HEADER HYDROLASE 05-MAY-16 5JR6
TITLE THE XRAY CRYSTAL STRUCTURE OF P. FALCIPARUM AMINOPEPTIDASE P IN
TITLE 2 COMPLEX WITH APSTATIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEPTIDASE, PUTATIVE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 108-764;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: APSTATIN;
COMPND 8 CHAIN: F;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM (ISOLATE 3D7);
SOURCE 3 ORGANISM_TAXID: 36329;
SOURCE 4 STRAIN: ISOLATE 3D7;
SOURCE 5 GENE: PF14_0517;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 11 ORGANISM_TAXID: 32630
KEYWDS AMINOPEPTIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.DRINKWATER,S.MCGOWAN
REVDAT 5 15-NOV-23 5JR6 1 LINK ATOM
REVDAT 4 27-SEP-23 5JR6 1 REMARK LINK
REVDAT 3 26-OCT-16 5JR6 1 REMARK
REVDAT 2 12-OCT-16 5JR6 1 JRNL
REVDAT 1 31-AUG-16 5JR6 0
JRNL AUTH N.DRINKWATER,K.K.SIVARAMAN,R.S.BAMERT,W.RUT,K.MOHAMED,
JRNL AUTH 2 N.B.VINH,P.J.SCAMMELLS,M.DRAG,S.MCGOWAN
JRNL TITL STRUCTURE AND SUBSTRATE FINGERPRINT OF AMINOPEPTIDASE P FROM
JRNL TITL 2 PLASMODIUM FALCIPARUM.
JRNL REF BIOCHEM.J. V. 473 3189 2016
JRNL REFN ESSN 1470-8728
JRNL PMID 27462122
JRNL DOI 10.1042/BCJ20160550
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.79
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 65020
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 3236
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 42.8001 - 6.5335 0.99 2762 130 0.1962 0.2563
REMARK 3 2 6.5335 - 5.1887 0.98 2662 158 0.2105 0.2249
REMARK 3 3 5.1887 - 4.5336 0.99 2692 139 0.1681 0.2192
REMARK 3 4 4.5336 - 4.1195 1.00 2702 158 0.1589 0.1990
REMARK 3 5 4.1195 - 3.8244 1.00 2673 150 0.1635 0.1931
REMARK 3 6 3.8244 - 3.5991 1.00 2670 174 0.1684 0.2051
REMARK 3 7 3.5991 - 3.4189 1.00 2676 139 0.1816 0.2185
REMARK 3 8 3.4189 - 3.2701 0.99 2705 135 0.1928 0.2722
REMARK 3 9 3.2701 - 3.1443 1.00 2675 135 0.1971 0.2446
REMARK 3 10 3.1443 - 3.0358 1.00 2712 133 0.2093 0.2613
REMARK 3 11 3.0358 - 2.9409 1.00 2689 131 0.2065 0.2711
REMARK 3 12 2.9409 - 2.8569 1.00 2668 141 0.2208 0.2976
REMARK 3 13 2.8569 - 2.7817 1.00 2673 130 0.2128 0.2629
REMARK 3 14 2.7817 - 2.7138 1.00 2720 137 0.2190 0.2612
REMARK 3 15 2.7138 - 2.6521 1.00 2669 144 0.2317 0.2956
REMARK 3 16 2.6521 - 2.5957 1.00 2678 143 0.2336 0.3084
REMARK 3 17 2.5957 - 2.5438 1.00 2657 135 0.2354 0.2990
REMARK 3 18 2.5438 - 2.4958 1.00 2697 140 0.2440 0.3028
REMARK 3 19 2.4958 - 2.4512 1.00 2678 144 0.2404 0.3130
REMARK 3 20 2.4512 - 2.4097 1.00 2672 131 0.2513 0.2835
REMARK 3 21 2.4097 - 2.3708 1.00 2744 131 0.2516 0.2823
REMARK 3 22 2.3708 - 2.3343 1.00 2637 129 0.2685 0.2990
REMARK 3 23 2.3343 - 2.3000 1.00 2673 149 0.2800 0.3364
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) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.230
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 9196
REMARK 3 ANGLE : 1.169 12488
REMARK 3 CHIRALITY : 0.047 1439
REMARK 3 PLANARITY : 0.007 1595
REMARK 3 DIHEDRAL : 13.926 3236
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -24.5105 58.7471 232.5463
REMARK 3 T TENSOR
REMARK 3 T11: 0.3282 T22: 0.4042
REMARK 3 T33: 0.3395 T12: 0.0791
REMARK 3 T13: -0.0102 T23: -0.1454
REMARK 3 L TENSOR
REMARK 3 L11: 2.7700 L22: 1.1168
REMARK 3 L33: 0.8560 L12: -0.5133
REMARK 3 L13: 0.6567 L23: -0.0927
REMARK 3 S TENSOR
REMARK 3 S11: 0.2561 S12: 0.6756 S13: -0.5184
REMARK 3 S21: -0.1164 S22: -0.1232 S23: 0.0894
REMARK 3 S31: 0.0956 S32: -0.0440 S33: -0.0361
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 5JR6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000221099.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-AUG-15
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 : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
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 : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65055
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 71.030
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.7000
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: 5JQK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 45% MPD, 0.1M SODIUM CACODYLATE PH 6,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
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 73.61000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.96500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 73.61000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 49.96500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 47980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, F
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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE APSTATIN IS PEPTIDE-LIKE, A MEMBER OF ENZYME INHIBITOR CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: APSTATIN
REMARK 400 CHAIN: F
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
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 120
REMARK 465 ASN A 121
REMARK 465 THR A 122
REMARK 465 VAL A 123
REMARK 465 ASP A 124
REMARK 465 VAL A 125
REMARK 465 ASN A 126
REMARK 465 MET A 127
REMARK 465 MET A 128
REMARK 465 GLU A 233
REMARK 465 ASN A 279
REMARK 465 LYS A 280
REMARK 465 LYS A 281
REMARK 465 ASP A 282
REMARK 465 ASP A 283
REMARK 465 GLU A 284
REMARK 465 ASN A 285
REMARK 465 VAL A 286
REMARK 465 LYS A 300
REMARK 465 ASP A 301
REMARK 465 GLU A 379
REMARK 465 HIS A 430
REMARK 465 ASN A 431
REMARK 465 ASP A 432
REMARK 465 ASP A 433
REMARK 465 ASN A 434
REMARK 465 PRO A 435
REMARK 465 HIS A 775
REMARK 465 ASN A 776
REMARK 465 ASN A 777
REMARK 465 HIS A 778
REMARK 465 HIS A 779
REMARK 465 HIS A 780
REMARK 465 HIS A 781
REMARK 465 HIS A 782
REMARK 465 HIS A 783
REMARK 465 MET B 120
REMARK 465 ASN B 121
REMARK 465 THR B 122
REMARK 465 VAL B 123
REMARK 465 ASP B 124
REMARK 465 VAL B 125
REMARK 465 ASN B 126
REMARK 465 MET B 127
REMARK 465 MET B 128
REMARK 465 ASP B 129
REMARK 465 ASN B 130
REMARK 465 ASN B 131
REMARK 465 PRO B 132
REMARK 465 ALA B 133
REMARK 465 ALA B 134
REMARK 465 ARG B 135
REMARK 465 LEU B 136
REMARK 465 GLU B 137
REMARK 465 GLU B 138
REMARK 465 LEU B 139
REMARK 465 ARG B 140
REMARK 465 THR B 141
REMARK 465 ILE B 142
REMARK 465 MET B 143
REMARK 465 LYS B 144
REMARK 465 LYS B 145
REMARK 465 ASN B 146
REMARK 465 LYS B 147
REMARK 465 ILE B 148
REMARK 465 ASP B 149
REMARK 465 VAL B 172
REMARK 465 LYS B 173
REMARK 465 ILE B 174
REMARK 465 THR B 175
REMARK 465 ASN B 176
REMARK 465 TYR B 177
REMARK 465 SER B 178
REMARK 465 GLY B 179
REMARK 465 THR B 187
REMARK 465 LYS B 188
REMARK 465 ASP B 189
REMARK 465 LYS B 190
REMARK 465 PRO B 191
REMARK 465 ILE B 192
REMARK 465 LEU B 193
REMARK 465 TYR B 194
REMARK 465 VAL B 195
REMARK 465 ASN B 196
REMARK 465 ALA B 197
REMARK 465 LEU B 198
REMARK 465 TYR B 199
REMARK 465 GLU B 200
REMARK 465 LEU B 201
REMARK 465 GLN B 202
REMARK 465 ALA B 203
REMARK 465 MET B 204
REMARK 465 ASN B 205
REMARK 465 GLU B 206
REMARK 465 LEU B 207
REMARK 465 ASP B 208
REMARK 465 GLN B 209
REMARK 465 ASN B 210
REMARK 465 LEU B 211
REMARK 465 PHE B 212
REMARK 465 THR B 213
REMARK 465 LEU B 214
REMARK 465 SER B 230
REMARK 465 SER B 231
REMARK 465 LEU B 232
REMARK 465 GLU B 233
REMARK 465 PHE B 234
REMARK 465 ASN B 235
REMARK 465 THR B 236
REMARK 465 LYS B 262
REMARK 465 LYS B 263
REMARK 465 ILE B 270
REMARK 465 TYR B 271
REMARK 465 ASN B 272
REMARK 465 ASN B 273
REMARK 465 ASN B 274
REMARK 465 PHE B 275
REMARK 465 ASP B 276
REMARK 465 ASP B 277
REMARK 465 VAL B 278
REMARK 465 ASN B 279
REMARK 465 LYS B 280
REMARK 465 LYS B 281
REMARK 465 ASP B 282
REMARK 465 ASP B 283
REMARK 465 GLU B 284
REMARK 465 ASN B 285
REMARK 465 VAL B 286
REMARK 465 LEU B 287
REMARK 465 ASN B 288
REMARK 465 GLU B 298
REMARK 465 ILE B 299
REMARK 465 LYS B 300
REMARK 465 ASP B 301
REMARK 465 GLU B 378
REMARK 465 GLU B 379
REMARK 465 PRO B 428
REMARK 465 LYS B 429
REMARK 465 HIS B 430
REMARK 465 ASN B 431
REMARK 465 ASP B 432
REMARK 465 ASP B 433
REMARK 465 ASN B 434
REMARK 465 PRO B 435
REMARK 465 THR B 555
REMARK 465 ILE B 774
REMARK 465 HIS B 775
REMARK 465 ASN B 776
REMARK 465 ASN B 777
REMARK 465 HIS B 778
REMARK 465 HIS B 779
REMARK 465 HIS B 780
REMARK 465 HIS B 781
REMARK 465 HIS B 782
REMARK 465 HIS B 783
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 ASP A 129 CG OD1 OD2
REMARK 470 ASN A 130 CG OD1 ND2
REMARK 470 ARG A 135 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 137 CG CD OE1 OE2
REMARK 470 GLU A 138 CG CD OE1 OE2
REMARK 470 LEU A 139 CG CD1 CD2
REMARK 470 ARG A 140 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 142 CG1 CG2 CD1
REMARK 470 LYS A 144 CG CD CE NZ
REMARK 470 LYS A 145 CG CD CE NZ
REMARK 470 LYS A 147 CG CD CE NZ
REMARK 470 ILE A 148 CG1 CG2 CD1
REMARK 470 ASP A 149 CG OD1 OD2
REMARK 470 VAL A 150 CG1 CG2
REMARK 470 ILE A 152 CG1 CG2 CD1
REMARK 470 LYS A 170 CE NZ
REMARK 470 ILE A 171 CG1 CG2 CD1
REMARK 470 LYS A 173 CG CD CE NZ
REMARK 470 LYS A 188 CG CD CE NZ
REMARK 470 ASP A 189 CG OD1 OD2
REMARK 470 LYS A 190 CG CD CE NZ
REMARK 470 ASN A 205 CG OD1 ND2
REMARK 470 GLU A 206 CG CD OE1 OE2
REMARK 470 LEU A 211 CG CD1 CD2
REMARK 470 LEU A 214 CG CD1 CD2
REMARK 470 ARG A 215 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 218 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 219 CG1 CG2 CD1
REMARK 470 ASN A 221 CG OD1 ND2
REMARK 470 ARG A 222 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 227 CG CD OE1 OE2
REMARK 470 SER A 230 OG
REMARK 470 LEU A 232 CG CD1 CD2
REMARK 470 PHE A 234 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN A 235 CG OD1 ND2
REMARK 470 THR A 236 OG1 CG2
REMARK 470 LYS A 242 CG CD CE NZ
REMARK 470 LYS A 262 CG CD CE NZ
REMARK 470 LYS A 263 CG CD CE NZ
REMARK 470 LYS A 264 CG CD CE NZ
REMARK 470 VAL A 266 CG1 CG2
REMARK 470 LYS A 268 CG CD CE NZ
REMARK 470 ASN A 274 CG OD1 ND2
REMARK 470 ASP A 276 CG OD1 OD2
REMARK 470 ASP A 277 CG OD1 OD2
REMARK 470 VAL A 278 CG1 CG2
REMARK 470 LEU A 287 CG CD1 CD2
REMARK 470 LEU A 290 CG CD1 CD2
REMARK 470 GLU A 298 CG CD OE1 OE2
REMARK 470 ILE A 299 CG1 CG2 CD1
REMARK 470 VAL A 304 CG1 CG2
REMARK 470 ASN A 306 CG OD1 ND2
REMARK 470 GLU A 323 OE1 OE2
REMARK 470 ILE A 336 CG2 CD1
REMARK 470 ASP A 376 CG OD1 OD2
REMARK 470 GLU A 378 CG CD OE1 OE2
REMARK 470 LYS A 384 CG CD CE NZ
REMARK 470 ASP A 397 CG OD1 OD2
REMARK 470 ASN A 400 CG OD1 ND2
REMARK 470 LEU A 401 CG CD1 CD2
REMARK 470 GLU A 403 CG CD OE1 OE2
REMARK 470 ILE A 404 CG1 CG2 CD1
REMARK 470 ASN A 405 CG OD1 ND2
REMARK 470 LYS A 406 CG CD CE NZ
REMARK 470 ILE A 408 CG1 CG2 CD1
REMARK 470 VAL A 422 CG1 CG2
REMARK 470 VAL A 423 CG1 CG2
REMARK 470 SER A 426 OG
REMARK 470 ILE A 427 CG1 CG2 CD1
REMARK 470 LYS A 429 CG CD CE NZ
REMARK 470 ASP A 436 CG OD1 OD2
REMARK 470 PHE A 437 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 438 CD CE NZ
REMARK 470 ASP A 457 CG OD1 OD2
REMARK 470 LYS A 459 CG CD CE NZ
REMARK 470 SER A 466 OG
REMARK 470 GLN A 503 CD OE1 NE2
REMARK 470 THR A 507 OG1 CG2
REMARK 470 GLU A 553 CG CD OE1 OE2
REMARK 470 THR A 555 OG1 CG2
REMARK 470 ASP A 556 CG OD1 OD2
REMARK 470 LYS A 557 CG CD CE NZ
REMARK 470 ASP A 702 CG OD1 OD2
REMARK 470 LYS A 733 CG CD CE NZ
REMARK 470 GLN A 755 CG CD OE1 NE2
REMARK 470 LYS A 763 CG CD CE NZ
REMARK 470 VAL B 150 CG1 CG2
REMARK 470 LEU B 153 CG CD1 CD2
REMARK 470 ASN B 155 CG OD1 ND2
REMARK 470 SER B 156 OG
REMARK 470 GLU B 158 CG CD OE1 OE2
REMARK 470 SER B 161 OG
REMARK 470 ILE B 163 CG1 CG2 CD1
REMARK 470 GLU B 166 CG CD OE1 OE2
REMARK 470 ILE B 171 CG1 CG2 CD1
REMARK 470 LEU B 184 CG CD1 CD2
REMARK 470 ILE B 185 CG1 CG2 CD1
REMARK 470 VAL B 186 CG1 CG2
REMARK 470 ARG B 215 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 216 CG1 CG2 CD1
REMARK 470 ARG B 218 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 219 CG1 CG2 CD1
REMARK 470 ASP B 220 CG OD1 OD2
REMARK 470 ASN B 221 CG OD1 ND2
REMARK 470 GLU B 227 CG CD OE1 OE2
REMARK 470 THR B 228 OG1 CG2
REMARK 470 ILE B 229 CG1 CG2 CD1
REMARK 470 ILE B 237 CG1 CG2 CD1
REMARK 470 LYS B 242 CG CD CE NZ
REMARK 470 LYS B 251 CG CD CE NZ
REMARK 470 ARG B 253 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 254 CG CD CE NZ
REMARK 470 LEU B 256 CG CD1 CD2
REMARK 470 ASN B 258 CG OD1 ND2
REMARK 470 TYR B 260 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 264 CG CD CE NZ
REMARK 470 ILE B 265 CG1 CG2 CD1
REMARK 470 VAL B 266 CG1 CG2
REMARK 470 GLU B 267 CG CD OE1 OE2
REMARK 470 LYS B 268 CG CD CE NZ
REMARK 470 ILE B 269 CG1 CG2 CD1
REMARK 470 LEU B 290 CG CD1 CD2
REMARK 470 LYS B 294 CG CD CE NZ
REMARK 470 SER B 295 OG
REMARK 470 LEU B 296 CG CD1 CD2
REMARK 470 VAL B 297 CG1 CG2
REMARK 470 TYR B 302 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 323 CG CD OE1 OE2
REMARK 470 LYS B 327 CG CD CE NZ
REMARK 470 LYS B 329 CG CD CE NZ
REMARK 470 SER B 331 OG
REMARK 470 LYS B 337 CG CD CE NZ
REMARK 470 LEU B 356 CG CD1 CD2
REMARK 470 LEU B 372 CG CD1 CD2
REMARK 470 ASP B 376 CG OD1 OD2
REMARK 470 GLN B 380 CG CD OE1 NE2
REMARK 470 PHE B 382 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 384 CG CD CE NZ
REMARK 470 LEU B 394 CG CD1 CD2
REMARK 470 ASP B 397 CG OD1 OD2
REMARK 470 VAL B 398 CG1 CG2
REMARK 470 LYS B 399 CG CD CE NZ
REMARK 470 ASN B 400 CG OD1 ND2
REMARK 470 LEU B 401 CG CD1 CD2
REMARK 470 GLU B 403 CG CD OE1 OE2
REMARK 470 ILE B 404 CG1 CG2 CD1
REMARK 470 ASN B 405 CG OD1 ND2
REMARK 470 LYS B 406 CG CD CE NZ
REMARK 470 LYS B 410 CG CD CE NZ
REMARK 470 GLU B 411 CG CD OE1 OE2
REMARK 470 GLU B 413 CG CD OE1 OE2
REMARK 470 GLU B 414 CG CD OE1 OE2
REMARK 470 ILE B 415 CG1 CG2 CD1
REMARK 470 ARG B 420 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 421 CG OD1 OD2
REMARK 470 VAL B 423 CG1 CG2
REMARK 470 ILE B 424 CG1 CG2 CD1
REMARK 470 ILE B 427 CG1 CG2 CD1
REMARK 470 ASP B 436 CG OD1 OD2
REMARK 470 PHE B 437 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 439 CG CD CE NZ
REMARK 470 LEU B 455 CG CD1 CD2
REMARK 470 LYS B 459 CG CD CE NZ
REMARK 470 ASN B 460 CG OD1 ND2
REMARK 470 VAL B 461 CG1 CG2
REMARK 470 GLN B 503 CG CD OE1 NE2
REMARK 470 HIS B 551 CG ND1 CD2 CE1 NE2
REMARK 470 GLU B 553 CG CD OE1 OE2
REMARK 470 ASP B 556 CG OD1 OD2
REMARK 470 LYS B 557 CG CD CE NZ
REMARK 470 THR B 558 OG1 CG2
REMARK 470 GLU B 590 CG CD OE1 OE2
REMARK 470 LYS B 669 CG CD CE NZ
REMARK 470 GLN B 752 CG CD OE1 NE2
REMARK 470 GLU B 756 CD OE1 OE2
REMARK 470 GLU B 767 CG CD OE1 OE2
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 O VAL B 468 O HOH B 901 1.98
REMARK 500 N LYS B 472 O HOH B 901 2.04
REMARK 500 OE2 GLU A 629 O HOH A 901 2.13
REMARK 500 O ARG B 377 CB GLN B 380 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 01B F 1 C PRO F 2 N 0.125
REMARK 500 PRO F 2 C PRO F 3 N 0.157
REMARK 500 PRO F 3 C ALA F 4 N 0.163
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 132 C - N - CA ANGL. DEV. = 12.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 156 175.90 179.03
REMARK 500 GLU A 206 -62.09 -103.54
REMARK 500 ILE A 533 -66.25 -99.04
REMARK 500 LEU A 650 -93.10 -121.83
REMARK 500 ASP A 683 -0.71 70.98
REMARK 500 LYS A 684 -70.54 -119.63
REMARK 500 TYR B 260 67.71 36.43
REMARK 500 TYR B 334 -60.32 -104.63
REMARK 500 ASP B 381 176.54 156.43
REMARK 500 VAL B 422 -67.22 -131.16
REMARK 500 LYS B 508 -3.54 67.20
REMARK 500 ILE B 533 -68.41 -105.81
REMARK 500 LEU B 650 -159.20 -155.82
REMARK 500 VAL B 662 -75.12 -91.23
REMARK 500 ASP B 683 -4.78 65.73
REMARK 500 LYS B 684 -78.37 -104.57
REMARK 500
REMARK 500 REMARK: NULL
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 MN A 802 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 570 OD1
REMARK 620 2 ASP A 570 OD2 53.1
REMARK 620 3 ASP A 581 OD2 105.0 153.1
REMARK 620 4 GLU A 690 OE1 98.8 106.2 91.4
REMARK 620 5 01B F 1 O2 121.5 72.5 117.7 117.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 801 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 581 OD1
REMARK 620 2 HIS A 644 NE2 91.7
REMARK 620 3 GLU A 676 OE2 156.3 78.5
REMARK 620 4 GLU A 690 OE2 80.0 122.2 87.0
REMARK 620 5 01B F 1 O2 81.8 139.4 119.5 96.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 802 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 570 OD1
REMARK 620 2 ASP B 581 OD1 109.3
REMARK 620 3 GLU B 690 OE1 113.8 91.9
REMARK 620 4 PO4 B 803 O4 105.7 114.1 121.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 801 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 581 OD2
REMARK 620 2 HIS B 644 NE2 92.2
REMARK 620 3 GLU B 676 OE2 161.8 76.8
REMARK 620 4 GLU B 690 OE2 88.0 122.1 85.8
REMARK 620 5 PO4 B 803 O2 97.5 91.2 97.1 146.1
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 01B F 1 and PRO F 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ALA F 4 and NH2 F 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5JQK RELATED DB: PDB
REMARK 900 5JQK CONTAINS THE SAME PROTEIN IN THE UNLIGANDED STATE
DBREF 5JR6 A 121 777 UNP Q8IKT5 Q8IKT5_PLAF7 108 764
DBREF 5JR6 B 121 777 UNP Q8IKT5 Q8IKT5_PLAF7 108 764
DBREF 5JR6 F 1 5 PDB 5JR6 5JR6 1 5
SEQADV 5JR6 MET A 120 UNP Q8IKT5 INITIATING METHIONINE
SEQADV 5JR6 HIS A 778 UNP Q8IKT5 EXPRESSION TAG
SEQADV 5JR6 HIS A 779 UNP Q8IKT5 EXPRESSION TAG
SEQADV 5JR6 HIS A 780 UNP Q8IKT5 EXPRESSION TAG
SEQADV 5JR6 HIS A 781 UNP Q8IKT5 EXPRESSION TAG
SEQADV 5JR6 HIS A 782 UNP Q8IKT5 EXPRESSION TAG
SEQADV 5JR6 HIS A 783 UNP Q8IKT5 EXPRESSION TAG
SEQADV 5JR6 MET B 120 UNP Q8IKT5 INITIATING METHIONINE
SEQADV 5JR6 HIS B 778 UNP Q8IKT5 EXPRESSION TAG
SEQADV 5JR6 HIS B 779 UNP Q8IKT5 EXPRESSION TAG
SEQADV 5JR6 HIS B 780 UNP Q8IKT5 EXPRESSION TAG
SEQADV 5JR6 HIS B 781 UNP Q8IKT5 EXPRESSION TAG
SEQADV 5JR6 HIS B 782 UNP Q8IKT5 EXPRESSION TAG
SEQADV 5JR6 HIS B 783 UNP Q8IKT5 EXPRESSION TAG
SEQRES 1 A 664 MET ASN THR VAL ASP VAL ASN MET MET ASP ASN ASN PRO
SEQRES 2 A 664 ALA ALA ARG LEU GLU GLU LEU ARG THR ILE MET LYS LYS
SEQRES 3 A 664 ASN LYS ILE ASP VAL TYR ILE LEU ILE ASN SER ASP GLU
SEQRES 4 A 664 HIS ASN SER GLU ILE ILE ASN GLU LYS ASP LYS LYS ILE
SEQRES 5 A 664 VAL LYS ILE THR ASN TYR SER GLY ALA ASP GLY ILE LEU
SEQRES 6 A 664 ILE VAL THR LYS ASP LYS PRO ILE LEU TYR VAL ASN ALA
SEQRES 7 A 664 LEU TYR GLU LEU GLN ALA MET ASN GLU LEU ASP GLN ASN
SEQRES 8 A 664 LEU PHE THR LEU ARG ILE SER ARG ILE ASP ASN ARG ASP
SEQRES 9 A 664 GLU ILE PHE GLU THR ILE SER SER LEU GLU PHE ASN THR
SEQRES 10 A 664 ILE ALA PHE ASP GLY LYS ASN THR SER VAL VAL PHE TYR
SEQRES 11 A 664 GLU LYS LEU ARG LYS ALA LEU LEU ASN ALA TYR PRO LYS
SEQRES 12 A 664 LYS LYS ILE VAL GLU LYS ILE ILE TYR ASN ASN ASN PHE
SEQRES 13 A 664 ASP ASP VAL ASN LYS LYS ASP ASP GLU ASN VAL LEU ASN
SEQRES 14 A 664 PHE LEU VAL LEU GLU LYS SER LEU VAL GLU ILE LYS ASP
SEQRES 15 A 664 TYR PRO VAL ASN ASN LYS THR LEU TYR ILE HIS ASP ARG
SEQRES 16 A 664 LYS TYR ASN GLY ALA CYS ALA GLY GLU LYS ILE ASP LYS
SEQRES 17 A 664 LEU LYS GLN SER LEU MET TYR ASP ILE LYS ASN VAL ASP
SEQRES 18 A 664 ASN LEU LEU LEU SER GLU LEU ASP GLU ILE ALA TYR LEU
SEQRES 19 A 664 LEU ASN LEU ARG GLY TYR ASP TYR GLN TYR SER PRO LEU
SEQRES 20 A 664 PHE TYR SER TYR LEU LEU PHE GLN PHE ASP ARG GLU GLU
SEQRES 21 A 664 GLN ASP PHE SER LYS ILE VAL PHE PHE THR THR VAL LYS
SEQRES 22 A 664 ASN LEU PRO ALA ASP VAL LYS ASN LEU LEU GLU ILE ASN
SEQRES 23 A 664 LYS VAL ILE VAL LYS GLU TYR GLU GLU ILE VAL PRO TYR
SEQRES 24 A 664 LEU ARG ASP VAL VAL ILE PRO SER ILE PRO LYS HIS ASN
SEQRES 25 A 664 ASP ASP ASN PRO ASP PHE LYS LYS TYR ASP ILE SER LEU
SEQRES 26 A 664 SER PRO TYR ILE ASN LEU MET ILE TYR LYS LEU PHE ASP
SEQRES 27 A 664 ARG LYS ASN VAL LEU LEU GLN ASN SER PRO VAL VAL LYS
SEQRES 28 A 664 MET LYS ALA VAL LYS ASN ASP VAL GLU ILE ASP ASN MET
SEQRES 29 A 664 LYS GLN ALA HIS ILE LEU ASP GLY LEU ALA LEU LEU GLN
SEQRES 30 A 664 PHE PHE HIS TRP CYS GLU GLN LYS ARG LYS THR LYS GLU
SEQRES 31 A 664 LEU PHE ASN GLU THR GLU MET SER LEU ARG HIS LYS VAL
SEQRES 32 A 664 ASP TYR PHE ARG SER THR LYS LYS ASN PHE ILE PHE PRO
SEQRES 33 A 664 SER PHE SER THR ILE SER ALA SER GLY PRO ASN ALA ALA
SEQRES 34 A 664 VAL ILE HIS TYR GLU CYS THR ASP LYS THR ASN ALA THR
SEQRES 35 A 664 ILE LYS PRO ALA ILE TYR LEU LEU ASP SER GLY GLY GLN
SEQRES 36 A 664 TYR LEU HIS GLY THR THR ASP VAL THR ARG THR THR HIS
SEQRES 37 A 664 PHE GLY GLU PRO THR ALA GLU GLU LYS ARG ILE TYR THR
SEQRES 38 A 664 LEU VAL LEU LYS GLY HIS LEU ARG LEU ARG LYS VAL ILE
SEQRES 39 A 664 PHE ALA SER TYR THR ASN SER SER ALA LEU ASP PHE ILE
SEQRES 40 A 664 ALA ARG GLU ASN LEU PHE ASN ASN PHE MET ASP TYR ASN
SEQRES 41 A 664 HIS GLY THR GLY HIS GLY VAL GLY LEU THR LEU ASN VAL
SEQRES 42 A 664 HIS GLU GLY GLY CYS SER ILE GLY PRO VAL GLY GLY ALA
SEQRES 43 A 664 PRO LEU LYS LYS ASN MET VAL LEU SER ASN GLU PRO GLY
SEQRES 44 A 664 TYR TYR MET LYS ASP LYS PHE GLY VAL ARG ILE GLU ASN
SEQRES 45 A 664 MET GLN TYR VAL ILE SER LYS GLU ILE THR ASP THR THR
SEQRES 46 A 664 GLU TYR LEU SER PHE ASP ASP LEU THR MET TYR PRO TYR
SEQRES 47 A 664 GLU LYS LYS LEU LEU ASP PHE SER LEU LEU THR ASN GLN
SEQRES 48 A 664 GLU ILE LYS GLU LEU ASN GLU TYR HIS THR THR ILE ARG
SEQRES 49 A 664 ASN THR LEU LEU PRO LEU VAL LYS GLN SER PRO GLN GLU
SEQRES 50 A 664 TYR GLY GLU SER VAL GLU LYS TYR LEU ILE GLU ILE THR
SEQRES 51 A 664 GLU PRO ILE ALA ILE HIS ASN ASN HIS HIS HIS HIS HIS
SEQRES 52 A 664 HIS
SEQRES 1 B 664 MET ASN THR VAL ASP VAL ASN MET MET ASP ASN ASN PRO
SEQRES 2 B 664 ALA ALA ARG LEU GLU GLU LEU ARG THR ILE MET LYS LYS
SEQRES 3 B 664 ASN LYS ILE ASP VAL TYR ILE LEU ILE ASN SER ASP GLU
SEQRES 4 B 664 HIS ASN SER GLU ILE ILE ASN GLU LYS ASP LYS LYS ILE
SEQRES 5 B 664 VAL LYS ILE THR ASN TYR SER GLY ALA ASP GLY ILE LEU
SEQRES 6 B 664 ILE VAL THR LYS ASP LYS PRO ILE LEU TYR VAL ASN ALA
SEQRES 7 B 664 LEU TYR GLU LEU GLN ALA MET ASN GLU LEU ASP GLN ASN
SEQRES 8 B 664 LEU PHE THR LEU ARG ILE SER ARG ILE ASP ASN ARG ASP
SEQRES 9 B 664 GLU ILE PHE GLU THR ILE SER SER LEU GLU PHE ASN THR
SEQRES 10 B 664 ILE ALA PHE ASP GLY LYS ASN THR SER VAL VAL PHE TYR
SEQRES 11 B 664 GLU LYS LEU ARG LYS ALA LEU LEU ASN ALA TYR PRO LYS
SEQRES 12 B 664 LYS LYS ILE VAL GLU LYS ILE ILE TYR ASN ASN ASN PHE
SEQRES 13 B 664 ASP ASP VAL ASN LYS LYS ASP ASP GLU ASN VAL LEU ASN
SEQRES 14 B 664 PHE LEU VAL LEU GLU LYS SER LEU VAL GLU ILE LYS ASP
SEQRES 15 B 664 TYR PRO VAL ASN ASN LYS THR LEU TYR ILE HIS ASP ARG
SEQRES 16 B 664 LYS TYR ASN GLY ALA CYS ALA GLY GLU LYS ILE ASP LYS
SEQRES 17 B 664 LEU LYS GLN SER LEU MET TYR ASP ILE LYS ASN VAL ASP
SEQRES 18 B 664 ASN LEU LEU LEU SER GLU LEU ASP GLU ILE ALA TYR LEU
SEQRES 19 B 664 LEU ASN LEU ARG GLY TYR ASP TYR GLN TYR SER PRO LEU
SEQRES 20 B 664 PHE TYR SER TYR LEU LEU PHE GLN PHE ASP ARG GLU GLU
SEQRES 21 B 664 GLN ASP PHE SER LYS ILE VAL PHE PHE THR THR VAL LYS
SEQRES 22 B 664 ASN LEU PRO ALA ASP VAL LYS ASN LEU LEU GLU ILE ASN
SEQRES 23 B 664 LYS VAL ILE VAL LYS GLU TYR GLU GLU ILE VAL PRO TYR
SEQRES 24 B 664 LEU ARG ASP VAL VAL ILE PRO SER ILE PRO LYS HIS ASN
SEQRES 25 B 664 ASP ASP ASN PRO ASP PHE LYS LYS TYR ASP ILE SER LEU
SEQRES 26 B 664 SER PRO TYR ILE ASN LEU MET ILE TYR LYS LEU PHE ASP
SEQRES 27 B 664 ARG LYS ASN VAL LEU LEU GLN ASN SER PRO VAL VAL LYS
SEQRES 28 B 664 MET LYS ALA VAL LYS ASN ASP VAL GLU ILE ASP ASN MET
SEQRES 29 B 664 LYS GLN ALA HIS ILE LEU ASP GLY LEU ALA LEU LEU GLN
SEQRES 30 B 664 PHE PHE HIS TRP CYS GLU GLN LYS ARG LYS THR LYS GLU
SEQRES 31 B 664 LEU PHE ASN GLU THR GLU MET SER LEU ARG HIS LYS VAL
SEQRES 32 B 664 ASP TYR PHE ARG SER THR LYS LYS ASN PHE ILE PHE PRO
SEQRES 33 B 664 SER PHE SER THR ILE SER ALA SER GLY PRO ASN ALA ALA
SEQRES 34 B 664 VAL ILE HIS TYR GLU CYS THR ASP LYS THR ASN ALA THR
SEQRES 35 B 664 ILE LYS PRO ALA ILE TYR LEU LEU ASP SER GLY GLY GLN
SEQRES 36 B 664 TYR LEU HIS GLY THR THR ASP VAL THR ARG THR THR HIS
SEQRES 37 B 664 PHE GLY GLU PRO THR ALA GLU GLU LYS ARG ILE TYR THR
SEQRES 38 B 664 LEU VAL LEU LYS GLY HIS LEU ARG LEU ARG LYS VAL ILE
SEQRES 39 B 664 PHE ALA SER TYR THR ASN SER SER ALA LEU ASP PHE ILE
SEQRES 40 B 664 ALA ARG GLU ASN LEU PHE ASN ASN PHE MET ASP TYR ASN
SEQRES 41 B 664 HIS GLY THR GLY HIS GLY VAL GLY LEU THR LEU ASN VAL
SEQRES 42 B 664 HIS GLU GLY GLY CYS SER ILE GLY PRO VAL GLY GLY ALA
SEQRES 43 B 664 PRO LEU LYS LYS ASN MET VAL LEU SER ASN GLU PRO GLY
SEQRES 44 B 664 TYR TYR MET LYS ASP LYS PHE GLY VAL ARG ILE GLU ASN
SEQRES 45 B 664 MET GLN TYR VAL ILE SER LYS GLU ILE THR ASP THR THR
SEQRES 46 B 664 GLU TYR LEU SER PHE ASP ASP LEU THR MET TYR PRO TYR
SEQRES 47 B 664 GLU LYS LYS LEU LEU ASP PHE SER LEU LEU THR ASN GLN
SEQRES 48 B 664 GLU ILE LYS GLU LEU ASN GLU TYR HIS THR THR ILE ARG
SEQRES 49 B 664 ASN THR LEU LEU PRO LEU VAL LYS GLN SER PRO GLN GLU
SEQRES 50 B 664 TYR GLY GLU SER VAL GLU LYS TYR LEU ILE GLU ILE THR
SEQRES 51 B 664 GLU PRO ILE ALA ILE HIS ASN ASN HIS HIS HIS HIS HIS
SEQRES 52 B 664 HIS
SEQRES 1 F 5 01B PRO PRO ALA NH2
HET 01B F 1 13
HET NH2 F 5 1
HET MN A 801 1
HET MN A 802 1
HET MN B 801 1
HET MN B 802 1
HET PO4 B 803 5
HETNAM 01B (2S,3R)-3-AMINO-2-HYDROXY-4-PHENYLBUTANOIC ACID
HETNAM NH2 AMINO GROUP
HETNAM MN MANGANESE (II) ION
HETNAM PO4 PHOSPHATE ION
FORMUL 3 01B C10 H13 N O3
FORMUL 3 NH2 H2 N
FORMUL 4 MN 4(MN 2+)
FORMUL 8 PO4 O4 P 3-
FORMUL 9 HOH *193(H2 O)
HELIX 1 AA1 ASN A 131 ASN A 146 1 16
HELIX 2 AA2 ASN A 165 LYS A 169 5 5
HELIX 3 AA3 LYS A 170 ASN A 176 1 7
HELIX 4 AA4 TYR A 199 LEU A 207 1 9
HELIX 5 AA5 ASP A 223 SER A 231 1 9
HELIX 6 AA6 SER A 245 TYR A 260 1 16
HELIX 7 AA7 ASP A 313 GLY A 318 1 6
HELIX 8 AA8 CYS A 320 ASP A 335 1 16
HELIX 9 AA9 GLU A 346 ASN A 355 1 10
HELIX 10 AB1 VAL A 391 LEU A 394 5 4
HELIX 11 AB2 PRO A 395 LEU A 401 1 7
HELIX 12 AB3 LEU A 402 ILE A 404 5 3
HELIX 13 AB4 GLU A 414 VAL A 422 1 9
HELIX 14 AB5 VAL A 423 ILE A 427 5 5
HELIX 15 AB6 ASN A 449 LEU A 455 1 7
HELIX 16 AB7 PHE A 456 LYS A 459 5 4
HELIX 17 AB8 SER A 466 VAL A 474 1 9
HELIX 18 AB9 ASN A 476 LYS A 508 1 33
HELIX 19 AC1 GLU A 509 GLU A 513 5 5
HELIX 20 AC2 THR A 514 THR A 528 1 15
HELIX 21 AC3 PRO A 545 VAL A 549 5 5
HELIX 22 AC4 THR A 592 VAL A 612 1 21
HELIX 23 AC5 ASN A 619 ASN A 633 1 15
HELIX 24 AC6 GLU A 718 LEU A 722 5 5
HELIX 25 AC7 THR A 728 GLN A 752 1 25
HELIX 26 AC8 GLY A 758 THR A 769 1 12
HELIX 27 AC9 ASN B 165 LYS B 169 5 5
HELIX 28 AD1 ASP B 223 ILE B 229 1 7
HELIX 29 AD2 SER B 245 ALA B 259 1 15
HELIX 30 AD3 ASP B 313 GLY B 318 1 6
HELIX 31 AD4 CYS B 320 TYR B 334 1 15
HELIX 32 AD5 GLU B 346 ASN B 355 1 10
HELIX 33 AD6 VAL B 391 LEU B 394 5 4
HELIX 34 AD7 PRO B 395 ASN B 405 1 11
HELIX 35 AD8 GLU B 414 VAL B 422 1 9
HELIX 36 AD9 ASN B 449 LYS B 454 1 6
HELIX 37 AE1 LEU B 455 PHE B 456 5 2
HELIX 38 AE2 ASP B 457 LYS B 459 5 3
HELIX 39 AE3 PRO B 467 LYS B 472 1 6
HELIX 40 AE4 ASN B 476 THR B 507 1 32
HELIX 41 AE5 LYS B 508 GLU B 513 5 6
HELIX 42 AE6 THR B 514 THR B 528 1 15
HELIX 43 AE7 PRO B 545 VAL B 549 5 5
HELIX 44 AE8 THR B 592 VAL B 612 1 21
HELIX 45 AE9 ASN B 619 ASN B 634 1 16
HELIX 46 AF1 GLU B 718 LEU B 722 5 5
HELIX 47 AF2 THR B 728 SER B 753 1 26
HELIX 48 AF3 GLY B 758 THR B 769 1 12
SHEET 1 AA1 7 THR A 213 SER A 217 0
SHEET 2 AA1 7 ILE A 192 ASN A 196 1 N VAL A 195 O SER A 217
SHEET 3 AA1 7 GLY A 182 VAL A 186 -1 N ILE A 183 O TYR A 194
SHEET 4 AA1 7 VAL A 150 ILE A 154 -1 N LEU A 153 O LEU A 184
SHEET 5 AA1 7 THR A 236 ASP A 240 1 O THR A 236 N VAL A 150
SHEET 6 AA1 7 ASN A 288 LEU A 292 1 O LEU A 292 N PHE A 239
SHEET 7 AA1 7 VAL A 266 ILE A 270 1 N LYS A 268 O VAL A 291
SHEET 1 AA2 2 TYR A 310 ILE A 311 0
SHEET 2 AA2 2 LEU A 356 ARG A 357 -1 O ARG A 357 N TYR A 310
SHEET 1 AA3 6 ILE A 408 GLU A 411 0
SHEET 2 AA3 6 ASP A 381 THR A 389 1 N PHE A 387 O ILE A 408
SHEET 3 AA3 6 SER A 369 ASP A 376 -1 N LEU A 372 O VAL A 386
SHEET 4 AA3 6 ASN A 341 LEU A 344 -1 N LEU A 342 O PHE A 373
SHEET 5 AA3 6 ILE A 442 LEU A 444 1 O SER A 443 N ASN A 341
SHEET 6 AA3 6 VAL A 461 LEU A 463 1 O LEU A 462 N ILE A 442
SHEET 1 AA4 3 PHE A 532 PRO A 535 0
SHEET 2 AA4 3 GLY A 573 TYR A 575 -1 O GLN A 574 N ILE A 533
SHEET 3 AA4 3 GLY A 578 THR A 579 -1 O GLY A 578 N TYR A 575
SHEET 1 AA5 3 ILE A 540 SER A 543 0
SHEET 2 AA5 3 ILE A 566 SER A 571 -1 O LEU A 568 N ALA A 542
SHEET 3 AA5 3 VAL A 582 HIS A 587 -1 O THR A 586 N TYR A 567
SHEET 1 AA6 4 PHE A 614 ALA A 615 0
SHEET 2 AA6 4 GLU A 705 ASP A 711 -1 O LEU A 707 N PHE A 614
SHEET 3 AA6 4 ASN A 691 ILE A 700 -1 N GLU A 699 O TYR A 706
SHEET 4 AA6 4 VAL A 672 ASN A 675 -1 N LEU A 673 O GLN A 693
SHEET 1 AA7 2 GLY A 643 GLY A 645 0
SHEET 2 AA7 2 GLU A 654 ILE A 659 -1 O ILE A 659 N GLY A 643
SHEET 1 AA8 2 GLY A 678 MET A 681 0
SHEET 2 AA8 2 PHE A 685 ARG A 688 -1 O PHE A 685 N MET A 681
SHEET 1 AA9 4 ILE B 183 ILE B 185 0
SHEET 2 AA9 4 TYR B 151 ILE B 154 -1 N LEU B 153 O LEU B 184
SHEET 3 AA9 4 ALA B 238 ASP B 240 1 O ALA B 238 N ILE B 152
SHEET 4 AA9 4 LEU B 290 LEU B 292 1 O LEU B 292 N PHE B 239
SHEET 1 AB1 2 TYR B 310 ILE B 311 0
SHEET 2 AB1 2 LEU B 356 ARG B 357 -1 O ARG B 357 N TYR B 310
SHEET 1 AB2 6 ILE B 408 GLU B 411 0
SHEET 2 AB2 6 PHE B 382 THR B 389 1 N PHE B 387 O ILE B 408
SHEET 3 AB2 6 SER B 369 PHE B 375 -1 N LEU B 372 O VAL B 386
SHEET 4 AB2 6 ASN B 341 LEU B 344 -1 N LEU B 344 O LEU B 371
SHEET 5 AB2 6 ILE B 442 LEU B 444 1 O SER B 443 N LEU B 343
SHEET 6 AB2 6 VAL B 461 LEU B 463 1 O LEU B 462 N ILE B 442
SHEET 1 AB3 3 PHE B 532 PRO B 535 0
SHEET 2 AB3 3 GLY B 573 TYR B 575 -1 O GLN B 574 N PHE B 534
SHEET 3 AB3 3 GLY B 578 THR B 579 -1 O GLY B 578 N TYR B 575
SHEET 1 AB4 3 ILE B 540 SER B 543 0
SHEET 2 AB4 3 ILE B 566 SER B 571 -1 O ASP B 570 N ILE B 540
SHEET 3 AB4 3 VAL B 582 HIS B 587 -1 O THR B 586 N TYR B 567
SHEET 1 AB5 4 PHE B 614 ALA B 615 0
SHEET 2 AB5 4 GLU B 705 ASP B 711 -1 O LEU B 707 N PHE B 614
SHEET 3 AB5 4 ASN B 691 ILE B 700 -1 N GLU B 699 O TYR B 706
SHEET 4 AB5 4 VAL B 672 ASN B 675 -1 N LEU B 673 O GLN B 693
SHEET 1 AB6 2 GLY B 643 GLY B 645 0
SHEET 2 AB6 2 GLU B 654 ILE B 659 -1 O GLU B 654 N GLY B 645
SHEET 1 AB7 2 GLY B 678 MET B 681 0
SHEET 2 AB7 2 PHE B 685 ARG B 688 -1 O PHE B 685 N MET B 681
LINK C 01B F 1 N PRO F 2 1555 1555 1.46
LINK C ALA F 4 N NH2 F 5 1555 1555 1.47
LINK OD1 ASP A 570 MN MN A 802 1555 1555 1.98
LINK OD2 ASP A 570 MN MN A 802 1555 1555 2.73
LINK OD1 ASP A 581 MN MN A 801 1555 1555 2.35
LINK OD2 ASP A 581 MN MN A 802 1555 1555 1.98
LINK NE2 HIS A 644 MN MN A 801 1555 1555 2.41
LINK OE2 GLU A 676 MN MN A 801 1555 1555 2.55
LINK OE2 GLU A 690 MN MN A 801 1555 1555 2.38
LINK OE1 GLU A 690 MN MN A 802 1555 1555 2.21
LINK MN MN A 801 O2 01B F 1 1555 1555 2.70
LINK MN MN A 802 O2 01B F 1 1555 1555 1.96
LINK OD1 ASP B 570 MN MN B 802 1555 1555 2.12
LINK OD2 ASP B 581 MN MN B 801 1555 1555 2.47
LINK OD1 ASP B 581 MN MN B 802 1555 1555 1.85
LINK NE2 HIS B 644 MN MN B 801 1555 1555 2.60
LINK OE2 GLU B 676 MN MN B 801 1555 1555 2.51
LINK OE2 GLU B 690 MN MN B 801 1555 1555 2.28
LINK OE1 GLU B 690 MN MN B 802 1555 1555 1.99
LINK MN MN B 801 O2 PO4 B 803 1555 1555 2.60
LINK MN MN B 802 O4 PO4 B 803 1555 1555 1.77
SITE 1 AC1 6 ASP A 581 HIS A 644 GLU A 676 GLU A 690
SITE 2 AC1 6 MN A 802 01B F 1
SITE 1 AC2 6 ASP A 570 ASP A 581 THR A 583 GLU A 690
SITE 2 AC2 6 MN A 801 01B F 1
SITE 1 AC3 6 ASP B 581 HIS B 644 GLU B 676 GLU B 690
SITE 2 AC3 6 MN B 802 PO4 B 803
SITE 1 AC4 6 ASP B 570 ASP B 581 THR B 583 GLU B 690
SITE 2 AC4 6 MN B 801 PO4 B 803
SITE 1 AC5 7 ASP B 570 ASP B 581 HIS B 653 GLU B 676
SITE 2 AC5 7 GLU B 690 MN B 801 MN B 802
SITE 1 AC6 16 GLU A 162 ILE A 163 PHE A 537 ILE A 550
SITE 2 AC6 16 ASP A 570 ASP A 581 HIS A 640 HIS A 644
SITE 3 AC6 16 VAL A 652 HIS A 653 GLU A 676 GLU A 690
SITE 4 AC6 16 MN A 801 MN A 802 PRO F 3 ALA F 4
SITE 1 AC7 3 GLY A 641 PRO F 2 PRO F 3
CRYST1 147.220 99.930 105.170 90.00 105.21 90.00 C 1 2 1 8
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 0.006793 0.000000 0.001847 0.00000
SCALE2 0.000000 0.010007 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009854 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
