HEADER PROTEIN BINDING 10-MAR-11 3R1G
TITLE STRUCTURE BASIS OF ALLOSTERIC INHIBITION OF BACE1 BY AN EXOSITE-
TITLE 2 BINDING ANTIBODY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-SECRETASE 1;
COMPND 3 CHAIN: B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 SYNONYM: ASPARTYL PROTEASE 2, ASP2, ASP 2, BETA-SITE AMYLOID
COMPND 6 PRECURSOR PROTEIN CLEAVING ENZYME 1, BETA-SITE APP CLEAVING ENZYME 1,
COMPND 7 MEMAPSIN-2, MEMBRANE-ASSOCIATED ASPARTIC PROTEASE 2;
COMPND 8 EC: 3.4.23.46;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: FAB OF YW412.8.31 ANTIBODY HEAVY CHAIN;
COMPND 12 CHAIN: H;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: FAB OF YW412.8.31 ANTIBODY LIGHT CHAIN;
COMPND 15 CHAIN: L
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BACE1, BACE, KIAA1149;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_TAXID: 9606
KEYWDS ASPARTAL PROTEASE, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR W.WANG,L.ROUGE,P.WU,C.CHIU,Y.CHEN,Y.WU,R.J.WATTS
REVDAT 1 08-JUN-11 3R1G 0
JRNL AUTH J.K.ATWAL,Y.CHEN,C.CHIU,D.L.MORTENSEN,W.J.MEILANDT,Y.LIU,
JRNL AUTH 2 C.E.HEISE,K.HOYTE,W.LUK,Y.LU,K.PENG,P.WU,L.ROUGE,Y.ZHANG,
JRNL AUTH 3 R.A.LAZARUS,K.SCEARCE-LEVIE,W.WANG,Y.WU,M.TESSIER-LAVIGNE,
JRNL AUTH 4 R.J.WATTS
JRNL TITL A THERAPEUTIC ANTIBODY TARGETING BACE1 INHIBITS
JRNL TITL 2 AMYLOID-{BETA} PRODUCTION IN VIVO.
JRNL REF SCI TRANSL MED V. 3 84RA4 2011
JRNL REFN ISSN 1946-6234
JRNL PMID 21613622
JRNL DOI 10.1126/SCITRANSLMED.3002254
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.79
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 17490
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 939
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 44.7964 - 5.3534 1.00 2609 152 0.2680 0.3060
REMARK 3 2 5.3534 - 4.2502 1.00 2539 129 0.1986 0.2463
REMARK 3 3 4.2502 - 3.7132 1.00 2595 123 0.2031 0.2210
REMARK 3 4 3.7132 - 3.3739 1.00 2515 155 0.1990 0.2836
REMARK 3 5 3.3739 - 3.1321 1.00 2548 127 0.2127 0.2604
REMARK 3 6 3.1321 - 2.9475 0.98 2487 145 0.2357 0.2781
REMARK 3 7 2.9475 - 2.8000 0.86 2194 108 0.2634 0.3078
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 : 0.33
REMARK 3 B_SOL : 31.48
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 55.69
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.77210
REMARK 3 B22 (A**2) : -5.48230
REMARK 3 B33 (A**2) : -1.28990
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -8.68640
REMARK 3 B23 (A**2) : 0.00000
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 : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN L AND RESID 1:110
REMARK 3 ORIGIN FOR THE GROUP (A): 38.5945 62.8801 49.2642
REMARK 3 T TENSOR
REMARK 3 T11: 0.1527 T22: 0.4046
REMARK 3 T33: 0.1846 T12: 0.0001
REMARK 3 T13: -0.0105 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.1443 L22: 0.1503
REMARK 3 L33: 0.1807 L12: 0.0931
REMARK 3 L13: -0.0808 L23: -0.1741
REMARK 3 S TENSOR
REMARK 3 S11: -0.0955 S12: -0.0971 S13: 0.1228
REMARK 3 S21: 0.1388 S22: 0.0694 S23: 0.0918
REMARK 3 S31: 0.0097 S32: 0.4361 S33: 0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN L AND RESID 111:214
REMARK 3 ORIGIN FOR THE GROUP (A): 25.3412 50.8494 16.2620
REMARK 3 T TENSOR
REMARK 3 T11: 0.1361 T22: 0.0978
REMARK 3 T33: 0.1145 T12: -0.0167
REMARK 3 T13: -0.0238 T23: -0.0505
REMARK 3 L TENSOR
REMARK 3 L11: 0.3069 L22: 0.0098
REMARK 3 L33: 0.2877 L12: -0.0410
REMARK 3 L13: -0.0135 L23: -0.1090
REMARK 3 S TENSOR
REMARK 3 S11: -0.2120 S12: 0.0644 S13: -0.0459
REMARK 3 S21: 0.0523 S22: 0.0808 S23: 0.1056
REMARK 3 S31: -0.0311 S32: 0.1574 S33: -0.0546
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN H AND RESID 1:114
REMARK 3 ORIGIN FOR THE GROUP (A): 16.8658 67.3834 52.3019
REMARK 3 T TENSOR
REMARK 3 T11: 0.2166 T22: 0.1267
REMARK 3 T33: 0.1252 T12: 0.0839
REMARK 3 T13: -0.0758 T23: -0.0450
REMARK 3 L TENSOR
REMARK 3 L11: 0.1997 L22: 0.2164
REMARK 3 L33: 0.3355 L12: -0.0267
REMARK 3 L13: 0.1010 L23: 0.2842
REMARK 3 S TENSOR
REMARK 3 S11: -0.1714 S12: -0.2171 S13: 0.0618
REMARK 3 S21: -0.1413 S22: 0.0495 S23: 0.0548
REMARK 3 S31: -0.1371 S32: -0.1216 S33: 0.0002
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN H AND RESID 115:218
REMARK 3 ORIGIN FOR THE GROUP (A): 15.1662 49.3585 28.8807
REMARK 3 T TENSOR
REMARK 3 T11: 0.1905 T22: 0.1426
REMARK 3 T33: 0.2294 T12: 0.0656
REMARK 3 T13: 0.0232 T23: -0.0254
REMARK 3 L TENSOR
REMARK 3 L11: 0.0386 L22: 0.0654
REMARK 3 L33: 0.1200 L12: 0.0273
REMARK 3 L13: -0.0646 L23: -0.0397
REMARK 3 S TENSOR
REMARK 3 S11: -0.0161 S12: -0.0928 S13: -0.1187
REMARK 3 S21: -0.2262 S22: -0.0379 S23: 0.2244
REMARK 3 S31: 0.0280 S32: -0.0430 S33: 0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): 27.8660 51.6992 92.4359
REMARK 3 T TENSOR
REMARK 3 T11: 0.0492 T22: 0.0065
REMARK 3 T33: 0.0745 T12: 0.0093
REMARK 3 T13: -0.0268 T23: -0.0240
REMARK 3 L TENSOR
REMARK 3 L11: 0.4495 L22: 0.8363
REMARK 3 L33: 0.8744 L12: 0.1125
REMARK 3 L13: 0.0182 L23: -0.3291
REMARK 3 S TENSOR
REMARK 3 S11: -0.0067 S12: 0.0561 S13: -0.0138
REMARK 3 S21: 0.0191 S22: 0.0136 S23: -0.0118
REMARK 3 S31: -0.0212 S32: -0.0120 S33: 0.0001
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 3R1G COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-11.
REMARK 100 THE RCSB ID CODE IS RCSB064369.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-09
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98057
REMARK 200 MONOCHROMATOR : SIDE SCATTERING I-BEAM BENT
REMARK 200 SINGLE CRYSTAL, ASYMMETRIC CUT
REMARK 200 4.9650 DEG
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17490
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 45.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.36600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 UL OF THE BACE1/FAB COMPLEX SOLUTION
REMARK 280 MIXED WITH 1 UL OF WELL SOLUTION CONTAINING 20% PEG 4000, 0.1M
REMARK 280 TRIS, 0.2 M SODIUM ACETATE, PH 8.5, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 292K
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 37.76850
REMARK 290 SMTRY3 2 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, H, L
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 GLY B 55
REMARK 465 GLY B 219
REMARK 465 PHE B 220
REMARK 465 PRO B 221
REMARK 465 LEU B 222
REMARK 465 ASN B 223
REMARK 465 GLN B 224
REMARK 465 SER B 225
REMARK 465 GLU B 226
REMARK 465 VAL B 227
REMARK 465 GLU B 371
REMARK 465 ASP B 372
REMARK 465 PRO B 448
REMARK 465 GLN B 449
REMARK 465 THR B 450
REMARK 465 ASP B 451
REMARK 465 GLU B 452
REMARK 465 SER B 453
REMARK 465 GLY B 454
REMARK 465 ASN B 455
REMARK 465 SER B 456
REMARK 465 SER H 129
REMARK 465 SER H 130
REMARK 465 LYS H 131
REMARK 465 SER H 132
REMARK 465 THR H 133
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 ASP B 65 38.15 70.44
REMARK 500 ARG B 125 43.59 39.37
REMARK 500 HIS B 150 54.22 -96.42
REMARK 500 PHE B 169 -69.13 -96.34
REMARK 500 ASN B 172 100.77 -50.72
REMARK 500 HIS B 206 30.66 -96.18
REMARK 500 ASN B 209 75.35 -68.76
REMARK 500 LEU B 210 144.08 -170.26
REMARK 500 TRP B 258 -71.75 -128.05
REMARK 500 ASN B 282 51.46 -114.00
REMARK 500 THR B 315 45.68 -143.56
REMARK 500 GLU B 326 -31.69 -130.39
REMARK 500 ALA B 333 125.60 -38.97
REMARK 500 ASN B 354 -9.29 70.78
REMARK 500 SER B 376 -55.59 -25.53
REMARK 500 ALA B 384 32.05 -81.86
REMARK 500 PHE B 426 -52.60 -146.32
REMARK 500 MET B 440 -129.97 52.33
REMARK 500 PHE H 29 -72.97 -38.25
REMARK 500 PRO H 52A 18.78 -62.28
REMARK 500 ALA H 53 58.46 -158.64
REMARK 500 ALA H 116 -179.96 -66.82
REMARK 500 PHE H 148 137.77 -174.19
REMARK 500 ASP L 28 108.33 -59.82
REMARK 500 SER L 30 -115.93 50.89
REMARK 500 ALA L 51 -44.92 82.10
REMARK 500 PRO L 59 156.73 -46.00
REMARK 500 ALA L 84 178.78 176.69
REMARK 500 PHE L 91 35.27 -158.82
REMARK 500 ASN L 138 79.97 53.48
REMARK 500 PRO L 141 -166.64 -77.57
REMARK 500 GLU L 213 -154.38 -104.03
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3R1G B 57 453 UNP P56817 BACE1_HUMAN 57 453
DBREF 3R1G H 1 218 PDB 3R1G 3R1G 1 218
DBREF 3R1G L 1 214 PDB 3R1G 3R1G 1 214
SEQADV 3R1G GLY B 55 UNP P56817 EXPRESSION TAG
SEQADV 3R1G SER B 56 UNP P56817 EXPRESSION TAG
SEQADV 3R1G GLY B 454 UNP P56817 EXPRESSION TAG
SEQADV 3R1G ASN B 455 UNP P56817 EXPRESSION TAG
SEQADV 3R1G SER B 456 UNP P56817 EXPRESSION TAG
SEQRES 1 B 402 GLY SER ARG GLY SER PHE VAL GLU MET VAL ASP ASN LEU
SEQRES 2 B 402 ARG GLY LYS SER GLY GLN GLY TYR TYR VAL GLU MET THR
SEQRES 3 B 402 VAL GLY SER PRO PRO GLN THR LEU ASN ILE LEU VAL ASP
SEQRES 4 B 402 THR GLY SER SER ASN PHE ALA VAL GLY ALA ALA PRO HIS
SEQRES 5 B 402 PRO PHE LEU HIS ARG TYR TYR GLN ARG GLN LEU SER SER
SEQRES 6 B 402 THR TYR ARG ASP LEU ARG LYS GLY VAL TYR VAL PRO TYR
SEQRES 7 B 402 THR GLN GLY LYS TRP GLU GLY GLU LEU GLY THR ASP LEU
SEQRES 8 B 402 VAL SER ILE PRO HIS GLY PRO ASN VAL THR VAL ARG ALA
SEQRES 9 B 402 ASN ILE ALA ALA ILE THR GLU SER ASP LYS PHE PHE ILE
SEQRES 10 B 402 ASN GLY SER ASN TRP GLU GLY ILE LEU GLY LEU ALA TYR
SEQRES 11 B 402 ALA GLU ILE ALA ARG PRO ASP ASP SER LEU GLU PRO PHE
SEQRES 12 B 402 PHE ASP SER LEU VAL LYS GLN THR HIS VAL PRO ASN LEU
SEQRES 13 B 402 PHE SER LEU GLN LEU CYS GLY ALA GLY PHE PRO LEU ASN
SEQRES 14 B 402 GLN SER GLU VAL LEU ALA SER VAL GLY GLY SER MET ILE
SEQRES 15 B 402 ILE GLY GLY ILE ASP HIS SER LEU TYR THR GLY SER LEU
SEQRES 16 B 402 TRP TYR THR PRO ILE ARG ARG GLU TRP TYR TYR GLU VAL
SEQRES 17 B 402 ILE ILE VAL ARG VAL GLU ILE ASN GLY GLN ASP LEU LYS
SEQRES 18 B 402 MET ASP CYS LYS GLU TYR ASN TYR ASP LYS SER ILE VAL
SEQRES 19 B 402 ASP SER GLY THR THR ASN LEU ARG LEU PRO LYS LYS VAL
SEQRES 20 B 402 PHE GLU ALA ALA VAL LYS SER ILE LYS ALA ALA SER SER
SEQRES 21 B 402 THR GLU LYS PHE PRO ASP GLY PHE TRP LEU GLY GLU GLN
SEQRES 22 B 402 LEU VAL CYS TRP GLN ALA GLY THR THR PRO TRP ASN ILE
SEQRES 23 B 402 PHE PRO VAL ILE SER LEU TYR LEU MET GLY GLU VAL THR
SEQRES 24 B 402 ASN GLN SER PHE ARG ILE THR ILE LEU PRO GLN GLN TYR
SEQRES 25 B 402 LEU ARG PRO VAL GLU ASP VAL ALA THR SER GLN ASP ASP
SEQRES 26 B 402 CYS TYR LYS PHE ALA ILE SER GLN SER SER THR GLY THR
SEQRES 27 B 402 VAL MET GLY ALA VAL ILE MET GLU GLY PHE TYR VAL VAL
SEQRES 28 B 402 PHE ASP ARG ALA ARG LYS ARG ILE GLY PHE ALA VAL SER
SEQRES 29 B 402 ALA CYS HIS VAL HIS ASP GLU PHE ARG THR ALA ALA VAL
SEQRES 30 B 402 GLU GLY PRO PHE VAL THR LEU ASP MET GLU ASP CYS GLY
SEQRES 31 B 402 TYR ASN ILE PRO GLN THR ASP GLU SER GLY ASN SER
SEQRES 1 H 222 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN
SEQRES 2 H 222 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 H 222 PHE THR PHE LEU GLY TYR GLY ILE HIS TRP VAL ARG GLN
SEQRES 4 H 222 ALA PRO GLY LYS GLY LEU GLU TRP VAL GLY TRP ILE SER
SEQRES 5 H 222 PRO ALA GLY GLY SER THR ASP TYR ALA ASP SER VAL LYS
SEQRES 6 H 222 GLY ARG PHE THR ILE SER ALA ASP THR SER LYS ASN THR
SEQRES 7 H 222 ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR
SEQRES 8 H 222 ALA VAL TYR TYR CYS ALA ARG GLY PRO PHE SER PRO TRP
SEQRES 9 H 222 VAL MET ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL
SEQRES 10 H 222 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU
SEQRES 11 H 222 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA
SEQRES 12 H 222 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL
SEQRES 13 H 222 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL
SEQRES 14 H 222 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR
SEQRES 15 H 222 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU
SEQRES 16 H 222 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO
SEQRES 17 H 222 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER
SEQRES 18 H 222 CYS
SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA
SEQRES 2 L 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER
SEQRES 3 L 214 GLN ASP VAL SER THR ALA VAL ALA TRP TYR GLN GLN LYS
SEQRES 4 L 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER
SEQRES 5 L 214 PHE LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 L 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU
SEQRES 7 L 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN PHE
SEQRES 8 L 214 PRO THR TYR LEU PRO THR PHE GLY GLN GLY THR LYS VAL
SEQRES 9 L 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE
SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA
SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU
SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER
SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS
SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER
SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU
SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER
SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS
FORMUL 4 HOH *95(H2 O)
HELIX 1 1 GLN B 114 SER B 118 5 5
HELIX 2 2 TYR B 184 ALA B 188 5 5
HELIX 3 3 PRO B 196 THR B 205 1 10
HELIX 4 4 ASP B 277 TYR B 281 5 5
HELIX 5 5 LYS B 299 ALA B 312 1 14
HELIX 6 6 PRO B 319 GLY B 325 1 7
HELIX 7 7 PRO B 337 PHE B 341 5 5
HELIX 8 8 LEU B 362 TYR B 366 1 5
HELIX 9 9 GLY B 395 GLU B 400 1 6
HELIX 10 10 ASP B 439 GLY B 444 5 6
HELIX 11 11 ARG H 83 THR H 87 5 5
HELIX 12 12 SER H 158 ALA H 160 5 3
HELIX 13 13 SER H 189 LEU H 191 5 3
HELIX 14 14 LYS H 203 ASN H 206 5 4
HELIX 15 15 GLN L 79 PHE L 83 5 5
HELIX 16 16 SER L 121 LYS L 126 1 6
HELIX 17 17 LYS L 183 LYS L 188 1 6
SHEET 1 A 9 TRP B 250 PRO B 253 0
SHEET 2 A 9 ARG B 412 PHE B 415 -1 O ILE B 413 N THR B 252
SHEET 3 A 9 VAL B 404 ASP B 407 -1 N VAL B 405 O GLY B 414
SHEET 4 A 9 PHE B 211 GLY B 217 -1 N LEU B 213 O VAL B 404
SHEET 5 A 9 SER B 230 ILE B 237 -1 O SER B 234 N GLN B 214
SHEET 6 A 9 LEU B 67 LYS B 70 -1 N LEU B 67 O GLY B 233
SHEET 7 A 9 TYR B 75 VAL B 81 -1 O TYR B 76 N ARG B 68
SHEET 8 A 9 LYS B 136 SER B 147 -1 O SER B 147 N THR B 80
SHEET 9 A 9 ARG B 122 VAL B 130 -1 N LYS B 126 O LEU B 141
SHEET 1 B13 THR B 155 ASN B 159 0
SHEET 2 B13 LYS B 136 SER B 147 -1 N VAL B 146 O VAL B 156
SHEET 3 B13 ALA B 161 ASP B 167 -1 O GLU B 165 N GLU B 138
SHEET 4 B13 PHE B 99 GLY B 102 1 N VAL B 101 O ILE B 163
SHEET 5 B13 GLY B 178 GLY B 181 -1 O ILE B 179 N ALA B 100
SHEET 6 B13 GLN B 86 ASP B 93 1 N LEU B 91 O GLY B 178
SHEET 7 B13 TYR B 75 VAL B 81 -1 N TYR B 75 O VAL B 92
SHEET 8 B13 LEU B 67 LYS B 70 -1 N ARG B 68 O TYR B 76
SHEET 9 B13 SER B 230 ILE B 237 -1 O GLY B 233 N LEU B 67
SHEET 10 B13 PHE B 211 GLY B 217 -1 N GLN B 214 O SER B 234
SHEET 11 B13 VAL B 404 ASP B 407 -1 O VAL B 404 N LEU B 213
SHEET 12 B13 ARG B 412 PHE B 415 -1 O GLY B 414 N VAL B 405
SHEET 13 B13 TRP B 250 PRO B 253 -1 N THR B 252 O ILE B 413
SHEET 1 C 5 GLU B 261 VAL B 262 0
SHEET 2 C 5 SER B 286 VAL B 288 -1 O SER B 286 N VAL B 262
SHEET 3 C 5 THR B 392 MET B 394 1 O MET B 394 N ILE B 287
SHEET 4 C 5 LEU B 295 PRO B 298 -1 N ARG B 296 O VAL B 393
SHEET 5 C 5 GLN B 387 SER B 388 1 O SER B 388 N LEU B 297
SHEET 1 D 5 GLN B 272 ASP B 273 0
SHEET 2 D 5 ILE B 264 ILE B 269 -1 N ILE B 269 O GLN B 272
SHEET 3 D 5 ILE B 344 MET B 349 -1 O TYR B 347 N ARG B 266
SHEET 4 D 5 GLN B 355 ILE B 361 -1 O PHE B 357 N LEU B 348
SHEET 5 D 5 ALA B 430 VAL B 436 -1 O PHE B 435 N SER B 356
SHEET 1 E 3 VAL B 329 GLN B 332 0
SHEET 2 E 3 ASP B 378 PHE B 383 -1 O ASP B 379 N TRP B 331
SHEET 3 E 3 LEU B 367 PRO B 369 -1 N ARG B 368 O LYS B 382
SHEET 1 F 4 GLN H 3 SER H 7 0
SHEET 2 F 4 GLY H 16 SER H 25 -1 O ALA H 23 N VAL H 5
SHEET 3 F 4 THR H 77 LEU H 82C-1 O MET H 82 N LEU H 18
SHEET 4 F 4 THR H 68 ASP H 72 -1 N ASP H 72 O THR H 77
SHEET 1 G 6 LEU H 11 VAL H 12 0
SHEET 2 G 6 THR H 109 VAL H 113 1 O THR H 112 N VAL H 12
SHEET 3 G 6 ALA H 88 GLY H 95 -1 N TYR H 90 O THR H 109
SHEET 4 G 6 GLY H 33 GLN H 39 -1 N GLN H 39 O VAL H 89
SHEET 5 G 6 LEU H 45 ILE H 51 -1 O VAL H 48 N TRP H 36
SHEET 6 G 6 THR H 57 TYR H 59 -1 O ASP H 58 N TRP H 50
SHEET 1 H 4 LEU H 11 VAL H 12 0
SHEET 2 H 4 THR H 109 VAL H 113 1 O THR H 112 N VAL H 12
SHEET 3 H 4 ALA H 88 GLY H 95 -1 N TYR H 90 O THR H 109
SHEET 4 H 4 TYR H 104 TRP H 105 -1 O TYR H 104 N ARG H 94
SHEET 1 I 4 SER H 122 LEU H 126 0
SHEET 2 I 4 THR H 137 TYR H 147 -1 O LEU H 143 N PHE H 124
SHEET 3 I 4 TYR H 178 PRO H 187 -1 O VAL H 186 N ALA H 138
SHEET 4 I 4 VAL H 165 THR H 167 -1 N HIS H 166 O VAL H 183
SHEET 1 J 4 SER H 122 LEU H 126 0
SHEET 2 J 4 THR H 137 TYR H 147 -1 O LEU H 143 N PHE H 124
SHEET 3 J 4 TYR H 178 PRO H 187 -1 O VAL H 186 N ALA H 138
SHEET 4 J 4 VAL H 171 LEU H 172 -1 N VAL H 171 O SER H 179
SHEET 1 K 3 THR H 153 TRP H 156 0
SHEET 2 K 3 ILE H 197 HIS H 202 -1 O ASN H 199 N SER H 155
SHEET 3 K 3 THR H 207 LYS H 212 -1 O THR H 207 N HIS H 202
SHEET 1 L 4 MET L 4 SER L 7 0
SHEET 2 L 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5
SHEET 3 L 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21
SHEET 4 L 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74
SHEET 1 M 6 SER L 10 SER L 14 0
SHEET 2 M 6 THR L 102 LYS L 107 1 O GLU L 105 N LEU L 11
SHEET 3 M 6 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104
SHEET 4 M 6 VAL L 33 GLN L 38 -1 N TYR L 36 O TYR L 87
SHEET 5 M 6 PRO L 44 TYR L 49 -1 O LYS L 45 N GLN L 37
SHEET 6 M 6 PHE L 53 LEU L 54 -1 O PHE L 53 N TYR L 49
SHEET 1 N 4 SER L 10 SER L 14 0
SHEET 2 N 4 THR L 102 LYS L 107 1 O GLU L 105 N LEU L 11
SHEET 3 N 4 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104
SHEET 4 N 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90
SHEET 1 O 4 SER L 114 PHE L 118 0
SHEET 2 O 4 THR L 129 PHE L 139 -1 O VAL L 133 N PHE L 118
SHEET 3 O 4 TYR L 173 SER L 182 -1 O LEU L 179 N VAL L 132
SHEET 4 O 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176
SHEET 1 P 3 ALA L 144 VAL L 150 0
SHEET 2 P 3 VAL L 191 HIS L 198 -1 O ALA L 193 N LYS L 149
SHEET 3 P 3 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196
SSBOND 1 CYS B 216 CYS B 420 1555 1555 2.03
SSBOND 2 CYS B 278 CYS B 443 1555 1555 2.03
SSBOND 3 CYS B 330 CYS B 380 1555 1555 2.03
SSBOND 4 CYS H 22 CYS H 92 1555 1555 2.03
SSBOND 5 CYS H 142 CYS H 198 1555 1555 2.03
SSBOND 6 CYS L 23 CYS L 88 1555 1555 2.03
SSBOND 7 CYS L 134 CYS L 194 1555 1555 2.03
CISPEP 1 SER B 83 PRO B 84 0 0.80
CISPEP 2 THR B 133 GLN B 134 0 0.45
CISPEP 3 ARG B 189 PRO B 190 0 -0.33
CISPEP 4 TYR B 283 ASP B 284 0 3.57
CISPEP 5 GLY B 433 PRO B 434 0 -1.03
CISPEP 6 ALA H 53 GLY H 54 0 -1.77
CISPEP 7 GLY H 55 SER H 56 0 -2.34
CISPEP 8 SER H 98 PRO H 99 0 2.62
CISPEP 9 PHE H 148 PRO H 149 0 -1.81
CISPEP 10 GLU H 150 PRO H 151 0 -2.72
CISPEP 11 SER L 7 PRO L 8 0 1.43
CISPEP 12 TYR L 140 PRO L 141 0 1.71
CRYST1 46.112 75.537 112.016 90.00 99.82 90.00 P 1 21 1 2
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 0.021686 0.000000 0.003754 0.00000
SCALE2 0.000000 0.013239 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009060 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
