| content |
HEADER HYDROLASE 22-NOV-23 8X6V
TITLE CRYSTAL STRUCTURE OF GLACPETASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLACPETASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS;
SOURCE 3 ORGANISM_TAXID: 286;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PET HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.QI,N.Y.ZHOU
REVDAT 1 14-FEB-24 8X6V 0
JRNL AUTH X.QI,N.Y.ZHOU
JRNL TITL THE UNIQUE SALT BRIDGE NETWORK IN GLACPETASE: A KEY TO ITS
JRNL TITL 2 STABILITY.
JRNL REF APPL.ENVIRON.MICROBIOL. 2024
JRNL REFN ESSN 1098-5336
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.16_3549: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.59
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 47595
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1999
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 4.3309 - 3.4379 1.00 3327 145 0.1527 0.1906
REMARK 3 2 3.4379 - 3.0034 1.00 3298 145 0.1729 0.2310
REMARK 3 3 3.0034 - 2.7289 1.00 3261 142 0.1824 0.2087
REMARK 3 4 2.7289 - 2.5333 1.00 3233 143 0.1784 0.2389
REMARK 3 5 2.5333 - 2.3839 1.00 3264 143 0.1755 0.2382
REMARK 3 6 2.3839 - 2.2645 1.00 3239 142 0.1806 0.2306
REMARK 3 7 2.2645 - 2.1660 1.00 3237 141 0.1760 0.2574
REMARK 3 8 2.1660 - 2.0826 1.00 3197 141 0.1834 0.2395
REMARK 3 9 2.0826 - 2.0107 1.00 3224 141 0.1996 0.2312
REMARK 3 10 2.0107 - 1.9479 1.00 3218 140 0.2099 0.2443
REMARK 3 11 1.9479 - 1.8922 1.00 3221 142 0.2241 0.3284
REMARK 3 12 1.8922 - 1.8424 1.00 3181 140 0.2350 0.2860
REMARK 3 13 1.8424 - 1.7974 1.00 3231 141 0.2639 0.3346
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.510
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 4052
REMARK 3 ANGLE : 0.764 5526
REMARK 3 CHIRALITY : 0.050 619
REMARK 3 PLANARITY : 0.005 709
REMARK 3 DIHEDRAL : 3.224 2384
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8X6V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-NOV-23.
REMARK 100 THE DEPOSITION ID IS D_1300042751.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000 7.21
REMARK 200 DATA SCALING SOFTWARE : HKL-3000 7.21
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47676
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.797
REMARK 200 RESOLUTION RANGE LOW (A) : 45.585
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 11.80
REMARK 200 R MERGE (I) : 0.14200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.95100
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.7.0
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, 0.1 M POTASSIUM
REMARK 280 THIOCYANATE, 0.1 M SODIUM BROMIDE AND 25% V/V PEG SMEAR BROAD
REMARK 280 (PH 7.8), VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
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 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-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 27.67150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.76100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.58500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.76100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.67150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.58500
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 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 SER B 25
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 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 147 -123.21 59.76
REMARK 500 SER A 224 -0.13 71.89
REMARK 500 ASP A 265 31.78 -149.55
REMARK 500 SER B 75 -2.18 72.87
REMARK 500 SER B 147 -127.25 64.34
REMARK 500 SER B 224 -2.37 70.94
REMARK 500 ASP B 265 21.08 -144.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 529 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH A 530 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH A 531 DISTANCE = 6.77 ANGSTROMS
DBREF 8X6V A 25 285 PDB 8X6V 8X6V 25 285
DBREF 8X6V B 25 285 PDB 8X6V 8X6V 25 285
SEQRES 1 A 261 SER ALA PRO ALA PRO ASN VAL PRO GLY GLY GLU ARG VAL
SEQRES 2 A 261 CYS ALA TYR THR SER GLY LEU SER SER LEU SER TYR ALA
SEQRES 3 A 261 SER ALA ARG VAL THR TYR PRO CYS THR LEU SER LYS ALA
SEQRES 4 A 261 ALA TYR PRO ALA THR THR LEU THR GLY GLY PHE SER ASN
SEQRES 5 A 261 THR LYS GLU GLN MET THR TRP LEU SER GLU HIS LEU SER
SEQRES 6 A 261 SER HIS GLY TYR ILE VAL ILE THR ILE THR PRO ARG ASN
SEQRES 7 A 261 ILE PHE GLY ALA PRO THR GLY TRP GLU SER ALA HIS LYS
SEQRES 8 A 261 ALA GLY ILE ALA LYS LEU ARG SER GLU ARG SER ARG ARG
SEQRES 9 A 261 ALA SER PRO LEU TYR ASN LYS LEU ASP PRO SER LYS PHE
SEQRES 10 A 261 ALA LEU THR GLY PHE SER MET GLY GLY GLY GLY ALA LEU
SEQRES 11 A 261 LEU ALA ALA ALA ASP LEU GLY SER GLN VAL LYS VAL ALA
SEQRES 12 A 261 VAL PRO MET ALA PRO PHE LEU GLY SER ASN ASN PRO ASN
SEQRES 13 A 261 TYR SER ALA ILE THR ALA LYS VAL LEU ILE GLN ALA GLY
SEQRES 14 A 261 ALA ASN ASP THR VAL ALA ASN PRO SER THR VAL ALA SER
SEQRES 15 A 261 TYR TYR GLN SER LEU PRO THR GLY ILE SER ARG ALA LEU
SEQRES 16 A 261 THR THR PHE ARG SER ALA SER HIS LEU ASP TRP ILE ASN
SEQRES 17 A 261 THR GLY ASN THR ASN ARG GLN ALA ARG LEU LYS THR LEU
SEQRES 18 A 261 VAL THR SER TRP LEU LYS VAL TYR LEU ASP GLY ASN SER
SEQRES 19 A 261 ASP TYR ALA THR TYR LEU ASP GLY ALA GLU HIS SER ARG
SEQRES 20 A 261 HIS LEU ALA GLU ASP TRP PHE THR ARG PHE GLU TYR VAL
SEQRES 21 A 261 ARG
SEQRES 1 B 261 SER ALA PRO ALA PRO ASN VAL PRO GLY GLY GLU ARG VAL
SEQRES 2 B 261 CYS ALA TYR THR SER GLY LEU SER SER LEU SER TYR ALA
SEQRES 3 B 261 SER ALA ARG VAL THR TYR PRO CYS THR LEU SER LYS ALA
SEQRES 4 B 261 ALA TYR PRO ALA THR THR LEU THR GLY GLY PHE SER ASN
SEQRES 5 B 261 THR LYS GLU GLN MET THR TRP LEU SER GLU HIS LEU SER
SEQRES 6 B 261 SER HIS GLY TYR ILE VAL ILE THR ILE THR PRO ARG ASN
SEQRES 7 B 261 ILE PHE GLY ALA PRO THR GLY TRP GLU SER ALA HIS LYS
SEQRES 8 B 261 ALA GLY ILE ALA LYS LEU ARG SER GLU ARG SER ARG ARG
SEQRES 9 B 261 ALA SER PRO LEU TYR ASN LYS LEU ASP PRO SER LYS PHE
SEQRES 10 B 261 ALA LEU THR GLY PHE SER MET GLY GLY GLY GLY ALA LEU
SEQRES 11 B 261 LEU ALA ALA ALA ASP LEU GLY SER GLN VAL LYS VAL ALA
SEQRES 12 B 261 VAL PRO MET ALA PRO PHE LEU GLY SER ASN ASN PRO ASN
SEQRES 13 B 261 TYR SER ALA ILE THR ALA LYS VAL LEU ILE GLN ALA GLY
SEQRES 14 B 261 ALA ASN ASP THR VAL ALA ASN PRO SER THR VAL ALA SER
SEQRES 15 B 261 TYR TYR GLN SER LEU PRO THR GLY ILE SER ARG ALA LEU
SEQRES 16 B 261 THR THR PHE ARG SER ALA SER HIS LEU ASP TRP ILE ASN
SEQRES 17 B 261 THR GLY ASN THR ASN ARG GLN ALA ARG LEU LYS THR LEU
SEQRES 18 B 261 VAL THR SER TRP LEU LYS VAL TYR LEU ASP GLY ASN SER
SEQRES 19 B 261 ASP TYR ALA THR TYR LEU ASP GLY ALA GLU HIS SER ARG
SEQRES 20 B 261 HIS LEU ALA GLU ASP TRP PHE THR ARG PHE GLU TYR VAL
SEQRES 21 B 261 ARG
FORMUL 3 HOH *442(H2 O)
HELIX 1 AA1 THR A 77 GLN A 80 5 4
HELIX 2 AA2 MET A 81 HIS A 91 1 11
HELIX 3 AA3 ALA A 106 ARG A 127 1 22
HELIX 4 AA4 SER A 147 GLY A 161 1 15
HELIX 5 AA5 SER A 162 VAL A 164 5 3
HELIX 6 AA6 ASN A 180 ILE A 184 5 5
HELIX 7 AA7 ASN A 200 LEU A 211 1 12
HELIX 8 AA8 SER A 226 ILE A 231 5 6
HELIX 9 AA9 ASN A 235 LEU A 254 1 20
HELIX 10 AB1 ASN A 257 TYR A 260 5 4
HELIX 11 AB2 ALA A 261 GLY A 266 1 6
HELIX 12 AB3 GLY A 266 GLU A 275 1 10
HELIX 13 AB4 THR B 77 GLN B 80 5 4
HELIX 14 AB5 MET B 81 HIS B 91 1 11
HELIX 15 AB6 ALA B 106 ARG B 127 1 22
HELIX 16 AB7 SER B 147 GLY B 161 1 15
HELIX 17 AB8 SER B 162 VAL B 164 5 3
HELIX 18 AB9 ASN B 180 ILE B 184 5 5
HELIX 19 AC1 ASN B 200 GLN B 209 1 10
HELIX 20 AC2 SER B 226 ILE B 231 5 6
HELIX 21 AC3 ASN B 235 LEU B 254 1 20
HELIX 22 AC4 ASN B 257 TYR B 260 5 4
HELIX 23 AC5 ALA B 261 GLY B 266 1 6
HELIX 24 AC6 GLY B 266 GLU B 275 1 10
SHEET 1 AA1 9 VAL A 37 TYR A 40 0
SHEET 2 AA1 9 TYR A 49 PRO A 57 -1 O TYR A 56 N CYS A 38
SHEET 3 AA1 9 ILE A 94 PRO A 100 -1 O THR A 99 N SER A 51
SHEET 4 AA1 9 TYR A 65 THR A 71 1 N LEU A 70 O ILE A 98
SHEET 5 AA1 9 LEU A 136 PHE A 146 1 O LYS A 140 N ALA A 67
SHEET 6 AA1 9 VAL A 166 MET A 170 1 O MET A 170 N GLY A 145
SHEET 7 AA1 9 LYS A 187 GLY A 193 1 O GLN A 191 N PRO A 169
SHEET 8 AA1 9 ARG A 217 PHE A 222 1 O ALA A 218 N ILE A 190
SHEET 9 AA1 9 PHE A 278 VAL A 284 -1 O VAL A 284 N ARG A 217
SHEET 1 AA2 9 VAL B 37 TYR B 40 0
SHEET 2 AA2 9 TYR B 49 PRO B 57 -1 O TYR B 56 N CYS B 38
SHEET 3 AA2 9 ILE B 94 PRO B 100 -1 O THR B 99 N SER B 51
SHEET 4 AA2 9 TYR B 65 THR B 71 1 N LEU B 70 O ILE B 98
SHEET 5 AA2 9 LEU B 136 PHE B 146 1 O ASP B 137 N TYR B 65
SHEET 6 AA2 9 VAL B 166 MET B 170 1 O MET B 170 N GLY B 145
SHEET 7 AA2 9 LYS B 187 GLY B 193 1 O GLN B 191 N PRO B 169
SHEET 8 AA2 9 ARG B 217 PHE B 222 1 O ALA B 218 N ILE B 190
SHEET 9 AA2 9 PHE B 278 VAL B 284 -1 O VAL B 284 N ARG B 217
SSBOND 1 CYS A 38 CYS A 58 1555 1555 2.05
SSBOND 2 CYS B 38 CYS B 58 1555 1555 2.04
CRYST1 55.343 91.170 99.522 90.00 90.00 90.00 P 21 21 21 8
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 0.018069 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010969 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010048 0.00000
TER 1980 ARG A 285
TER 3954 ARG B 285
MASTER 247 0 0 24 18 0 0 6 4394 2 4 42
END |