REMARK 2 REMARK 2 RESOLUTION. 1.85 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.7.0029 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU, REMARK 3 STEINER,NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.68 REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE REMARK 3 COMPLETENESS FOR RANGE (%) : 90.01 REMARK 3 NUMBER OF REFLECTIONS : 63767 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.18336 REMARK 3 R VALUE (WORKING SET) : 0.18130 REMARK 3 FREE R VALUE : 0.22234 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0 REMARK 3 FREE R VALUE TEST SET COUNT : 3380 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.850 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.898 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2829 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 54.52 REMARK 3 BIN R VALUE (WORKING SET) : 0.357 REMARK 3 BIN FREE R VALUE SET COUNT : 155 REMARK 3 BIN FREE R VALUE : 0.357 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 7408 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 39 REMARK 3 SOLVENT ATOMS : 618 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.453 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.13 REMARK 3 B22 (A**2) : -1.18 REMARK 3 B33 (A**2) : 0.02 REMARK 3 B12 (A**2) : 0.00 REMARK 3 B13 (A**2) : 0.08 REMARK 3 B23 (A**2) : 0.00 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.179 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.154 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.113 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.959 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7642 ; 0.009 ; 0.020 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10416 ; 1.324 ; 1.956 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 978 ; 6.380 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 318 ;34.637 ;23.711 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1200 ;13.724 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 43 ;21.053 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1149 ; 0.087 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5850 ; 0.006 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS. BUT NOT OUTPUT. U VALUES REFINED REMARK 3 INDIVIDUALLY. IF THE HETERODIMERS ARE REMARK 3 SUPERPOSED USING BACE2 (B ON A) THEN THE XA4813 MONOMERS ( REMARK 3 E ON D) ARE ROTATED WITH CA DISPLACEMENTS UP TO 7 ANGS. REMARK 4 REMARK 4 4BEL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-MAR-13. REMARK 100 THE PDBE ID CODE IS EBI-56111. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 13-SEP-11 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X10SA 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 : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL (PILATUS 6M) REMARK 200 DETECTOR MANUFACTURER : DECTRIS REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SADABS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70362 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.85 REMARK 200 RESOLUTION RANGE LOW (A) : 43.68 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.3 REMARK 200 DATA REDUNDANCY : 3.42 REMARK 200 R MERGE (I) : 0.10 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.34 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95 REMARK 200 COMPLETENESS FOR SHELL (%) : 68.5 REMARK 200 DATA REDUNDANCY IN SHELL : 1.90 REMARK 200 R MERGE FOR SHELL (I) : 0.62 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.11 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: PDB ENTRY 3ZKQ REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 40.8 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM MGCL2, 30% MME 550, 100MM REMARK 280 HEPES PH 7.5 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 30.87850 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2430 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19170 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.2 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2100 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19340 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.2 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E 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 13 REMARK 465 LEU A 175 REMARK 465 PRO A 176 REMARK 465 VAL A 177 REMARK 465 ALA A 178 REMARK 465 GLY A 179 REMARK 465 SER A 180 REMARK 465 GLY A 181 REMARK 465 THR A 182 REMARK 465 ASN A 183 REMARK 465 LEU A 266 REMARK 465 ILE A 267 REMARK 465 PRO A 268 REMARK 465 GLU A 269 REMARK 465 PHE A 270 REMARK 465 ASN A 285 REMARK 465 SER A 286 REMARK 465 GLU A 287 REMARK 465 THR A 288 REMARK 465 MET A 323 REMARK 465 GLY A 324 REMARK 465 ALA A 325 REMARK 465 GLY A 326 REMARK 465 LEU A 327 REMARK 465 ASN A 328 REMARK 465 TYR A 329 REMARK 465 GLU A 330 REMARK 465 ALA A 398 REMARK 465 ALA B 13 REMARK 465 LEU B 175 REMARK 465 PRO B 176 REMARK 465 VAL B 177 REMARK 465 ALA B 178 REMARK 465 GLY B 179 REMARK 465 SER B 180 REMARK 465 GLY B 181 REMARK 465 THR B 182 REMARK 465 ASN B 183 REMARK 465 SER B 265 REMARK 465 LEU B 266 REMARK 465 ILE B 267 REMARK 465 PRO B 268 REMARK 465 GLU B 269 REMARK 465 PHE B 270 REMARK 465 SER B 271 REMARK 465 THR B 284 REMARK 465 ASN B 285 REMARK 465 SER B 286 REMARK 465 GLU B 287 REMARK 465 MET B 323 REMARK 465 GLY B 324 REMARK 465 ALA B 325 REMARK 465 GLY B 326 REMARK 465 LEU B 327 REMARK 465 ASN B 328 REMARK 465 TYR B 329 REMARK 465 ALA B 398 REMARK 465 HIS D 272 REMARK 465 HIS D 273 REMARK 465 HIS D 274 REMARK 465 HIS D 275 REMARK 465 HIS D 276 REMARK 465 HIS D 277 REMARK 465 GLU D 278 REMARK 465 PRO D 279 REMARK 465 GLU D 280 REMARK 465 ALA D 281 REMARK 465 HIS E 273 REMARK 465 HIS E 274 REMARK 465 HIS E 275 REMARK 465 HIS E 276 REMARK 465 HIS E 277 REMARK 465 GLU E 278 REMARK 465 PRO E 279 REMARK 465 GLU E 280 REMARK 465 ALA E 281 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 D 257 O HOH A 2112 2.19 REMARK 500 NE A ARG E 178 O HOH E 2023 1.49 REMARK 500 CZ A ARG E 178 O HOH E 2023 1.71 REMARK 500 NH1A ARG E 178 O HOH E 2022 2.14 REMARK 500 NH2A ARG E 178 O HOH E 2023 1.63 REMARK 500 NE B ARG E 178 O HOH E 2023 1.84 REMARK 500 CG ASN E 236 O HOH E 2080 2.19 REMARK 500 O HOH A 2013 O HOH A 2016 1.89 REMARK 500 O HOH B 2081 O HOH B 2082 2.01 REMARK 500 O HOH E 2088 O HOH E 2092 2.16 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 ALA A 138 -169.88 -77.81 REMARK 500 TRP A 210 -83.80 -142.34 REMARK 500 LYS A 218 142.52 -170.29 REMARK 500 ALA A 264 31.95 -93.47 REMARK 500 ASN A 341 14.56 -141.46 REMARK 500 TRP B 210 -80.12 -143.63 REMARK 500 ALA D 251 160.16 179.53 REMARK 500 ALA E 251 165.10 176.37 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 ASN B 227 LEU B 228 -144.55 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1398 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B3P A1399 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B3P B1398 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3ZKG RELATED DB: PDB REMARK 900 BACE2 MUTANT APO STRUCTURE REMARK 900 RELATED ID: 3ZKI RELATED DB: PDB REMARK 900 BACE2 MUTANT STRUCTURE WITH LIGAND REMARK 900 RELATED ID: 3ZKM RELATED DB: PDB REMARK 900 BACE2 FAB COMPLEX REMARK 900 RELATED ID: 3ZKN RELATED DB: PDB REMARK 900 BACE2 FAB INHIBITOR COMPLEX REMARK 900 RELATED ID: 3ZKQ RELATED DB: PDB REMARK 900 BACE2 XAPERONE COMPLEX REMARK 900 RELATED ID: 3ZKS RELATED DB: PDB REMARK 900 BACE2 XAPERONE COMPLEX WITH INHIBITOR REMARK 900 RELATED ID: 3ZKX RELATED DB: PDB REMARK 900 TERNARY BACE2 XAPERONE COMPLEX REMARK 900 RELATED ID: 3ZL7 RELATED DB: PDB REMARK 900 BACE2 FYNOMER COMPLEX REMARK 900 RELATED ID: 3ZOV RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF BACE-1 IN COMPLEX WITH CHEMICAL REMARK 900 LIGAND REMARK 900 RELATED ID: 4BFB RELATED DB: PDB REMARK 900 BACE2 XAPERONE COMPLEX REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE PDB FILE IS NUMBERED AFTER PDB-ENTRY 2EWY WHICH HAS REMARK 999 NUMBERS 62 LESS THAN THE DATA BANK SEQUENCE. REMARK 999 ANTIBODY RAISED IN LLAMA AGAINST BACE2. V(HH) EXPRESSED IN REMARK 999 E. COLI. WITH 6HIS AND EPEA TAG.