE
REMARK 850 DATE REVISED: 14-MAY-1998 TRACKING NUMBER: T14241
REMARK 860
REMARK 860 CORRECTION AFTER RELEASE
REMARK 860 DATE: 23-FEB-99
REMARK 860 MODID: 2BCEA
REMARK 860 MODIFIED BY: PDB
REMARK 860 DESCRIPTION: CORRECTION TO LAYER 1
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE GAP 131-137 IS BECUASE OF A LOOP REGION NOT SEEN IN
REMARK 999 ELECTRON DENSITY. THE 40 RESIDUES 534-573 ARE IN A LINKER
REMARK 999 REGION AND ARE DISORDERED. HOWEVER, THE LAST SIX AMINO
REMARK 999 ACIDS 574-579 ARE IN CLEAR DENSITY.
REMARK 999 2BCE SWS P30122 1 - 18 NOT IN ATOMS LIST
DBREF 2BCE 1 112 SWS P30122 BAL_BOVIN 19 130
DBREF 2BCE 120 533 SWS P30122 BAL_BOVIN 138 551
DBREF 2BCE 574 579 SWS P30122 BAL_BOVIN 592 597
SEQADV 2BCE VAL 27 SWS P30122 ILE 45 CONFLICT
SEQADV 2BCE SWS P30122 ALA 131 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 SER 132 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 GLN 133 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 GLY 134 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 ALA 135 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 ASN 136 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 PHE 137 GAP IN PDB ENTRY
SEQADV 2BCE GLN 187 SWS P30122 ASN 205 MUTATION
SEQADV 2BCE GLN 361 SWS P30122 ASN 379 MUTATION
SEQADV 2BCE SWS P30122 SER 552 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 ALA 553 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 GLY 554 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 ALA 555 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 SER 556 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 LEU 557 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 LEU 558 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 PRO 559 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 PRO 560 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 GLU 561 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 ASP 562 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 ASN 563 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 SER 564 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 GLN 565 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 ALA 566 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 SER 567 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 PRO 568 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 VAL 569 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 PRO 570 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 PRO 571 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 ALA 572 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 ASP 573 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 ASN 574 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 SER 575 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 GLY 576 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 ALA 577 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 PRO 578 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 THR 579 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 GLU 580 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 PRO 581 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 SER 582 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 ALA 583 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 GLY 584 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 ASP 585 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 SER 586 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 GLU 587 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 VAL 588 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 ALA 589 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 GLN 590 GAP IN PDB ENTRY
SEQADV 2BCE SWS P30122 MET 591 GAP IN PDB ENTRY
SEQRES 1 579 ALA LYS LEU GLY SER VAL TYR THR GLU GLY GLY PHE VAL
SEQRES 2 579 GLU GLY VAL ASN LYS LYS LEU SER LEU PHE GLY ASP SER
SEQRES 3 579 VAL ASP ILE PHE LYS GLY ILE PRO PHE ALA ALA ALA PRO
SEQRES 4 579 LYS ALA LEU GLU LYS PRO GLU ARG HIS PRO GLY TRP GLN
SEQRES 5 579 GLY THR LEU LYS ALA LYS SER PHE LYS LYS ARG CYS LEU
SEQRES 6 579 GLN ALA THR LEU THR GLN ASP SER THR TYR GLY ASN GLU
SEQRES 7 579 ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO GLN GLY ARG
SEQRES 8 579 LYS GLU VAL SER HIS ASP LEU PRO VAL MET ILE TRP ILE
SEQRES 9 579 TYR GLY GLY ALA PHE LEU MET GLY ALA SER GLN GLY ALA
SEQRES 10 579 ASN PHE LEU SER ASN TYR LEU TYR ASP GLY GLU GLU ILE
SEQRES 11 579 ALA THR ARG GLY ASN VAL ILE VAL VAL THR PHE ASN TYR
SEQRES 12 579 ARG VAL GLY PRO LEU GLY PHE LEU SER THR GLY ASP SER
SEQRES 13 579 ASN LEU PRO GLY ASN TYR GLY LEU TRP ASP GLN HIS MET
SEQRES 14 579 ALA ILE ALA TRP VAL LYS ARG ASN ILE GLU ALA PHE GLY
SEQRES 15 579 GLY ASP PRO ASP ASN ILE THR LEU PHE GLY GLU SER ALA
SEQRES 16 579 GLY GLY ALA SER VAL SER LEU GLN THR LEU SER PRO TYR
SEQRES 17 579 ASN LYS GLY LEU ILE LYS ARG ALA ILE SER GLN SER GLY
SEQRES 18 579 VAL GLY LEU CYS PRO TRP ALA ILE GLN GLN ASP PRO LEU
SEQRES 19 579 PHE TRP ALA LYS ARG ILE ALA GLU LYS VAL GLY CYS PRO
SEQRES 20 579 VAL ASP ASP THR SER LYS MET ALA GLY CYS LEU LYS ILE
SEQRES 21 579 THR ASP PRO ARG ALA LEU THR LEU ALA TYR LYS LEU PRO
SEQRES 22 579 LEU GLY SER THR GLU TYR PRO LYS LEU HIS TYR LEU SER
SEQRES 23 579 PHE VAL PRO VAL ILE ASP GLY ASP PHE ILE PRO ASP ASP
SEQRES 24 579 PRO VAL ASN LEU TYR ALA ASN ALA ALA ASP VAL ASP TYR
SEQRES 25 579 ILE ALA GLY THR ASN ASP MET ASP GLY HIS LEU PHE VAL
SEQRES 26 579 GLY MET ASP VAL PRO ALA ILE ASN SER ASN LYS GLN ASP
SEQRES 27 579 VAL THR GLU GLU ASP PHE TYR LYS LEU VAL SER GLY LEU
SEQRES 28 579 THR VAL THR LYS GLY LEU ARG GLY ALA ASN ALA THR TYR
SEQRES 29 579 GLU VAL TYR THR GLU PRO TRP ALA GLN ASP SER SER GLN
SEQRES 30 579 GLU THR ARG LYS LYS THR MET VAL ASP LEU GLU THR ASP
SEQRES 31 579 ILE LEU PHE LEU ILE PRO THR LYS ILE ALA VAL ALA GLN
SEQRES 32 579 HIS LYS SER HIS ALA LYS SER ALA ASN THR TYR THR TYR
SEQRES 33 579 LEU PHE SER GLN PRO SER ARG MET PRO ILE TYR PRO LYS
SEQRES 34 579 TRP MET GLY ALA ASP HIS ALA ASP ASP LEU GLN TYR VAL
SEQRES 35 579 PHE GLY LYS PRO PHE ALA THR PRO LEU GLY TYR ARG ALA
SEQRES 36 579 GLN ASP ARG THR VAL SER LYS ALA MET ILE ALA TYR TRP
SEQRES 37 579 THR ASN PHE ALA ARG THR GLY ASP PRO ASN THR GLY HIS
SEQRES 38 579 SER THR VAL PRO ALA ASN TRP ASP PRO TYR THR LEU GLU
SEQRES 39 579 ASP ASP ASN TYR LEU GLU ILE ASN LYS GLN MET ASP SER
SEQRES 40 579 ASN SER MET LYS LEU HIS LEU ARG THR ASN TYR LEU GLN
SEQRES 41 579 PHE TRP THR GLN THR TYR GLN ALA LEU PRO THR VAL THR
SEQRES 42 579 SER ALA GLY ALA SER LEU LEU PRO PRO GLU ASP ASN SER
SEQRES 43 579 GLN ALA SER PRO VAL PRO PRO ALA ASP ASN SER GLY ALA
SEQRES 44 579 PRO THR GLU PRO SER ALA GLY ASP SER GLU VAL ALA GLN
SEQRES 45 579 MET PRO VAL VAL ILE GLY PHE
FORMUL 2 HOH *219(H2 O1)
HELIX 1 1 TYR 123 TYR 125 5 3
HELIX 2 2 GLU 128 GLY 134 1 7
HELIX 3 3 GLY 146 PHE 150 1 5
HELIX 4 4 SER 156 LEU 158 5 3
HELIX 5 5 TYR 162 PHE 181 1 20
HELIX 6 6 ALA 195 LEU 205 1 11
HELIX 7 7 PRO 207 ASN 209 5 3
HELIX 8 8 PRO 226 ALA 228 5 3
HELIX 9 9 PRO 233 VAL 244 1 12
HELIX 10 10 THR 251 LEU 258 1 8
HELIX 11 11 PRO 263 LEU 268 1 6
HELIX 12 12 LYS 281 TYR 284 1 4
HELIX 13 13 PRO 300 ASN 302 5 3
HELIX 14 14 TYR 304 ALA 307 5 4
HELIX 15 15 HIS 322 ASP 328 1 7
HELIX 16 16 PRO 330 ILE 332 5 3
HELIX 17 17 GLU 341 TRP 371 1 31
HELIX 18 18 GLN 377 LEU 392 1 16
HELIX 19 19 LEU 394 HIS 407 1 14
HELIX 20 20 LEU 439 VAL 442 1 4
HELIX 21 21 LYS 445 ALA 448 1 4
HELIX 22 22 PRO 450 GLY 452 5 3
HELIX 23 23 ALA 455 THR 474 1 20
HELIX 24 24 THR 516 THR 523 1 8
HELIX 25 25 THR 525 ALA 528 1 4
SHEET 1 A 3 VAL 6 THR 8 0
SHEET 2 A 3 GLY 11 GLU 14 -1 N VAL 13 O VAL 6
SHEET 3 A 3 THR 54 LYS 56 1 N LEU 55 O PHE 12
SHEET 1 B11 VAL 16 LYS 19 0
SHEET 2 B11 SER 26 PRO 34 -1 N ILE 29 O VAL 16
SHEET 3 B11 TYR 82 GLN 89 -1 N GLN 89 O SER 26
SHEET 4 B11 ILE 137 PHE 141 -1 N THR 140 O ASN 84
SHEET 5 B11 VAL 100 TRP 103 1 N MET 101 O ILE 137
SHEET 6 B11 ILE 188 GLU 193 1 N THR 189 O VAL 100
SHEET 7 B11 ARG 215 GLN 219 1 N ARG 215 O LEU 190
SHEET 8 B11 ASP 311 ASN 317 1 N ASP 311 O ALA 216
SHEET 9 B11 THR 413 PHE 418 1 N TYR 414 O TYR 312
SHEET 10 B11 ASN 497 ILE 501 1 N LEU 499 O LEU 417
SHEET 11 B11 MET 510 LEU 512 -1 N LYS 511 O TYR 498
SHEET 1 C 2 PHE 109 MET 111 0
SHEET 2 C 2 VAL 575 ILE 577 -1 N ILE 577 O PHE 109
SSBOND 1 CYS 64 CYS 80
SSBOND 2 CYS 246 CYS 257
CRYST1 100.420 54.250 106.340 90.00 104.12 90.00 C 1 2 1 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 0.009958 0.000000 0.002505 0.00000
SCALE2 0.000000 0.018433 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009697 0.00000 |