| content |
HEADER HYDROLASE 03-NOV-00 1G66
TITLE ACETYLXYLAN ESTERASE AT 0.90 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYL XYLAN ESTERASE II;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.6
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PENICILLIUM PURPUROGENUM;
SOURCE 3 ORGANISM_COMMON: FUNGUS
KEYWDS SERINE HYDROLASE, ACETYL XYLOPYRANOSE, XYLAN, ULTRA-HIGH
KEYWDS 2 RESOLUTION
EXPDTA X-RAY DIFFRACTION
AUTHOR D.GHOSH,M.SAWICKI,P.LALA,M.ERMAN,W.PANGBORN,J.EYZAGUIRRE,
AUTHOR 2 R.GUTIERREZ,H.JORNVALL,D.J.THIEL
REVDAT 2 11-APR-01 1G66 1 JRNL ATOM
REVDAT 1 17-JAN-01 1G66 0
JRNL AUTH D.GHOSH,M.SAWICKI,P.LALA,M.ERMAN,W.PANGBORN,
JRNL AUTH 2 J.EYZAGUIRRE,R.GUTIERREZ,H.JORNVALL,D.J.THIEL
JRNL TITL MULTIPLE CONFORMATIONS OF CATALYTIC SERINE AND
JRNL TITL 2 HISTIDINE IN ACETYLXYLAN ESTERASE AT 0.90 ANGSTROM
JRNL REF J.BIOL.CHEM. V. 276 11159 2001
JRNL REFN ASTM JBCHA3 US ISSN 0021-9258
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.GHOSH,M.ERMAN,M.SAWICKI,P.LALA,D.R.WEEKS,N.LI,
REMARK 1 AUTH 2 W.PANGBORN,D.J.THIEL,H.JORNVALL,R.GUTIERREZ,
REMARK 1 AUTH 3 J.EYZAGUIRRE
REMARK 1 TITL DETERMINATION OF A PROTEIN STRUCTURE BY
REMARK 1 TITL 2 IODINATION: THE STRUCTURE OF IODINATED ACETYLXYLAN
REMARK 1 TITL 3 ESTERASE
REMARK 1 REF ACTA CRYSTALLOGR., SECT.D V. 55 779 1999
REMARK 1 REFN ASTM ABCRE6 DK ISSN 0907-4449
REMARK 1 REFERENCE 2
REMARK 1 TITL CHARACTERIZATION OF CRYSTALS OF P. PURPUROGENUM
REMARK 1 TITL 2 ACETYL XYLAN ESTERASE FROM HIGH RESOLUTION X-RAY
REMARK 1 TITL 3 DIFFRACTION
REMARK 1 REF PROTEINS: STRUCT., FUNCT., V. 24 523 1996
REMARK 1 REF 2 GENET.
REMARK 1 REFN ASTM PSFGEY US ISSN 0887-3585
REMARK 2
REMARK 2 RESOLUTION. 0.90 ANGSTROM.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 0.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 99.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.107
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.107
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.132
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 4800
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 95283
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2880
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 323
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : NULL
REMARK 3 NUMBER OF RESTRAINTS : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.016
REMARK 3 ANGLE DISTANCES (A) : 1.982
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 1.717
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : NULL
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1G66 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-DEC-2000.
REMARK 100 THE RCSB ID CODE IS RCSB012282.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-1995
REMARK 200 TEMPERATURE (KELVIN) : 85.0
REMARK 200 PH : 5.30
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSSED SI
REMARK 200 (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : PRINCETON 2K
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 95283
REMARK 200 RESOLUTION RANGE HIGH (A) : 0.900
REMARK 200 RESOLUTION RANGE LOW (A) : 99.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.6
REMARK 200 DATA REDUNDANCY : 4.410
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 29.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 0.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 40.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.18500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: AB INITIO PHASING
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: NULL
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: AMMONIUM SULFATE
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 17.27050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.69600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.94900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 35.69600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 17.27050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.94900
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: 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 O HOH 349 O HOH 596 1.37
REMARK 500 O HOH 587 O GLY A 54 1.41
REMARK 500 O HOH 599 O HOH 473 1.49
REMARK 500 O HOH 375 O HOH 557 1.53
REMARK 500 O HOH 591 O HOH 582 1.66
REMARK 500 O HOH 586 O HOH 555 1.72
REMARK 500 OG SER A 160 O1 GOL 223 1.77
REMARK 500 O HOH 550 O1 GOL 222 1.83
REMARK 500 O HOH 393 O2 GOL 223 1.85
REMARK 500 O HOH 547 O HOH 537 1.92
REMARK 500 O1 GOL 220 O HOH 473 1.96
REMARK 500 O HOH 319 O HOH 443 2.00
REMARK 500 OH TYR A 177 O HOH 533 2.02
REMARK 500 O HOH 399 O HOH 587 2.03
REMARK 500 O HOH 568 O HOH 561 2.09
REMARK 500 O HOH 575 O HOH 379 2.10
REMARK 500 O HOH 590 O HOH 581 2.11
REMARK 500 O1 GOL 220 O3 GOL 222 2.14
REMARK 500 O3 GOL 220 O HOH 600 2.19
REMARK 500 O2 GOL 222 O HOH 561 2.19
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. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED 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 O HOH 593 O HOH 469 3655 1.22
REMARK 500 O HOH 583 N GLU A 193 3545 2.14
REMARK 500 O HOH 583 O HOH 585 2555 2.15
REMARK 500 O HOH 479 O HOH 570 3655 2.17
REMARK 500 OD1 ASN A 27 O HOH 316 3655 2.17
REMARK 500 C SER A 192 O HOH 583 3555 2.18
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 LYS A 166 CG - CD - CE ANGL. DEV. = 23.3 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 90 -116.51 62.01
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 301 DISTANCE = 5.12 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BS9 RELATED DB: PDB
REMARK 900 ROOM TEMPERATURE STRUCTURE OF ACETYLXYLAN ESTERASE AT 1.1
REMARK 900 ANGSTROM
REMARK 900 RELATED ID: 2AXE RELATED DB: PDB
REMARK 900 IODINATED COMPLEX OF ACETYLXYLAN ESTERASE AT 1.80 ANGSTROM
DBREF 1G66 A 1 207 GB 2944191 AAC39371 28 234
SEQRES 1 A 207 SER CYS PRO ALA ILE HIS VAL PHE GLY ALA ARG GLU THR
SEQRES 2 A 207 THR ALA SER PRO GLY TYR GLY SER SER SER THR VAL VAL
SEQRES 3 A 207 ASN GLY VAL LEU SER ALA TYR PRO GLY SER THR ALA GLU
SEQRES 4 A 207 ALA ILE ASN TYR PRO ALA CYS GLY GLY GLN SER SER CYS
SEQRES 5 A 207 GLY GLY ALA SER TYR SER SER SER VAL ALA GLN GLY ILE
SEQRES 6 A 207 ALA ALA VAL ALA SER ALA VAL ASN SER PHE ASN SER GLN
SEQRES 7 A 207 CYS PRO SER THR LYS ILE VAL LEU VAL GLY TYR SER GLN
SEQRES 8 A 207 GLY GLY GLU ILE MET ASP VAL ALA LEU CYS GLY GLY GLY
SEQRES 9 A 207 ASP PRO ASN GLN GLY TYR THR ASN THR ALA VAL GLN LEU
SEQRES 10 A 207 SER SER SER ALA VAL ASN MET VAL LYS ALA ALA ILE PHE
SEQRES 11 A 207 MET GLY ASP PRO MET PHE ARG ALA GLY LEU SER TYR GLU
SEQRES 12 A 207 VAL GLY THR CYS ALA ALA GLY GLY PHE ASP GLN ARG PRO
SEQRES 13 A 207 ALA GLY PHE SER CYS PRO SER ALA ALA LYS ILE LYS SER
SEQRES 14 A 207 TYR CYS ASP ALA SER ASP PRO TYR CYS CYS ASN GLY SER
SEQRES 15 A 207 ASN ALA ALA THR HIS GLN GLY TYR GLY SER GLU TYR GLY
SEQRES 16 A 207 SER GLN ALA LEU ALA PHE VAL LYS SER LYS LEU GLY
HET SO4 210 5
HET SO4 211 5
HET SO4 212 5
HET SO4 213 5
HET GOL 220 6
HET GOL 222 6
HET GOL 223 6
HET GOL 224 6
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
FORMUL 2 SO4 4(O4 S1 2-)
FORMUL 6 GOL 4(C3 H8 O3)
FORMUL 10 HOH *299(H2 O1)
HELIX 1 1 TYR A 19 SER A 21 5 3
HELIX 2 2 SER A 22 TYR A 33 1 12
HELIX 3 3 GLN A 49 GLY A 53 5 5
HELIX 4 4 SER A 56 CYS A 79 1 24
HELIX 5 5 SER A 90 GLY A 102 1 13
HELIX 6 6 PRO A 106 GLY A 109 5 4
HELIX 7 7 SER A 118 MET A 124 1 7
HELIX 8 8 SER A 163 ALA A 165 5 3
HELIX 9 9 ASN A 183 GLY A 189 1 7
HELIX 10 10 GLY A 189 GLY A 207 1 19
SHEET 1 A 6 THR A 37 ALA A 40 0
SHEET 2 A 6 ILE A 5 ALA A 10 1 O ILE A 5 N THR A 37
SHEET 3 A 6 LYS A 83 TYR A 89 1 O LYS A 83 N HIS A 6
SHEET 4 A 6 VAL A 125 MET A 131 1 N LYS A 126 O ILE A 84
SHEET 5 A 6 ILE A 167 TYR A 170 1 O LYS A 168 N PHE A 130
SHEET 6 A 6 GLU A 143 VAL A 144 1 N VAL A 144 O SER A 169
SSBOND 1 CYS A 2 CYS A 79
SSBOND 2 CYS A 46 CYS A 52
SSBOND 3 CYS A 101 CYS A 161
SSBOND 4 CYS A 147 CYS A 179
SSBOND 5 CYS A 171 CYS A 178
CRYST1 34.541 59.898 71.392 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 0.028951 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016695 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014007 0.00000
END |