HEADER HORMONE/GROWTH FACTOR 23-JUL-01 1JNE
TITLE CRYSTAL STRUCTURE OF IMAGINAL DISC GROWTH FACTOR-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IMAGINAL DISC GROWTH FACTOR-2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: IMAGINAL DISC GROWTH FACTOR-2
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227
KEYWDS IDGF, IMAGINAL DISC, GROWTH FACTOR, CHITINASE, INSULIN RECEPTOR,
KEYWDS 2 HEPARIN, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.F.VARELA,A.S.LLERA,R.A.MARIUZZA,J.TORMO
REVDAT 6 16-AUG-23 1JNE 1 REMARK HETSYN
REVDAT 5 29-JUL-20 1JNE 1 COMPND REMARK SEQADV HETNAM
REVDAT 5 2 1 LINK SITE ATOM
REVDAT 4 13-JUL-11 1JNE 1 VERSN
REVDAT 3 24-FEB-09 1JNE 1 VERSN
REVDAT 2 01-APR-03 1JNE 1 JRNL
REVDAT 1 01-MAY-02 1JNE 0
JRNL AUTH P.F.VARELA,A.S.LLERA,R.A.MARIUZZA,J.TORMO
JRNL TITL CRYSTAL STRUCTURE OF IMAGINAL DISC GROWTH FACTOR-2. A MEMBER
JRNL TITL 2 OF A NEW FAMILY OF GROWTH-PROMOTING GLYCOPROTEINS FROM
JRNL TITL 3 DROSOPHILA MELANOGASTER.
JRNL REF J.BIOL.CHEM. V. 277 13229 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 11821393
JRNL DOI 10.1074/JBC.M110502200
REMARK 2
REMARK 2 RESOLUTION. 1.70 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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.9
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.195
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 4114
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 40966
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 : 3166
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 382
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) : 0.006
REMARK 3 ANGLE DISTANCES (A) : 1.540
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : NULL
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 1JNE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-01.
REMARK 100 THE DEPOSITION ID IS D_1000013969.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAY-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.927
REMARK 200 MONOCHROMATOR : BENT CRYSTAL GERMANIUM
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
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 : 40966
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 1.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.84
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.27400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.050
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1CTN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, TRIS, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING 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 24.76000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.89000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.08500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.89000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.76000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.08500
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 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 ALA A 1
REMARK 465 HIS A 142
REMARK 465 GLY A 143
REMARK 465 ASP A 144
REMARK 465 LEU A 145
REMARK 465 GLY A 146
REMARK 465 LEU A 147
REMARK 465 ALA A 148
REMARK 465 TRP A 149
REMARK 465 LYS A 150
REMARK 465 SER A 151
REMARK 465 ILE A 152
REMARK 465 LYS A 153
REMARK 465 LYS A 154
REMARK 465 LEU A 155
REMARK 465 PHE A 156
REMARK 465 THR A 157
REMARK 465 GLY A 158
REMARK 465 ASP A 159
REMARK 465 PHE A 160
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 SER A 326 CB OG
REMARK 480 ASN A 327 CB CG OD1 ND2
REMARK 480 GLN A 329 CB CG CD OE1 NE2
REMARK 480 PHE A 332 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 480 ARG A 341 CB CG CD NE CZ NH1 NH2
REMARK 480 TYR A 355 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 480 TYR A 355 OH
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 O HOH A 1039 O HOH A 1161 1.39
REMARK 500 O HOH A 1071 O HOH A 1419 1.49
REMARK 500 O HOH A 1208 O HOH A 1351 1.55
REMARK 500 NH1 ARG A 341 O HOH A 1182 1.58
REMARK 500 O HOH A 1406 O HOH A 1407 1.74
REMARK 500 O3 BMA B 3 C2 MAN B 4 1.78
REMARK 500 OH TYR A 418 O HOH A 1347 1.89
REMARK 500 C3 BMA B 3 C1 MAN B 4 1.93
REMARK 500 NH2 ARG A 341 CG PRO A 357 2.00
REMARK 500 O LYS A 348 ND2 ASN A 378 2.02
REMARK 500 O HOH A 1320 O HOH A 1334 2.04
REMARK 500 O4 NAG B 1 O5 NAG B 2 2.04
REMARK 500 OD1 ASP A 163 O HOH A 1390 2.07
REMARK 500 O HOH A 1122 O HOH A 1253 2.07
REMARK 500 OD1 ASN A 327 O HOH A 1435 2.09
REMARK 500 O HOH A 1011 O HOH A 1316 2.09
REMARK 500 O4 NAG B 2 O5 BMA B 3 2.09
REMARK 500 CD2 PHE A 32 O HOH A 1138 2.10
REMARK 500 O GLU A 260 OG SER A 264 2.10
REMARK 500 O SER A 246 O HOH A 1238 2.11
REMARK 500 O GLY A 335 OG SER A 338 2.11
REMARK 500 O GLU A 66 O HOH A 1153 2.15
REMARK 500 O HOH A 1166 O HOH A 1177 2.16
REMARK 500 O3 BMA B 3 C3 MAN B 4 2.17
REMARK 500 O HOH A 1350 O HOH A 1421 2.17
REMARK 500 NZ LYS A 409 O HOH A 1098 2.18
REMARK 500 NH2 ARG A 341 CD PRO A 357 2.18
REMARK 500 OH TYR A 236 O HOH A 1093 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 OD2 ASP A 215 O HOH A 1203 4555 2.16
REMARK 500 O HOH A 1193 O HOH A 1432 1655 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 LEU A 420 C LEU A 420 OXT 0.462
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 ARG A 342 CD - NE - CZ ANGL. DEV. = 22.6 DEGREES
REMARK 500 ARG A 342 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG A 342 NE - CZ - NH2 ANGL. DEV. = -3.0 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 ASN A 47 5.11 -156.39
REMARK 500 ASN A 54 69.83 -154.01
REMARK 500 ALA A 238 52.10 -155.00
REMARK 500 ASP A 359 117.26 -169.30
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1JNE A 1 420 GB 4092089 AAC99418 21 440
SEQADV 1JNE PHE A 257 GB 4092089 VAL 277 CONFLICT
SEQRES 1 A 420 ALA SER ASN LEU VAL CYS TYR TYR ASP SER SER SER TYR
SEQRES 2 A 420 THR ARG GLU GLY LEU GLY LYS LEU LEU ASN PRO ASP LEU
SEQRES 3 A 420 GLU ILE ALA LEU GLN PHE CYS SER HIS LEU VAL TYR GLY
SEQRES 4 A 420 TYR ALA GLY LEU ARG GLY GLU ASN LEU GLN ALA TYR SER
SEQRES 5 A 420 MET ASN GLU ASN LEU ASP ILE TYR LYS HIS GLN PHE SER
SEQRES 6 A 420 GLU VAL THR SER LEU LYS ARG LYS TYR PRO HIS LEU LYS
SEQRES 7 A 420 VAL LEU LEU SER VAL GLY GLY ASP HIS ASP ILE ASP PRO
SEQRES 8 A 420 ASP HIS PRO ASN LYS TYR ILE ASP LEU LEU GLU GLY GLU
SEQRES 9 A 420 LYS VAL ARG GLN ILE GLY PHE ILE ARG SER ALA TYR GLU
SEQRES 10 A 420 LEU VAL LYS THR TYR GLY PHE ASP GLY LEU ASP LEU ALA
SEQRES 11 A 420 TYR GLN PHE PRO LYS ASN LYS PRO ARG LYS VAL HIS GLY
SEQRES 12 A 420 ASP LEU GLY LEU ALA TRP LYS SER ILE LYS LYS LEU PHE
SEQRES 13 A 420 THR GLY ASP PHE ILE VAL ASP PRO HIS ALA ALA LEU HIS
SEQRES 14 A 420 LYS GLU GLN PHE THR ALA LEU VAL ARG ASP VAL LYS ASP
SEQRES 15 A 420 SER LEU ARG ALA ASP GLY PHE LEU LEU SER LEU THR VAL
SEQRES 16 A 420 LEU PRO ASN VAL ASN SER THR TRP TYR PHE ASP ILE PRO
SEQRES 17 A 420 ALA LEU ASN GLY LEU VAL ASP PHE VAL ASN LEU ALA THR
SEQRES 18 A 420 PHE ASP PHE LEU THR PRO ALA ARG ASN PRO GLU GLU ALA
SEQRES 19 A 420 ASP TYR SER ALA PRO ILE TYR HIS PRO ASP GLY SER LYS
SEQRES 20 A 420 ASP ARG LEU ALA HIS LEU ASN ALA ASP PHE GLN VAL GLU
SEQRES 21 A 420 TYR TRP LEU SER GLN GLY PHE PRO SER ASN LYS ILE ASN
SEQRES 22 A 420 LEU GLY VAL ALA THR TYR GLY ASN ALA TRP LYS LEU THR
SEQRES 23 A 420 LYS ASP SER GLY LEU GLU GLY VAL PRO VAL VAL PRO GLU
SEQRES 24 A 420 THR SER GLY PRO ALA PRO GLU GLY PHE GLN SER GLN LYS
SEQRES 25 A 420 PRO GLY LEU LEU SER TYR ALA GLU ILE CYS GLY LYS LEU
SEQRES 26 A 420 SER ASN PRO GLN ASN GLN PHE LEU LYS GLY ASN GLU SER
SEQRES 27 A 420 PRO LEU ARG ARG VAL SER ASP PRO THR LYS ARG PHE GLY
SEQRES 28 A 420 GLY ILE ALA TYR ARG PRO VAL ASP GLY GLN ILE THR GLU
SEQRES 29 A 420 GLY ILE TRP VAL SER TYR ASP ASP PRO ASP SER ALA SER
SEQRES 30 A 420 ASN LYS ALA ALA TYR ALA ARG VAL LYS ASN LEU GLY GLY
SEQRES 31 A 420 VAL ALA LEU PHE ASP LEU SER TYR ASP ASP PHE ARG GLY
SEQRES 32 A 420 GLN CYS SER GLY ASP LYS TYR PRO ILE LEU ARG ALA ILE
SEQRES 33 A 420 LYS TYR ARG LEU
MODRES 1JNE ASN A 200 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET BMA B 3 11
HET MAN B 4 11
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
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
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 2 NAG 2(C8 H15 N O6)
FORMUL 2 BMA C6 H12 O6
FORMUL 2 MAN C6 H12 O6
FORMUL 3 HOH *382(H2 O)
HELIX 1 1 SER A 11 ARG A 15 5 5
HELIX 2 2 GLU A 16 LYS A 20 5 5
HELIX 3 3 LEU A 22 ALA A 29 1 8
HELIX 4 4 LEU A 30 PHE A 32 5 3
HELIX 5 5 ASN A 54 ILE A 59 1 6
HELIX 6 6 HIS A 62 SER A 69 1 8
HELIX 7 7 LEU A 70 LYS A 73 5 4
HELIX 8 8 ASN A 95 GLU A 102 1 8
HELIX 9 9 GLU A 104 TYR A 122 1 19
HELIX 10 10 HIS A 165 ARG A 185 1 21
HELIX 11 11 ASN A 200 PHE A 205 1 6
HELIX 12 12 ASP A 206 ASN A 211 1 6
HELIX 13 13 ASN A 254 GLN A 265 1 12
HELIX 14 14 PRO A 268 ASN A 270 5 3
HELIX 15 15 THR A 286 GLY A 290 5 5
HELIX 16 16 TYR A 318 GLY A 323 1 6
HELIX 17 17 PRO A 328 LEU A 333 5 6
HELIX 18 18 LYS A 334 SER A 338 5 5
HELIX 19 19 ASP A 372 LYS A 386 1 15
HELIX 20 20 ASP A 395 ASP A 399 5 5
HELIX 21 21 TYR A 410 LEU A 420 1 11
SHEET 1 A10 ALA A 50 SER A 52 0
SHEET 2 A10 HIS A 35 LEU A 43 -1 N GLY A 42 O TYR A 51
SHEET 3 A10 ASN A 3 ASP A 9 1 O LEU A 4 N HIS A 35
SHEET 4 A10 GLY A 390 PHE A 394 1 O VAL A 391 N VAL A 5
SHEET 5 A10 ILE A 272 ALA A 277 1 O ILE A 272 N GLY A 390
SHEET 6 A10 PHE A 216 LEU A 219 1 O VAL A 217 N ASN A 273
SHEET 7 A10 LEU A 190 VAL A 195 1 O LEU A 191 N PHE A 216
SHEET 8 A10 GLY A 126 ALA A 130 1 O LEU A 127 N SER A 192
SHEET 9 A10 LYS A 78 GLY A 84 1 O VAL A 79 N GLY A 126
SHEET 10 A10 HIS A 35 LEU A 43 1 O LEU A 36 N LEU A 80
SHEET 1 B 5 LEU A 315 SER A 317 0
SHEET 2 B 5 TYR A 279 LYS A 284 -1 N GLY A 280 O LEU A 316
SHEET 3 B 5 ILE A 366 TYR A 370 -1 O TRP A 367 N TRP A 283
SHEET 4 B 5 GLY A 352 ARG A 356 -1 O GLY A 352 N TYR A 370
SHEET 5 B 5 ARG A 341 VAL A 343 -1 N ARG A 341 O TYR A 355
SSBOND 1 CYS A 6 CYS A 33 1555 1555 2.02
SSBOND 2 CYS A 322 CYS A 405 1555 1555 2.02
LINK ND2 ASN A 200 C1 NAG B 1 1555 1555 1.47
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.30
LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.46
LINK O3 BMA B 3 C1 MAN B 4 1555 1555 1.30
CISPEP 1 GLY A 39 TYR A 40 0 -10.82
CISPEP 2 PRO A 295 VAL A 296 0 4.38
CISPEP 3 PHE A 394 ASP A 395 0 -12.57
CRYST1 49.520 72.170 105.780 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 0.020194 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013856 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009454 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
