HEADER HYDROLASE, ALLERGEN 04-JAN-05 1YG9
TITLE THE STRUCTURE OF MUTANT (N93Q) OF BLA G 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASPARTIC PROTEASE BLA G 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: NIG2;
COMPND 5 SYNONYM: ALLERGEN BLA G II;
COMPND 6 EC: 3.4.23.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BLATTELLA GERMANICA;
SOURCE 3 ORGANISM_COMMON: GERMAN COCKROACH;
SOURCE 4 ORGANISM_TAXID: 6973;
SOURCE 5 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: GS115;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGAPZAC
KEYWDS BLA G 2, ALLEGREN, HYDROLASE, ALLERGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.LI,A.GUSTCHINA,S.WUENSCHMANN,A.POMES,A.WLODAWER
REVDAT 7 20-OCT-21 1YG9 1 REMARK SEQADV HETSYN SHEET
REVDAT 6 29-JUL-20 1YG9 1 COMPND REMARK SEQADV HETNAM
REVDAT 6 2 1 LINK SITE ATOM
REVDAT 5 13-JUL-11 1YG9 1 VERSN
REVDAT 4 24-FEB-09 1YG9 1 VERSN
REVDAT 3 09-MAY-06 1YG9 1 JRNL
REVDAT 2 17-JAN-06 1YG9 1 JRNL
REVDAT 1 22-MAR-05 1YG9 0
JRNL AUTH A.GUSTCHINA,M.LI,S.WUENSCHMANN,M.D.CHAPMAN,A.POMES,
JRNL AUTH 2 A.WLODAWER
JRNL TITL CRYSTAL STRUCTURE OF COCKROACH ALLERGEN BLA G 2, AN UNUSUAL
JRNL TITL 2 ZINC BINDING ASPARTIC PROTEASE WITH A NOVEL MODE OF
JRNL TITL 3 SELF-INHIBITION.
JRNL REF J.MOL.BIOL. V. 348 433 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 15811379
JRNL DOI 10.1016/J.JMB.2005.02.062
REMARK 2
REMARK 2 RESOLUTION. 1.30 ANGSTROMS.
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) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 3 CROSS-VALIDATION METHOD : FREE R
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) : 0.181
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.180
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 4622
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 87692
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.159
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.159
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 3539
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 67631
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2547
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 478
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 3059.5
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 8
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 12361
REMARK 3 NUMBER OF RESTRAINTS : 10762
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 ANGLE DISTANCES (A) : 0.029
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.031
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.073
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.078
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.047
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.000
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.060
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ANISOTROPIC SCALING APPLIED BY THE
REMARK 3 METHOD OF PARKIN, MOEZZI & HOPE, J.APPL.CRYST.28(1995)53-56
REMARK 4
REMARK 4 1YG9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1000031479.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-MAR-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 94652
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.49400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: AB INITIO
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG8K, 10MM DTT AND 0.2M
REMARK 280 MGACETATE, PH 5.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
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 X+1/2,Y+1/2,Z
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 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 70.80000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 19.30000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 70.80000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 19.30000
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, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1262 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1273 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1341 LIES ON A SPECIAL POSITION.
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 N2 NAG A 601 O HOH A 1149 2.16
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PHE A 75A CB - CG - CD1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 PHE A 140 CB - CG - CD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 VAL A 150 CG1 - CB - CG2 ANGL. DEV. = -14.7 DEGREES
REMARK 500 ARG A 157 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 193 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 265 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 TYR A 274 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 TYR A 274 CB - CG - CD1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 PHE A 305 CB - CG - CD1 ANGL. DEV. = -5.5 DEGREES
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 ASP A 76 -51.82 68.86
REMARK 500 SER A 92 -128.25 51.85
REMARK 500 ILE A 220 -162.97 -126.60
REMARK 500 ARG A 242C -178.15 175.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 NAG A 601
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 155 ND1
REMARK 620 2 HIS A 161 NE2 97.6
REMARK 620 3 ASP A 303 OD1 98.4 117.9
REMARK 620 4 ASP A 307 OD1 110.9 123.1 105.6
REMARK 620 N 1 2 3
DBREF 1YG9 A 0 325 UNP P54958 ASP2_BLAGE 25 350
SEQADV 1YG9 GLY A -8 UNP P54958 CLONING ARTIFACT
SEQADV 1YG9 ALA A -7 UNP P54958 CLONING ARTIFACT
SEQADV 1YG9 SER A -6 UNP P54958 CLONING ARTIFACT
SEQADV 1YG9 ILE A -5 UNP P54958 CLONING ARTIFACT
SEQADV 1YG9 GLN A 93 UNP P54958 ASN 117 ENGINEERED MUTATION
SEQADV 1YG9 CSX A 289 UNP P54958 CYS 316 MODIFIED RESIDUE
SEQRES 1 A 330 GLY ALA SER ILE VAL PRO LEU TYR LYS LEU VAL HIS VAL
SEQRES 2 A 330 PHE ILE ASN THR GLN TYR ALA GLY ILE THR LYS ILE GLY
SEQRES 3 A 330 ASN GLN ASN PHE LEU THR VAL PHE ASP SER THR SER CYS
SEQRES 4 A 330 ASN VAL VAL VAL ALA SER GLN GLU CYS VAL GLY GLY ALA
SEQRES 5 A 330 CYS VAL CYS PRO ASN LEU GLN LYS TYR GLU LYS LEU LYS
SEQRES 6 A 330 PRO LYS TYR ILE SER ASP GLY ASN VAL GLN VAL LYS PHE
SEQRES 7 A 330 PHE ASP THR GLY SER ALA VAL GLY ARG GLY ILE GLU ASP
SEQRES 8 A 330 SER LEU THR ILE SER GLN LEU THR THR SER GLN GLN ASP
SEQRES 9 A 330 ILE VAL LEU ALA ASP GLU LEU SER GLN GLU VAL CYS ILE
SEQRES 10 A 330 LEU SER ALA ASP VAL VAL VAL GLY ILE ALA ALA PRO GLY
SEQRES 11 A 330 CYS PRO ASN ALA LEU LYS GLY LYS THR VAL LEU GLU ASN
SEQRES 12 A 330 PHE VAL GLU GLU ASN LEU ILE ALA PRO VAL PHE SER ILE
SEQRES 13 A 330 HIS HIS ALA ARG PHE GLN ASP GLY GLU HIS PHE GLY GLU
SEQRES 14 A 330 ILE ILE PHE GLY GLY SER ASP TRP LYS TYR VAL ASP GLY
SEQRES 15 A 330 GLU PHE THR TYR VAL PRO LEU VAL GLY ASP ASP SER TRP
SEQRES 16 A 330 LYS PHE ARG LEU ASP GLY VAL LYS ILE GLY ASP THR THR
SEQRES 17 A 330 VAL ALA PRO ALA GLY THR GLN ALA ILE ILE ASP THR SER
SEQRES 18 A 330 LYS ALA ILE ILE VAL GLY PRO LYS ALA TYR VAL ASN PRO
SEQRES 19 A 330 ILE ASN GLU ALA ILE GLY CYS VAL VAL GLU LYS THR THR
SEQRES 20 A 330 THR ARG ARG ILE CYS LYS LEU ASP CYS SER LYS ILE PRO
SEQRES 21 A 330 SER LEU PRO ASP VAL THR PHE VAL ILE ASN GLY ARG ASN
SEQRES 22 A 330 PHE ASN ILE SER SER GLN TYR TYR ILE GLN GLN ASN GLY
SEQRES 23 A 330 ASN LEU CYS TYR SER GLY PHE GLN PRO CSX GLY HIS SER
SEQRES 24 A 330 ASP HIS PHE PHE ILE GLY ASP PHE PHE VAL ASP HIS TYR
SEQRES 25 A 330 TYR SER GLU PHE ASN TRP GLU ASN LYS THR MET GLY PHE
SEQRES 26 A 330 GLY ARG SER VAL GLU
MODRES 1YG9 ASN A 268 ASN GLYCOSYLATION SITE
MODRES 1YG9 ASN A 317 ASN GLYCOSYLATION SITE
MODRES 1YG9 CSX A 289 CYS S-OXY CYSTEINE
HET CSX A 289 7
HET NAG B 1 14
HET NAG B 2 14
HET NAG A 601 14
HET ZN A 401 1
HETNAM CSX S-OXY CYSTEINE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM ZN ZINC ION
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 1 CSX C3 H7 N O3 S
FORMUL 2 NAG 3(C8 H15 N O6)
FORMUL 4 ZN ZN 2+
FORMUL 5 HOH *478(H2 O)
HELIX 1 1 GLY A 47 CYS A 51A 5 6
HELIX 2 2 GLN A 110 LEU A 115 1 6
HELIX 3 3 THR A 135 GLU A 143 1 9
HELIX 4 4 ASP A 171 LYS A 173 5 3
HELIX 5 5 LYS A 225 GLY A 236 1 12
HELIX 6 6 ASP A 248 LEU A 255 5 8
HELIX 7 7 SER A 270 TYR A 274 1 5
HELIX 8 8 GLY A 302 ASP A 307 1 6
SHEET 1 A 6 VAL A 2 ILE A 6 0
SHEET 2 A 6 HIS A 161 PHE A 167 -1 O GLY A 163 N ILE A 6
SHEET 3 A 6 VAL A 150 ARG A 157 -1 N SER A 152 O ILE A 166
SHEET 4 A 6 TYR A 309 ASN A 314 -1 O PHE A 313 N PHE A 151
SHEET 5 A 6 THR A 319 SER A 325 -1 O GLY A 321 N GLU A 312
SHEET 6 A 6 VAL A 175 PRO A 183 -1 N ASP A 176 O ARG A 324
SHEET 1 B 9 LYS A 65 TYR A 66 0
SHEET 2 B 9 VAL A 71 PHE A 75 0
SHEET 3 B 9 ALA A 15 ILE A 20 0
SHEET 4 B 9 GLN A 25 ASP A 32 -1 O THR A 29 N GLY A 16
SHEET 5 B 9 VAL A 119 GLY A 122 1 O VAL A 121 N VAL A 30
SHEET 6 B 9 VAL A 38 ALA A 41 -1 N VAL A 39 O VAL A 120
SHEET 7 B 9 LEU A 94 LEU A 107 1 O VAL A 102 N VAL A 38
SHEET 8 B 9 GLY A 78 ILE A 91 -1 N ARG A 83 O LEU A 103
SHEET 9 B 9 VAL A 71 PHE A 75 -1 N VAL A 71 O GLY A 82
SHEET 1 C 5 PHE A 192 ARG A 193 0
SHEET 2 C 5 GLN A 211 ILE A 214 -1 O ALA A 212 N PHE A 192
SHEET 3 C 5 PHE A 299 ILE A 301 1 O ILE A 301 N ILE A 213
SHEET 4 C 5 ILE A 221 PRO A 224 -1 N VAL A 222 O PHE A 300
SHEET 5 C 5 PHE A 286 CSX A 289 1 O GLN A 287 N ILE A 221
SHEET 1 D 4 THR A 202 ALA A 205 0
SHEET 2 D 4 GLY A 196 ILE A 199 -1 N VAL A 197 O VAL A 204
SHEET 3 D 4 VAL A 258 ILE A 262 -1 O VAL A 261 N GLY A 196
SHEET 4 D 4 ARG A 265 ILE A 269 -1 O PHE A 267 N PHE A 260
SHEET 1 E 3 VAL A 238 LYS A 241 0
SHEET 2 E 3 LEU A 281 SER A 284 -1 O SER A 284 N CYS A 245
SHEET 3 E 3 ILE A 275 ASN A 278 -1 N GLN A 276 O TYR A 283
SSBOND 1 CYS A 36 CYS A 127 1555 1555 2.01
SSBOND 2 CYS A 45 CYS A 50 1555 1555 2.04
SSBOND 3 CYS A 51A CYS A 113 1555 1555 2.00
SSBOND 4 CYS A 237 CYS A 245 1555 1555 2.10
SSBOND 5 CYS A 249 CYS A 282 1555 1555 2.05
LINK ND2 ASN A 268 C1 NAG B 1 1555 1555 1.46
LINK C PRO A 288 N CSX A 289 1555 1555 1.32
LINK C CSX A 289 N GLY A 290 1555 1555 1.33
LINK ND2 ASN A 317 C1 NAG A 601 1555 1555 1.48
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.43
LINK ND1 HIS A 155 ZN ZN A 401 1555 1555 2.05
LINK NE2 HIS A 161 ZN ZN A 401 1555 1555 1.97
LINK OD1 ASP A 303 ZN ZN A 401 1555 1555 1.95
LINK OD1 ASP A 307 ZN ZN A 401 1555 1555 1.91
CRYST1 141.600 38.600 71.500 90.00 100.90 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 0.007062 0.000000 0.001360 0.00000
SCALE2 0.000000 0.025907 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014243 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
