HEADER HYDROLASE 08-SEP-11 3TPL
TITLE APO STRUCTURE OF BACE1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-SECRETASE 1;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: UNP RESIDUES 43-454;
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 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BACE, BACE1, KIAA1149;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS HYDROLASE, MEMAPSIN 2, PROTEASE, BETA-SECRETASE 1
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.C.XU,M.J.LI,H.GREENBLATT,T.T.CHEN,I.SILMAN,J.L.SUSSMAN
REVDAT 4 01-NOV-23 3TPL 1 REMARK SEQADV
REVDAT 3 08-NOV-17 3TPL 1 REMARK
REVDAT 2 13-JUN-12 3TPL 1 JRNL
REVDAT 1 23-NOV-11 3TPL 0
JRNL AUTH Y.C.XU,M.J.LI,H.GREENBLATT,W.Y.CHEN,A.PAZ,O.DYM,Y.PELEG,
JRNL AUTH 2 T.T.CHEN,X.SHEN,J.H.HE,H.L.JIANG,I.SILMAN,J.L.SUSSMAN
JRNL TITL FLEXIBILITY OF THE FLAP IN THE ACTIVE SITE OF BACE1 AS
JRNL TITL 2 REVEALED BY CRYSTAL STRUCTURES AND MOLECULAR DYNAMICS
JRNL TITL 3 SIMULATIONS
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 68 13 2012
JRNL REFN ISSN 0907-4449
JRNL PMID 22194329
JRNL DOI 10.1107/S0907444911047251
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7_650
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 : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.76
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 50910
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1528
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 46.7628 - 5.5570 0.95 4381 136 0.2087 0.2417
REMARK 3 2 5.5570 - 4.4118 0.99 4500 139 0.1701 0.2118
REMARK 3 3 4.4118 - 3.8544 0.99 4476 139 0.1735 0.2153
REMARK 3 4 3.8544 - 3.5022 0.99 4524 140 0.1946 0.2332
REMARK 3 5 3.5022 - 3.2512 1.00 4494 139 0.2180 0.2711
REMARK 3 6 3.2512 - 3.0596 0.99 4525 140 0.2497 0.2972
REMARK 3 7 3.0596 - 2.9064 1.00 4505 139 0.2645 0.3490
REMARK 3 8 2.9064 - 2.7799 1.00 4502 139 0.2814 0.3432
REMARK 3 9 2.7799 - 2.6729 1.00 4510 140 0.2980 0.3937
REMARK 3 10 2.6729 - 2.5806 1.00 4460 138 0.3131 0.3979
REMARK 3 11 2.5806 - 2.4999 1.00 4505 139 0.3351 0.4068
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 : 0.35
REMARK 3 B_SOL : 53.18
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.420
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.960
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.64250
REMARK 3 B22 (A**2) : -3.71310
REMARK 3 B33 (A**2) : 5.35550
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -3.13750
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 : 0.009 8742
REMARK 3 ANGLE : 1.174 11910
REMARK 3 CHIRALITY : 0.076 1329
REMARK 3 PLANARITY : 0.005 1527
REMARK 3 DIHEDRAL : 13.935 3001
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 3TPL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-SEP-11.
REMARK 100 THE DEPOSITION ID IS D_1000067763.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-11
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 6.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54129
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 47.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 4.640
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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 <I/SIGMA(I)> 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: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2B8L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-25%(W/V)PEG 5000, 200MM MONOMETHYL
REMARK 280 ETHER, 200MM AMMONIUM IODIDE, 200MM SODIUM CITRATE, PH 6.4,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 X+1/2,Y+1/2,Z
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 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 1.000000 0.000000 0.000000 112.55000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.58500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 112.55000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 52.58500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 A -39
REMARK 465 GLY A -38
REMARK 465 SER A -37
REMARK 465 SER A -36
REMARK 465 HIS A -35
REMARK 465 HIS A -34
REMARK 465 HIS A -33
REMARK 465 HIS A -32
REMARK 465 HIS A -31
REMARK 465 HIS A -30
REMARK 465 SER A -29
REMARK 465 ALA A -28
REMARK 465 GLY A -27
REMARK 465 GLU A -26
REMARK 465 ASN A -25
REMARK 465 LEU A -24
REMARK 465 TYR A -23
REMARK 465 PHE A -22
REMARK 465 GLN A -21
REMARK 465 GLY A -20
REMARK 465 THR A -19
REMARK 465 LEU A -18
REMARK 465 PRO A -17
REMARK 465 ARG A -16
REMARK 465 GLU A -15
REMARK 465 THR A -14
REMARK 465 ASP A -13
REMARK 465 GLU A -12
REMARK 465 GLU A -11
REMARK 465 PRO A -10
REMARK 465 GLU A -9
REMARK 465 GLU A -8
REMARK 465 PRO A -7
REMARK 465 GLY A -6
REMARK 465 GLY A 158
REMARK 465 PHE A 159
REMARK 465 PRO A 160
REMARK 465 LEU A 161
REMARK 465 ASN A 162
REMARK 465 GLN A 163
REMARK 465 SER A 164
REMARK 465 GLU A 165
REMARK 465 VAL A 166
REMARK 465 LEU A 167
REMARK 465 ALA A 168
REMARK 465 SER A 169
REMARK 465 ASP A 311
REMARK 465 VAL A 312
REMARK 465 ALA A 313
REMARK 465 THR A 314
REMARK 465 SER A 315
REMARK 465 GLN A 316
REMARK 465 ASP A 317
REMARK 465 MET A 379
REMARK 465 GLU A 380
REMARK 465 PRO A 387
REMARK 465 GLN A 388
REMARK 465 THR A 389
REMARK 465 ASP A 390
REMARK 465 GLU A 391
REMARK 465 SER A 392
REMARK 465 THR A 393
REMARK 465 MET B -39
REMARK 465 GLY B -38
REMARK 465 SER B -37
REMARK 465 SER B -36
REMARK 465 HIS B -35
REMARK 465 HIS B -34
REMARK 465 HIS B -33
REMARK 465 HIS B -32
REMARK 465 HIS B -31
REMARK 465 HIS B -30
REMARK 465 SER B -29
REMARK 465 ALA B -28
REMARK 465 GLY B -27
REMARK 465 GLU B -26
REMARK 465 ASN B -25
REMARK 465 LEU B -24
REMARK 465 TYR B -23
REMARK 465 PHE B -22
REMARK 465 GLN B -21
REMARK 465 GLY B -20
REMARK 465 THR B -19
REMARK 465 LEU B -18
REMARK 465 PRO B -17
REMARK 465 ARG B -16
REMARK 465 GLU B -15
REMARK 465 THR B -14
REMARK 465 ASP B -13
REMARK 465 GLU B -12
REMARK 465 GLU B -11
REMARK 465 PRO B -10
REMARK 465 GLU B -9
REMARK 465 GLU B -8
REMARK 465 PRO B -7
REMARK 465 GLY B -6
REMARK 465 ARG B -5
REMARK 465 GLY B 158
REMARK 465 PHE B 159
REMARK 465 PRO B 160
REMARK 465 LEU B 161
REMARK 465 ASN B 162
REMARK 465 GLN B 163
REMARK 465 SER B 164
REMARK 465 GLU B 165
REMARK 465 VAL B 166
REMARK 465 LEU B 167
REMARK 465 ALA B 168
REMARK 465 SER B 169
REMARK 465 GLN B 316
REMARK 465 ASP B 317
REMARK 465 PRO B 387
REMARK 465 GLN B 388
REMARK 465 THR B 389
REMARK 465 ASP B 390
REMARK 465 GLU B 391
REMARK 465 SER B 392
REMARK 465 THR B 393
REMARK 465 MET C -39
REMARK 465 GLY C -38
REMARK 465 SER C -37
REMARK 465 SER C -36
REMARK 465 HIS C -35
REMARK 465 HIS C -34
REMARK 465 HIS C -33
REMARK 465 HIS C -32
REMARK 465 HIS C -31
REMARK 465 HIS C -30
REMARK 465 SER C -29
REMARK 465 ALA C -28
REMARK 465 GLY C -27
REMARK 465 GLU C -26
REMARK 465 ASN C -25
REMARK 465 LEU C -24
REMARK 465 TYR C -23
REMARK 465 PHE C -22
REMARK 465 GLN C -21
REMARK 465 GLY C -20
REMARK 465 THR C -19
REMARK 465 LEU C -18
REMARK 465 PRO C -17
REMARK 465 ARG C -16
REMARK 465 GLU C -15
REMARK 465 THR C -14
REMARK 465 ASP C -13
REMARK 465 GLU C -12
REMARK 465 GLU C -11
REMARK 465 PRO C -10
REMARK 465 GLU C -9
REMARK 465 GLU C -8
REMARK 465 PRO C -7
REMARK 465 GLY C -6
REMARK 465 ARG C -5
REMARK 465 ARG C -4
REMARK 465 GLY C -3
REMARK 465 ALA C 157
REMARK 465 GLY C 158
REMARK 465 PHE C 159
REMARK 465 PRO C 160
REMARK 465 LEU C 161
REMARK 465 ASN C 162
REMARK 465 GLN C 163
REMARK 465 SER C 164
REMARK 465 GLU C 165
REMARK 465 VAL C 166
REMARK 465 LEU C 167
REMARK 465 ALA C 168
REMARK 465 SER C 169
REMARK 465 ASP C 311
REMARK 465 VAL C 312
REMARK 465 ALA C 313
REMARK 465 THR C 314
REMARK 465 SER C 315
REMARK 465 ILE C 386
REMARK 465 PRO C 387
REMARK 465 GLN C 388
REMARK 465 THR C 389
REMARK 465 ASP C 390
REMARK 465 GLU C 391
REMARK 465 SER C 392
REMARK 465 THR C 393
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 -5 CG CD NE CZ NH1 NH2
REMARK 470 ARG A -4 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 7 NE CZ NH1 NH2
REMARK 470 LYS A 9 CG CD CE NZ
REMARK 470 THR A 72 OG1 CG2
REMARK 470 GLN A 73 CG CD OE1 NE2
REMARK 470 GLU A 104 CD OE1 OE2
REMARK 470 ASP A 106 CG OD1 OD2
REMARK 470 LYS A 107 CG CD CE NZ
REMARK 470 ARG A 128 NH1 NH2
REMARK 470 LYS A 142 NZ
REMARK 470 VAL A 170 CG1 CG2
REMARK 470 LYS A 218 NZ
REMARK 470 GLU A 219 CG CD OE1 OE2
REMARK 470 LYS A 239 CD CE NZ
REMARK 470 LYS A 246 CD CE NZ
REMARK 470 LYS A 256 CG CD CE NZ
REMARK 470 GLN A 271 CG CD OE1 NE2
REMARK 470 ARG A 307 CD NE CZ NH1 NH2
REMARK 470 GLU A 310 CG CD OE1 OE2
REMARK 470 LYS A 321 CD CE NZ
REMARK 470 GLN A 326 CG CD OE1 NE2
REMARK 470 LEU A 377 CD1 CD2
REMARK 470 ASP A 381 OD1 OD2
REMARK 470 ILE A 386 CG1 CG2 CD1
REMARK 470 ARG B -4 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 4 OD1 OD2
REMARK 470 ARG B 7 CD NE CZ NH1 NH2
REMARK 470 LYS B 9 CG CD CE NZ
REMARK 470 SER B 10 OG
REMARK 470 GLU B 17 OE1 OE2
REMARK 470 HIS B 49 ND1 CD2 CE1 NE2
REMARK 470 ARG B 64 CG CD NE CZ NH1 NH2
REMARK 470 TYR B 68 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 THR B 72 OG1 CG2
REMARK 470 GLN B 73 CG CD OE1 NE2
REMARK 470 GLU B 79 CG CD OE1 OE2
REMARK 470 GLU B 104 CG CD OE1 OE2
REMARK 470 LYS B 107 CG CD CE NZ
REMARK 470 GLU B 125 OE1 OE2
REMARK 470 ARG B 128 CZ NH1 NH2
REMARK 470 LYS B 142 CD CE NZ
REMARK 470 LYS B 214 CE NZ
REMARK 470 MET B 215 CE
REMARK 470 LYS B 218 NZ
REMARK 470 LYS B 238 NZ
REMARK 470 LYS B 239 CD CE NZ
REMARK 470 GLU B 242 OE1 OE2
REMARK 470 LYS B 246 CD CE NZ
REMARK 470 LYS B 256 CG CD CE NZ
REMARK 470 ASP B 259 CG OD1 OD2
REMARK 470 GLN B 271 CD OE1 NE2
REMARK 470 GLN B 294 OE1 NE2
REMARK 470 ARG B 307 CD NE CZ NH1 NH2
REMARK 470 ASP B 311 CG OD1 OD2
REMARK 470 THR B 314 OG1 CG2
REMARK 470 SER B 315 OG
REMARK 470 MET B 333 CE
REMARK 470 LYS B 350 CE NZ
REMARK 470 GLU B 364 OE1 OE2
REMARK 470 GLU B 371 OE1 OE2
REMARK 470 VAL C 0 CG1 CG2
REMARK 470 GLU C 1 CD OE1 OE2
REMARK 470 ARG C 7 CD NE CZ NH1 NH2
REMARK 470 LYS C 9 CG CD CE NZ
REMARK 470 SER C 10 OG
REMARK 470 HIS C 49 CG ND1 CD2 CE1 NE2
REMARK 470 LYS C 65 NZ
REMARK 470 TYR C 68 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN C 73 CG CD OE1 NE2
REMARK 470 GLU C 79 CG CD OE1 OE2
REMARK 470 GLU C 104 CG CD OE1 OE2
REMARK 470 ASP C 106 CG OD1 OD2
REMARK 470 LYS C 107 CG CD CE NZ
REMARK 470 MET C 174 CE
REMARK 470 LYS C 214 CG CD CE NZ
REMARK 470 MET C 215 CE
REMARK 470 LYS C 218 NZ
REMARK 470 LYS C 238 CE NZ
REMARK 470 GLU C 242 CD OE1 OE2
REMARK 470 LYS C 246 CD CE NZ
REMARK 470 LYS C 256 CG CD CE NZ
REMARK 470 GLU C 265 CD OE1 OE2
REMARK 470 GLN C 266 CD OE1 NE2
REMARK 470 ARG C 307 NE CZ NH1 NH2
REMARK 470 GLU C 310 CG CD OE1 OE2
REMARK 470 GLN C 316 CG CD OE1 NE2
REMARK 470 LYS C 321 CD CE NZ
REMARK 470 LYS C 350 CD CE NZ
REMARK 470 GLU C 364 CG CD OE1 OE2
REMARK 470 LEU C 377 CG CD1 CD2
REMARK 470 GLU C 380 CG CD OE1 OE2
REMARK 470 ASP C 381 CG OD1 OD2
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 PHE A -1 66.40 -117.08
REMARK 500 SER A 10 92.96 31.33
REMARK 500 ALA A 42 38.94 -145.53
REMARK 500 ALA A 43 143.17 -179.35
REMARK 500 GLN A 73 -79.87 -91.14
REMARK 500 HIS A 89 53.96 -95.89
REMARK 500 ALA A 122 -166.86 -77.31
REMARK 500 LEU A 149 141.03 -179.08
REMARK 500 TRP A 197 -82.93 -138.55
REMARK 500 ARG A 205 142.60 -174.24
REMARK 500 LYS A 214 67.07 60.42
REMARK 500 GLN A 271 151.34 -48.49
REMARK 500 ALA B 43 140.38 -172.11
REMARK 500 HIS B 45 139.48 -172.84
REMARK 500 LEU B 56 8.17 -69.06
REMARK 500 HIS B 89 42.40 -92.23
REMARK 500 PHE B 108 -63.95 -98.91
REMARK 500 ASN B 114 3.51 80.37
REMARK 500 LEU B 133 97.69 -68.11
REMARK 500 LEU B 149 138.56 -170.99
REMARK 500 TRP B 197 -84.60 -135.12
REMARK 500 ASP B 223 -74.64 92.94
REMARK 500 ASP B 311 -66.83 -137.77
REMARK 500 VAL B 312 60.22 37.17
REMARK 500 LEU C 48 100.43 80.67
REMARK 500 TRP C 197 -81.47 -136.08
REMARK 500 ASP C 223 -75.51 88.13
REMARK 500 GLU C 339 1.24 -65.13
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 SO4 A 394
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 394
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 394
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 395
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3TPJ RELATED DB: PDB
REMARK 900 RELATED ID: 3TPP RELATED DB: PDB
REMARK 900 RELATED ID: 3TPR RELATED DB: PDB
DBREF 3TPL A -18 393 UNP P56817 BACE1_HUMAN 43 454
DBREF 3TPL B -18 393 UNP P56817 BACE1_HUMAN 43 454
DBREF 3TPL C -18 393 UNP P56817 BACE1_HUMAN 43 454
SEQADV 3TPL MET A -39 UNP P56817 EXPRESSION TAG
SEQADV 3TPL GLY A -38 UNP P56817 EXPRESSION TAG
SEQADV 3TPL SER A -37 UNP P56817 EXPRESSION TAG
SEQADV 3TPL SER A -36 UNP P56817 EXPRESSION TAG
SEQADV 3TPL HIS A -35 UNP P56817 EXPRESSION TAG
SEQADV 3TPL HIS A -34 UNP P56817 EXPRESSION TAG
SEQADV 3TPL HIS A -33 UNP P56817 EXPRESSION TAG
SEQADV 3TPL HIS A -32 UNP P56817 EXPRESSION TAG
SEQADV 3TPL HIS A -31 UNP P56817 EXPRESSION TAG
SEQADV 3TPL HIS A -30 UNP P56817 EXPRESSION TAG
SEQADV 3TPL SER A -29 UNP P56817 EXPRESSION TAG
SEQADV 3TPL ALA A -28 UNP P56817 EXPRESSION TAG
SEQADV 3TPL GLY A -27 UNP P56817 EXPRESSION TAG
SEQADV 3TPL GLU A -26 UNP P56817 EXPRESSION TAG
SEQADV 3TPL ASN A -25 UNP P56817 EXPRESSION TAG
SEQADV 3TPL LEU A -24 UNP P56817 EXPRESSION TAG
SEQADV 3TPL TYR A -23 UNP P56817 EXPRESSION TAG
SEQADV 3TPL PHE A -22 UNP P56817 EXPRESSION TAG
SEQADV 3TPL GLN A -21 UNP P56817 EXPRESSION TAG
SEQADV 3TPL GLY A -20 UNP P56817 EXPRESSION TAG
SEQADV 3TPL THR A -19 UNP P56817 EXPRESSION TAG
SEQADV 3TPL ALA A 75 UNP P56817 LYS 136 ENGINEERED MUTATION
SEQADV 3TPL ALA A 77 UNP P56817 GLU 138 ENGINEERED MUTATION
SEQADV 3TPL MET B -39 UNP P56817 EXPRESSION TAG
SEQADV 3TPL GLY B -38 UNP P56817 EXPRESSION TAG
SEQADV 3TPL SER B -37 UNP P56817 EXPRESSION TAG
SEQADV 3TPL SER B -36 UNP P56817 EXPRESSION TAG
SEQADV 3TPL HIS B -35 UNP P56817 EXPRESSION TAG
SEQADV 3TPL HIS B -34 UNP P56817 EXPRESSION TAG
SEQADV 3TPL HIS B -33 UNP P56817 EXPRESSION TAG
SEQADV 3TPL HIS B -32 UNP P56817 EXPRESSION TAG
SEQADV 3TPL HIS B -31 UNP P56817 EXPRESSION TAG
SEQADV 3TPL HIS B -30 UNP P56817 EXPRESSION TAG
SEQADV 3TPL SER B -29 UNP P56817 EXPRESSION TAG
SEQADV 3TPL ALA B -28 UNP P56817 EXPRESSION TAG
SEQADV 3TPL GLY B -27 UNP P56817 EXPRESSION TAG
SEQADV 3TPL GLU B -26 UNP P56817 EXPRESSION TAG
SEQADV 3TPL ASN B -25 UNP P56817 EXPRESSION TAG
SEQADV 3TPL LEU B -24 UNP P56817 EXPRESSION TAG
SEQADV 3TPL TYR B -23 UNP P56817 EXPRESSION TAG
SEQADV 3TPL PHE B -22 UNP P56817 EXPRESSION TAG
SEQADV 3TPL GLN B -21 UNP P56817 EXPRESSION TAG
SEQADV 3TPL GLY B -20 UNP P56817 EXPRESSION TAG
SEQADV 3TPL THR B -19 UNP P56817 EXPRESSION TAG
SEQADV 3TPL ALA B 75 UNP P56817 LYS 136 ENGINEERED MUTATION
SEQADV 3TPL ALA B 77 UNP P56817 GLU 138 ENGINEERED MUTATION
SEQADV 3TPL MET C -39 UNP P56817 EXPRESSION TAG
SEQADV 3TPL GLY C -38 UNP P56817 EXPRESSION TAG
SEQADV 3TPL SER C -37 UNP P56817 EXPRESSION TAG
SEQADV 3TPL SER C -36 UNP P56817 EXPRESSION TAG
SEQADV 3TPL HIS C -35 UNP P56817 EXPRESSION TAG
SEQADV 3TPL HIS C -34 UNP P56817 EXPRESSION TAG
SEQADV 3TPL HIS C -33 UNP P56817 EXPRESSION TAG
SEQADV 3TPL HIS C -32 UNP P56817 EXPRESSION TAG
SEQADV 3TPL HIS C -31 UNP P56817 EXPRESSION TAG
SEQADV 3TPL HIS C -30 UNP P56817 EXPRESSION TAG
SEQADV 3TPL SER C -29 UNP P56817 EXPRESSION TAG
SEQADV 3TPL ALA C -28 UNP P56817 EXPRESSION TAG
SEQADV 3TPL GLY C -27 UNP P56817 EXPRESSION TAG
SEQADV 3TPL GLU C -26 UNP P56817 EXPRESSION TAG
SEQADV 3TPL ASN C -25 UNP P56817 EXPRESSION TAG
SEQADV 3TPL LEU C -24 UNP P56817 EXPRESSION TAG
SEQADV 3TPL TYR C -23 UNP P56817 EXPRESSION TAG
SEQADV 3TPL PHE C -22 UNP P56817 EXPRESSION TAG
SEQADV 3TPL GLN C -21 UNP P56817 EXPRESSION TAG
SEQADV 3TPL GLY C -20 UNP P56817 EXPRESSION TAG
SEQADV 3TPL THR C -19 UNP P56817 EXPRESSION TAG
SEQADV 3TPL ALA C 75 UNP P56817 LYS 136 ENGINEERED MUTATION
SEQADV 3TPL ALA C 77 UNP P56817 GLU 138 ENGINEERED MUTATION
SEQRES 1 A 433 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER ALA GLY
SEQRES 2 A 433 GLU ASN LEU TYR PHE GLN GLY THR LEU PRO ARG GLU THR
SEQRES 3 A 433 ASP GLU GLU PRO GLU GLU PRO GLY ARG ARG GLY SER PHE
SEQRES 4 A 433 VAL GLU MET VAL ASP ASN LEU ARG GLY LYS SER GLY GLN
SEQRES 5 A 433 GLY TYR TYR VAL GLU MET THR VAL GLY SER PRO PRO GLN
SEQRES 6 A 433 THR LEU ASN ILE LEU VAL ASP THR GLY SER SER ASN PHE
SEQRES 7 A 433 ALA VAL GLY ALA ALA PRO HIS PRO PHE LEU HIS ARG TYR
SEQRES 8 A 433 TYR GLN ARG GLN LEU SER SER THR TYR ARG ASP LEU ARG
SEQRES 9 A 433 LYS GLY VAL TYR VAL PRO TYR THR GLN GLY ALA TRP ALA
SEQRES 10 A 433 GLY GLU LEU GLY THR ASP LEU VAL SER ILE PRO HIS GLY
SEQRES 11 A 433 PRO ASN VAL THR VAL ARG ALA ASN ILE ALA ALA ILE THR
SEQRES 12 A 433 GLU SER ASP LYS PHE PHE ILE ASN GLY SER ASN TRP GLU
SEQRES 13 A 433 GLY ILE LEU GLY LEU ALA TYR ALA GLU ILE ALA ARG PRO
SEQRES 14 A 433 ASP ASP SER LEU GLU PRO PHE PHE ASP SER LEU VAL LYS
SEQRES 15 A 433 GLN THR HIS VAL PRO ASN LEU PHE SER LEU GLN LEU CYS
SEQRES 16 A 433 GLY ALA GLY PHE PRO LEU ASN GLN SER GLU VAL LEU ALA
SEQRES 17 A 433 SER VAL GLY GLY SER MET ILE ILE GLY GLY ILE ASP HIS
SEQRES 18 A 433 SER LEU TYR THR GLY SER LEU TRP TYR THR PRO ILE ARG
SEQRES 19 A 433 ARG GLU TRP TYR TYR GLU VAL ILE ILE VAL ARG VAL GLU
SEQRES 20 A 433 ILE ASN GLY GLN ASP LEU LYS MET ASP CYS LYS GLU TYR
SEQRES 21 A 433 ASN TYR ASP LYS SER ILE VAL ASP SER GLY THR THR ASN
SEQRES 22 A 433 LEU ARG LEU PRO LYS LYS VAL PHE GLU ALA ALA VAL LYS
SEQRES 23 A 433 SER ILE LYS ALA ALA SER SER THR GLU LYS PHE PRO ASP
SEQRES 24 A 433 GLY PHE TRP LEU GLY GLU GLN LEU VAL CYS TRP GLN ALA
SEQRES 25 A 433 GLY THR THR PRO TRP ASN ILE PHE PRO VAL ILE SER LEU
SEQRES 26 A 433 TYR LEU MET GLY GLU VAL THR ASN GLN SER PHE ARG ILE
SEQRES 27 A 433 THR ILE LEU PRO GLN GLN TYR LEU ARG PRO VAL GLU ASP
SEQRES 28 A 433 VAL ALA THR SER GLN ASP ASP CYS TYR LYS PHE ALA ILE
SEQRES 29 A 433 SER GLN SER SER THR GLY THR VAL MET GLY ALA VAL ILE
SEQRES 30 A 433 MET GLU GLY PHE TYR VAL VAL PHE ASP ARG ALA ARG LYS
SEQRES 31 A 433 ARG ILE GLY PHE ALA VAL SER ALA CYS HIS VAL HIS ASP
SEQRES 32 A 433 GLU PHE ARG THR ALA ALA VAL GLU GLY PRO PHE VAL THR
SEQRES 33 A 433 LEU ASP MET GLU ASP CYS GLY TYR ASN ILE PRO GLN THR
SEQRES 34 A 433 ASP GLU SER THR
SEQRES 1 B 433 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER ALA GLY
SEQRES 2 B 433 GLU ASN LEU TYR PHE GLN GLY THR LEU PRO ARG GLU THR
SEQRES 3 B 433 ASP GLU GLU PRO GLU GLU PRO GLY ARG ARG GLY SER PHE
SEQRES 4 B 433 VAL GLU MET VAL ASP ASN LEU ARG GLY LYS SER GLY GLN
SEQRES 5 B 433 GLY TYR TYR VAL GLU MET THR VAL GLY SER PRO PRO GLN
SEQRES 6 B 433 THR LEU ASN ILE LEU VAL ASP THR GLY SER SER ASN PHE
SEQRES 7 B 433 ALA VAL GLY ALA ALA PRO HIS PRO PHE LEU HIS ARG TYR
SEQRES 8 B 433 TYR GLN ARG GLN LEU SER SER THR TYR ARG ASP LEU ARG
SEQRES 9 B 433 LYS GLY VAL TYR VAL PRO TYR THR GLN GLY ALA TRP ALA
SEQRES 10 B 433 GLY GLU LEU GLY THR ASP LEU VAL SER ILE PRO HIS GLY
SEQRES 11 B 433 PRO ASN VAL THR VAL ARG ALA ASN ILE ALA ALA ILE THR
SEQRES 12 B 433 GLU SER ASP LYS PHE PHE ILE ASN GLY SER ASN TRP GLU
SEQRES 13 B 433 GLY ILE LEU GLY LEU ALA TYR ALA GLU ILE ALA ARG PRO
SEQRES 14 B 433 ASP ASP SER LEU GLU PRO PHE PHE ASP SER LEU VAL LYS
SEQRES 15 B 433 GLN THR HIS VAL PRO ASN LEU PHE SER LEU GLN LEU CYS
SEQRES 16 B 433 GLY ALA GLY PHE PRO LEU ASN GLN SER GLU VAL LEU ALA
SEQRES 17 B 433 SER VAL GLY GLY SER MET ILE ILE GLY GLY ILE ASP HIS
SEQRES 18 B 433 SER LEU TYR THR GLY SER LEU TRP TYR THR PRO ILE ARG
SEQRES 19 B 433 ARG GLU TRP TYR TYR GLU VAL ILE ILE VAL ARG VAL GLU
SEQRES 20 B 433 ILE ASN GLY GLN ASP LEU LYS MET ASP CYS LYS GLU TYR
SEQRES 21 B 433 ASN TYR ASP LYS SER ILE VAL ASP SER GLY THR THR ASN
SEQRES 22 B 433 LEU ARG LEU PRO LYS LYS VAL PHE GLU ALA ALA VAL LYS
SEQRES 23 B 433 SER ILE LYS ALA ALA SER SER THR GLU LYS PHE PRO ASP
SEQRES 24 B 433 GLY PHE TRP LEU GLY GLU GLN LEU VAL CYS TRP GLN ALA
SEQRES 25 B 433 GLY THR THR PRO TRP ASN ILE PHE PRO VAL ILE SER LEU
SEQRES 26 B 433 TYR LEU MET GLY GLU VAL THR ASN GLN SER PHE ARG ILE
SEQRES 27 B 433 THR ILE LEU PRO GLN GLN TYR LEU ARG PRO VAL GLU ASP
SEQRES 28 B 433 VAL ALA THR SER GLN ASP ASP CYS TYR LYS PHE ALA ILE
SEQRES 29 B 433 SER GLN SER SER THR GLY THR VAL MET GLY ALA VAL ILE
SEQRES 30 B 433 MET GLU GLY PHE TYR VAL VAL PHE ASP ARG ALA ARG LYS
SEQRES 31 B 433 ARG ILE GLY PHE ALA VAL SER ALA CYS HIS VAL HIS ASP
SEQRES 32 B 433 GLU PHE ARG THR ALA ALA VAL GLU GLY PRO PHE VAL THR
SEQRES 33 B 433 LEU ASP MET GLU ASP CYS GLY TYR ASN ILE PRO GLN THR
SEQRES 34 B 433 ASP GLU SER THR
SEQRES 1 C 433 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER ALA GLY
SEQRES 2 C 433 GLU ASN LEU TYR PHE GLN GLY THR LEU PRO ARG GLU THR
SEQRES 3 C 433 ASP GLU GLU PRO GLU GLU PRO GLY ARG ARG GLY SER PHE
SEQRES 4 C 433 VAL GLU MET VAL ASP ASN LEU ARG GLY LYS SER GLY GLN
SEQRES 5 C 433 GLY TYR TYR VAL GLU MET THR VAL GLY SER PRO PRO GLN
SEQRES 6 C 433 THR LEU ASN ILE LEU VAL ASP THR GLY SER SER ASN PHE
SEQRES 7 C 433 ALA VAL GLY ALA ALA PRO HIS PRO PHE LEU HIS ARG TYR
SEQRES 8 C 433 TYR GLN ARG GLN LEU SER SER THR TYR ARG ASP LEU ARG
SEQRES 9 C 433 LYS GLY VAL TYR VAL PRO TYR THR GLN GLY ALA TRP ALA
SEQRES 10 C 433 GLY GLU LEU GLY THR ASP LEU VAL SER ILE PRO HIS GLY
SEQRES 11 C 433 PRO ASN VAL THR VAL ARG ALA ASN ILE ALA ALA ILE THR
SEQRES 12 C 433 GLU SER ASP LYS PHE PHE ILE ASN GLY SER ASN TRP GLU
SEQRES 13 C 433 GLY ILE LEU GLY LEU ALA TYR ALA GLU ILE ALA ARG PRO
SEQRES 14 C 433 ASP ASP SER LEU GLU PRO PHE PHE ASP SER LEU VAL LYS
SEQRES 15 C 433 GLN THR HIS VAL PRO ASN LEU PHE SER LEU GLN LEU CYS
SEQRES 16 C 433 GLY ALA GLY PHE PRO LEU ASN GLN SER GLU VAL LEU ALA
SEQRES 17 C 433 SER VAL GLY GLY SER MET ILE ILE GLY GLY ILE ASP HIS
SEQRES 18 C 433 SER LEU TYR THR GLY SER LEU TRP TYR THR PRO ILE ARG
SEQRES 19 C 433 ARG GLU TRP TYR TYR GLU VAL ILE ILE VAL ARG VAL GLU
SEQRES 20 C 433 ILE ASN GLY GLN ASP LEU LYS MET ASP CYS LYS GLU TYR
SEQRES 21 C 433 ASN TYR ASP LYS SER ILE VAL ASP SER GLY THR THR ASN
SEQRES 22 C 433 LEU ARG LEU PRO LYS LYS VAL PHE GLU ALA ALA VAL LYS
SEQRES 23 C 433 SER ILE LYS ALA ALA SER SER THR GLU LYS PHE PRO ASP
SEQRES 24 C 433 GLY PHE TRP LEU GLY GLU GLN LEU VAL CYS TRP GLN ALA
SEQRES 25 C 433 GLY THR THR PRO TRP ASN ILE PHE PRO VAL ILE SER LEU
SEQRES 26 C 433 TYR LEU MET GLY GLU VAL THR ASN GLN SER PHE ARG ILE
SEQRES 27 C 433 THR ILE LEU PRO GLN GLN TYR LEU ARG PRO VAL GLU ASP
SEQRES 28 C 433 VAL ALA THR SER GLN ASP ASP CYS TYR LYS PHE ALA ILE
SEQRES 29 C 433 SER GLN SER SER THR GLY THR VAL MET GLY ALA VAL ILE
SEQRES 30 C 433 MET GLU GLY PHE TYR VAL VAL PHE ASP ARG ALA ARG LYS
SEQRES 31 C 433 ARG ILE GLY PHE ALA VAL SER ALA CYS HIS VAL HIS ASP
SEQRES 32 C 433 GLU PHE ARG THR ALA ALA VAL GLU GLY PRO PHE VAL THR
SEQRES 33 C 433 LEU ASP MET GLU ASP CYS GLY TYR ASN ILE PRO GLN THR
SEQRES 34 C 433 ASP GLU SER THR
HET SO4 A 394 5
HET CL B 394 1
HET SO4 C 394 5
HET SO4 C 395 5
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
FORMUL 4 SO4 3(O4 S 2-)
FORMUL 5 CL CL 1-
FORMUL 8 HOH *98(H2 O)
HELIX 1 1 GLN A 53 SER A 57 5 5
HELIX 2 2 TYR A 123 ALA A 127 5 5
HELIX 3 3 PRO A 135 THR A 144 1 10
HELIX 4 4 LYS A 218 TYR A 222 5 5
HELIX 5 5 LYS A 238 SER A 252 1 15
HELIX 6 6 PRO A 276 PHE A 280 5 5
HELIX 7 7 LEU A 301 TYR A 305 1 5
HELIX 8 8 GLY A 334 GLU A 339 1 6
HELIX 9 9 ARG A 347 ARG A 349 5 3
HELIX 10 10 TYR B 123 ALA B 127 5 5
HELIX 11 11 PRO B 135 THR B 144 1 10
HELIX 12 12 ASP B 180 SER B 182 5 3
HELIX 13 13 ASP B 216 ASN B 221 1 6
HELIX 14 14 LYS B 238 SER B 252 1 15
HELIX 15 15 GLY B 260 GLY B 264 5 5
HELIX 16 16 PRO B 276 PHE B 280 5 5
HELIX 17 17 LEU B 301 TYR B 305 1 5
HELIX 18 18 GLY B 334 GLU B 339 1 6
HELIX 19 19 ARG B 347 ARG B 349 5 3
HELIX 20 20 PHE C -1 VAL C 3 5 5
HELIX 21 21 GLN C 53 SER C 57 5 5
HELIX 22 22 TYR C 123 ALA C 127 5 5
HELIX 23 23 PRO C 135 THR C 144 1 10
HELIX 24 24 ASP C 180 SER C 182 5 3
HELIX 25 25 ASP C 216 TYR C 222 5 7
HELIX 26 26 LYS C 238 SER C 252 1 15
HELIX 27 27 PRO C 276 PHE C 280 5 5
HELIX 28 28 LEU C 301 TYR C 305 1 5
HELIX 29 29 GLY C 334 GLU C 339 1 6
HELIX 30 30 ARG C 347 ARG C 349 5 3
HELIX 31 31 MET C 379 GLY C 383 5 5
SHEET 1 A 2 ARG A -4 GLY A -3 0
SHEET 2 A 2 ILE A 179 ASP A 180 1 O ILE A 179 N GLY A -3
SHEET 1 B 9 ARG A 61 PRO A 70 0
SHEET 2 B 9 ALA A 75 SER A 86 -1 O GLY A 78 N VAL A 67
SHEET 3 B 9 TYR A 14 VAL A 20 -1 N THR A 19 O SER A 86
SHEET 4 B 9 LEU A 6 GLY A 8 -1 N ARG A 7 O TYR A 15
SHEET 5 B 9 GLY A 171 ILE A 176 -1 O GLY A 172 N LEU A 6
SHEET 6 B 9 PHE A 150 CYS A 155 -1 N CYS A 155 O GLY A 171
SHEET 7 B 9 PHE A 341 ASP A 346 -1 O VAL A 343 N LEU A 152
SHEET 8 B 9 ARG A 351 SER A 357 -1 O ALA A 355 N TYR A 342
SHEET 9 B 9 TYR A 184 PRO A 192 -1 N THR A 191 O ILE A 352
SHEET 1 C13 ARG A 61 PRO A 70 0
SHEET 2 C13 ALA A 75 SER A 86 -1 O GLY A 78 N VAL A 67
SHEET 3 C13 THR A 94 ASP A 106 -1 O ASP A 106 N ALA A 75
SHEET 4 C13 PHE A 38 GLY A 41 1 N VAL A 40 O ILE A 102
SHEET 5 C13 GLY A 117 GLY A 120 -1 O ILE A 118 N ALA A 39
SHEET 6 C13 GLN A 25 ASP A 32 1 N LEU A 30 O LEU A 119
SHEET 7 C13 TYR A 14 VAL A 20 -1 N VAL A 16 O ILE A 29
SHEET 8 C13 LEU A 6 GLY A 8 -1 N ARG A 7 O TYR A 15
SHEET 9 C13 GLY A 171 ILE A 176 -1 O GLY A 172 N LEU A 6
SHEET 10 C13 PHE A 150 CYS A 155 -1 N CYS A 155 O GLY A 171
SHEET 11 C13 PHE A 341 ASP A 346 -1 O VAL A 343 N LEU A 152
SHEET 12 C13 ARG A 351 SER A 357 -1 O ALA A 355 N TYR A 342
SHEET 13 C13 TYR A 184 PRO A 192 -1 N THR A 191 O ILE A 352
SHEET 1 D 5 GLN A 211 ASP A 212 0
SHEET 2 D 5 ILE A 203 ILE A 208 -1 N ILE A 208 O GLN A 211
SHEET 3 D 5 ILE A 283 MET A 288 -1 O TYR A 286 N ARG A 205
SHEET 4 D 5 GLN A 294 ILE A 300 -1 O ILE A 300 N ILE A 283
SHEET 5 D 5 ALA A 369 VAL A 375 -1 O GLU A 371 N ARG A 297
SHEET 1 E 4 SER A 225 VAL A 227 0
SHEET 2 E 4 THR A 331 MET A 333 1 O MET A 333 N ILE A 226
SHEET 3 E 4 LEU A 234 PRO A 237 -1 N ARG A 235 O VAL A 332
SHEET 4 E 4 ILE A 324 SER A 327 1 O SER A 325 N LEU A 236
SHEET 1 F 3 VAL A 268 CYS A 269 0
SHEET 2 F 3 CYS A 319 PHE A 322 -1 O TYR A 320 N VAL A 268
SHEET 3 F 3 LEU A 306 PRO A 308 -1 N ARG A 307 O LYS A 321
SHEET 1 G 9 ARG B 61 PRO B 70 0
SHEET 2 G 9 ALA B 75 SER B 86 -1 O GLY B 78 N VAL B 67
SHEET 3 G 9 TYR B 14 VAL B 20 -1 N THR B 19 O SER B 86
SHEET 4 G 9 LEU B 6 GLY B 8 -1 N ARG B 7 O TYR B 15
SHEET 5 G 9 GLY B 171 ILE B 176 -1 O GLY B 172 N LEU B 6
SHEET 6 G 9 PHE B 150 CYS B 155 -1 N SER B 151 O ILE B 175
SHEET 7 G 9 PHE B 341 ASP B 346 -1 O VAL B 343 N LEU B 152
SHEET 8 G 9 ARG B 351 SER B 357 -1 O GLY B 353 N VAL B 344
SHEET 9 G 9 TYR B 184 PRO B 192 -1 N THR B 191 O ILE B 352
SHEET 1 H13 ARG B 61 PRO B 70 0
SHEET 2 H13 ALA B 75 SER B 86 -1 O GLY B 78 N VAL B 67
SHEET 3 H13 VAL B 95 ASP B 106 -1 O GLU B 104 N ALA B 77
SHEET 4 H13 PHE B 38 GLY B 41 1 N VAL B 40 O ILE B 102
SHEET 5 H13 GLY B 117 GLY B 120 -1 O ILE B 118 N ALA B 39
SHEET 6 H13 GLN B 25 ASP B 32 1 N LEU B 30 O GLY B 117
SHEET 7 H13 TYR B 14 VAL B 20 -1 N VAL B 20 O GLN B 25
SHEET 8 H13 LEU B 6 GLY B 8 -1 N ARG B 7 O TYR B 15
SHEET 9 H13 GLY B 171 ILE B 176 -1 O GLY B 172 N LEU B 6
SHEET 10 H13 PHE B 150 CYS B 155 -1 N SER B 151 O ILE B 175
SHEET 11 H13 PHE B 341 ASP B 346 -1 O VAL B 343 N LEU B 152
SHEET 12 H13 ARG B 351 SER B 357 -1 O GLY B 353 N VAL B 344
SHEET 13 H13 TYR B 184 PRO B 192 -1 N THR B 191 O ILE B 352
SHEET 1 I 5 GLN B 211 ASP B 212 0
SHEET 2 I 5 ILE B 203 ILE B 208 -1 N ILE B 208 O GLN B 211
SHEET 3 I 5 ILE B 283 MET B 288 -1 O TYR B 286 N ARG B 205
SHEET 4 I 5 GLN B 294 ILE B 300 -1 O PHE B 296 N LEU B 287
SHEET 5 I 5 ALA B 369 VAL B 375 -1 O ALA B 369 N THR B 299
SHEET 1 J 4 SER B 225 VAL B 227 0
SHEET 2 J 4 THR B 331 MET B 333 1 O MET B 333 N ILE B 226
SHEET 3 J 4 LEU B 234 PRO B 237 -1 N ARG B 235 O VAL B 332
SHEET 4 J 4 ILE B 324 SER B 327 1 O SER B 325 N LEU B 236
SHEET 1 K 3 VAL B 268 CYS B 269 0
SHEET 2 K 3 CYS B 319 PHE B 322 -1 O TYR B 320 N VAL B 268
SHEET 3 K 3 LEU B 306 PRO B 308 -1 N ARG B 307 O LYS B 321
SHEET 1 L 8 ARG C 7 GLY C 8 0
SHEET 2 L 8 TYR C 14 VAL C 20 -1 O TYR C 15 N ARG C 7
SHEET 3 L 8 GLN C 25 ASP C 32 -1 O ILE C 29 N VAL C 16
SHEET 4 L 8 GLY C 117 GLY C 120 1 O GLY C 117 N LEU C 30
SHEET 5 L 8 PHE C 38 GLY C 41 -1 N ALA C 39 O ILE C 118
SHEET 6 L 8 THR C 94 ASP C 106 1 O ILE C 102 N VAL C 40
SHEET 7 L 8 ALA C 75 SER C 86 -1 N ALA C 77 O GLU C 104
SHEET 8 L 8 ARG C 61 PRO C 70 -1 N LYS C 65 O LEU C 80
SHEET 1 M 4 ARG C 7 GLY C 8 0
SHEET 2 M 4 TYR C 14 VAL C 20 -1 O TYR C 15 N ARG C 7
SHEET 3 M 4 ALA C 75 SER C 86 -1 O SER C 86 N THR C 19
SHEET 4 M 4 ARG C 61 PRO C 70 -1 N LYS C 65 O LEU C 80
SHEET 1 N 5 GLY C 172 ILE C 176 0
SHEET 2 N 5 PHE C 150 LEU C 154 -1 N GLN C 153 O SER C 173
SHEET 3 N 5 PHE C 341 ASP C 346 -1 O PHE C 345 N PHE C 150
SHEET 4 N 5 ARG C 351 SER C 357 -1 O GLY C 353 N VAL C 344
SHEET 5 N 5 TYR C 184 PRO C 192 -1 N TRP C 189 O PHE C 354
SHEET 1 O 5 GLN C 211 ASP C 212 0
SHEET 2 O 5 ILE C 203 ILE C 208 -1 N ILE C 208 O GLN C 211
SHEET 3 O 5 ILE C 283 MET C 288 -1 O TYR C 286 N ARG C 205
SHEET 4 O 5 GLN C 294 ILE C 300 -1 O PHE C 296 N LEU C 287
SHEET 5 O 5 ALA C 369 VAL C 375 -1 O PHE C 374 N SER C 295
SHEET 1 P 4 SER C 225 VAL C 227 0
SHEET 2 P 4 THR C 331 MET C 333 1 O MET C 333 N ILE C 226
SHEET 3 P 4 LEU C 234 PRO C 237 -1 N ARG C 235 O VAL C 332
SHEET 4 P 4 ILE C 324 SER C 327 1 O SER C 325 N LEU C 236
SHEET 1 Q 3 VAL C 268 GLN C 271 0
SHEET 2 Q 3 ASP C 317 PHE C 322 -1 O ASP C 318 N TRP C 270
SHEET 3 Q 3 LEU C 306 VAL C 309 -1 N ARG C 307 O LYS C 321
SSBOND 1 CYS A 155 CYS A 359 1555 1555 2.05
SSBOND 2 CYS A 217 CYS A 382 1555 1555 2.06
SSBOND 3 CYS A 269 CYS A 319 1555 1555 2.05
SSBOND 4 CYS B 155 CYS B 359 1555 1555 2.06
SSBOND 5 CYS B 217 CYS B 382 1555 1555 2.04
SSBOND 6 CYS B 269 CYS B 319 1555 1555 2.05
SSBOND 7 CYS C 155 CYS C 359 1555 1555 2.06
SSBOND 8 CYS C 217 CYS C 382 1555 1555 2.05
SSBOND 9 CYS C 269 CYS C 319 1555 1555 2.05
CISPEP 1 SER A 22 PRO A 23 0 -6.89
CISPEP 2 ARG A 128 PRO A 129 0 -3.69
CISPEP 3 TYR A 222 ASP A 223 0 3.97
CISPEP 4 GLY A 372 PRO A 373 0 0.27
CISPEP 5 SER B 22 PRO B 23 0 -3.84
CISPEP 6 ARG B 128 PRO B 129 0 0.50
CISPEP 7 GLU B 310 ASP B 311 0 -0.80
CISPEP 8 GLY B 372 PRO B 373 0 -2.14
CISPEP 9 SER C 22 PRO C 23 0 -0.99
CISPEP 10 ARG C 128 PRO C 129 0 1.20
CISPEP 11 GLY C 372 PRO C 373 0 4.43
SITE 1 AC1 2 ARG A 64 GLY B 186
SITE 1 AC2 1 TYR B 184
SITE 1 AC3 3 THR A 185 GLY A 186 ARG C 64
SITE 1 AC4 2 ARG C 349 ARG C 351
CRYST1 225.100 105.170 65.140 90.00 102.05 90.00 C 1 2 1 12
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 0.004442 0.000000 0.000949 0.00000
SCALE2 0.000000 0.009508 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015698 0.00000
(ATOM LINES ARE NOT SHOWN.)
END