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HEADER SERINE ESTERASE 13-JUL-96 1GPL
TITLE RP2 LIPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RP2 LIPASE;
COMPND 3 CHAIN: NULL;
COMPND 4 SYNONYM: RELATED PROTEIN 2 LIPASE;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: DOMAIN EXCHANGE (C-TERMINUS, RESIDUES 336 - 449)
COMPND 8 WITH HUMAN PANCREATIC LIPASE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CAVIA PORCELLUS;
SOURCE 3 ORGANISM_COMMON: GUINEA PIG;
SOURCE 4 EXPRESSION_SYSTEM: SF9 CELLS;
SOURCE 5 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PVL1393
KEYWDS SERINE ESTERASE, HYDROLASE, LIPID DEGRADATION, PANCREAS,
KEYWDS 2 GLYCOPROTEIN, CHIMERIC
EXPDTA X-RAY DIFFRACTION
AUTHOR C.WITHERS-MARTINEZ,C.CAMBILLAU
REVDAT 1 12-FEB-97 1GPL 0
JRNL AUTH C.WITHERS-MARTINEZ,F.CARRIERE,R.VERGER,D.BOURGEOIS,
JRNL AUTH 2 C.CAMBILLAU
JRNL TITL A PANCREATIC LIPASE WITH A PHOSPHOLIPASE A1
JRNL TITL 2 ACTIVITY: CRYSTAL STRUCTURE OF A CHIMERIC PLRP2
JRNL TITL 3 FROM GUINEA PIG
JRNL REF TO BE PUBLISHED REF NOW ASSIGNED AS
JRNL REFN 0353
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.THIRSTRUP,R.VERGER,F.CARRIERE
REMARK 1 TITL EVIDENCE FOR A PANCREATIC LIPASE SUBFAMILY WITH NEW
REMARK 1 TITL 2 KINETIC PROPERTIES
REMARK 1 REF BIOCHEMISTRY V. 33 2748 1994
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033
REMARK 1 REFERENCE 2
REMARK 1 AUTH F.CARRIERE,K.THIRSTRUP,E.BOEL,R.VERGER,L.THIM
REMARK 1 TITL STRUCTURE-FUNCTION RELATIONSHIPS IN NATURALLY
REMARK 1 TITL 2 OCCURRING MUTANTS OF PANCREATIC LIPASE
REMARK 1 REF PROTEIN ENG. V. 7 563 1994
REMARK 1 REFN ASTM PRENE9 UK ISSN 0269-2139 0859
REMARK 1 REFERENCE 3
REMARK 1 AUTH A.HJORTH,F.CARRIERE,C.CUDREY,H.WOLDIKE,E.BOEL,
REMARK 1 AUTH 2 D.M.LAWSON,F.FERRATO,C.CAMBILLAU,G.G.DODSON,L.THIM,
REMARK 1 AUTH 3 ET AL.
REMARK 1 TITL A STRUCTURAL DOMAIN (THE LID) FOUND IN PANCREATIC
REMARK 1 TITL 2 LIPASES IS ABSENT IN THE GUINEA PIG (PHOSPHO)LIPASE
REMARK 1 REF BIOCHEMISTRY V. 32 4702 1993
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033
REMARK 2
REMARK 2 RESOLUTION. 2.1 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 23574
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : 4121
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 245
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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) : 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) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 1.67
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:
REMARK 3 FINAL RMS COORD. SHIFT 0.01 ANGSTROMS
REMARK 3 MEAN B VALUE (MAIN, A**2) : 25.9
REMARK 3 MEAN B VALUE (SIDE, A**2) : 29.5
REMARK 3 MEAN B VALUE (SOLVENT, A**2) : 42.6
REMARK 4
REMARK 4 1GPL COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996
REMARK 6
REMARK 6 THE C-TERMINAL DOMAIN OF GPLRP2 (336 - 449) HAS BEEN
REMARK 6 REPLACED BY THE C-TERMINAL DOMAIN OF HPL BY MUTAGENESIS
REMARK 6 EXPERIMENTS.
REMARK 7
REMARK 7 REGION 207 - 214 IS DISORDERED AND MODELLED
REMARK 7 STEREOCHEMICALLY, BASED ON HUMAN PANCREATIC LIPASE (HPL)
REMARK 7 STRUCTURE. OCCUPATION OF THESE RESIDUES HAS BEEN SET TO
REMARK 7 0.0.
REMARK 8
REMARK 8 THE SHORT LOOP CONTAINED BETWEEN THE TWO SIDES OF THE
REMARK 8 DISULFIDE BRIDGE (CYS 4 - CYS 10) PRESENTS IN THE TURN A
REMARK 8 SER CLOSE TO THE EPSILON CONFORMATION.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N; Y; Y
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418; 0.9; 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : 18 CM IMAGE PLATE;
REMARK 200 30 CM IMAGE PLATE;
REMARK 200 30 CM CCD PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH; MARRESEARCH;
REMARK 200 NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO; DENZO; DENZO
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27079; NULL; NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.; NULL; NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.6; NULL; NULL
REMARK 200 DATA REDUNDANCY : 3.5; 1.2; 1.8
REMARK 200 R MERGE (I) : 0.113; 0.049; 0.040
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
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 31.00006
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.95014
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 31.00006
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 27.95014
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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 623 DISTANCE = 5.08 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD. THE NUCLEOPHILE SER 152
REMARK 800 IS LOCATED IN A BETA TURN AND HAS AN EPSILON CONFORMATION,
REMARK 800 COMMON FEATURE OF SERINE HYDROLASES.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1GPL SWS P16233 1 - 353 NOT IN ATOMS LIST
REMARK 999
REMARK 999 THE GUINEA PIG SEQUENCE WAS PUBLISHED IN A.HJORTH ET AL.,
REMARK 999 BIOCHEMISTRY 32, 4702-4707 (1993).
DBREF 1GPL 1 336 PDB 1GPL 1GPL 1 336
DBREF 1GPL 337 449 SWS P16233 LIPP_HUMAN 354 465
SEQRES 1 432 ALA GLU VAL CYS TYR SER HIS LEU GLY CYS PHE SER ASP
SEQRES 2 432 GLU LYS PRO TRP ALA GLY THR SER GLN ARG PRO ILE LYS
SEQRES 3 432 SER LEU PRO SER ASP PRO LYS LYS ILE ASN THR ARG PHE
SEQRES 4 432 LEU LEU TYR THR ASN GLU ASN GLN ASN SER TYR GLN LEU
SEQRES 5 432 ILE THR ALA THR ASP ILE ALA THR ILE LYS ALA SER ASN
SEQRES 6 432 PHE ASN LEU ASN ARG LYS THR ARG PHE ILE ILE HIS GLY
SEQRES 7 432 PHE THR ASP SER GLY GLU ASN SER TRP LEU SER ASP MET
SEQRES 8 432 CYS LYS ASN MET PHE GLN VAL GLU LYS VAL ASN CYS ILE
SEQRES 9 432 CYS VAL ASP TRP LYS GLY GLY SER LYS ALA GLN TYR SER
SEQRES 10 432 GLN ALA SER GLN ASN ILE ARG VAL VAL GLY ALA GLU VAL
SEQRES 11 432 ALA TYR LEU VAL GLN VAL LEU SER THR SER LEU ASN TYR
SEQRES 12 432 ALA PRO GLU ASN VAL HIS ILE ILE GLY HIS SER LEU GLY
SEQRES 13 432 ALA HIS THR ALA GLY GLU ALA GLY LYS ARG LEU ASN GLY
SEQRES 14 432 LEU VAL GLY ARG ILE THR GLY LEU ASP PRO ALA GLU PRO
SEQRES 15 432 TYR PHE GLN ASP THR PRO GLU GLU VAL ARG LEU ASP PRO
SEQRES 16 432 SER ASP ALA LYS PHE VAL ASP VAL ILE HIS THR ASP ILE
SEQRES 17 432 SER PRO ILE LEU PRO SER LEU GLY PHE GLY MET SER GLN
SEQRES 18 432 LYS VAL GLY HIS MET ASP PHE PHE PRO ASN GLY GLY LYS
SEQRES 19 432 ASP MET PRO GLY CYS LYS THR GLY ILE SER CYS ASN HIS
SEQRES 20 432 HIS ARG SER ILE GLU TYR TYR HIS SER SER ILE LEU ASN
SEQRES 21 432 PRO GLU GLY PHE LEU GLY TYR PRO CYS ALA SER TYR ASP
SEQRES 22 432 GLU PHE GLN GLU SER GLY CYS PHE PRO CYS PRO ALA LYS
SEQRES 23 432 GLY CYS PRO LYS MET GLY HIS PHE ALA ASP GLN TYR PRO
SEQRES 24 432 GLY LYS THR ASN ALA VAL GLU GLN THR PHE PHE LEU ASN
SEQRES 25 432 THR GLY ALA SER ASP ASN PHE THR ARG TRP ARG TYR LYS
SEQRES 26 432 VAL SER VAL THR LEU SER GLY LYS LYS VAL THR GLY HIS
SEQRES 27 432 ILE LEU VAL SER LEU PHE GLY ASN LYS GLY ASN SER LYS
SEQRES 28 432 GLN TYR GLU ILE PHE LYS GLY THR LEU LYS PRO ASP SER
SEQRES 29 432 THR HIS SER ASN GLU PHE ASP SER ASP VAL ASP VAL GLY
SEQRES 30 432 ASP LEU GLN MET VAL LYS PHE ILE TRP TYR ASN ASN VAL
SEQRES 31 432 ILE ASN PRO THR LEU PRO ARG VAL GLY ALA SER LYS ILE
SEQRES 32 432 ILE VAL GLU THR ASN VAL GLY LYS GLN PHE ASN PHE CYS
SEQRES 33 432 SER PRO GLU THR VAL ARG GLU GLU VAL LEU LEU THR LEU
SEQRES 34 432 THR PRO CYS
HET CA 500 1
HETNAM CA CALCIUM ION
FORMUL 2 CA CA1 2+
FORMUL 3 HOH *247(H2 O1)
HELIX 1 1 SER 6 LEU 8 5 3
HELIX 2 2 PRO 31 ILE 34 1 4
HELIX 3 3 ILE 56 ALA 61 1 6
HELIX 4 4 SER 84 VAL 96 1 13
HELIX 5 5 LYS 107 SER 110 1 4
HELIX 6 6 TYR 114 LEU 139 1 26
HELIX 7 7 PRO 143 ASN 145 5 3
HELIX 8 8 SER 152 ARG 164 5 13
HELIX 9 9 PRO 193 ASP 195 5 3
HELIX 10 10 ILE 209 SER 212 1 4
HELIX 11 11 PRO 228 GLY 231 5 4
HELIX 12 12 CYS 261 ILE 274 1 14
HELIX 13 13 PRO 277 PHE 280 5 4
HELIX 14 14 TYR 288 GLN 292 1 5
HELIX 15 15 ALA 311 GLN 313 5 3
SHEET 1 A 2 GLU 2 TYR 5 0
SHEET 2 A 2 GLY 9 SER 12 -1 N PHE 11 O VAL 3
SHEET 1 B 9 GLN 50 ILE 52 0
SHEET 2 B 9 ARG 37 THR 42 -1 N LEU 40 O GLN 50
SHEET 3 B 9 VAL 99 ASP 105 -1 N ASP 105 O ARG 37
SHEET 4 B 9 LYS 69 ILE 74 1 N LYS 69 O ASN 100
SHEET 5 B 9 VAL 146 HIS 151 1 N HIS 147 O THR 70
SHEET 6 B 9 ARG 171 LEU 175 1 N ARG 171 O ILE 148
SHEET 7 B 9 PHE 198 ILE 202 1 N PHE 198 O ILE 172
SHEET 8 B 9 MET 224 PRO 228 1 N MET 224 O VAL 201
SHEET 9 B 9 GLN 323 LEU 327 1 N GLN 323 O ASP 225
SHEET 1 C 4 THR 381 SER 388 0
SHEET 2 C 4 TRP 338 GLY 348 -1 N VAL 344 O HIS 382
SHEET 3 C 4 VAL 415 GLU 423 -1 N GLU 423 O LYS 341
SHEET 4 C 4 GLN 429 CYS 433 -1 N PHE 432 O ILE 420
SHEET 1 D 4 LEU 444 LEU 446 0
SHEET 2 D 4 LEU 395 ASN 404 -1 N PHE 400 O LEU 444
SHEET 3 D 4 VAL 351 GLY 361 -1 N PHE 360 O GLN 396
SHEET 4 D 4 GLN 368 LEU 376 -1 N LEU 376 O VAL 351
SSBOND 1 CYS 4 CYS 10
SSBOND 2 CYS 90 CYS 101
SSBOND 3 CYS 237 CYS 261
SSBOND 4 CYS 285 CYS 296
SSBOND 5 CYS 299 CYS 304
SSBOND 6 CYS 433 CYS 449
LINK CA CA 500 O GLU 187
LINK CA CA 500 OD1 ASP 192
CISPEP 1 LYS 15 PRO 16 0 1.10
CISPEP 2 LEU 210 PRO 211 0 0.98
CISPEP 3 PHE 297 PRO 298 0 0.24
SITE 1 CAT 3 SER 152 ASP 176 HIS 263
CRYST1 62.000 55.900 144.000 90.00 93.20 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 0.016129 0.000000 0.000902 0.00000
SCALE2 0.000000 0.017889 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006955 0.00000 |