LongText Report for: 1AC5-pdb
1AC5-pdb | HEADER CARBOXYPEPTIDASE 13-FEB-97 1AC5
TITLE CRYSTAL STRUCTURE OF KEX1(DELTA)P, A PROHORMONE-PROCESSING
TITLE 2 CARBOXYPEPTIDASE FROM SACCHAROMYCES CEREVISIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KEX1(DELTA)P;
COMPND 3 CHAIN: NULL;
COMPND 4 EC: 3.4.16.6
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: YEAST
KEYWDS CARBOXYPEPTIDASE, HYDROLASE, GLYCOPROTEIN, TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.H.SHILTON,D.Y.THOMAS,M.CYGLER
REVDAT 1 15-MAY-97 1AC5 0
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.H.SHILTON,Y.LI,D.TESSIER,D.Y.THOMAS,M.CYGLER
REMARK 1 TITL CRYSTALLIZATION OF A SOLUBLE FORM OF THE KEX1P
REMARK 1 TITL 2 SERINE CARBOXYPEPTIDASE FROM SACCHAROMYCES
REMARK 1 TITL 3 CEREVISIAE
REMARK 1 REF PROTEIN SCI. V. 5 395 1996
REMARK 1 REFN ASTM PRCIEI US ISSN 0961-8368 0795
REMARK 1 REFERENCE 2
REMARK 1 AUTH L.LATCHINIAN-SADEK,D.Y.THOMAS
REMARK 1 TITL SECRETION, PURIFICATION AND CHARACTERIZATION OF A
REMARK 1 TITL 2 SOLUBLE FORM OF THE YEAST KEX1-ENCODED PROTEIN FROM
REMARK 1 TITL 3 INSECT-CELL CULTURES
REMARK 1 REF EUR.J.BIOCHEM. V. 219 647 1994
REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 0262
REMARK 2
REMARK 2 RESOLUTION. 2.4 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.4
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1000000.00
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.001
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 20663
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) : 0.195
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.9
REMARK 3 FREE R VALUE TEST SET COUNT : 2018
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.7
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 787
REMARK 3 BIN R VALUE (WORKING SET) : 0.254
REMARK 3 BIN FREE R VALUE : 0.338
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.9
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 101
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.034
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3757
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 258
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.8
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.5
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -22.92
REMARK 3 B22 (A**2) : 1.74
REMARK 3 B33 (A**2) : 2.51
REMARK 3 B12 (A**2) : 0.0
REMARK 3 B13 (A**2) : 0.0
REMARK 3 B23 (A**2) : 0.0
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM SIGMAA (A) : 0.24
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.34
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.27
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.245
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.9
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.06
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) : 1.33 ; 1.50
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.76 ; 2.00
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.37 ; 2.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.84 ; 2.50
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM19.SOL
REMARK 3 PARAMETER FILE 3 : PARAM3.CHO
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH3.CHO
REMARK 3 TOPOLOGY FILE 3 : TOPH19.SOL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: X-PLOR BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 1AC5 COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : JUN-1995
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE CRYSTAL
REMARK 200 OPTICS : COLLIMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : R-AXIS II IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20693
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.4
REMARK 200 RESOLUTION RANGE LOW (A) : 40.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 5.1
REMARK 200 R MERGE (I) : 0.051
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.1
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.2
REMARK 200 R MERGE FOR SHELL (I) : 0.154
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.
REMARK 200
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR, MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE, MLPHARE, OTHER CCP4 PROGRAMS
REMARK 200 STARTING MODEL: PDB ENTRY 3SC2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.5
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM
REMARK 280 17% PEG-MME 5000, 400 MM AMMONIUM ACETATE, 5% GLYCEROL,
REMARK 280 10 MM SODIUM AZIDE, PH 6.5.
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 28.57470
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.55556
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.52479
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.55556
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.57470
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.52479
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 ASP 40 CG OD1 OD2
REMARK 470 ASP 42 CG OD1 OD2
REMARK 470 GLU 43 CG CD OE1 OE2
REMARK 470 GLN 44 CG CD OE1 NE2
REMARK 470 ASP 45 CG OD1 OD2
REMARK 470 ASN 59 CG OD1 ND2
REMARK 470 ASP 60 CG OD1 OD2
REMARK 470 SER 61 OG
REMARK 470 ASN 62 CG OD1 ND2
REMARK 470 ASN 64 CG OD1 ND2
REMARK 470 VAL 65 CG1 CG2
REMARK 470 PHE 195 CG CD1 CE1 CZ CE2 CD2
REMARK 470 SER 196 OG
REMARK 470 LYS 197 CG CD CE NZ
REMARK 470 ASP 199 CG OD1 OD2
REMARK 470 LYS 288 CG CD CE NZ
REMARK 470 ASP 473 CG OD1 OD2
REMARK 470 ASN 474 CG OD1 ND2
REMARK 470 ASN 475 CG OD1 ND2
REMARK 470 LYS 477 CG CD CE NZ
REMARK 470 ASN 478 CG OD1 ND2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. SOME OF THESE MAY BE ATOMS
REMARK 500 LOCATED ON SPECIAL POSITIONS IN THE CELL. ATOMS WITH
REMARK 500 NON-BLANK ALTERNATE LOCATION INDICATORS ARE NOT INCLUDED
REMARK 500 IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 HG SER 259 H LYS 314 3545 1.22
REMARK 500 H LYS 314 HG SER 259 3555 1.22
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 NAG 900 IS COVALENTLY ATTACHED TO ASN 445.
REMARK 600 NAG 901 IS COVALENTLY ATTACHED TO ASN 437.
REMARK 600 NAG 902 IS COVALENTLY ATTACHED TO NAG 901.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: 176
REMARK 800 SITE_DESCRIPTION: MEMBER OF CATALYTIC TRIAD.
REMARK 800
REMARK 800 SITE_IDENTIFIER: 383
REMARK 800 SITE_DESCRIPTION: MEMBER OF CATALYTIC TRIAD.
REMARK 800
REMARK 800 SITE_IDENTIFIER: 448
REMARK 800 SITE_DESCRIPTION: MEMBER OF CATALYTIC TRIAD.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1AC5 SWS P09620 1 - 22 NOT IN ATOMS LIST
REMARK 999 1AC5 SWS P09620 506 - 729 NOT IN ATOMS LIST
DBREF 1AC5 1 483 SWS P09620 KEX1_YEAST 23 505
SEQRES 1 483 LEU PRO SER SER GLU GLU TYR LYS VAL ALA TYR GLU LEU
SEQRES 2 483 LEU PRO GLY LEU SER GLU VAL PRO ASP PRO SER ASN ILE
SEQRES 3 483 PRO GLN MET HIS ALA GLY HIS ILE PRO LEU ARG SER GLU
SEQRES 4 483 ASP ALA ASP GLU GLN ASP SER SER ASP LEU GLU TYR PHE
SEQRES 5 483 PHE TRP LYS PHE THR ASN ASN ASP SER ASN GLY ASN VAL
SEQRES 6 483 ASP ARG PRO LEU ILE ILE TRP LEU ASN GLY GLY PRO GLY
SEQRES 7 483 CYS SER SER MET ASP GLY ALA LEU VAL GLU SER GLY PRO
SEQRES 8 483 PHE ARG VAL ASN SER ASP GLY LYS LEU TYR LEU ASN GLU
SEQRES 9 483 GLY SER TRP ILE SER LYS GLY ASP LEU LEU PHE ILE ASP
SEQRES 10 483 GLN PRO THR GLY THR GLY PHE SER VAL GLU GLN ASN LYS
SEQRES 11 483 ASP GLU GLY LYS ILE ASP LYS ASN LYS PHE ASP GLU ASP
SEQRES 12 483 LEU GLU ASP VAL THR LYS HIS PHE MET ASP PHE LEU GLU
SEQRES 13 483 ASN TYR PHE LYS ILE PHE PRO GLU ASP LEU THR ARG LYS
SEQRES 14 483 ILE ILE LEU SER GLY GLU SER TYR ALA GLY GLN TYR ILE
SEQRES 15 483 PRO PHE PHE ALA ASN ALA ILE LEU ASN HIS ASN LYS PHE
SEQRES 16 483 SER LYS ILE ASP GLY ASP THR TYR ASP LEU LYS ALA LEU
SEQRES 17 483 LEU ILE GLY ASN GLY TRP ILE ASP PRO ASN THR GLN SER
SEQRES 18 483 LEU SER TYR LEU PRO PHE ALA MET GLU LYS LYS LEU ILE
SEQRES 19 483 ASP GLU SER ASN PRO ASN PHE LYS HIS LEU THR ASN ALA
SEQRES 20 483 HIS GLU ASN CYS GLN ASN LEU ILE ASN SER ALA SER THR
SEQRES 21 483 ASP GLU ALA ALA HIS PHE SER TYR GLN GLU CYS GLU ASN
SEQRES 22 483 ILE LEU ASN LEU LEU LEU SER TYR THR ARG GLU SER SER
SEQRES 23 483 GLN LYS GLY THR ALA ASP CYS LEU ASN MET TYR ASN PHE
SEQRES 24 483 ASN LEU LYS ASP SER TYR PRO SER CYS GLY MET ASN TRP
SEQRES 25 483 PRO LYS ASP ILE SER PHE VAL SER LYS PHE PHE SER THR
SEQRES 26 483 PRO GLY VAL ILE ASP SER LEU HIS LEU ASP SER ASP LYS
SEQRES 27 483 ILE ASP HIS TRP LYS GLU CYS THR ASN SER VAL GLY THR
SEQRES 28 483 LYS LEU SER ASN PRO ILE SER LYS PRO SER ILE HIS LEU
SEQRES 29 483 LEU PRO GLY LEU LEU GLU SER GLY ILE GLU ILE VAL LEU
SEQRES 30 483 PHE ASN GLY ASP LYS ASP LEU ILE CYS ASN ASN LYS GLY
SEQRES 31 483 VAL LEU ASP THR ILE ASP ASN LEU LYS TRP GLY GLY ILE
SEQRES 32 483 LYS GLY PHE SER ASP ASP ALA VAL SER PHE ASP TRP ILE
SEQRES 33 483 HIS LYS SER LYS SER THR ASP ASP SER GLU GLU PHE SER
SEQRES 34 483 GLY TYR VAL LYS TYR ASP ARG ASN LEU THR PHE VAL SER
SEQRES 35 483 VAL TYR ASN ALA SER HIS MET VAL PRO PHE ASP LYS SER
SEQRES 36 483 LEU VAL SER ARG GLY ILE VAL ASP ILE TYR SER ASN ASP
SEQRES 37 483 VAL MET ILE ILE ASP ASN ASN GLY LYS ASN VAL MET ILE
SEQRES 38 483 THR THR
HET NAG 900 28
HET NAG 901 27
HET NAG 902 28
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 2 NAG 3(C8 H15 N1 O6)
FORMUL 3 HOH *258(H2 O1)
HELIX 1 1 SER 4 GLU 6 5 3
HELIX 2 2 TYR 11 LEU 13 5 3
HELIX 3 3 ASN 62 ASN 64 5 3
HELIX 4 4 MET 82 VAL 87 1 6
HELIX 5 5 TRP 107 SER 109 5 3
HELIX 6 6 GLU 132 LYS 134 5 3
HELIX 7 7 LEU 144 ILE 161 1 18
HELIX 8 8 ASP 165 THR 167 5 3
HELIX 9 9 SER 176 PHE 195 5 20
HELIX 10 10 PRO 217 GLU 230 1 14
HELIX 11 11 PHE 241 SER 257 1 17
HELIX 12 12 ASP 261 ALA 264 5 4
HELIX 13 13 GLN 269 TYR 281 1 13
HELIX 14 14 LYS 314 PHE 323 5 10
HELIX 15 15 VAL 328 SER 331 1 4
HELIX 16 16 ASN 347 LYS 352 1 6
HELIX 17 17 SER 361 GLU 370 5 10
HELIX 18 18 ASN 388 ASP 396 1 9
HELIX 19 19 VAL 450 ASP 453 1 4
HELIX 20 20 SER 455 TYR 465 1 11
SHEET 1 A12 GLN 28 PRO 35 0
SHEET 2 A12 GLU 50 THR 57 -1 N THR 57 O GLN 28
SHEET 3 A12 GLY 111 ILE 116 -1 N PHE 115 O TRP 54
SHEET 4 A12 PRO 68 LEU 73 1 N PRO 68 O ASP 112
SHEET 5 A12 ILE 170 GLU 175 1 N ILE 171 O LEU 69
SHEET 6 A12 LEU 205 GLY 211 1 N LYS 206 O ILE 170
SHEET 7 A12 GLU 374 GLY 380 1 N GLU 374 O LEU 208
SHEET 8 A12 LEU 438 VAL 443 1 N THR 439 O ILE 375
SHEET 9 A12 GLY 430 ASP 435 -1 N ASP 435 O LEU 438
SHEET 10 A12 VAL 411 HIS 417 -1 N TRP 415 O GLY 430
SHEET 11 A12 LYS 477 THR 482 1 N MET 480 O ASP 414
SHEET 12 A12 MET 470 ASN 474 -1 N ASN 474 O LYS 477
SHEET 1 B 2 PHE 92 VAL 94 0
SHEET 2 B 2 LEU 100 LEU 102 -1 N TYR 101 O ARG 93
SSBOND 1 CYS 79 CYS 345
SSBOND 2 CYS 251 CYS 271
SSBOND 3 CYS 293 CYS 308
LINK C1 NAG 900 ND2 ASN 445
LINK C1 NAG 901 ND2 ASN 437
LINK O4 NAG 901 C1 NAG 902
CISPEP 1 GLY 76 PRO 77 0 -0.13
CISPEP 2 GLN 118 PRO 119 0 -1.49
CISPEP 3 TYR 305 PRO 306 0 0.00
CISPEP 4 TRP 312 PRO 313 0 0.20
SITE 1 176 1 SER 176
SITE 1 383 1 ASP 383
SITE 1 448 1 HIS 448
CRYST1 57.150 83.050 111.110 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 0.017498 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012041 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009000 0.00000
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