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HEADER HYDROLASE 15-OCT-09 3K9B
TITLE CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE 1 (HCE1)
TITLE 2 IN COVALENT COMPLEX WITH THE NERVE AGENT CYCLOSARIN (GF)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIVER CARBOXYLESTERASE 1;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: ACYL COENZYME A:CHOLESTEROL ACYLTRANSFERASE, ACAT,
COMPND 5 MONOCYTE/MACROPHAGE SERINE ESTERASE, HMSE, SERINE ESTERASE
COMPND 6 1, BRAIN CARBOXYLESTERASE HBR1, TRIACYLGLYCEROL HYDROLASE,
COMPND 7 TGH, EGASYN, RETINYL ESTER HYDROLASE, REH;
COMPND 8 EC: 3.1.1.1;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CES1, CES2, SES1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PBAK
KEYWDS HYDROLASE, ORGANOPHOSPHORUS NERVE AGENT, ALTERNATIVE
KEYWDS 2 SPLICING, DISULFIDE BOND, ENDOPLASMIC RETICULUM,
KEYWDS 3 GLYCOPROTEIN, POLYMORPHISM, SERINE ESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.HEMMERT,M.R.REDINBO
REVDAT 1 19-JAN-10 3K9B 0
JRNL AUTH A.C.HEMMERT,T.C.OTTO,M.WEIRDL,P.M.POTTER,
JRNL AUTH 2 D.M.CERASOLI,M.R.REDINBO
JRNL TITL STEREOSPECIFIC REACTIONS OF HCE1 WITH NERVE AGENTS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 36488
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.266
REMARK 3 FREE R VALUE : 0.299
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.700
REMARK 3 FREE R VALUE TEST SET COUNT : 3643
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.30
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2680
REMARK 3 BIN FREE R VALUE : 0.2960
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11155
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 66
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 53.94
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.19
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -9.64200
REMARK 3 B22 (A**2) : 11.39900
REMARK 3 B33 (A**2) : -1.75800
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 1.70
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ANISOTROPIC OVERALL TEMPERATURE
REMARK 3 FACTORS
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 53.94
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : GFC.PAR
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3K9B COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-OCT-09.
REMARK 100 THE RCSB ID CODE IS RCSB055708.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36488
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 48.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.100
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.13100
REMARK 200 R SYM (I) : 0.13100
REMARK 200 FOR THE DATA SET : 13.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : 0.48100
REMARK 200 R SYM FOR SHELL (I) : 0.48100
REMARK 200 FOR SHELL : 4.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1MX1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 3350, 0.3 M LI2SO4, 0.1 M
REMARK 280 CITRATE PH 5.5, 0.1 M NACL, 0.1 M LICL, 5% GLYCEROL, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 27.80500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 100.03000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 89.94000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 100.03000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.80500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 89.94000
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, 4
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 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 3
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: 4
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 LEU A 1304
REMARK 465 SER A 1305
REMARK 465 LEU A 1306
REMARK 465 ASP A 1307
REMARK 465 LEU A 1308
REMARK 465 GLN A 1309
REMARK 465 GLY A 1310
REMARK 465 ASP A 1311
REMARK 465 PRO A 1312
REMARK 465 ARG A 1313
REMARK 465 GLU A 1314
REMARK 465 SER A 1315
REMARK 465 GLN A 1316
REMARK 465 PRO A 1317
REMARK 465 LEU A 1318
REMARK 465 ASN A 1340
REMARK 465 PHE A 1341
REMARK 465 HIS A 1342
REMARK 465 SER A 1369
REMARK 465 GLU A 1370
REMARK 465 GLY A 1371
REMARK 465 GLN A 1372
REMARK 465 LEU A 1373
REMARK 465 ASP A 1374
REMARK 465 GLY A 1406
REMARK 465 THR A 1407
REMARK 465 ASP A 1408
REMARK 465 ASP A 1409
REMARK 465 THR A 1410
REMARK 465 GLN A 1450
REMARK 465 TYR A 1451
REMARK 465 ARG A 1452
REMARK 465 PRO A 1453
REMARK 465 SER A 1454
REMARK 465 GLU A 1483
REMARK 465 GLY A 1484
REMARK 465 ALA A 1485
REMARK 465 SER A 1486
REMARK 465 GLU A 1487
REMARK 465 GLU A 1488
REMARK 465 LEU A 1550
REMARK 465 PHE A 1551
REMARK 465 ALA A 1552
REMARK 465 LYS A 1553
REMARK 465 ASP B 2307
REMARK 465 LEU B 2308
REMARK 465 GLN B 2309
REMARK 465 GLY B 2310
REMARK 465 ASP B 2311
REMARK 465 PRO B 2312
REMARK 465 ARG B 2313
REMARK 465 GLU B 2314
REMARK 465 SER B 2315
REMARK 465 GLN B 2316
REMARK 465 PRO B 2317
REMARK 465 LEU B 2318
REMARK 465 ALA B 2337
REMARK 465 GLU B 2338
REMARK 465 ARG B 2339
REMARK 465 ASN B 2340
REMARK 465 SER B 2369
REMARK 465 GLU B 2370
REMARK 465 GLY B 2371
REMARK 465 GLN B 2372
REMARK 465 LEU B 2373
REMARK 465 ASP B 2374
REMARK 465 GLN B 2375
REMARK 465 LYS B 2376
REMARK 465 THR B 2377
REMARK 465 CYS B 2390
REMARK 465 ILE B 2391
REMARK 465 ALA B 2392
REMARK 465 LYS B 2393
REMARK 465 GLU B 2394
REMARK 465 GLU C 3041
REMARK 465 GLY C 3042
REMARK 465 PHE C 3043
REMARK 465 ALA C 3044
REMARK 465 GLN C 3045
REMARK 465 SER C 3305
REMARK 465 LEU C 3306
REMARK 465 ASP C 3307
REMARK 465 LEU C 3308
REMARK 465 GLN C 3309
REMARK 465 GLY C 3310
REMARK 465 ASP C 3311
REMARK 465 PRO C 3312
REMARK 465 ARG C 3313
REMARK 465 GLU C 3314
REMARK 465 SER C 3315
REMARK 465 GLN C 3316
REMARK 465 PRO C 3317
REMARK 465 LEU C 3318
REMARK 465 GLU C 3338
REMARK 465 ARG C 3339
REMARK 465 ASN C 3340
REMARK 465 PHE C 3341
REMARK 465 MET C 3364
REMARK 465 SER C 3365
REMARK 465 TYR C 3366
REMARK 465 PRO C 3367
REMARK 465 LEU C 3368
REMARK 465 SER C 3369
REMARK 465 GLU C 3370
REMARK 465 GLY C 3371
REMARK 465 GLN C 3372
REMARK 465 LEU C 3373
REMARK 465 ASP C 3374
REMARK 465 GLN C 3375
REMARK 465 LYS C 3376
REMARK 465 THR C 3377
REMARK 465 ALA C 3378
REMARK 465 MET C 3379
REMARK 465 SER C 3380
REMARK 465 LEU C 3381
REMARK 465 LEU C 3382
REMARK 465 TRP C 3383
REMARK 465 LYS C 3384
REMARK 465 SER C 3385
REMARK 465 TYR C 3386
REMARK 465 PRO C 3387
REMARK 465 LEU C 3388
REMARK 465 VAL C 3389
REMARK 465 CYS C 3390
REMARK 465 ILE C 3391
REMARK 465 ALA C 3392
REMARK 465 LYS C 3393
REMARK 465 GLU C 3394
REMARK 465 LEU C 3395
REMARK 465 THR C 3410
REMARK 465 VAL C 3411
REMARK 465 LYS C 3412
REMARK 465 LYS C 3413
REMARK 465 LYS C 3414
REMARK 465 SER C 3456
REMARK 465 SER C 3457
REMARK 465 ASP C 3458
REMARK 465 MET C 3459
REMARK 465 LYS C 3460
REMARK 465 PRO C 3461
REMARK 465 LYS C 3462
REMARK 465 THR C 3463
REMARK 465 LYS C 3482
REMARK 465 GLU C 3483
REMARK 465 GLY C 3484
REMARK 465 ASN C 3549
REMARK 465 LEU C 3550
REMARK 465 PHE C 3551
REMARK 465 ALA C 3552
REMARK 465 LYS C 3553
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 ALA A 1337
REMARK 475 GLY A 1356
REMARK 475 LYS A 1376
REMARK 475 GLN A 1534
REMARK 475 PHE B 2303
REMARK 475 HIS B 2342
REMARK 475 LEU B 2368
REMARK 475 TRP B 2383
REMARK 475 LYS B 2384
REMARK 475 TYR B 2386
REMARK 475 LEU B 2404
REMARK 475 GLY B 2405
REMARK 475 GLY B 2406
REMARK 475 SER B 2456
REMARK 475 ALA B 2545
REMARK 475 THR C 3252
REMARK 475 SER C 3253
REMARK 475 PHE C 3303
REMARK 475 GLY C 3405
REMARK 475 GLY C 3511
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 1041 CB CG CD OE1 OE2
REMARK 480 GLU A 1106 CB CG CD OE1 OE2
REMARK 480 LYS A 1237 CB CG CD CE NZ
REMARK 480 LYS A 1258 CB CG CD CE NZ
REMARK 480 LYS A 1352 CB CG CD CE NZ
REMARK 480 GLN A 1375 CB CG CD OE1 NE2
REMARK 480 LYS A 1384 CB CG CD CE NZ
REMARK 480 GLU A 1394 CB CG CD OE1 OE2
REMARK 480 SER A 1457 C CB OG
REMARK 480 ASP A 1458 CB CG OD1 OD2
REMARK 480 MET A 1459 CB CG SD CE
REMARK 480 LYS A 1462 CB CG CD CE NZ
REMARK 480 LYS A 1482 CB CG CD CE NZ
REMARK 480 ARG A 1491 CB CG CD NE CZ NH1 NH2
REMARK 480 LYS A 1494 CB CG CD CE NZ
REMARK 480 LEU A 1514 CB CG CD1 CD2
REMARK 480 LYS A 1523 CB CG CD CE NZ
REMARK 480 ASN A 1532 CB CG OD1 ND2
REMARK 480 GLN A 1537 CB CG CD OE1 NE2
REMARK 480 LYS A 1538 CB CG CD CE NZ
REMARK 480 LYS A 1542 CB CG CD CE NZ
REMARK 480 LYS B 2036 CB CG CD CE NZ
REMARK 480 LYS B 2092 CB CG CD CE NZ
REMARK 480 LYS B 2105 CB CG CD CE NZ
REMARK 480 GLU B 2106 CB CG CD OE1 OE2
REMARK 480 LYS B 2111 CB CG CD CE NZ
REMARK 480 LYS B 2130 CB CG CD CE NZ
REMARK 480 THR B 2252 CB OG1 CG2
REMARK 480 SER B 2253 CB OG
REMARK 480 VAL B 2254 CB CG1 CG2
REMARK 480 LYS B 2258 CB CG CD CE NZ
REMARK 480 LYS B 2262 CB CG CD CE NZ
REMARK 480 LYS B 2302 CB CG CD CE NZ
REMARK 480 LEU B 2306 CB CG CD1 CD2
REMARK 480 LYS B 2330 CB CG CD CE NZ
REMARK 480 GLN B 2336 CB CG CD OE1 NE2
REMARK 480 THR B 2343 CB OG1 CG2
REMARK 480 LEU B 2358 CB CG CD1 CD2
REMARK 480 MET B 2379 CB CG SD CE
REMARK 480 SER B 2380 CA CB OG
REMARK 480 LEU B 2395 CB CG CD1 CD2
REMARK 480 TYR B 2403 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 480 TYR B 2403 OH
REMARK 480 ASP B 2409 CB CG OD1 OD2
REMARK 480 LYS B 2412 CB CG CD CE NZ
REMARK 480 LYS B 2413 CB CG CD CE NZ
REMARK 480 ASP B 2415 CB CG OD1 OD2
REMARK 480 ARG B 2452 CB CG CD NE CZ NH1 NH2
REMARK 480 SER B 2457 CB OG
REMARK 480 ASP B 2458 CB CG OD1 OD2
REMARK 480 MET B 2459 CB CG SD CE
REMARK 480 LYS B 2462 CB CG CD CE NZ
REMARK 480 ASN B 2532 CB CG OD1 ND2
REMARK 480 LEU C 3040 CB CG CD1 CD2
REMARK 480 PHE C 3076 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 480 LYS C 3092 CB CG CD CE NZ
REMARK 480 LYS C 3105 CB CG CD CE NZ
REMARK 480 GLU C 3106 CB CG CD OE1 OE2
REMARK 480 LYS C 3129 CB CG CD CE NZ
REMARK 480 ASP C 3260 CB CG OD1 OD2
REMARK 480 LEU C 3264 CB CG CD1 CD2
REMARK 480 GLN C 3267 CB CG CD OE1 NE2
REMARK 480 LYS C 3275 CB CG CD CE NZ
REMARK 480 LYS C 3330 N CA C O
REMARK 480 GLN C 3336 CB CG CD OE1 NE2
REMARK 480 LYS C 3352 CB CG CD CE NZ
REMARK 480 GLU C 3401 CB CG CD OE1 OE2
REMARK 480 LEU C 3404 CB CG CD1 CD2
REMARK 480 ASN C 3436 CB CG OD1 ND2
REMARK 480 ASP C 3439 CB CG OD1 OD2
REMARK 480 ARG C 3452 CB CG CD NE CZ NH1 NH2
REMARK 480 ILE C 3465 CB CG1 CG2 CD1
REMARK 480 LYS C 3494 CB CG CD CE NZ
REMARK 480 GLU C 3512 CB CG CD OE1 OE2
REMARK 480 LYS C 3523 CB CG CD CE NZ
REMARK 480 GLN C 3537 CB CG CD OE1 NE2
REMARK 480 LYS C 3538 CB CG CD CE NZ
REMARK 480 PHE C 3546 CB CG CD1 CD2 CE1 CE2 CZ
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 CG MET A 1086 O HOH A 75 1.22
REMARK 500 CG2 THR C 3088 OE2 GLU C 3291 1.87
REMARK 500 CG2 THR B 2088 OE2 GLU B 2291 1.91
REMARK 500 OG SER B 2245 OH TYR B 2346 1.97
REMARK 500 OG SER A 1221 O1 WW2 A 193 1.98
REMARK 500 SG CYS C 3087 CB CYS C 3116 2.06
REMARK 500 O ASN B 2532 OE1 GLN B 2534 2.09
REMARK 500 SG CYS A 1087 CB CYS A 1116 2.09
REMARK 500 SG CYS B 2087 CB CYS B 2116 2.10
REMARK 500 N HIS B 2030 O HOH B 28 2.11
REMARK 500 O ASN A 1532 OE1 GLN A 1534 2.11
REMARK 500 N CYS B 2087 O HOH B 76 2.15
REMARK 500 ND1 HIS B 2030 O HOH B 28 2.17
REMARK 500 OG SER B 2221 O1 WW2 B 194 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE1 GLN A 1045 O HOH C 23 2465 1.42
REMARK 500 OG SER A 1039 NH1 ARG C 3491 2465 1.98
REMARK 500 CD ARG B 2132 CG LYS B 2275 1455 2.00
REMARK 500 NE2 GLN A 1095 ND2 ASN B 2238 1655 2.08
REMARK 500 CG2 THR A 1128 OE2 GLU C 3487 2465 2.14
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 PRO A1024 CD PRO A1024 N -0.098
REMARK 500 PRO A1046 CD PRO A1046 N -0.189
REMARK 500 PRO A1054 CD PRO A1054 N -0.102
REMARK 500 PRO A1058 CD PRO A1058 N -0.136
REMARK 500 PRO A1059 CD PRO A1059 N -0.147
REMARK 500 PRO A1062 CD PRO A1062 N -0.157
REMARK 500 PRO A1067 CD PRO A1067 N -0.135
REMARK 500 PRO A1068 CD PRO A1068 N -0.100
REMARK 500 PRO A1070 CD PRO A1070 N -0.109
REMARK 500 PRO A1084 CD PRO A1084 N -0.122
REMARK 500 PRO A1085 CB PRO A1085 CG -0.356
REMARK 500 PRO A1085 C PRO A1085 O -0.150
REMARK 500 CYS A1087 CA CYS A1087 C 0.182
REMARK 500 CYS A1087 C CYS A1087 O -0.118
REMARK 500 PRO A1091 CD PRO A1091 N -0.097
REMARK 500 PRO A1109 CD PRO A1109 N -0.141
REMARK 500 PRO A1124 CD PRO A1124 N -0.117
REMARK 500 PRO A1212 CD PRO A1212 N -0.099
REMARK 500 PRO A1263 CD PRO A1263 N -0.123
REMARK 500 PRO A1332 CD PRO A1332 N -0.133
REMARK 500 PRO A1345 CB PRO A1345 CG -0.404
REMARK 500 PRO A1345 CG PRO A1345 CD -0.231
REMARK 500 PRO A1345 C PRO A1345 O -0.209
REMARK 500 TYR A1346 CB TYR A1346 CG -0.104
REMARK 500 TYR A1346 CG TYR A1346 CD2 -0.157
REMARK 500 TYR A1346 CG TYR A1346 CD1 -0.198
REMARK 500 TYR A1346 CD1 TYR A1346 CE1 -0.202
REMARK 500 TYR A1346 CE1 TYR A1346 CZ -0.285
REMARK 500 TYR A1346 CZ TYR A1346 OH -0.162
REMARK 500 TYR A1346 CZ TYR A1346 CE2 -0.256
REMARK 500 TYR A1346 CE2 TYR A1346 CD2 -0.196
REMARK 500 TYR A1346 C TYR A1346 O -0.180
REMARK 500 MET A1347 CG MET A1347 SD -0.194
REMARK 500 MET A1347 C MET A1347 O -0.218
REMARK 500 PRO A1387 CD PRO A1387 N -0.108
REMARK 500 PRO A1397 CD PRO A1397 N -0.110
REMARK 500 PRO A1429 CD PRO A1429 N -0.128
REMARK 500 PRO A1479 CD PRO A1479 N -0.141
REMARK 500 PRO A1509 CD PRO A1509 N -0.122
REMARK 500 PRO B2024 CD PRO B2024 N -0.104
REMARK 500 PRO B2046 CD PRO B2046 N -0.161
REMARK 500 PRO B2054 CD PRO B2054 N -0.101
REMARK 500 PRO B2058 CD PRO B2058 N -0.147
REMARK 500 PRO B2059 CD PRO B2059 N -0.137
REMARK 500 PRO B2062 CD PRO B2062 N -0.138
REMARK 500 PRO B2067 CD PRO B2067 N -0.137
REMARK 500 PRO B2068 CD PRO B2068 N -0.099
REMARK 500 PRO B2070 CD PRO B2070 N -0.121
REMARK 500 PRO B2073 CD PRO B2073 N -0.115
REMARK 500 PRO B2084 CD PRO B2084 N -0.139
REMARK 500
REMARK 500 THIS ENTRY HAS 117 BOND DEVIATIONS.
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 A1024 CA - N - CD ANGL. DEV. = -12.8 DEGREES
REMARK 500 PRO A1046 CA - N - CD ANGL. DEV. = -13.0 DEGREES
REMARK 500 PRO A1054 CA - N - CD ANGL. DEV. = -14.0 DEGREES
REMARK 500 PRO A1058 CA - N - CD ANGL. DEV. = -13.8 DEGREES
REMARK 500 PRO A1058 C - N - CD ANGL. DEV. = -19.1 DEGREES
REMARK 500 PRO A1059 CA - N - CD ANGL. DEV. = -14.0 DEGREES
REMARK 500 PRO A1062 CA - N - CD ANGL. DEV. = -13.8 DEGREES
REMARK 500 PRO A1067 CA - N - CD ANGL. DEV. = -13.3 DEGREES
REMARK 500 PRO A1068 CA - N - CD ANGL. DEV. = -14.3 DEGREES
REMARK 500 PRO A1070 CA - N - CD ANGL. DEV. = -12.6 DEGREES
REMARK 500 PRO A1084 CA - N - CD ANGL. DEV. = -13.4 DEGREES
REMARK 500 CYS A1087 CB - CA - C ANGL. DEV. = 15.5 DEGREES
REMARK 500 CYS A1087 O - C - N ANGL. DEV. = -11.5 DEGREES
REMARK 500 PRO A1091 CA - N - CD ANGL. DEV. = -13.8 DEGREES
REMARK 500 PRO A1109 CA - N - CD ANGL. DEV. = -13.1 DEGREES
REMARK 500 PRO A1124 CA - N - CD ANGL. DEV. = -13.2 DEGREES
REMARK 500 PRO A1134 CA - N - CD ANGL. DEV. = -12.7 DEGREES
REMARK 500 PRO A1212 CA - N - CD ANGL. DEV. = -13.6 DEGREES
REMARK 500 PRO A1263 CA - N - CD ANGL. DEV. = -13.0 DEGREES
REMARK 500 PRO A1263 C - N - CD ANGL. DEV. = -14.1 DEGREES
REMARK 500 PRO A1332 CA - N - CD ANGL. DEV. = -13.1 DEGREES
REMARK 500 PRO A1345 CA - N - CD ANGL. DEV. = -8.6 DEGREES
REMARK 500 PRO A1345 N - CA - CB ANGL. DEV. = -8.3 DEGREES
REMARK 500 PRO A1345 CA - C - O ANGL. DEV. = -20.9 DEGREES
REMARK 500 PRO A1345 CA - C - N ANGL. DEV. = 15.9 DEGREES
REMARK 500 MET A1347 CB - CA - C ANGL. DEV. = -15.7 DEGREES
REMARK 500 PRO A1360 CA - N - CD ANGL. DEV. = -13.6 DEGREES
REMARK 500 PRO A1360 C - N - CD ANGL. DEV. = -16.8 DEGREES
REMARK 500 PRO A1387 CA - N - CD ANGL. DEV. = -12.8 DEGREES
REMARK 500 PRO A1387 C - N - CD ANGL. DEV. = -15.5 DEGREES
REMARK 500 PRO A1397 CA - N - CD ANGL. DEV. = -13.5 DEGREES
REMARK 500 PRO A1397 C - N - CD ANGL. DEV. = -17.9 DEGREES
REMARK 500 PRO A1429 CA - N - CD ANGL. DEV. = -13.3 DEGREES
REMARK 500 PRO A1443 CA - N - CD ANGL. DEV. = -12.6 DEGREES
REMARK 500 PRO A1479 CA - N - CD ANGL. DEV. = -13.5 DEGREES
REMARK 500 PRO A1479 C - N - CD ANGL. DEV. = -13.6 DEGREES
REMARK 500 PRO A1509 CA - N - CD ANGL. DEV. = -13.7 DEGREES
REMARK 500 PRO A1518 CA - N - CD ANGL. DEV. = -14.6 DEGREES
REMARK 500 PRO B2024 CA - N - CD ANGL. DEV. = -13.2 DEGREES
REMARK 500 PRO B2046 CA - N - CD ANGL. DEV. = -13.3 DEGREES
REMARK 500 PRO B2054 CA - N - CD ANGL. DEV. = -13.7 DEGREES
REMARK 500 PRO B2058 CA - N - CD ANGL. DEV. = -13.4 DEGREES
REMARK 500 PRO B2059 CA - N - CD ANGL. DEV. = -13.6 DEGREES
REMARK 500 PRO B2062 CA - N - CD ANGL. DEV. = -13.3 DEGREES
REMARK 500 PRO B2067 CA - N - CD ANGL. DEV. = -13.2 DEGREES
REMARK 500 PRO B2068 CA - N - CD ANGL. DEV. = -14.0 DEGREES
REMARK 500 PRO B2070 CA - N - CD ANGL. DEV. = -12.6 DEGREES
REMARK 500 PRO B2073 CA - N - CD ANGL. DEV. = -13.0 DEGREES
REMARK 500 PRO B2073 C - N - CD ANGL. DEV. = -20.6 DEGREES
REMARK 500 PRO B2084 CA - N - CD ANGL. DEV. = -13.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 106 ANGLE DEVIATIONS.
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 GLU A1041 127.91 -38.75
REMARK 500 PHE A1076 -133.15 83.44
REMARK 500 CYS A1087 131.92 -38.33
REMARK 500 LEU A1127 -18.11 -45.61
REMARK 500 MET A1145 -35.72 -131.59
REMARK 500 GLU A1183 7.00 -61.18
REMARK 500 SER A1185 75.70 174.90
REMARK 500 SER A1221 -130.40 62.03
REMARK 500 THR A1252 81.08 -65.21
REMARK 500 SER A1253 -39.76 -38.83
REMARK 500 TRP A1357 -55.31 -161.37
REMARK 500 ILE A1396 -61.16 -25.26
REMARK 500 PHE A1426 -52.14 -128.64
REMARK 500 ASN A1521 -140.27 -106.35
REMARK 500 LYS A1540 16.16 47.82
REMARK 500 GLU B2041 126.56 -36.53
REMARK 500 PRO B2059 55.38 -69.77
REMARK 500 PHE B2076 -163.22 68.57
REMARK 500 ALA B2080 60.77 -115.34
REMARK 500 LEU B2127 -18.15 -47.59
REMARK 500 MET B2145 -34.86 -130.96
REMARK 500 GLU B2183 8.08 -61.59
REMARK 500 SER B2185 75.82 175.57
REMARK 500 SER B2221 -129.63 62.35
REMARK 500 THR B2252 82.15 -64.64
REMARK 500 LEU B2304 6.80 57.06
REMARK 500 HIS B2342 109.81 -52.54
REMARK 500 TRP B2357 -54.48 -161.74
REMARK 500 ILE B2396 -60.82 -26.83
REMARK 500 PHE B2426 -53.02 -129.88
REMARK 500 TYR B2451 141.35 -172.74
REMARK 500 ASN B2521 -139.11 -105.22
REMARK 500 LYS B2538 71.09 44.22
REMARK 500 LYS B2540 15.33 47.78
REMARK 500 PRO C3059 54.58 -69.21
REMARK 500 PHE C3076 -162.73 68.71
REMARK 500 ALA C3080 61.72 -113.97
REMARK 500 MET C3086 -174.97 -56.14
REMARK 500 LEU C3127 -17.53 -46.76
REMARK 500 MET C3145 -35.07 -131.13
REMARK 500 GLU C3183 6.91 -61.50
REMARK 500 SER C3185 75.57 176.50
REMARK 500 SER C3221 -129.69 61.71
REMARK 500 THR C3252 81.09 -65.36
REMARK 500 TRP C3357 -54.45 -161.87
REMARK 500 PHE C3426 -52.52 -130.15
REMARK 500 TYR C3451 141.11 -172.65
REMARK 500 ASN C3521 -140.11 -107.04
REMARK 500 LYS C3540 14.88 48.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 CYS B2087 10.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 CYS A1087 16.3 L L OUTSIDE RANGE
REMARK 500 CYS B2087 22.5 L L OUTSIDE RANGE
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 WW2 A 193
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WW2 B 194
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WW2 C 195
DBREF 3K9B A 1024 1553 UNP P23141 EST1_HUMAN 24 553
DBREF 3K9B B 2024 2553 UNP P23141 EST1_HUMAN 24 553
DBREF 3K9B C 3024 3553 UNP P23141 EST1_HUMAN 24 553
SEQADV 3K9B A UNP P23141 GLN 362 DELETION
SEQADV 3K9B B UNP P23141 GLN 362 DELETION
SEQADV 3K9B C UNP P23141 GLN 362 DELETION
SEQRES 1 A 529 PRO VAL VAL ASP THR VAL HIS GLY LYS VAL LEU GLY LYS
SEQRES 2 A 529 PHE VAL SER LEU GLU GLY PHE ALA GLN PRO VAL ALA ILE
SEQRES 3 A 529 PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO LEU GLY PRO
SEQRES 4 A 529 LEU ARG PHE THR PRO PRO GLN PRO ALA GLU PRO TRP SER
SEQRES 5 A 529 PHE VAL LYS ASN ALA THR SER TYR PRO PRO MET CYS THR
SEQRES 6 A 529 GLN ASP PRO LYS ALA GLY GLN LEU LEU SER GLU LEU PHE
SEQRES 7 A 529 THR ASN ARG LYS GLU ASN ILE PRO LEU LYS LEU SER GLU
SEQRES 8 A 529 ASP CYS LEU TYR LEU ASN ILE TYR THR PRO ALA ASP LEU
SEQRES 9 A 529 THR LYS LYS ASN ARG LEU PRO VAL MET VAL TRP ILE HIS
SEQRES 10 A 529 GLY GLY GLY LEU MET VAL GLY ALA ALA SER THR TYR ASP
SEQRES 11 A 529 GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL VAL VAL VAL
SEQRES 12 A 529 THR ILE GLN TYR ARG LEU GLY ILE TRP GLY PHE PHE SER
SEQRES 13 A 529 THR GLY ASP GLU HIS SER ARG GLY ASN TRP GLY HIS LEU
SEQRES 14 A 529 ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN ASP ASN ILE
SEQRES 15 A 529 ALA SER PHE GLY GLY ASN PRO GLY SER VAL THR ILE PHE
SEQRES 16 A 529 GLY GLU SER ALA GLY GLY GLU SER VAL SER VAL LEU VAL
SEQRES 17 A 529 LEU SER PRO LEU ALA LYS ASN LEU PHE HIS ARG ALA ILE
SEQRES 18 A 529 SER GLU SER GLY VAL ALA LEU THR SER VAL LEU VAL LYS
SEQRES 19 A 529 LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN ILE ALA ILE
SEQRES 20 A 529 THR ALA GLY CYS LYS THR THR THR SER ALA VAL MET VAL
SEQRES 21 A 529 HIS CYS LEU ARG GLN LYS THR GLU GLU GLU LEU LEU GLU
SEQRES 22 A 529 THR THR LEU LYS MET LYS PHE LEU SER LEU ASP LEU GLN
SEQRES 23 A 529 GLY ASP PRO ARG GLU SER GLN PRO LEU LEU GLY THR VAL
SEQRES 24 A 529 ILE ASP GLY MET LEU LEU LEU LYS THR PRO GLU GLU LEU
SEQRES 25 A 529 GLN ALA GLU ARG ASN PHE HIS THR VAL PRO TYR MET VAL
SEQRES 26 A 529 GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU ILE PRO MET
SEQRES 27 A 529 LEU MET SER TYR PRO LEU SER GLU GLY GLN LEU ASP GLN
SEQRES 28 A 529 LYS THR ALA MET SER LEU LEU TRP LYS SER TYR PRO LEU
SEQRES 29 A 529 VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU ALA THR GLU
SEQRES 30 A 529 LYS TYR LEU GLY GLY THR ASP ASP THR VAL LYS LYS LYS
SEQRES 31 A 529 ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL MET PHE GLY
SEQRES 32 A 529 VAL PRO SER VAL ILE VAL ALA ARG ASN HIS ARG ASP ALA
SEQRES 33 A 529 GLY ALA PRO THR TYR MET TYR GLU PHE GLN TYR ARG PRO
SEQRES 34 A 529 SER PHE SER SER ASP MET LYS PRO LYS THR VAL ILE GLY
SEQRES 35 A 529 ASP HIS GLY ASP GLU LEU PHE SER VAL PHE GLY ALA PRO
SEQRES 36 A 529 PHE LEU LYS GLU GLY ALA SER GLU GLU GLU ILE ARG LEU
SEQRES 37 A 529 SER LYS MET VAL MET LYS PHE TRP ALA ASN PHE ALA ARG
SEQRES 38 A 529 ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO HIS TRP PRO
SEQRES 39 A 529 GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN ILE GLY ALA
SEQRES 40 A 529 ASN THR GLN ALA ALA GLN LYS LEU LYS ASP LYS GLU VAL
SEQRES 41 A 529 ALA PHE TRP THR ASN LEU PHE ALA LYS
SEQRES 1 B 529 PRO VAL VAL ASP THR VAL HIS GLY LYS VAL LEU GLY LYS
SEQRES 2 B 529 PHE VAL SER LEU GLU GLY PHE ALA GLN PRO VAL ALA ILE
SEQRES 3 B 529 PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO LEU GLY PRO
SEQRES 4 B 529 LEU ARG PHE THR PRO PRO GLN PRO ALA GLU PRO TRP SER
SEQRES 5 B 529 PHE VAL LYS ASN ALA THR SER TYR PRO PRO MET CYS THR
SEQRES 6 B 529 GLN ASP PRO LYS ALA GLY GLN LEU LEU SER GLU LEU PHE
SEQRES 7 B 529 THR ASN ARG LYS GLU ASN ILE PRO LEU LYS LEU SER GLU
SEQRES 8 B 529 ASP CYS LEU TYR LEU ASN ILE TYR THR PRO ALA ASP LEU
SEQRES 9 B 529 THR LYS LYS ASN ARG LEU PRO VAL MET VAL TRP ILE HIS
SEQRES 10 B 529 GLY GLY GLY LEU MET VAL GLY ALA ALA SER THR TYR ASP
SEQRES 11 B 529 GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL VAL VAL VAL
SEQRES 12 B 529 THR ILE GLN TYR ARG LEU GLY ILE TRP GLY PHE PHE SER
SEQRES 13 B 529 THR GLY ASP GLU HIS SER ARG GLY ASN TRP GLY HIS LEU
SEQRES 14 B 529 ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN ASP ASN ILE
SEQRES 15 B 529 ALA SER PHE GLY GLY ASN PRO GLY SER VAL THR ILE PHE
SEQRES 16 B 529 GLY GLU SER ALA GLY GLY GLU SER VAL SER VAL LEU VAL
SEQRES 17 B 529 LEU SER PRO LEU ALA LYS ASN LEU PHE HIS ARG ALA ILE
SEQRES 18 B 529 SER GLU SER GLY VAL ALA LEU THR SER VAL LEU VAL LYS
SEQRES 19 B 529 LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN ILE ALA ILE
SEQRES 20 B 529 THR ALA GLY CYS LYS THR THR THR SER ALA VAL MET VAL
SEQRES 21 B 529 HIS CYS LEU ARG GLN LYS THR GLU GLU GLU LEU LEU GLU
SEQRES 22 B 529 THR THR LEU LYS MET LYS PHE LEU SER LEU ASP LEU GLN
SEQRES 23 B 529 GLY ASP PRO ARG GLU SER GLN PRO LEU LEU GLY THR VAL
SEQRES 24 B 529 ILE ASP GLY MET LEU LEU LEU LYS THR PRO GLU GLU LEU
SEQRES 25 B 529 GLN ALA GLU ARG ASN PHE HIS THR VAL PRO TYR MET VAL
SEQRES 26 B 529 GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU ILE PRO MET
SEQRES 27 B 529 LEU MET SER TYR PRO LEU SER GLU GLY GLN LEU ASP GLN
SEQRES 28 B 529 LYS THR ALA MET SER LEU LEU TRP LYS SER TYR PRO LEU
SEQRES 29 B 529 VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU ALA THR GLU
SEQRES 30 B 529 LYS TYR LEU GLY GLY THR ASP ASP THR VAL LYS LYS LYS
SEQRES 31 B 529 ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL MET PHE GLY
SEQRES 32 B 529 VAL PRO SER VAL ILE VAL ALA ARG ASN HIS ARG ASP ALA
SEQRES 33 B 529 GLY ALA PRO THR TYR MET TYR GLU PHE GLN TYR ARG PRO
SEQRES 34 B 529 SER PHE SER SER ASP MET LYS PRO LYS THR VAL ILE GLY
SEQRES 35 B 529 ASP HIS GLY ASP GLU LEU PHE SER VAL PHE GLY ALA PRO
SEQRES 36 B 529 PHE LEU LYS GLU GLY ALA SER GLU GLU GLU ILE ARG LEU
SEQRES 37 B 529 SER LYS MET VAL MET LYS PHE TRP ALA ASN PHE ALA ARG
SEQRES 38 B 529 ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO HIS TRP PRO
SEQRES 39 B 529 GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN ILE GLY ALA
SEQRES 40 B 529 ASN THR GLN ALA ALA GLN LYS LEU LYS ASP LYS GLU VAL
SEQRES 41 B 529 ALA PHE TRP THR ASN LEU PHE ALA LYS
SEQRES 1 C 529 PRO VAL VAL ASP THR VAL HIS GLY LYS VAL LEU GLY LYS
SEQRES 2 C 529 PHE VAL SER LEU GLU GLY PHE ALA GLN PRO VAL ALA ILE
SEQRES 3 C 529 PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO LEU GLY PRO
SEQRES 4 C 529 LEU ARG PHE THR PRO PRO GLN PRO ALA GLU PRO TRP SER
SEQRES 5 C 529 PHE VAL LYS ASN ALA THR SER TYR PRO PRO MET CYS THR
SEQRES 6 C 529 GLN ASP PRO LYS ALA GLY GLN LEU LEU SER GLU LEU PHE
SEQRES 7 C 529 THR ASN ARG LYS GLU ASN ILE PRO LEU LYS LEU SER GLU
SEQRES 8 C 529 ASP CYS LEU TYR LEU ASN ILE TYR THR PRO ALA ASP LEU
SEQRES 9 C 529 THR LYS LYS ASN ARG LEU PRO VAL MET VAL TRP ILE HIS
SEQRES 10 C 529 GLY GLY GLY LEU MET VAL GLY ALA ALA SER THR TYR ASP
SEQRES 11 C 529 GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL VAL VAL VAL
SEQRES 12 C 529 THR ILE GLN TYR ARG LEU GLY ILE TRP GLY PHE PHE SER
SEQRES 13 C 529 THR GLY ASP GLU HIS SER ARG GLY ASN TRP GLY HIS LEU
SEQRES 14 C 529 ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN ASP ASN ILE
SEQRES 15 C 529 ALA SER PHE GLY GLY ASN PRO GLY SER VAL THR ILE PHE
SEQRES 16 C 529 GLY GLU SER ALA GLY GLY GLU SER VAL SER VAL LEU VAL
SEQRES 17 C 529 LEU SER PRO LEU ALA LYS ASN LEU PHE HIS ARG ALA ILE
SEQRES 18 C 529 SER GLU SER GLY VAL ALA LEU THR SER VAL LEU VAL LYS
SEQRES 19 C 529 LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN ILE ALA ILE
SEQRES 20 C 529 THR ALA GLY CYS LYS THR THR THR SER ALA VAL MET VAL
SEQRES 21 C 529 HIS CYS LEU ARG GLN LYS THR GLU GLU GLU LEU LEU GLU
SEQRES 22 C 529 THR THR LEU LYS MET LYS PHE LEU SER LEU ASP LEU GLN
SEQRES 23 C 529 GLY ASP PRO ARG GLU SER GLN PRO LEU LEU GLY THR VAL
SEQRES 24 C 529 ILE ASP GLY MET LEU LEU LEU LYS THR PRO GLU GLU LEU
SEQRES 25 C 529 GLN ALA GLU ARG ASN PHE HIS THR VAL PRO TYR MET VAL
SEQRES 26 C 529 GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU ILE PRO MET
SEQRES 27 C 529 LEU MET SER TYR PRO LEU SER GLU GLY GLN LEU ASP GLN
SEQRES 28 C 529 LYS THR ALA MET SER LEU LEU TRP LYS SER TYR PRO LEU
SEQRES 29 C 529 VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU ALA THR GLU
SEQRES 30 C 529 LYS TYR LEU GLY GLY THR ASP ASP THR VAL LYS LYS LYS
SEQRES 31 C 529 ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL MET PHE GLY
SEQRES 32 C 529 VAL PRO SER VAL ILE VAL ALA ARG ASN HIS ARG ASP ALA
SEQRES 33 C 529 GLY ALA PRO THR TYR MET TYR GLU PHE GLN TYR ARG PRO
SEQRES 34 C 529 SER PHE SER SER ASP MET LYS PRO LYS THR VAL ILE GLY
SEQRES 35 C 529 ASP HIS GLY ASP GLU LEU PHE SER VAL PHE GLY ALA PRO
SEQRES 36 C 529 PHE LEU LYS GLU GLY ALA SER GLU GLU GLU ILE ARG LEU
SEQRES 37 C 529 SER LYS MET VAL MET LYS PHE TRP ALA ASN PHE ALA ARG
SEQRES 38 C 529 ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO HIS TRP PRO
SEQRES 39 C 529 GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN ILE GLY ALA
SEQRES 40 C 529 ASN THR GLN ALA ALA GLN LYS LEU LYS ASP LYS GLU VAL
SEQRES 41 C 529 ALA PHE TRP THR ASN LEU PHE ALA LYS
HET WW2 A 193 10
HET WW2 B 194 10
HET WW2 C 195 10
HETNAM WW2 CYCLOHEXYL (S)-METHYLPHOSPHONOFLUORIDOATE
HETSYN WW2 CYCLOSARIN
FORMUL 4 WW2 3(C7 H14 F O2 P)
FORMUL 7 HOH *66(H2 O)
HELIX 1 1 LEU A 1060 ARG A 1064 5 5
HELIX 2 2 ASP A 1090 THR A 1102 1 13
HELIX 3 3 ALA A 1148 TYR A 1152 5 5
HELIX 4 4 GLY A 1154 ASN A 1162 1 9
HELIX 5 5 LEU A 1172 PHE A 1178 1 7
HELIX 6 6 ASN A 1188 ILE A 1205 1 18
HELIX 7 7 ALA A 1206 PHE A 1208 5 3
HELIX 8 8 SER A 1221 SER A 1233 1 13
HELIX 9 9 PRO A 1234 LYS A 1237 5 4
HELIX 10 10 THR A 1252 VAL A 1254 5 3
HELIX 11 11 VAL A 1261 ALA A 1272 1 12
HELIX 12 12 THR A 1278 LYS A 1289 1 12
HELIX 13 13 THR A 1290 LYS A 1302 1 13
HELIX 14 14 THR A 1331 GLU A 1338 1 8
HELIX 15 15 TRP A 1357 MET A 1364 1 7
HELIX 16 16 GLN A 1375 SER A 1385 1 11
HELIX 17 17 SER A 1385 CYS A 1390 1 6
HELIX 18 18 LEU A 1395 GLY A 1405 1 11
HELIX 19 19 VAL A 1411 PHE A 1426 1 16
HELIX 20 20 PHE A 1426 ALA A 1440 1 15
HELIX 21 21 GLU A 1471 PHE A 1476 1 6
HELIX 22 22 GLY A 1477 LEU A 1481 5 5
HELIX 23 23 GLU A 1489 GLY A 1507 1 19
HELIX 24 24 LYS A 1540 ASN A 1549 1 10
HELIX 25 25 LEU B 2060 ARG B 2064 5 5
HELIX 26 26 ASP B 2090 THR B 2102 1 13
HELIX 27 27 ALA B 2148 TYR B 2152 5 5
HELIX 28 28 GLY B 2154 ASN B 2162 1 9
HELIX 29 29 LEU B 2172 PHE B 2178 1 7
HELIX 30 30 ASN B 2188 ILE B 2205 1 18
HELIX 31 31 ALA B 2206 PHE B 2208 5 3
HELIX 32 32 SER B 2221 SER B 2233 1 13
HELIX 33 33 PRO B 2234 LYS B 2237 5 4
HELIX 34 34 THR B 2252 VAL B 2254 5 3
HELIX 35 35 VAL B 2261 ALA B 2272 1 12
HELIX 36 36 THR B 2278 LYS B 2289 1 12
HELIX 37 37 THR B 2290 LYS B 2302 1 13
HELIX 38 38 THR B 2331 GLN B 2336 1 6
HELIX 39 39 TRP B 2357 MET B 2364 1 7
HELIX 40 40 ALA B 2378 SER B 2385 1 8
HELIX 41 41 LEU B 2395 GLY B 2405 1 11
HELIX 42 42 ASP B 2409 PHE B 2426 1 18
HELIX 43 43 PHE B 2426 ALA B 2440 1 15
HELIX 44 44 GLU B 2471 PHE B 2476 1 6
HELIX 45 45 GLY B 2477 LEU B 2481 5 5
HELIX 46 46 SER B 2486 GLY B 2507 1 22
HELIX 47 47 LYS B 2540 PHE B 2551 1 12
HELIX 48 48 LEU C 3060 ARG C 3064 5 5
HELIX 49 49 ASP C 3090 THR C 3102 1 13
HELIX 50 50 ALA C 3148 TYR C 3152 5 5
HELIX 51 51 GLY C 3154 ASN C 3162 1 9
HELIX 52 52 LEU C 3172 PHE C 3178 1 7
HELIX 53 53 ASN C 3188 ILE C 3205 1 18
HELIX 54 54 ALA C 3206 PHE C 3208 5 3
HELIX 55 55 SER C 3221 SER C 3233 1 13
HELIX 56 56 PRO C 3234 LYS C 3237 5 4
HELIX 57 57 THR C 3252 VAL C 3254 5 3
HELIX 58 58 VAL C 3261 ALA C 3272 1 12
HELIX 59 59 THR C 3278 LYS C 3289 1 12
HELIX 60 60 THR C 3290 LYS C 3302 1 13
HELIX 61 61 THR C 3331 ALA C 3337 1 7
HELIX 62 62 TRP C 3357 LEU C 3363 1 6
HELIX 63 63 ILE C 3396 GLY C 3405 1 10
HELIX 64 64 ASP C 3415 PHE C 3426 1 12
HELIX 65 65 PHE C 3426 ALA C 3440 1 15
HELIX 66 66 GLU C 3471 PHE C 3476 1 6
HELIX 67 67 GLY C 3477 LEU C 3481 5 5
HELIX 68 68 SER C 3486 GLY C 3507 1 22
HELIX 69 69 LYS C 3540 THR C 3548 1 9
SHEET 1 A 3 VAL A1025 THR A1028 0
SHEET 2 A 3 GLY A1031 LEU A1034 -1 O VAL A1033 N VAL A1026
SHEET 3 A 3 VAL A1077 ASN A1079 1 O LYS A1078 N LYS A1032
SHEET 1 B11 LYS A1036 VAL A1038 0
SHEET 2 B11 VAL A1047 PRO A1054 -1 O VAL A1047 N VAL A1038
SHEET 3 B11 TYR A1118 THR A1123 -1 O ILE A1121 N PHE A1050
SHEET 4 B11 VAL A1164 ILE A1168 -1 O VAL A1165 N TYR A1122
SHEET 5 B11 LEU A1133 ILE A1139 1 N TRP A1138 O VAL A1166
SHEET 6 B11 GLY A1210 GLU A1220 1 O THR A1216 N VAL A1135
SHEET 7 B11 ARG A1242 GLU A1246 1 O GLU A1246 N GLY A1219
SHEET 8 B11 TYR A1346 ASN A1351 1 O MET A1347 N ALA A1243
SHEET 9 B11 THR A1444 PHE A1449 1 O TYR A1445 N VAL A1348
SHEET 10 B11 GLY A1525 GLN A1528 1 O LEU A1527 N GLU A1448
SHEET 11 B11 GLN A1534 GLN A1537 -1 O ALA A1536 N TYR A1526
SHEET 1 C 2 MET A1086 CYS A1087 0
SHEET 2 C 2 LEU A1112 SER A1113 1 O SER A1113 N MET A1086
SHEET 1 D 2 VAL A1256 LYS A1257 0
SHEET 2 D 2 THR A1321 VAL A1322 1 O THR A1321 N LYS A1257
SHEET 1 E 3 VAL B2025 ASP B2027 0
SHEET 2 E 3 LYS B2032 LEU B2034 -1 O VAL B2033 N VAL B2026
SHEET 3 E 3 VAL B2077 ASN B2079 1 O LYS B2078 N LYS B2032
SHEET 1 F11 LYS B2036 VAL B2038 0
SHEET 2 F11 VAL B2047 PRO B2054 -1 O VAL B2047 N VAL B2038
SHEET 3 F11 TYR B2118 THR B2123 -1 O ILE B2121 N PHE B2050
SHEET 4 F11 VAL B2164 ILE B2168 -1 O VAL B2165 N TYR B2122
SHEET 5 F11 LEU B2133 ILE B2139 1 N TRP B2138 O VAL B2166
SHEET 6 F11 GLY B2210 GLU B2220 1 O THR B2216 N VAL B2135
SHEET 7 F11 ARG B2242 GLU B2246 1 O GLU B2246 N GLY B2219
SHEET 8 F11 TYR B2346 ASN B2351 1 O GLY B2349 N SER B2245
SHEET 9 F11 THR B2444 GLN B2450 1 O TYR B2445 N VAL B2348
SHEET 10 F11 GLY B2525 GLY B2530 1 O ILE B2529 N GLN B2450
SHEET 11 F11 GLN B2534 GLN B2537 -1 O ALA B2536 N TYR B2526
SHEET 1 G 2 MET B2086 CYS B2087 0
SHEET 2 G 2 LEU B2112 SER B2113 1 O SER B2113 N MET B2086
SHEET 1 H 2 VAL B2256 LYS B2257 0
SHEET 2 H 2 THR B2321 VAL B2322 1 O THR B2321 N LYS B2257
SHEET 1 I 3 VAL C3025 THR C3028 0
SHEET 2 I 3 GLY C3031 LEU C3034 -1 O VAL C3033 N VAL C3026
SHEET 3 I 3 VAL C3077 ASN C3079 1 O LYS C3078 N LYS C3032
SHEET 1 J11 LYS C3036 VAL C3038 0
SHEET 2 J11 VAL C3047 PRO C3054 -1 O VAL C3047 N VAL C3038
SHEET 3 J11 TYR C3118 THR C3123 -1 O ILE C3121 N PHE C3050
SHEET 4 J11 VAL C3164 ILE C3168 -1 O VAL C3165 N TYR C3122
SHEET 5 J11 LEU C3133 ILE C3139 1 N TRP C3138 O VAL C3166
SHEET 6 J11 GLY C3210 GLU C3220 1 O THR C3216 N VAL C3135
SHEET 7 J11 ARG C3242 GLU C3246 1 O GLU C3246 N GLY C3219
SHEET 8 J11 TYR C3346 ASN C3351 1 O MET C3347 N ALA C3243
SHEET 9 J11 THR C3444 GLN C3450 1 O TYR C3445 N VAL C3348
SHEET 10 J11 GLY C3525 GLY C3530 1 O ILE C3529 N GLN C3450
SHEET 11 J11 GLN C3534 GLN C3537 -1 O ALA C3536 N TYR C3526
SHEET 1 K 2 MET C3086 CYS C3087 0
SHEET 2 K 2 LEU C3112 SER C3113 1 O SER C3113 N MET C3086
SHEET 1 L 2 VAL C3256 LYS C3257 0
SHEET 2 L 2 THR C3321 VAL C3322 1 O THR C3321 N LYS C3257
SSBOND 1 CYS A 1087 CYS A 1116 1555 1555 1.15
SSBOND 2 CYS A 1274 CYS A 1285 1555 1555 2.04
SSBOND 3 CYS B 2087 CYS B 2116 1555 1555 0.87
SSBOND 4 CYS B 2274 CYS B 2285 1555 1555 2.05
SSBOND 5 CYS C 3087 CYS C 3116 1555 1555 0.83
SSBOND 6 CYS C 3274 CYS C 3285 1555 1555 2.05
LINK OG SER A1221 P1 WW2 A 193 1555 1555 1.45
LINK OG SER B2221 P1 WW2 B 194 1555 1555 1.48
LINK OG SER C3221 P1 WW2 C 195 1555 1555 1.43
SITE 1 AC1 6 GLY A1141 GLY A1142 GLY A1143 SER A1221
SITE 2 AC1 6 ALA A1222 LEU A1363
SITE 1 AC2 7 GLY B2141 GLY B2142 GLY B2143 SER B2221
SITE 2 AC2 7 ALA B2222 LEU B2363 HIS B2468
SITE 1 AC3 6 GLY C3141 GLY C3142 GLY C3143 SER C3221
SITE 2 AC3 6 ALA C3222 HIS C3468
CRYST1 55.610 179.880 200.060 90.00 90.00 90.00 P 21 21 21 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 0.017982 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005559 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004999 0.00000
TER 3769 ASN A1549
TER 7648 LYS B2553
TER 11158 THR C3548
MASTER 806 0 3 69 54 0 6 611251 3 45 123
END |