HEADER HYDROLASE 12-MAR-24 9ENA TITLE LYSOSOMAL GLUCOCEREBROSIDASE IN COMPLEX WITH A STABILIZING NANOBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: GLUCOSYLCERAMIDASE; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ACID BETA-GLUCOSIDASE,ALGLUCERASE,BETA-GLUCOCEREBROSIDASE, COMPND 5 BETA-GC,D-GLUCOSYL-N-ACYLSPHINGOSINE GLUCOHYDROLASE,IMIGLUCERASE; COMPND 6 EC: 3.2.1.45,2.4.1.-,3.2.1.104; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: CHAINS: B; COMPND 11 CHAIN: B; COMPND 12 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: GBA, GC, GLUC; SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 10 ORGANISM_TAXID: 9844; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 13 EXPRESSION_SYSTEM_STRAIN: WK6 KEYWDS GLUCOSIDASE, GLUCOSYLTRANSFERASE, LIPID METABOLISM, GCASE, NANOBODY, KEYWDS 2 COMPLEX, ALLOSTERIC, STABILIZER, HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR T.DAL MASO,W.VERSEES REVDAT 1 04-JUN-25 9ENA 0 JRNL AUTH T.DAL MASO,C.SINISGALLI,G.ZILIO,E.FRANZIN,I.TESSARI, JRNL AUTH 2 E.PARDON,J.STEYAERT,S.BALLET,E.GREGGIO,W.VERSEES,N.PLOTEGHER JRNL TITL DEVELOPING NANOBODIES AS ALLOSTERIC MOLECULAR CHAPERONES OF JRNL TITL 2 GLUCOCEREBROSIDASE FUNCTION. JRNL REF NAT COMMUN V. 16 4890 2025 JRNL REFN ESSN 2041-1723 JRNL PMID 40425544 JRNL DOI 10.1038/S41467-025-60134-4 REMARK 2 REMARK 2 RESOLUTION. 1.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.86 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 85.3 REMARK 3 NUMBER OF REFLECTIONS : 78272 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.165 REMARK 3 R VALUE (WORKING SET) : 0.163 REMARK 3 FREE R VALUE : 0.194 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990 REMARK 3 FREE R VALUE TEST SET COUNT : 3902 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 46.8600 - 5.1600 1.00 3373 182 0.1722 0.1958 REMARK 3 2 5.1600 - 4.1000 1.00 3222 158 0.1297 0.1438 REMARK 3 3 4.1000 - 3.5800 1.00 3188 171 0.1290 0.1430 REMARK 3 4 3.5800 - 3.2500 1.00 3151 160 0.1407 0.1832 REMARK 3 5 3.2500 - 3.0200 1.00 3132 177 0.1561 0.1880 REMARK 3 6 3.0200 - 2.8400 1.00 3134 162 0.1661 0.1789 REMARK 3 7 2.8400 - 2.7000 1.00 3117 173 0.1661 0.1937 REMARK 3 8 2.7000 - 2.5800 1.00 3107 171 0.1689 0.2058 REMARK 3 9 2.5800 - 2.4800 1.00 3117 171 0.1672 0.1947 REMARK 3 10 2.4800 - 2.4000 1.00 3107 160 0.1637 0.1971 REMARK 3 11 2.4000 - 2.3200 1.00 3090 169 0.1599 0.2057 REMARK 3 12 2.3200 - 2.2500 1.00 3102 162 0.1568 0.1986 REMARK 3 13 2.2500 - 2.2000 1.00 3090 166 0.1594 0.2181 REMARK 3 14 2.2000 - 2.1400 1.00 3096 161 0.1610 0.2057 REMARK 3 15 2.1400 - 2.0900 1.00 3103 145 0.1686 0.2121 REMARK 3 16 2.0900 - 2.0500 1.00 3092 172 0.1695 0.2213 REMARK 3 17 2.0500 - 2.0100 1.00 3089 159 0.1814 0.2284 REMARK 3 18 2.0100 - 1.9700 0.98 3020 153 0.1915 0.2349 REMARK 3 19 1.9700 - 1.9300 0.94 2897 161 0.1916 0.2438 REMARK 3 20 1.9300 - 1.9000 0.87 2692 133 0.2097 0.2818 REMARK 3 21 1.9000 - 1.8700 0.80 2463 121 0.2133 0.2384 REMARK 3 22 1.8700 - 1.8400 0.70 2166 105 0.2165 0.2290 REMARK 3 23 1.8400 - 1.8200 0.61 1887 101 0.2277 0.2732 REMARK 3 24 1.8200 - 1.7900 0.54 1670 88 0.2236 0.2545 REMARK 3 25 1.7900 - 1.7700 0.48 1472 73 0.2230 0.2455 REMARK 3 26 1.7700 - 1.7400 0.42 1258 79 0.2364 0.2469 REMARK 3 27 1.7400 - 1.7200 0.33 1026 41 0.0000 0.2176 REMARK 3 28 1.7200 - 1.7000 0.00 509 28 0.0000 0.2289 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) : 0.151 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.935 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 15.88 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.88 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 5185 REMARK 3 ANGLE : 0.962 7075 REMARK 3 CHIRALITY : 0.057 763 REMARK 3 PLANARITY : 0.009 902 REMARK 3 DIHEDRAL : 6.395 715 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 9ENA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-MAR-24. REMARK 100 THE DEPOSITION ID IS D_1292137217. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 18-SEP-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SOLEIL REMARK 200 BEAMLINE : PROXIMA 2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9801 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78278 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700 REMARK 200 RESOLUTION RANGE LOW (A) : 46.860 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 84.9 REMARK 200 DATA REDUNDANCY : 17.10 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.4000 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) : 1.78 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: PHENIX 2.8.3 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.35 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M MAGNESIUM SULFATE HEPTAHYDRATE, REMARK 280 0.1 M MES PH6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2 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 -Y,X,Z REMARK 290 4555 Y,-X,Z REMARK 290 5555 -X,Y,-Z REMARK 290 6555 X,-Y,-Z REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z REMARK 290 9555 X+1/2,Y+1/2,Z+1/2 REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2 REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2 REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2 REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2 REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2 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 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 -1.000000 0.000000 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 0.00000 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 56.60450 REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 56.60450 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 128.68650 REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 56.60450 REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 56.60450 REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 128.68650 REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 56.60450 REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 56.60450 REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 128.68650 REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 56.60450 REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 56.60450 REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 128.68650 REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 56.60450 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 56.60450 REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 128.68650 REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 56.60450 REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 56.60450 REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 128.68650 REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 56.60450 REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 56.60450 REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 128.68650 REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 56.60450 REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 56.60450 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 128.68650 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 A 751 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 827 LIES ON A SPECIAL POSITION. REMARK 375 HOH A1167 LIES ON A SPECIAL POSITION. REMARK 375 HOH A1184 LIES ON A SPECIAL POSITION. REMARK 375 HOH A1250 LIES ON A SPECIAL POSITION. 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 MET B 1 REMARK 465 ALA B 2 REMARK 465 HIS B 133 REMARK 465 HIS B 134 REMARK 465 HIS B 135 REMARK 465 HIS B 136 REMARK 465 HIS B 137 REMARK 465 HIS B 138 REMARK 465 GLU B 139 REMARK 465 PRO B 140 REMARK 465 GLU B 141 REMARK 465 ALA B 142 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 OG SER A 8 O HOH A 601 2.08 REMARK 500 O HOH A 780 O HOH A 1159 2.19 REMARK 500 O HOH A 1015 O HOH A 1240 2.19 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 TYR A 11 -169.24 -109.18 REMARK 500 THR A 63 -132.76 -94.15 REMARK 500 GLN A 70 77.18 -117.05 REMARK 500 PHE A 75 -133.34 -121.58 REMARK 500 ALA A 124 -152.97 69.84 REMARK 500 LEU A 156 -66.90 -109.35 REMARK 500 ASN A 192 -169.85 -119.50 REMARK 500 GLU A 233 135.59 173.88 REMARK 500 ASP A 263 -64.55 -120.97 REMARK 500 LEU A 281 -80.49 69.56 REMARK 500 TYR A 313 114.64 -164.06 REMARK 500 THR A 323 -75.41 -101.74 REMARK 500 TRP A 381 -132.60 -85.10 REMARK 500 ASN A 392 119.46 -160.76 REMARK 500 TYR B 33 -72.67 -92.80 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A1253 DISTANCE = 5.90 ANGSTROMS REMARK 525 HOH A1254 DISTANCE = 5.92 ANGSTROMS REMARK 525 HOH A1255 DISTANCE = 5.95 ANGSTROMS REMARK 525 HOH A1256 DISTANCE = 6.11 ANGSTROMS REMARK 525 HOH A1257 DISTANCE = 6.15 ANGSTROMS REMARK 525 HOH A1259 DISTANCE = 6.42 ANGSTROMS REMARK 525 HOH A1260 DISTANCE = 6.84 ANGSTROMS 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 MG A 502 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 235 OE2 REMARK 620 2 GLU A 340 OE2 98.8 REMARK 620 3 HOH A 653 O 92.0 89.4 REMARK 620 4 HOH A 704 O 177.4 80.5 90.5 REMARK 620 5 HOH A 752 O 92.1 168.7 87.1 88.8 REMARK 620 6 HOH A 836 O 86.9 88.9 177.8 90.6 94.9 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG A 503 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH A 621 O REMARK 620 2 HOH A 660 O 93.9 REMARK 620 3 HOH A 663 O 160.7 103.4 REMARK 620 4 HOH A 777 O 81.3 94.7 88.7 REMARK 620 5 HOH A1103 O 66.1 159.9 96.2 81.0 REMARK 620 N 1 2 3 4 DBREF 9ENA A 1 497 UNP P04062 GLCM_HUMAN 40 536 DBREF 9ENA B 1 142 PDB 9ENA 9ENA 1 142 SEQADV 9ENA HIS A 495 UNP P04062 ARG 534 ENGINEERED MUTATION SEQRES 1 A 497 ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER SEQRES 2 A 497 VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE SEQRES 3 A 497 ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG SEQRES 4 A 497 TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER SEQRES 5 A 497 MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU SEQRES 6 A 497 LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL SEQRES 7 A 497 LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU SEQRES 8 A 497 ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU SEQRES 9 A 497 LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN SEQRES 10 A 497 ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE SEQRES 11 A 497 ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN SEQRES 12 A 497 LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU SEQRES 13 A 497 LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN SEQRES 14 A 497 ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO SEQRES 15 A 497 THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY SEQRES 16 A 497 SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR SEQRES 17 A 497 TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA SEQRES 18 A 497 GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN SEQRES 19 A 497 GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN SEQRES 20 A 497 CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE SEQRES 21 A 497 ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS SEQRES 22 A 497 HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU SEQRES 23 A 497 LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO SEQRES 24 A 497 GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP SEQRES 25 A 497 TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY SEQRES 26 A 497 GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA SEQRES 27 A 497 SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER SEQRES 28 A 497 VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER SEQRES 29 A 497 HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY SEQRES 30 A 497 TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY SEQRES 31 A 497 PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE SEQRES 32 A 497 VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET SEQRES 33 A 497 PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU SEQRES 34 A 497 GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN SEQRES 35 A 497 ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER SEQRES 36 A 497 ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL SEQRES 37 A 497 PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU SEQRES 38 A 497 THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP SEQRES 39 A 497 HIS ARG GLN SEQRES 1 B 142 MET ALA GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU SEQRES 2 B 142 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 B 142 SER GLY PHE THR LEU ASP TYR TYR ALA ILE GLY TRP PHE SEQRES 4 B 142 ARG GLN ALA PRO GLY LYS GLU ARG GLU GLY VAL SER CYS SEQRES 5 B 142 ILE SER SER SER ASP GLY SER THR TYR TYR ALA ASP SER SEQRES 6 B 142 ALA LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS SEQRES 7 B 142 ASN THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8 B 142 ASP THR ALA VAL TYR TYR CYS ALA THR ASP ARG GLY GLN SEQRES 9 B 142 CYS THR TYR TYR SER SER GLY TYR TYR ARG ASP LEU ARG SEQRES 10 B 142 TRP TYR ASP TYR TRP GLY GLN GLY THR GLN VAL THR VAL SEQRES 11 B 142 SER SER HIS HIS HIS HIS HIS HIS GLU PRO GLU ALA HET NAG C 1 14 HET NAG C 2 14 HET NAG A 501 14 HET MG A 502 1 HET MG A 503 1 HET SO4 A 504 5 HET SO4 A 505 5 HET SO4 A 506 5 HET SO4 A 507 5 HET SO4 A 508 5 HET SO4 A 509 5 HET SO4 B 201 5 HET SO4 B 202 5 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM MG MAGNESIUM ION 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 3 NAG 3(C8 H15 N O6) FORMUL 5 MG 2(MG 2+) FORMUL 7 SO4 8(O4 S 2-) FORMUL 15 HOH *808(H2 O) HELIX 1 AA1 THR A 86 ALA A 95 1 10 HELIX 2 AA2 SER A 97 SER A 110 1 14 HELIX 3 AA3 PRO A 150 LYS A 155 1 6 HELIX 4 AA4 LEU A 156 ALA A 168 1 13 HELIX 5 AA5 PRO A 182 LYS A 186 5 5 HELIX 6 AA6 ASP A 203 HIS A 223 1 21 HELIX 7 AA7 GLU A 235 LEU A 241 5 7 HELIX 8 AA8 THR A 252 ASP A 263 1 12 HELIX 9 AA9 ASP A 263 ASN A 270 1 8 HELIX 10 AB1 LEU A 286 LEU A 288 5 3 HELIX 11 AB2 PRO A 289 THR A 297 1 9 HELIX 12 AB3 ASP A 298 LYS A 303 1 6 HELIX 13 AB4 THR A 323 PHE A 331 1 9 HELIX 14 AB5 SER A 356 TYR A 373 1 18 HELIX 15 AB6 ILE A 406 ASP A 409 5 4 HELIX 16 AB7 GLN A 414 LYS A 425 1 12 HELIX 17 AB8 LYS B 89 THR B 93 5 5 HELIX 18 AB9 CYS B 105 SER B 110 1 6 SHEET 1 AA1 4 PRO A 6 LYS A 7 0 SHEET 2 AA1 4 VAL A 15 CYS A 18 -1 O VAL A 15 N LYS A 7 SHEET 3 AA1 4 THR A 410 LYS A 413 -1 O PHE A 411 N CYS A 18 SHEET 4 AA1 4 ILE A 402 ASP A 405 -1 N ILE A 403 O TYR A 412 SHEET 1 AA2 9 GLU A 50 PRO A 55 0 SHEET 2 AA2 9 THR A 36 THR A 43 -1 N ARG A 39 O SER A 52 SHEET 3 AA2 9 SER A 488 TRP A 494 -1 O LEU A 493 N SER A 38 SHEET 4 AA2 9 ALA A 456 ASN A 462 -1 N VAL A 458 O TYR A 492 SHEET 5 AA2 9 ASP A 445 MET A 450 -1 N ASP A 445 O LEU A 461 SHEET 6 AA2 9 GLN A 432 ALA A 438 -1 N GLN A 432 O MET A 450 SHEET 7 AA2 9 LEU A 65 LYS A 77 -1 N THR A 68 O VAL A 437 SHEET 8 AA2 9 VAL A 468 ASP A 474 1 O THR A 471 N LEU A 67 SHEET 9 AA2 9 GLY A 478 SER A 484 -1 O LEU A 480 N ILE A 472 SHEET 1 AA3 9 GLY A 80 ALA A 84 0 SHEET 2 AA3 9 ILE A 118 MET A 123 1 O ARG A 120 N GLY A 83 SHEET 3 AA3 9 SER A 173 PRO A 178 1 O LEU A 175 N VAL A 121 SHEET 4 AA3 9 ALA A 229 THR A 231 1 O THR A 231 N ALA A 176 SHEET 5 AA3 9 ARG A 277 GLN A 284 1 O LEU A 279 N VAL A 230 SHEET 6 AA3 9 GLY A 307 TRP A 312 1 O ALA A 309 N MET A 280 SHEET 7 AA3 9 MET A 335 ALA A 341 1 O GLU A 340 N TRP A 312 SHEET 8 AA3 9 GLY A 377 ASN A 382 1 O GLY A 377 N ALA A 338 SHEET 9 AA3 9 GLY A 80 ALA A 84 1 N GLY A 82 O ASP A 380 SHEET 1 AA4 4 GLN B 5 SER B 9 0 SHEET 2 AA4 4 LEU B 20 SER B 27 -1 O SER B 27 N GLN B 5 SHEET 3 AA4 4 THR B 80 MET B 85 -1 O MET B 85 N LEU B 20 SHEET 4 AA4 4 PHE B 70 ASP B 75 -1 N ASP B 75 O THR B 80 SHEET 1 AA5 6 GLY B 12 VAL B 14 0 SHEET 2 AA5 6 THR B 126 VAL B 130 1 O THR B 129 N GLY B 12 SHEET 3 AA5 6 ALA B 94 ASP B 101 -1 N TYR B 96 O THR B 126 SHEET 4 AA5 6 ALA B 35 GLN B 41 -1 N PHE B 39 O TYR B 97 SHEET 5 AA5 6 GLU B 48 ILE B 53 -1 O SER B 51 N TRP B 38 SHEET 6 AA5 6 THR B 60 TYR B 62 -1 O TYR B 61 N CYS B 52 SHEET 1 AA6 4 GLY B 12 VAL B 14 0 SHEET 2 AA6 4 THR B 126 VAL B 130 1 O THR B 129 N GLY B 12 SHEET 3 AA6 4 ALA B 94 ASP B 101 -1 N TYR B 96 O THR B 126 SHEET 4 AA6 4 TYR B 119 TRP B 122 -1 O TYR B 121 N THR B 100 SSBOND 1 CYS A 4 CYS A 16 1555 1555 2.08 SSBOND 2 CYS A 18 CYS A 23 1555 1555 2.13 SSBOND 3 CYS B 24 CYS B 98 1555 1555 2.05 SSBOND 4 CYS B 52 CYS B 105 1555 1555 2.04 LINK ND2 ASN A 19 C1 NAG C 1 1555 1555 1.46 LINK ND2 ASN A 270 C1 NAG A 501 1555 1555 1.46 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44 LINK OE2 GLU A 235 MG MG A 502 1555 1555 2.09 LINK OE2 GLU A 340 MG MG A 502 1555 1555 2.08 LINK MG MG A 502 O HOH A 653 1555 1555 2.07 LINK MG MG A 502 O HOH A 704 1555 1555 2.06 LINK MG MG A 502 O HOH A 752 1555 1555 2.07 LINK MG MG A 502 O HOH A 836 1555 1555 1.99 LINK MG MG A 503 O HOH A 621 1555 1555 2.46 LINK MG MG A 503 O HOH A 660 1555 1555 2.23 LINK MG MG A 503 O HOH A 663 1555 1555 2.19 LINK MG MG A 503 O HOH A 777 1555 1555 2.27 LINK MG MG A 503 O HOH A1103 1555 1555 2.46 CISPEP 1 LEU A 288 PRO A 289 0 -0.73 CISPEP 2 GLY A 390 PRO A 391 0 4.11 CRYST1 113.209 113.209 257.373 90.00 90.00 90.00 I 4 2 2 16 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 0.008833 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008833 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003885 0.00000