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HEADER SIGNALING PROTEIN 24-AUG-21 7PJR
TITLE NOTUM_ARUK3000438
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PALMITOLEOYL-PROTEIN CARBOXYLESTERASE NOTUM;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HNOTUM;
COMPND 5 EC: 3.1.1.98;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: NOTUM, OK/SW-CL.30;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-
KEYWDS NOTUM INHIBITOR, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR L.VECCHIA,Y.ZHAO,P.FISH,E.Y.JONES
REVDAT 1 07-SEP-22 7PJR 0
JRNL AUTH L.VECCHIA,Y.ZHAO,P.FISH,E.Y.JONES
JRNL TITL NOTUM INHIBITORS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.51 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.18.2_3874
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) : 1.51
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.12
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 54770
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 2801
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 36.1200 - 4.1000 1.00 2838 108 0.1942 0.1947
REMARK 3 2 4.1000 - 3.2500 1.00 2652 157 0.1773 0.2023
REMARK 3 3 3.2500 - 2.8400 1.00 2638 152 0.1775 0.2146
REMARK 3 4 2.8400 - 2.5800 1.00 2605 161 0.1767 0.2025
REMARK 3 5 2.5800 - 2.4000 1.00 2618 143 0.1733 0.1762
REMARK 3 6 2.4000 - 2.2600 1.00 2585 152 0.1682 0.1904
REMARK 3 7 2.2600 - 2.1400 1.00 2594 142 0.1668 0.2112
REMARK 3 8 2.1400 - 2.0500 1.00 2577 160 0.1666 0.2003
REMARK 3 9 2.0500 - 1.9700 1.00 2580 129 0.1758 0.1949
REMARK 3 10 1.9700 - 1.9000 1.00 2601 131 0.1730 0.1995
REMARK 3 11 1.9000 - 1.8400 1.00 2571 131 0.1730 0.2040
REMARK 3 12 1.8400 - 1.7900 1.00 2603 126 0.1790 0.2145
REMARK 3 13 1.7900 - 1.7400 1.00 2592 131 0.1984 0.2269
REMARK 3 14 1.7400 - 1.7000 1.00 2569 131 0.1975 0.2392
REMARK 3 15 1.7000 - 1.6600 1.00 2557 156 0.2127 0.2274
REMARK 3 16 1.6600 - 1.6300 1.00 2570 134 0.2202 0.2636
REMARK 3 17 1.6300 - 1.5900 1.00 2548 133 0.2384 0.2369
REMARK 3 18 1.5900 - 1.5600 1.00 2597 134 0.2563 0.2844
REMARK 3 19 1.5600 - 1.5400 1.00 2528 150 0.2724 0.2750
REMARK 3 20 1.5400 - 1.5100 1.00 2546 140 0.3080 0.3369
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.970
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.97
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 7PJR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-AUG-21.
REMARK 100 THE DEPOSITION ID IS D_1292117861.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAY-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9686
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54858
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.510
REMARK 200 RESOLUTION RANGE LOW (A) : 47.960
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 12.50
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.51
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: SAD
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M AMMONIUM SULPHATE 0.1 M SODIUM
REMARK 280 CITRATE, PH4.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 296K
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 30.24500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.35000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.12500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.35000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.24500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.12500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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 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 GLU A 1
REMARK 465 THR A 2
REMARK 465 GLY A 3
REMARK 465 SER A 4
REMARK 465 ALA A 5
REMARK 465 GLN A 6
REMARK 465 GLN A 7
REMARK 465 LEU A 8
REMARK 465 ASN A 9
REMARK 465 THR A 200
REMARK 465 ASP A 201
REMARK 465 CYS A 202
REMARK 465 VAL A 203
REMARK 465 LEU A 274
REMARK 465 THR A 275
REMARK 465 GLY A 276
REMARK 465 GLN A 277
REMARK 465 ASP A 343
REMARK 465 SER A 344
REMARK 465 HIS A 345
REMARK 465 LYS A 346
REMARK 465 ALA A 347
REMARK 465 SER A 348
REMARK 465 LYS A 349
REMARK 465 THR A 376
REMARK 465 LYS A 377
REMARK 465 HIS A 378
REMARK 465 HIS A 379
REMARK 465 HIS A 380
REMARK 465 HIS A 381
REMARK 465 HIS A 382
REMARK 465 HIS A 383
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 10 CG CD OE1 OE2
REMARK 470 ARG A 38 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 119 CG CD OE1 OE2
REMARK 470 LYS A 120 CG CD CE NZ
REMARK 470 ARG A 136 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 147 CG CD CE NZ
REMARK 470 LYS A 195 CG CD CE NZ
REMARK 470 HIS A 199 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 235 CG CD OE1 OE2
REMARK 470 ARG A 252 CG CD NE CZ NH1 NH2
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 OD2 ASP A 11 O HOH A 501 2.13
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 TRP A 51 -141.47 53.43
REMARK 500 SER A 155 -125.73 61.75
REMARK 500 SER A 155 -125.91 62.02
REMARK 500 GLN A 234 -176.72 62.88
REMARK 500 SER A 311 -162.28 -163.37
REMARK 500 HIS A 312 124.11 -170.75
REMARK 500 GLU A 313 154.82 69.69
REMARK 500 ILE A 314 -30.33 -150.59
REMARK 500 HIS A 319 30.51 -99.58
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7PJR A 4 374 UNP Q6P988 NOTUM_HUMAN 81 451
SEQADV 7PJR GLU A 1 UNP Q6P988 CLONING ARTIFACT
SEQADV 7PJR THR A 2 UNP Q6P988 CLONING ARTIFACT
SEQADV 7PJR GLY A 3 UNP Q6P988 CLONING ARTIFACT
SEQADV 7PJR SER A 253 UNP Q6P988 CYS 330 ENGINEERED MUTATION
SEQADV 7PJR GLY A 375 UNP Q6P988 EXPRESSION TAG
SEQADV 7PJR THR A 376 UNP Q6P988 EXPRESSION TAG
SEQADV 7PJR LYS A 377 UNP Q6P988 EXPRESSION TAG
SEQADV 7PJR HIS A 378 UNP Q6P988 EXPRESSION TAG
SEQADV 7PJR HIS A 379 UNP Q6P988 EXPRESSION TAG
SEQADV 7PJR HIS A 380 UNP Q6P988 EXPRESSION TAG
SEQADV 7PJR HIS A 381 UNP Q6P988 EXPRESSION TAG
SEQADV 7PJR HIS A 382 UNP Q6P988 EXPRESSION TAG
SEQADV 7PJR HIS A 383 UNP Q6P988 EXPRESSION TAG
SEQRES 1 A 383 GLU THR GLY SER ALA GLN GLN LEU ASN GLU ASP LEU ARG
SEQRES 2 A 383 LEU HIS LEU LEU LEU ASN THR SER VAL THR CYS ASN ASP
SEQRES 3 A 383 GLY SER PRO ALA GLY TYR TYR LEU LYS GLU SER ARG GLY
SEQRES 4 A 383 SER ARG ARG TRP LEU LEU PHE LEU GLU GLY GLY TRP TYR
SEQRES 5 A 383 CYS PHE ASN ARG GLU ASN CYS ASP SER ARG TYR ASP THR
SEQRES 6 A 383 MET ARG ARG LEU MET SER SER ARG ASP TRP PRO ARG THR
SEQRES 7 A 383 ARG THR GLY THR GLY ILE LEU SER SER GLN PRO GLU GLU
SEQRES 8 A 383 ASN PRO TYR TRP TRP ASN ALA ASN MET VAL PHE ILE PRO
SEQRES 9 A 383 TYR CYS SER SER ASP VAL TRP SER GLY ALA SER SER LYS
SEQRES 10 A 383 SER GLU LYS ASN GLU TYR ALA PHE MET GLY ALA LEU ILE
SEQRES 11 A 383 ILE GLN GLU VAL VAL ARG GLU LEU LEU GLY ARG GLY LEU
SEQRES 12 A 383 SER GLY ALA LYS VAL LEU LEU LEU ALA GLY SER SER ALA
SEQRES 13 A 383 GLY GLY THR GLY VAL LEU LEU ASN VAL ASP ARG VAL ALA
SEQRES 14 A 383 GLU GLN LEU GLU LYS LEU GLY TYR PRO ALA ILE GLN VAL
SEQRES 15 A 383 ARG GLY LEU ALA ASP SER GLY TRP PHE LEU ASP ASN LYS
SEQRES 16 A 383 GLN TYR ARG HIS THR ASP CYS VAL ASP THR ILE THR CYS
SEQRES 17 A 383 ALA PRO THR GLU ALA ILE ARG ARG GLY ILE ARG TYR TRP
SEQRES 18 A 383 ASN GLY VAL VAL PRO GLU ARG CYS ARG ARG GLN PHE GLN
SEQRES 19 A 383 GLU GLY GLU GLU TRP ASN CYS PHE PHE GLY TYR LYS VAL
SEQRES 20 A 383 TYR PRO THR LEU ARG SER PRO VAL PHE VAL VAL GLN TRP
SEQRES 21 A 383 LEU PHE ASP GLU ALA GLN LEU THR VAL ASP ASN VAL HIS
SEQRES 22 A 383 LEU THR GLY GLN PRO VAL GLN GLU GLY LEU ARG LEU TYR
SEQRES 23 A 383 ILE GLN ASN LEU GLY ARG GLU LEU ARG HIS THR LEU LYS
SEQRES 24 A 383 ASP VAL PRO ALA SER PHE ALA PRO ALA CYS LEU SER HIS
SEQRES 25 A 383 GLU ILE ILE ILE ARG SER HIS TRP THR ASP VAL GLN VAL
SEQRES 26 A 383 LYS GLY THR SER LEU PRO ARG ALA LEU HIS CYS TRP ASP
SEQRES 27 A 383 ARG SER LEU HIS ASP SER HIS LYS ALA SER LYS THR PRO
SEQRES 28 A 383 LEU LYS GLY CYS PRO VAL HIS LEU VAL ASP SER CYS PRO
SEQRES 29 A 383 TRP PRO HIS CYS ASN PRO SER CYS PRO THR GLY THR LYS
SEQRES 30 A 383 HIS HIS HIS HIS HIS HIS
HET NAG A 401 14
HET DMS A 402 4
HET DMS A 403 4
HET 7SQ A 404 42
HET SO4 A 405 5
HET SO4 A 406 5
HET SO4 A 407 5
HET SO4 A 408 5
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM 7SQ 1-[4-CHLORANYL-3-(TRIFLUOROMETHYL)PHENYL]-1,2,3-
HETNAM 2 7SQ TRIAZOLE
HETNAM SO4 SULFATE 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 2 NAG C8 H15 N O6
FORMUL 3 DMS 2(C2 H6 O S)
FORMUL 5 7SQ C9 H5 CL F3 N3
FORMUL 6 SO4 4(O4 S 2-)
FORMUL 10 HOH *77(H2 O)
HELIX 1 AA1 ASN A 55 MET A 66 1 12
HELIX 2 AA2 ARG A 67 MET A 70 5 4
HELIX 3 AA3 THR A 82 SER A 86 5 5
HELIX 4 AA4 MET A 126 GLY A 140 1 15
HELIX 5 AA5 ARG A 141 ALA A 146 5 6
HELIX 6 AA6 SER A 155 GLY A 176 1 22
HELIX 7 AA7 ALA A 209 ASN A 222 1 14
HELIX 8 AA8 PRO A 226 GLN A 234 1 9
HELIX 9 AA9 GLU A 237 PHE A 242 5 6
HELIX 10 AB1 PHE A 243 TYR A 248 1 6
HELIX 11 AB2 PRO A 249 LEU A 251 5 3
HELIX 12 AB3 GLU A 264 ASP A 270 1 7
HELIX 13 AB4 GLN A 280 LEU A 298 1 19
HELIX 14 AB5 LEU A 330 LEU A 341 1 12
SHEET 1 AA110 THR A 78 ARG A 79 0
SHEET 2 AA110 LEU A 12 LEU A 16 -1 N LEU A 12 O ARG A 79
SHEET 3 AA110 GLY A 31 LYS A 35 -1 O TYR A 32 N HIS A 15
SHEET 4 AA110 ASN A 99 ILE A 103 -1 O PHE A 102 N TYR A 33
SHEET 5 AA110 ARG A 42 LEU A 47 1 N PHE A 46 O ILE A 103
SHEET 6 AA110 VAL A 148 SER A 154 1 O ALA A 152 N LEU A 47
SHEET 7 AA110 GLN A 181 ASP A 187 1 O ARG A 183 N LEU A 151
SHEET 8 AA110 VAL A 255 VAL A 258 1 O VAL A 258 N ALA A 186
SHEET 9 AA110 SER A 304 ALA A 306 1 O PHE A 305 N VAL A 257
SHEET 10 AA110 HIS A 358 VAL A 360 1 O LEU A 359 N SER A 304
SHEET 1 AA2 2 PHE A 262 ASP A 263 0
SHEET 2 AA2 2 LEU A 310 SER A 311 1 O SER A 311 N PHE A 262
SHEET 1 AA3 2 GLN A 324 VAL A 325 0
SHEET 2 AA3 2 THR A 328 SER A 329 -1 O THR A 328 N VAL A 325
SSBOND 1 CYS A 24 CYS A 106 1555 1555 2.09
SSBOND 2 CYS A 53 CYS A 59 1555 1555 2.05
SSBOND 3 CYS A 229 CYS A 241 1555 1555 2.14
SSBOND 4 CYS A 309 CYS A 372 1555 1555 2.02
SSBOND 5 CYS A 336 CYS A 355 1555 1555 2.00
SSBOND 6 CYS A 363 CYS A 368 1555 1555 2.01
LINK ND2 ASN A 19 C1 NAG A 401 1555 1555 1.44
CRYST1 60.490 72.250 78.700 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 0.016532 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013841 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012706 0.00000
TER 5455 GLY A 375
MASTER 302 0 8 14 14 0 0 6 2902 1 97 30
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