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HEADER HYDROLASE 19-APR-23 8J45
TITLE CRYSTAL STRUCTURE OF A PICHIA PASTORIS-EXPRESSED ISPETASE VARIANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PET HYDROLASE,PETASE,PET-DIGESTING ENZYME;
COMPND 5 EC: 3.1.1.101;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS;
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 GENE: ISF6_4831;
SOURCE 5 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS PET HYDROLASE, ALPHA/BETA HYDROLASE, IDEONELLA SAKAIENSIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.LI,H.L.HE,X.LONG,D.NIU,J.-W.HUANG,C.-C.CHEN,R.-T.GUO
REVDAT 1 17-JAN-24 8J45 0
JRNL AUTH C.C.CHEN,X.LI,J.MIN,Z.ZENG,Z.NING,H.HE,X.LONG,D.NIU,R.PENG,
JRNL AUTH 2 X.LIU,Y.YANG,J.W.HUANG,R.T.GUO
JRNL TITL COMPLETE DECOMPOSITION OF POLY(ETHYLENE TEREPHTHALATE) BY
JRNL TITL 2 CRUDE PET HYDROLYTIC ENZYME PRODUCED IN PICHIA PASTORIS
JRNL REF CHEM ENG J 48418 2023
JRNL REFN ISSN 1873-3212
JRNL DOI 10.1016/J.CEJ.2023.148418
REMARK 2
REMARK 2 RESOLUTION. 1.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.21
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 33672
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 + TEST SET) : 0.137
REMARK 3 R VALUE (WORKING SET) : 0.136
REMARK 3 FREE R VALUE : 0.160
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1766
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) : 1.49
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.53
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2408
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.94
REMARK 3 BIN R VALUE (WORKING SET) : 0.1440
REMARK 3 BIN FREE R VALUE SET COUNT : 135
REMARK 3 BIN FREE R VALUE : 0.1890
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1937
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 348
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 9.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.07000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : -0.09000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.065
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.065
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.034
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.884
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2064 ; 0.015 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 1804 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2826 ; 1.986 ; 1.683
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4214 ; 1.676 ; 1.601
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 270 ; 6.663 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 89 ;31.178 ;22.135
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 294 ;11.161 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;18.063 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 290 ; 0.106 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2367 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 431 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1059 ; 0.859 ; 0.825
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1058 ; 0.859 ; 0.824
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1324 ; 1.300 ; 1.238
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1325 ; 1.300 ; 1.239
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1005 ; 1.695 ; 1.059
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1006 ; 1.694 ; 1.062
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1499 ; 2.522 ; 1.533
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2425 ; 4.009 ;12.148
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2333 ; 3.659 ;11.137
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 8J45 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-MAY-23.
REMARK 100 THE DEPOSITION ID IS D_1300037169.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-OCT-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : LIQUID ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : BRUKER METALJET
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.34138
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : BRUKER PHOTON III
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SAINT
REMARK 200 DATA SCALING SOFTWARE : SAINT
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35713
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.490
REMARK 200 RESOLUTION RANGE LOW (A) : 36.210
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 11.00
REMARK 200 R MERGE (I) : 0.04280
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 38.8200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.51
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.08880
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 11.47
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CHLORIDE, 0.1M SODIUM
REMARK 280 FORMATE, 0.1M BIS-TRIS PROPANE PH 8.5, 25% V/V PEG SMEAR MEDIUM,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 25.53700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.26950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.63550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.26950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.53700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 25.63550
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: MONOMERIC
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 DISTANCE
REMARK 500 ND2 ASN A 114 O5 NAG A 301 2.16
REMARK 500
REMARK 500 REMARK: NULL
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 ASN A 73 34.55 -145.18
REMARK 500 THR A 88 -7.14 75.23
REMARK 500 SER A 160 -121.64 65.14
REMARK 500 SER A 214 -85.76 -128.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 123 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 8J45 A 30 290 UNP PETH_IDESA
DBREF2 8J45 A A0A0K8P6T7 30 290
SEQADV 8J45 GLU A 28 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J45 PHE A 29 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J45 GLU A 121 UNP A0A0K8P6T SER 121 ENGINEERED MUTATION
SEQADV 8J45 HIS A 186 UNP A0A0K8P6T ASP 186 ENGINEERED MUTATION
SEQADV 8J45 GLN A 224 UNP A0A0K8P6T ARG 224 ENGINEERED MUTATION
SEQADV 8J45 LYS A 233 UNP A0A0K8P6T ASN 233 ENGINEERED MUTATION
SEQADV 8J45 ALA A 280 UNP A0A0K8P6T ARG 280 ENGINEERED MUTATION
SEQRES 1 A 263 GLU PHE ASN PRO TYR ALA ARG GLY PRO ASN PRO THR ALA
SEQRES 2 A 263 ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL ARG
SEQRES 3 A 263 SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA GLY
SEQRES 4 A 263 THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL GLY
SEQRES 5 A 263 ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN SER
SEQRES 6 A 263 SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS GLY
SEQRES 7 A 263 PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU ASP
SEQRES 8 A 263 GLN PRO GLU SER ARG SER SER GLN GLN MET ALA ALA LEU
SEQRES 9 A 263 ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER PRO
SEQRES 10 A 263 ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL MET
SEQRES 11 A 263 GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER ALA
SEQRES 12 A 263 ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN ALA
SEQRES 13 A 263 PRO TRP HIS SER SER THR ASN PHE SER SER VAL THR VAL
SEQRES 14 A 263 PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE ALA
SEQRES 15 A 263 PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER MET
SEQRES 16 A 263 SER GLN ASN ALA LYS GLN PHE LEU GLU ILE LYS GLY GLY
SEQRES 17 A 263 SER HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN ALA
SEQRES 18 A 263 LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG PHE
SEQRES 19 A 263 MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS GLU
SEQRES 20 A 263 ASN PRO ASN SER THR ALA VAL SER ASP PHE ARG THR ALA
SEQRES 21 A 263 ASN CYS SER
HET NAG A 301 14
HET NAG A 302 14
HET NAG A 303 14
HET NAG A 304 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 2 NAG 4(C8 H15 N O6)
FORMUL 6 HOH *348(H2 O)
HELIX 1 AA1 THR A 39 ALA A 45 1 7
HELIX 2 AA2 ARG A 90 LYS A 95 5 6
HELIX 3 AA3 TRP A 96 PHE A 106 1 11
HELIX 4 AA4 GLN A 119 GLY A 139 1 21
HELIX 5 AA5 SER A 160 ASN A 173 1 14
HELIX 6 AA6 SER A 214 MET A 222 1 9
HELIX 7 AA7 ASN A 246 ASP A 263 1 18
HELIX 8 AA8 ASP A 265 ARG A 267 5 3
HELIX 9 AA9 TYR A 268 GLU A 274 1 7
SHEET 1 AA1 6 VAL A 52 THR A 56 0
SHEET 2 AA1 6 ALA A 65 PRO A 71 -1 O VAL A 68 N PHE A 55
SHEET 3 AA1 6 VAL A 107 ASP A 112 -1 O VAL A 108 N TYR A 69
SHEET 4 AA1 6 VAL A 78 VAL A 84 1 N ILE A 81 O ILE A 109
SHEET 5 AA1 6 VAL A 149 GLY A 158 1 O ASP A 150 N VAL A 78
SHEET 6 AA1 6 ALA A 178 ALA A 179 1 O ALA A 178 N VAL A 156
SHEET 1 AA2 3 THR A 198 CYS A 203 0
SHEET 2 AA2 3 LYS A 227 ILE A 232 1 O GLN A 228 N ILE A 200
SHEET 3 AA2 3 VAL A 281 ALA A 287 -1 O ASP A 283 N GLU A 231
SSBOND 1 CYS A 203 CYS A 239 1555 1555 2.05
SSBOND 2 CYS A 273 CYS A 289 1555 1555 2.08
LINK ND2 ASN A 114 C1 NAG A 301 1555 1555 1.40
LINK ND2 ASN A 138 C1 NAG A 302 1555 1555 1.50
LINK ND2 ASN A 190 C1 NAG A 304 1555 1555 1.42
LINK ND2 ASN A 277 C1 NAG A 303 1555 1555 1.41
CRYST1 51.074 51.271 84.539 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 0.019579 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019504 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011829 0.00000
TER 1952 SER A 290
MASTER 282 0 4 9 9 0 0 6 2341 1 64 21
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