HEADER HYDROLASE 16-NOV-13 3WMB
TITLE CRYSTAL STRUCTURE OF INSECT BETA-N-ACETYL-D-HEXOSAMINIDASE OFHEX1
TITLE 2 COMPLEXED WITH NAPHTHALIMIDE DERIVATIVE Q1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-HEXOSAMINIDASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.2.1.52;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OSTRINIA FURNACALIS;
SOURCE 3 ORGANISM_COMMON: ASIAN CORN BORER;
SOURCE 4 ORGANISM_TAXID: 93504;
SOURCE 5 GENE: OFHEX1;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 644223;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: GS115;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPIC9
KEYWDS CHITINASE, GLYCOSYL HYDROLASE, INSECT, OSTRINIA FURNACALIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.LIU,Y.ZHOU,L.CHEN,Q.YANG
REVDAT 3 08-NOV-23 3WMB 1 HETSYN
REVDAT 2 29-JUL-20 3WMB 1 COMPND REMARK SEQADV HETNAM
REVDAT 2 2 1 LINK SITE
REVDAT 1 05-NOV-14 3WMB 0
JRNL AUTH T.LIU,P.GUO,Y.ZHOU,J.WANG,L.CHEN,H.YANG,X.QIAN,Q.YANG
JRNL TITL A CRYSTAL STRUCTURE-GUIDED RATIONAL DESIGN SWITCHING
JRNL TITL 2 NON-CARBOHYDRATE INHIBITORS' SPECIFICITY BETWEEN TWO
JRNL TITL 3 BETA-GLCNACASE HOMOLOGS
JRNL REF SCI REP V. 4 6188 2014
JRNL REFN ESSN 2045-2322
JRNL PMID 25155420
JRNL DOI 10.1038/SREP06188
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.47
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.7
REMARK 3 NUMBER OF REFLECTIONS : 30268
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 1518
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 36.4721 - 5.9958 1.00 3019 158 0.1799 0.2112
REMARK 3 2 5.9958 - 4.7624 1.00 2903 157 0.1655 0.1641
REMARK 3 3 4.7624 - 4.1614 1.00 2855 149 0.1449 0.1862
REMARK 3 4 4.1614 - 3.7813 1.00 2840 157 0.1617 0.1742
REMARK 3 5 3.7813 - 3.5106 1.00 2836 142 0.1703 0.2041
REMARK 3 6 3.5106 - 3.3037 1.00 2836 168 0.1890 0.2352
REMARK 3 7 3.3037 - 3.1384 1.00 2811 130 0.2118 0.2510
REMARK 3 8 3.1384 - 3.0018 0.99 2803 139 0.2208 0.3009
REMARK 3 9 3.0018 - 2.8863 0.93 2610 148 0.2228 0.2957
REMARK 3 10 2.8863 - 2.7867 0.65 1816 87 0.2008 0.2115
REMARK 3 11 2.7867 - 2.6996 0.51 1421 83 0.2068 0.3195
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.450
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.79
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.81
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 : 0.008 4801
REMARK 3 ANGLE : 0.987 6526
REMARK 3 CHIRALITY : 0.075 685
REMARK 3 PLANARITY : 0.004 834
REMARK 3 DIHEDRAL : 14.782 1761
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 51.0371 -13.4378 17.0441
REMARK 3 T TENSOR
REMARK 3 T11: 0.0407 T22: -0.1415
REMARK 3 T33: 0.0281 T12: -0.0486
REMARK 3 T13: 0.0064 T23: 0.0212
REMARK 3 L TENSOR
REMARK 3 L11: -0.0061 L22: 0.0139
REMARK 3 L33: 0.0200 L12: -0.0132
REMARK 3 L13: -0.0008 L23: 0.0192
REMARK 3 S TENSOR
REMARK 3 S11: -0.1124 S12: 0.0197 S13: -0.0035
REMARK 3 S21: 0.0219 S22: 0.0972 S23: 0.0152
REMARK 3 S31: 0.1361 S32: 0.0248 S33: -0.0000
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 3WMB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-DEC-13.
REMARK 100 THE DEPOSITION ID IS D_1000096514.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33031
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 9.300
REMARK 200 R MERGE (I) : 0.13200
REMARK 200 R SYM (I) : 0.13200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.1200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.80
REMARK 200 R MERGE FOR SHELL (I) : 0.39700
REMARK 200 R SYM FOR SHELL (I) : 0.39700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.290
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: 3NSN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES, 100MM MGCL2, 30% PEG 400,
REMARK 280 PH 7.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 116.89733
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 58.44867
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 58.44867
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 116.89733
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 3.0 KCAL/MOL
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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 58.44867
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 86 40.95 -105.06
REMARK 500 PRO A 138 11.12 -66.56
REMARK 500 LYS A 141 23.45 -147.50
REMARK 500 ARG A 388 -5.81 86.69
REMARK 500 SER A 469 45.04 -143.84
REMARK 500 LEU A 510 -141.19 58.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3NSM RELATED DB: PDB
REMARK 900 RELATED ID: 3NSN RELATED DB: PDB
REMARK 900 RELATED ID: 3OZO RELATED DB: PDB
REMARK 900 RELATED ID: 3OZP RELATED DB: PDB
REMARK 900 RELATED ID: 3S6T RELATED DB: PDB
REMARK 900 RELATED ID: 3VTR RELATED DB: PDB
REMARK 900 RELATED ID: 3WMC RELATED DB: PDB
DBREF 3WMB A 23 594 UNP Q06GJ0 Q06GJ0_OSTFU 23 594
SEQADV 3WMB LEU A 243 UNP Q06GJ0 PHE 243 ENGINEERED MUTATION
SEQADV 3WMB PHE A 570 UNP Q06GJ0 LEU 570 ENGINEERED MUTATION
SEQRES 1 A 572 GLU ASP VAL VAL TRP ARG TRP SER CYS ASP ASN GLY LYS
SEQRES 2 A 572 CYS VAL LYS LEU LYS ASN ASP PRO ARG SER SER GLU PRO
SEQRES 3 A 572 ALA LEU SER LEU GLU ALA CYS LYS MET PHE CYS ASN GLU
SEQRES 4 A 572 TYR GLY LEU LEU TRP PRO ARG PRO THR GLY GLU ALA ASP
SEQRES 5 A 572 LEU GLY ASN PHE LEU SER LYS ILE ASN LEU ASN SER ILE
SEQRES 6 A 572 GLU VAL LYS ILE LEU LYS LYS GLY ALA THR ASP ASP LEU
SEQRES 7 A 572 MET GLU ALA ALA ALA LYS ARG PHE LYS GLU GLN VAL SER
SEQRES 8 A 572 LEU ALA ILE PRO ARG GLY SER THR PRO LYS LEU THR GLY
SEQRES 9 A 572 LYS ALA VAL ASP VAL TYR LEU VAL ASN GLU ASN PRO ASN
SEQRES 10 A 572 GLU LYS ALA PHE SER LEU GLU MET ASP GLU SER TYR GLY
SEQRES 11 A 572 LEU ARG VAL SER PRO SER GLY ALA ASP ARG VAL ASN ALA
SEQRES 12 A 572 THR ILE THR ALA ASN SER PHE PHE GLY MET ARG HIS GLY
SEQRES 13 A 572 LEU GLU THR LEU SER GLN LEU PHE VAL PHE ASP ASP ILE
SEQRES 14 A 572 ARG ASP HIS LEU LEU MET VAL ARG ASP VAL ASN ILE SER
SEQRES 15 A 572 ASP LYS PRO VAL TYR PRO TYR ARG GLY ILE LEU LEU ASP
SEQRES 16 A 572 THR ALA ARG ASN TYR TYR SER ILE GLU SER ILE LYS ARG
SEQRES 17 A 572 THR ILE GLU ALA MET ALA ALA VAL LYS LEU ASN THR LEU
SEQRES 18 A 572 HIS TRP HIS ILE THR ASP SER GLN SER PHE PRO PHE VAL
SEQRES 19 A 572 THR THR LYS ARG PRO ASN LEU TYR LYS PHE GLY ALA LEU
SEQRES 20 A 572 SER PRO GLN LYS VAL TYR THR LYS ALA ALA ILE ARG GLU
SEQRES 21 A 572 VAL VAL ARG PHE GLY LEU GLU ARG GLY VAL ARG VAL LEU
SEQRES 22 A 572 PRO GLU PHE ASP ALA PRO ALA HIS VAL GLY GLU GLY TRP
SEQRES 23 A 572 GLN ASP THR ASP LEU THR VAL CYS PHE LYS ALA GLU PRO
SEQRES 24 A 572 TRP LYS SER TYR CYS VAL GLU PRO PRO CYS GLY GLN LEU
SEQRES 25 A 572 ASN PRO THR LYS ASP GLU LEU TYR GLN TYR LEU GLU ASP
SEQRES 26 A 572 ILE TYR SER ASP MET ALA GLU VAL PHE ASP THR THR ASP
SEQRES 27 A 572 ILE PHE HIS MET GLY GLY ASP GLU VAL SER GLU ALA CYS
SEQRES 28 A 572 TRP ASN SER SER ASP SER ILE GLN ASN PHE MET MET GLN
SEQRES 29 A 572 ASN ARG TRP ASP LEU ASP LYS GLU SER PHE LEU LYS LEU
SEQRES 30 A 572 TRP ASN TYR PHE GLN GLN LYS ALA GLN ASP LYS ALA TYR
SEQRES 31 A 572 LYS ALA PHE GLY LYS LYS LEU PRO LEU ILE LEU TRP THR
SEQRES 32 A 572 SER THR LEU THR ASN TYR LYS HIS ILE ASP ASP TYR LEU
SEQRES 33 A 572 ASN LYS ASP ASP TYR ILE ILE GLN VAL TRP THR THR GLY
SEQRES 34 A 572 VAL ASP PRO GLN ILE LYS GLY LEU LEU GLU LYS GLY TYR
SEQRES 35 A 572 ARG LEU ILE MET SER ASN TYR ASP ALA LEU TYR PHE ASP
SEQRES 36 A 572 CYS GLY TYR GLY ALA TRP VAL GLY ALA GLY ASN ASN TRP
SEQRES 37 A 572 CYS SER PRO TYR ILE GLY TRP GLN LYS VAL TYR ASP ASN
SEQRES 38 A 572 SER PRO ALA VAL ILE ALA LEU GLU HIS ARG ASP GLN VAL
SEQRES 39 A 572 LEU GLY GLY GLU ALA ALA LEU TRP SER GLU GLN SER ASP
SEQRES 40 A 572 THR SER THR LEU ASP GLY ARG LEU TRP PRO ARG ALA ALA
SEQRES 41 A 572 ALA LEU ALA GLU ARG LEU TRP ALA GLU PRO ALA THR SER
SEQRES 42 A 572 TRP GLN ASP ALA GLU TYR ARG MET LEU HIS ILE ARG GLU
SEQRES 43 A 572 ARG PHE VAL ARG MET GLY ILE GLN ALA GLU SER LEU GLN
SEQRES 44 A 572 PRO GLU TRP CYS TYR GLN ASN GLU GLY TYR CYS TYR SER
MODRES 3WMB ASN A 375 ASN GLYCOSYLATION SITE
MODRES 3WMB ASN A 164 ASN GLYCOSYLATION SITE
HET NF1 A 601 25
HET NAG A 602 14
HET NAG A 603 14
HETNAM NF1 2-(2-{[(5-METHYL-1,3,4-THIADIAZOL-2-YL)
HETNAM 2 NF1 METHYL]AMINO}ETHYL)-1H-BENZO[DE]ISOQUINOLINE-1,3(2H)-
HETNAM 3 NF1 DIONE
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 NF1 C18 H16 N4 O2 S
FORMUL 3 NAG 2(C8 H15 N O6)
FORMUL 5 HOH *158(H2 O)
HELIX 1 1 SER A 51 ASN A 60 1 10
HELIX 2 2 THR A 97 SER A 113 1 17
HELIX 3 3 LEU A 114 ILE A 116 5 3
HELIX 4 4 SER A 171 GLN A 184 1 14
HELIX 5 5 SER A 224 VAL A 238 1 15
HELIX 6 6 PRO A 261 ALA A 268 1 8
HELIX 7 7 THR A 276 GLU A 289 1 14
HELIX 8 8 PRO A 321 TYR A 325 5 5
HELIX 9 9 LYS A 338 PHE A 356 1 19
HELIX 10 10 SER A 370 SER A 376 1 7
HELIX 11 11 SER A 377 GLN A 386 1 10
HELIX 12 12 ASP A 392 GLY A 416 1 25
HELIX 13 13 HIS A 433 TYR A 437 5 5
HELIX 14 14 ASP A 453 LYS A 462 1 10
HELIX 15 15 ASN A 470 TYR A 475 1 6
HELIX 16 16 GLY A 496 ASN A 503 1 8
HELIX 17 17 SER A 504 LEU A 510 1 7
HELIX 18 18 GLU A 511 ASP A 514 5 4
HELIX 19 19 THR A 532 TRP A 538 1 7
HELIX 20 20 PRO A 539 GLU A 551 1 13
HELIX 21 21 SER A 555 ASP A 558 5 4
HELIX 22 22 ALA A 559 MET A 573 1 15
HELIX 23 23 PRO A 582 ASN A 588 1 7
SHEET 1 A 2 TRP A 27 ASP A 32 0
SHEET 2 A 2 LYS A 35 LYS A 40 -1 O LEU A 39 N ARG A 28
SHEET 1 B 8 ALA A 73 ASP A 74 0
SHEET 2 B 8 VAL A 201 ASP A 205 -1 O ASN A 202 N ASP A 74
SHEET 3 B 8 TYR A 151 SER A 158 -1 N LEU A 153 O ILE A 203
SHEET 4 B 8 ARG A 162 ALA A 169 -1 O ARG A 162 N SER A 158
SHEET 5 B 8 LYS A 127 ASN A 135 1 N TYR A 132 O ALA A 165
SHEET 6 B 8 LEU A 79 ILE A 91 1 N LYS A 90 O VAL A 131
SHEET 7 B 8 HIS A 194 VAL A 198 -1 O LEU A 195 N ILE A 82
SHEET 8 B 8 PHE A 186 ASP A 189 -1 N ASP A 189 O HIS A 194
SHEET 1 C 9 TYR A 211 ASP A 217 0
SHEET 2 C 9 THR A 242 HIS A 246 1 O HIS A 244 N ILE A 214
SHEET 3 C 9 ARG A 293 ALA A 300 1 O ARG A 293 N LEU A 243
SHEET 4 C 9 PHE A 362 GLY A 365 1 O HIS A 363 N PHE A 298
SHEET 5 C 9 LEU A 421 TRP A 424 1 O ILE A 422 N MET A 364
SHEET 6 C 9 TYR A 443 VAL A 447 1 O ILE A 444 N LEU A 421
SHEET 7 C 9 ARG A 465 MET A 468 1 O ILE A 467 N VAL A 447
SHEET 8 C 9 VAL A 516 LEU A 523 1 O GLY A 518 N MET A 468
SHEET 9 C 9 TYR A 211 ASP A 217 1 N LEU A 215 O ALA A 521
SHEET 1 D 2 THR A 314 VAL A 315 0
SHEET 2 D 2 GLN A 333 LEU A 334 -1 O GLN A 333 N VAL A 315
SSBOND 1 CYS A 31 CYS A 59 1555 1555 2.05
SSBOND 2 CYS A 36 CYS A 55 1555 1555 2.08
SSBOND 3 CYS A 316 CYS A 373 1555 1555 2.04
SSBOND 4 CYS A 326 CYS A 331 1555 1555 2.04
SSBOND 5 CYS A 478 CYS A 491 1555 1555 2.05
SSBOND 6 CYS A 585 CYS A 592 1555 1555 2.05
LINK ND2 ASN A 164 C1 NAG A 602 1555 1555 1.44
LINK ND2 ASN A 375 C1 NAG A 603 1555 1555 1.44
CISPEP 1 TRP A 66 PRO A 67 0 -1.36
CISPEP 2 ALA A 300 PRO A 301 0 0.83
CISPEP 3 GLU A 320 PRO A 321 0 -0.32
CISPEP 4 PRO A 329 PRO A 330 0 -3.64
CISPEP 5 SER A 492 PRO A 493 0 4.60
CISPEP 6 TRP A 538 PRO A 539 0 4.41
CRYST1 107.773 107.773 175.346 90.00 90.00 120.00 P 32 2 1 6
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 0.009279 0.005357 0.000000 0.00000
SCALE2 0.000000 0.010714 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005703 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
