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HEADER HYDROLASE 30-NOV-20 7B3F
TITLE NOTUM S232A IN COMPLEX WITH ARUK3003718
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_TAXID: 9606
KEYWDS NOTUM INHIBITOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZHAO,E.Y.JONE
REVDAT 1 04-AUG-21 7B3F 0
JRNL AUTH Y.ZHAO,F.SVENSSON,D.STEADMAN,S.FREW,A.MONAGHAN,M.BICTASH,
JRNL AUTH 2 T.MOREIRA,R.CHALK,W.LU,P.V.FISH,E.Y.JONES
JRNL TITL STRUCTURAL INSIGHTS INTO NOTUM COVALENT INHIBITION.
JRNL REF J.MED.CHEM. 2021
JRNL REFN ISSN 0022-2623
JRNL PMID 34292747
JRNL DOI 10.1021/ACS.JMEDCHEM.1C00701
REMARK 2
REMARK 2 RESOLUTION. 1.39 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) : 1.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.78
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 68366
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 3400
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 47.7800 - 4.0100 1.00 2933 145 0.1864 0.1909
REMARK 3 2 4.0100 - 3.1800 1.00 2798 135 0.1805 0.2171
REMARK 3 3 3.1800 - 2.7800 1.00 2775 145 0.1909 0.2131
REMARK 3 4 2.7800 - 2.5300 1.00 2730 132 0.1885 0.2445
REMARK 3 5 2.5300 - 2.3400 1.00 2746 139 0.1796 0.1911
REMARK 3 6 2.3400 - 2.2100 1.00 2725 145 0.1722 0.2280
REMARK 3 7 2.2100 - 2.1000 1.00 2698 145 0.1630 0.1726
REMARK 3 8 2.1000 - 2.0000 1.00 2708 151 0.1638 0.1854
REMARK 3 9 2.0000 - 1.9300 1.00 2686 171 0.1718 0.1897
REMARK 3 10 1.9300 - 1.8600 1.00 2701 144 0.1706 0.2109
REMARK 3 11 1.8600 - 1.8000 1.00 2715 124 0.1693 0.2078
REMARK 3 12 1.8000 - 1.7500 1.00 2697 140 0.1723 0.2158
REMARK 3 13 1.7500 - 1.7100 1.00 2678 138 0.1857 0.2472
REMARK 3 14 1.7100 - 1.6600 1.00 2695 150 0.1973 0.2301
REMARK 3 15 1.6600 - 1.6300 1.00 2676 124 0.2074 0.2757
REMARK 3 16 1.6300 - 1.5900 1.00 2700 147 0.2167 0.2480
REMARK 3 17 1.5900 - 1.5600 1.00 2677 146 0.2284 0.2428
REMARK 3 18 1.5600 - 1.5300 1.00 2689 129 0.2298 0.2666
REMARK 3 19 1.5300 - 1.5000 1.00 2694 132 0.2509 0.2809
REMARK 3 20 1.5000 - 1.4800 1.00 2675 135 0.2555 0.2755
REMARK 3 21 1.4800 - 1.4500 1.00 2670 137 0.2797 0.2881
REMARK 3 22 1.4500 - 1.4300 1.00 2635 159 0.3041 0.3133
REMARK 3 23 1.4300 - 1.4100 0.99 2666 150 0.3292 0.3577
REMARK 3 24 1.4100 - 1.3900 0.97 2599 137 0.3656 0.3614
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) : 20.530
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.78
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 : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 25.7169 69.9285 80.2548
REMARK 3 T TENSOR
REMARK 3 T11: 0.1231 T22: 0.1225
REMARK 3 T33: 0.1212 T12: -0.0061
REMARK 3 T13: -0.0064 T23: -0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 0.8193 L22: 1.0918
REMARK 3 L33: 0.7179 L12: -0.0770
REMARK 3 L13: -0.1620 L23: -0.0549
REMARK 3 S TENSOR
REMARK 3 S11: -0.0039 S12: -0.0216 S13: 0.0088
REMARK 3 S21: -0.0223 S22: 0.0029 S23: 0.0051
REMARK 3 S31: -0.0257 S32: 0.0282 S33: 0.0040
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 7B3F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-NOV-20.
REMARK 100 THE DEPOSITION ID IS D_1292112575.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-NOV-20
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 : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68561
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.390
REMARK 200 RESOLUTION RANGE LOW (A) : 47.780
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.39
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.41
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 7AGR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M AMMONIUM SULPHATE 0.1 M SODIUM
REMARK 280 CITRATE, PH 4.2, EVAPORATION, 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 30.15250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.14800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.62800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.14800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.15250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.62800
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: MONOMER
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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 78
REMARK 465 THR A 79
REMARK 465 GLY A 80
REMARK 465 SER A 81
REMARK 465 ALA A 82
REMARK 465 GLN A 83
REMARK 465 GLN A 84
REMARK 465 LEU A 85
REMARK 465 ASN A 86
REMARK 465 THR A 352
REMARK 465 GLY A 353
REMARK 465 GLN A 354
REMARK 465 ASP A 420
REMARK 465 SER A 421
REMARK 465 HIS A 422
REMARK 465 LYS A 423
REMARK 465 ALA A 424
REMARK 465 SER A 425
REMARK 465 LYS A 426
REMARK 465 GLY A 452
REMARK 465 THR A 453
REMARK 465 LYS A 454
REMARK 465 HIS A 455
REMARK 465 HIS A 456
REMARK 465 HIS A 457
REMARK 465 HIS A 458
REMARK 465 HIS A 459
REMARK 465 HIS A 460
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 ARG A 115 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 292 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 OD1 ASN A 366 NH2 ARG A 369 1.99
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 119 NE - CZ - NH1 ANGL. DEV. = -3.1 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 TRP A 128 -143.62 61.39
REMARK 500 ALA A 191 56.91 -144.75
REMARK 500 ALA A 232 -132.08 61.74
REMARK 500 TYR A 254 60.86 -119.55
REMARK 500 ASP A 281 -167.07 -165.35
REMARK 500 GLN A 311 178.31 70.73
REMARK 500 PHE A 339 65.58 -117.69
REMARK 500 GLU A 390 151.96 75.65
REMARK 500 ILE A 391 -43.23 -147.18
REMARK 500 HIS A 444 23.14 87.35
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7B3F A 81 451 UNP Q6P988 NOTUM_HUMAN 81 451
SEQADV 7B3F GLU A 78 UNP Q6P988 CLONING ARTIFACT
SEQADV 7B3F THR A 79 UNP Q6P988 CLONING ARTIFACT
SEQADV 7B3F GLY A 80 UNP Q6P988 CLONING ARTIFACT
SEQADV 7B3F ALA A 232 UNP Q6P988 SER 232 ENGINEERED MUTATION
SEQADV 7B3F SER A 330 UNP Q6P988 CYS 330 ENGINEERED MUTATION
SEQADV 7B3F GLY A 452 UNP Q6P988 EXPRESSION TAG
SEQADV 7B3F THR A 453 UNP Q6P988 EXPRESSION TAG
SEQADV 7B3F LYS A 454 UNP Q6P988 EXPRESSION TAG
SEQADV 7B3F HIS A 455 UNP Q6P988 EXPRESSION TAG
SEQADV 7B3F HIS A 456 UNP Q6P988 EXPRESSION TAG
SEQADV 7B3F HIS A 457 UNP Q6P988 EXPRESSION TAG
SEQADV 7B3F HIS A 458 UNP Q6P988 EXPRESSION TAG
SEQADV 7B3F HIS A 459 UNP Q6P988 EXPRESSION TAG
SEQADV 7B3F HIS A 460 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 ALA 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 501 14
HET SO4 A 502 5
HET SO4 A 503 5
HET SO4 A 504 5
HET DMS A 505 4
HET EDO A 506 4
HET EDO A 507 4
HET SRK A 508 16
HET DMS A 509 4
HET DMS A 510 4
HET SO4 A 511 5
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM SO4 SULFATE ION
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM SRK 4-(2,3-DIHYDROINDOL-1-YL)-4-OXIDANYLIDENE-BUTANOIC ACID
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 EDO ETHYLENE GLYCOL
FORMUL 2 NAG C8 H15 N O6
FORMUL 3 SO4 4(O4 S 2-)
FORMUL 6 DMS 3(C2 H6 O S)
FORMUL 7 EDO 2(C2 H6 O2)
FORMUL 9 SRK C12 H13 N O3
FORMUL 13 HOH *89(H2 O)
HELIX 1 AA1 ASN A 132 MET A 143 1 12
HELIX 2 AA2 ARG A 144 MET A 147 5 4
HELIX 3 AA3 THR A 159 SER A 163 5 5
HELIX 4 AA4 MET A 203 GLY A 217 1 15
HELIX 5 AA5 ARG A 218 ALA A 223 5 6
HELIX 6 AA6 ALA A 232 LEU A 252 1 21
HELIX 7 AA7 ALA A 286 ASN A 299 1 14
HELIX 8 AA8 PRO A 303 GLN A 311 1 9
HELIX 9 AA9 GLU A 314 PHE A 319 5 6
HELIX 10 AB1 PHE A 320 TYR A 325 1 6
HELIX 11 AB2 PRO A 326 LEU A 328 5 3
HELIX 12 AB3 GLU A 341 ASP A 347 1 7
HELIX 13 AB4 GLN A 357 LYS A 376 1 20
HELIX 14 AB5 LEU A 407 LEU A 418 1 12
SHEET 1 AA110 THR A 155 ARG A 156 0
SHEET 2 AA110 LEU A 89 LEU A 93 -1 N LEU A 89 O ARG A 156
SHEET 3 AA110 GLY A 108 LYS A 112 -1 O LEU A 111 N ARG A 90
SHEET 4 AA110 ASN A 176 ILE A 180 -1 O PHE A 179 N TYR A 110
SHEET 5 AA110 ARG A 119 LEU A 124 1 N PHE A 123 O ILE A 180
SHEET 6 AA110 VAL A 225 SER A 231 1 O LEU A 227 N TRP A 120
SHEET 7 AA110 GLN A 258 ASP A 264 1 O ARG A 260 N LEU A 228
SHEET 8 AA110 VAL A 332 VAL A 335 1 O VAL A 335 N ALA A 263
SHEET 9 AA110 SER A 381 ALA A 383 1 O PHE A 382 N VAL A 334
SHEET 10 AA110 HIS A 435 VAL A 437 1 O LEU A 436 N ALA A 383
SHEET 1 AA2 2 PHE A 339 ASP A 340 0
SHEET 2 AA2 2 LEU A 387 SER A 388 1 O SER A 388 N PHE A 339
SHEET 1 AA3 2 GLN A 401 VAL A 402 0
SHEET 2 AA3 2 THR A 405 SER A 406 -1 O THR A 405 N VAL A 402
SSBOND 1 CYS A 101 CYS A 183 1555 1555 2.04
SSBOND 2 CYS A 130 CYS A 136 1555 1555 2.04
SSBOND 3 CYS A 279 CYS A 285 1555 1555 2.05
SSBOND 4 CYS A 306 CYS A 318 1555 1555 2.09
SSBOND 5 CYS A 386 CYS A 449 1555 1555 2.03
SSBOND 6 CYS A 413 CYS A 432 1555 1555 2.04
SSBOND 7 CYS A 440 CYS A 445 1555 1555 2.03
LINK ND2 ASN A 96 C1 NAG A 501 1555 1555 1.44
CRYST1 60.305 71.256 78.296 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 0.016582 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014034 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012772 0.00000
TER 2850 THR A 451
MASTER 329 0 11 14 14 0 0 6 2992 1 85 30
END |