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HEADER HYDROLASE 14-JUN-22 7Y4F
TITLE BACTERIAL DPP4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE IV;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: NCBI ACCESSION CODE: WP_022302284.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTEROIDES THETAIOTAOMICRON;
SOURCE 3 ORGANISM_TAXID: 818;
SOURCE 4 GENE: BT_4193;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 83333
KEYWDS GUT MICROBIOTA, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.HANG,C.JIANG,K.WANG,Z.ZHANG,F.GUO,J.LIU,G.WANG,X.LEI,F.GONZALEZ,
AUTHOR 2 J.QIAO
REVDAT 1 14-JUN-23 7Y4F 0
JRNL AUTH J.HANG,C.T.JIANG
JRNL TITL BACTERIAL DPP4
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.92 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14_3260
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) : 1.92
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.36
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 282594
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 14246
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 46.3640 - 5.9553 0.99 8991 523 0.1610 0.1752
REMARK 3 2 5.9553 - 4.7284 0.99 9054 450 0.1383 0.1489
REMARK 3 3 4.7284 - 4.1311 0.99 8934 486 0.1220 0.1418
REMARK 3 4 4.1311 - 3.7536 1.00 9026 486 0.1364 0.1649
REMARK 3 5 3.7536 - 3.4846 1.00 8960 505 0.1473 0.1560
REMARK 3 6 3.4846 - 3.2792 1.00 9017 470 0.1567 0.1915
REMARK 3 7 3.2792 - 3.1150 0.99 8864 495 0.1619 0.1865
REMARK 3 8 3.1150 - 2.9795 1.00 8949 499 0.1629 0.1914
REMARK 3 9 2.9795 - 2.8648 1.00 9012 457 0.1672 0.2047
REMARK 3 10 2.8648 - 2.7659 1.00 8963 468 0.1709 0.1978
REMARK 3 11 2.7659 - 2.6795 1.00 9011 484 0.1759 0.2112
REMARK 3 12 2.6795 - 2.6029 1.00 8997 451 0.1758 0.2134
REMARK 3 13 2.6029 - 2.5344 1.00 8952 474 0.1747 0.2208
REMARK 3 14 2.5344 - 2.4725 0.99 8970 462 0.1832 0.2142
REMARK 3 15 2.4725 - 2.4163 1.00 8976 464 0.1796 0.2306
REMARK 3 16 2.4163 - 2.3649 1.00 8957 469 0.1752 0.2055
REMARK 3 17 2.3649 - 2.3176 1.00 8976 502 0.1776 0.2157
REMARK 3 18 2.3176 - 2.2739 1.00 8910 473 0.1844 0.2241
REMARK 3 19 2.2739 - 2.2333 1.00 8971 513 0.1854 0.2107
REMARK 3 20 2.2333 - 2.1954 1.00 8954 480 0.1915 0.2322
REMARK 3 21 2.1954 - 2.1600 1.00 8965 453 0.1936 0.2120
REMARK 3 22 2.1600 - 2.1268 1.00 8922 483 0.2023 0.2524
REMARK 3 23 2.1268 - 2.0955 1.00 9079 442 0.2149 0.2380
REMARK 3 24 2.0955 - 2.0660 1.00 8925 463 0.2183 0.2448
REMARK 3 25 2.0660 - 2.0381 0.99 8939 449 0.2365 0.2612
REMARK 3 26 2.0381 - 2.0116 1.00 8954 485 0.2402 0.2756
REMARK 3 27 2.0116 - 1.9864 1.00 8924 480 0.2467 0.2601
REMARK 3 28 1.9864 - 1.9625 0.99 8890 478 0.2576 0.2809
REMARK 3 29 1.9625 - 1.9397 0.99 8959 449 0.2776 0.2881
REMARK 3 30 1.9397 - 1.9180 0.93 8347 453 0.2974 0.3319
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.510
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.69
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 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 7Y4F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-JUN-22.
REMARK 100 THE DEPOSITION ID IS D_1300030235.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUL-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
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) : 0.9783
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 283945
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.918
REMARK 200 RESOLUTION RANGE LOW (A) : 46.364
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.92
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
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 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: PHENIX
REMARK 200 STARTING MODEL: 1R9N
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BICINE PH 9.0, 10% W/V PEG 20,000
REMARK 280 AND 3% 6-AMINOHEXANOIC ACID SOLUTION, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 291.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 74.42850
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 53810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 54050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 1
REMARK 465 ARG A 2
REMARK 465 LYS A 3
REMARK 465 VAL A 4
REMARK 465 SER A 5
REMARK 465 LEU A 6
REMARK 465 ALA A 7
REMARK 465 LEU A 8
REMARK 465 LEU A 9
REMARK 465 LEU A 10
REMARK 465 CYS A 11
REMARK 465 LEU A 12
REMARK 465 LEU A 13
REMARK 465 CYS A 14
REMARK 465 LEU A 15
REMARK 465 ALA A 16
REMARK 465 GLY A 17
REMARK 465 MET A 18
REMARK 465 ALA A 19
REMARK 465 GLN A 20
REMARK 465 GLY A 21
REMARK 465 GLN A 22
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 LYS B 3
REMARK 465 VAL B 4
REMARK 465 SER B 5
REMARK 465 LEU B 6
REMARK 465 ALA B 7
REMARK 465 LEU B 8
REMARK 465 LEU B 9
REMARK 465 LEU B 10
REMARK 465 CYS B 11
REMARK 465 LEU B 12
REMARK 465 LEU B 13
REMARK 465 CYS B 14
REMARK 465 LEU B 15
REMARK 465 ALA B 16
REMARK 465 GLY B 17
REMARK 465 MET B 18
REMARK 465 ALA B 19
REMARK 465 GLN B 20
REMARK 465 GLY B 21
REMARK 465 GLN B 22
REMARK 465 MET C 1
REMARK 465 ARG C 2
REMARK 465 LYS C 3
REMARK 465 VAL C 4
REMARK 465 SER C 5
REMARK 465 LEU C 6
REMARK 465 ALA C 7
REMARK 465 LEU C 8
REMARK 465 LEU C 9
REMARK 465 LEU C 10
REMARK 465 CYS C 11
REMARK 465 LEU C 12
REMARK 465 LEU C 13
REMARK 465 CYS C 14
REMARK 465 LEU C 15
REMARK 465 ALA C 16
REMARK 465 GLY C 17
REMARK 465 MET C 18
REMARK 465 ALA C 19
REMARK 465 GLN C 20
REMARK 465 GLY C 21
REMARK 465 GLN C 22
REMARK 465 MET D 1
REMARK 465 ARG D 2
REMARK 465 LYS D 3
REMARK 465 VAL D 4
REMARK 465 SER D 5
REMARK 465 LEU D 6
REMARK 465 ALA D 7
REMARK 465 LEU D 8
REMARK 465 LEU D 9
REMARK 465 LEU D 10
REMARK 465 CYS D 11
REMARK 465 LEU D 12
REMARK 465 LEU D 13
REMARK 465 CYS D 14
REMARK 465 LEU D 15
REMARK 465 ALA D 16
REMARK 465 GLY D 17
REMARK 465 MET D 18
REMARK 465 ALA D 19
REMARK 465 GLN D 20
REMARK 465 GLY D 21
REMARK 465 GLN D 22
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 HOH C 1469 O HOH C 1490 1.81
REMARK 500 OE1 GLU D 655 O HOH D 801 1.83
REMARK 500 O HOH B 1488 O HOH B 1511 1.83
REMARK 500 O HOH B 1458 O HOH B 1500 1.84
REMARK 500 O HOH B 1315 O HOH B 1368 1.84
REMARK 500 O HOH B 1425 O HOH B 1490 1.85
REMARK 500 OE1 GLU B 210 O HOH B 801 1.85
REMARK 500 O HOH A 1067 O HOH A 1087 1.87
REMARK 500 O HOH C 1335 O HOH C 1447 1.88
REMARK 500 O HOH B 1396 O HOH B 1436 1.92
REMARK 500 O HOH A 1509 O HOH A 1546 1.92
REMARK 500 O HOH D 1258 O HOH D 1344 1.92
REMARK 500 O HOH D 807 O HOH D 1079 1.92
REMARK 500 O HOH A 950 O HOH A 1289 1.92
REMARK 500 O HOH A 1260 O HOH A 1427 1.93
REMARK 500 OD2 ASP D 394 O HOH D 802 1.93
REMARK 500 O HOH A 1169 O HOH A 1500 1.95
REMARK 500 O HOH B 1191 O HOH B 1455 1.95
REMARK 500 O HOH A 1395 O HOH A 1455 1.96
REMARK 500 O HOH A 804 O HOH A 1008 1.96
REMARK 500 O HOH C 1436 O HOH C 1508 1.96
REMARK 500 O HOH D 1157 O HOH D 1332 1.96
REMARK 500 O HOH A 1332 O HOH A 1388 1.97
REMARK 500 O HOH B 1016 O HOH B 1294 1.97
REMARK 500 O HOH B 1190 O HOH B 1354 1.97
REMARK 500 O HOH C 1284 O HOH C 1409 1.97
REMARK 500 O HOH A 1425 O HOH A 1496 1.98
REMARK 500 O HOH B 1413 O HOH B 1466 1.98
REMARK 500 O HOH A 1169 O HOH A 1253 1.98
REMARK 500 O HOH B 847 O HOH B 1453 1.98
REMARK 500 O HOH B 961 O HOH B 1427 1.99
REMARK 500 O HOH A 1407 O HOH A 1469 1.99
REMARK 500 O HOH B 975 O HOH B 1378 1.99
REMARK 500 O HOH B 1123 O HOH B 1492 2.00
REMARK 500 O HOH D 1133 O HOH D 1221 2.00
REMARK 500 O HOH A 1554 O HOH A 1555 2.01
REMARK 500 O HOH C 1347 O HOH C 1422 2.01
REMARK 500 O HOH B 985 O HOH B 1483 2.01
REMARK 500 O HOH B 1380 O HOH B 1422 2.01
REMARK 500 O HOH B 1340 O HOH B 1487 2.02
REMARK 500 NE2 GLN A 531 O HOH A 801 2.02
REMARK 500 OD1 ASN A 89 O HOH A 802 2.02
REMARK 500 O HOH B 1284 O HOH B 1350 2.02
REMARK 500 O HOH D 936 O HOH D 1305 2.02
REMARK 500 O HOH B 1297 O HOH B 1338 2.02
REMARK 500 O PRO A 352 O HOH A 803 2.02
REMARK 500 O HOH C 850 O HOH C 1393 2.02
REMARK 500 O HOH B 1063 O HOH B 1262 2.03
REMARK 500 O HOH C 821 O HOH C 1313 2.03
REMARK 500 NH1 ARG D 599 O HOH D 803 2.03
REMARK 500
REMARK 500 THIS ENTRY HAS 116 CLOSE CONTACTS
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 O HOH A 1475 O HOH C 1498 1455 2.06
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 ARG A 294 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG C 294 NE - CZ - NH2 ANGL. DEV. = -3.1 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 ILE A 111 -74.37 -108.70
REMARK 500 TYR A 112 -149.48 -110.29
REMARK 500 VAL A 149 52.31 37.42
REMARK 500 SER A 189 -61.91 -137.66
REMARK 500 THR A 326 -0.96 74.11
REMARK 500 TYR A 338 -78.53 -125.54
REMARK 500 GLU A 353 -6.62 77.83
REMARK 500 SER A 408 147.74 179.32
REMARK 500 MET A 455 116.05 -22.06
REMARK 500 SER A 525 -4.53 81.81
REMARK 500 LYS A 573 62.67 -154.29
REMARK 500 SER A 606 -124.32 66.01
REMARK 500 ARG A 648 -161.40 54.56
REMARK 500 ALA A 680 30.03 -96.89
REMARK 500 ASN A 683 -73.95 -106.89
REMARK 500 ASN A 712 -156.90 -101.85
REMARK 500 ILE A 715 76.36 35.47
REMARK 500 THR B 31 20.74 -68.53
REMARK 500 SER B 32 72.46 -115.53
REMARK 500 ILE B 111 -76.37 -110.21
REMARK 500 TYR B 112 -148.96 -108.06
REMARK 500 VAL B 149 49.76 37.96
REMARK 500 SER B 189 -58.59 -135.93
REMARK 500 THR B 326 -2.81 73.06
REMARK 500 TYR B 338 -81.18 -117.38
REMARK 500 SER B 408 147.86 179.90
REMARK 500 MET B 455 119.55 -168.06
REMARK 500 SER B 525 0.94 81.00
REMARK 500 LYS B 573 67.61 -154.60
REMARK 500 SER B 606 -122.97 66.61
REMARK 500 ARG B 648 -159.03 52.69
REMARK 500 ASN B 683 -73.94 -107.54
REMARK 500 ASN B 712 -158.47 -100.09
REMARK 500 ILE B 715 75.11 38.11
REMARK 500 ILE C 111 -78.76 -108.37
REMARK 500 TYR C 112 -152.34 -107.99
REMARK 500 VAL C 149 54.29 39.58
REMARK 500 SER C 189 -60.73 -133.88
REMARK 500 THR C 326 -0.01 70.33
REMARK 500 TYR C 338 -73.15 -127.48
REMARK 500 GLU C 353 -10.71 74.68
REMARK 500 SER C 408 143.50 170.91
REMARK 500 MET C 455 115.53 -170.65
REMARK 500 SER C 525 -1.99 77.59
REMARK 500 LYS C 573 61.10 -153.38
REMARK 500 SER C 606 -121.53 61.44
REMARK 500 ARG C 648 -153.88 57.40
REMARK 500 ALA C 680 31.33 -95.69
REMARK 500 ASN C 683 -72.78 -103.86
REMARK 500 ASN C 712 -161.85 -101.83
REMARK 500
REMARK 500 THIS ENTRY HAS 70 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1557 DISTANCE = 6.81 ANGSTROMS
REMARK 525 HOH B1525 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH C1547 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH C1548 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH D1372 DISTANCE = 6.04 ANGSTROMS
DBREF 7Y4F A 1 736 PDB 7Y4F 7Y4F 1 736
DBREF 7Y4F B 1 736 PDB 7Y4F 7Y4F 1 736
DBREF 7Y4F C 1 736 PDB 7Y4F 7Y4F 1 736
DBREF 7Y4F D 1 736 PDB 7Y4F 7Y4F 1 736
SEQRES 1 A 736 MET ARG LYS VAL SER LEU ALA LEU LEU LEU CYS LEU LEU
SEQRES 2 A 736 CYS LEU ALA GLY MET ALA GLN GLY GLN LYS ALA LEU ASP
SEQRES 3 A 736 LEU LYS ASP ILE THR SER GLY ARG PHE ARG PRO GLU ASN
SEQRES 4 A 736 ILE GLN GLY VAL ILE PRO MET PRO ASP GLY GLU HIS TYR
SEQRES 5 A 736 THR GLN MET SER ALA ASP GLY THR GLN ILE ILE LYS TYR
SEQRES 6 A 736 SER PHE ARG THR GLY GLU LYS VAL GLU VAL ILE PHE ASP
SEQRES 7 A 736 VAL ASN GLN ALA ARG GLU CYS ASP PHE LYS ASN PHE ASP
SEQRES 8 A 736 SER TYR GLN PHE SER PRO ASP GLY ASP LYS LEU LEU ILE
SEQRES 9 A 736 ALA THR ARG THR THR PRO ILE TYR ARG HIS SER TYR THR
SEQRES 10 A 736 ALA VAL HIS TYR ILE TYR PRO LEU LYS ARG ASN ASP LYS
SEQRES 11 A 736 GLY VAL THR THR ASN ASN ILE ILE GLU ARG LEU SER ASP
SEQRES 12 A 736 GLY GLY PRO GLN GLN VAL PRO VAL PHE SER PRO ASP GLY
SEQRES 13 A 736 THR MET ILE ALA PHE VAL ARG ASP ASN ASN ILE PHE LEU
SEQRES 14 A 736 VAL LYS LEU LEU TYR GLY ASN SER GLU SER GLN VAL THR
SEQRES 15 A 736 GLU ASP GLY LYS GLN ASN SER VAL LEU ASN GLY ILE PRO
SEQRES 16 A 736 ASP TRP VAL TYR GLU GLU GLU PHE GLY PHE ASN ARG ALA
SEQRES 17 A 736 LEU GLU PHE SER ALA ASP ASN THR MET ILE ALA PHE ILE
SEQRES 18 A 736 ARG PHE ASP GLU SER GLU VAL PRO SER TYR SER PHE PRO
SEQRES 19 A 736 MET PHE ALA GLY GLU ALA PRO GLN ILE THR PRO LEU LYS
SEQRES 20 A 736 ASP TYR PRO GLY GLU TYR THR TYR LYS TYR PRO LYS ALA
SEQRES 21 A 736 GLY TYR PRO ASN SER LYS VAL GLU VAL ARG THR TYR ASP
SEQRES 22 A 736 ILE LYS SER HIS VAL THR ARG THR MET LYS LEU PRO ILE
SEQRES 23 A 736 ASP ALA ASP GLY TYR ILE PRO ARG ILE ARG PHE THR LYS
SEQRES 24 A 736 ASP ALA SER LYS LEU ALA VAL MET THR LEU ASN ARG HIS
SEQRES 25 A 736 GLN ASP ARG PHE ASP LEU TYR PHE ALA ASP PRO ARG SER
SEQRES 26 A 736 THR LEU CYS LYS LEU VAL LEU ARG ASP GLU SER PRO TYR
SEQRES 27 A 736 TYR ILE LYS GLU ASN VAL PHE ASP ASN ILE LYS PHE TYR
SEQRES 28 A 736 PRO GLU THR PHE SER LEU LEU SER GLU ARG ASP GLY PHE
SEQRES 29 A 736 SER HIS LEU TYR TRP TYR SER MET GLY GLY ASN LEU ILE
SEQRES 30 A 736 LYS LYS VAL THR ASN GLY LYS TYR GLU VAL LYS ASP PHE
SEQRES 31 A 736 LEU GLY TYR ASP GLU ALA ASP GLY SER PHE TYR TYR THR
SEQRES 32 A 736 SER ASN GLU GLU SER PRO LEU ARG LYS ALA VAL TYR LYS
SEQRES 33 A 736 ILE ASP LYS LYS GLY LYS LYS LEU LYS LEU SER GLN ARG
SEQRES 34 A 736 GLU GLY THR ASN THR PRO LEU PHE SER GLN SER MET LYS
SEQRES 35 A 736 TYR TYR MET ASN LYS PHE SER ASN LEU ASP THR PRO MET
SEQRES 36 A 736 LEU VAL THR LEU ASN ASP ASN THR GLY LYS THR LEU LYS
SEQRES 37 A 736 THR LEU ILE ASN ASN ASP GLN LEU LYS GLN THR LEU SER
SEQRES 38 A 736 GLY TYR ALA ILE PRO GLN LYS GLU PHE PHE THR PHE GLN
SEQRES 39 A 736 THR THR ASP GLY VAL THR LEU ASN GLY TRP MET MET LYS
SEQRES 40 A 736 PRO ALA ASN PHE SER THR SER LYS LYS TYR PRO VAL LEU
SEQRES 41 A 736 MET TYR GLN TYR SER GLY PRO GLY SER GLN GLN VAL LEU
SEQRES 42 A 736 ASP THR TRP GLY ILE SER TRP GLU THR TYR MET ALA SER
SEQRES 43 A 736 LEU GLY TYR ILE VAL VAL CYS VAL ASP GLY ARG GLY THR
SEQRES 44 A 736 GLY GLY ARG GLY GLU ALA PHE GLU LYS CYS THR TYR LEU
SEQRES 45 A 736 LYS ILE GLY VAL LYS GLU ALA LYS ASP GLN VAL GLU THR
SEQRES 46 A 736 ALA LEU TYR LEU GLY LYS GLN PRO TYR VAL ASP LYS ASP
SEQRES 47 A 736 ARG ILE GLY ILE TRP GLY TRP SER TYR GLY GLY TYR MET
SEQRES 48 A 736 THR LEU MET SER MET SER GLU GLY THR PRO VAL PHE LYS
SEQRES 49 A 736 ALA GLY VAL ALA VAL ALA ALA PRO THR ASP TRP ARG PHE
SEQRES 50 A 736 TYR ASP THR ILE TYR THR GLU ARG PHE MET ARG THR PRO
SEQRES 51 A 736 LYS GLU ASN ALA GLU GLY TYR LYS GLU SER SER ALA PHE
SEQRES 52 A 736 THR ARG ALA ASP LYS LEU HIS GLY ASN LEU LEU LEU VAL
SEQRES 53 A 736 HIS GLY MET ALA ASP ASP ASN VAL HIS PHE GLN ASN CYS
SEQRES 54 A 736 ALA GLU TYR ALA GLU HIS LEU VAL GLN LEU GLY LYS GLN
SEQRES 55 A 736 PHE ASP MET GLN VAL TYR THR ASN ARG ASN HIS GLY ILE
SEQRES 56 A 736 TYR GLY GLY ASN THR ARG GLN HIS LEU TYR THR ARG LEU
SEQRES 57 A 736 THR ASN PHE PHE LEU ASN ASN LEU
SEQRES 1 B 736 MET ARG LYS VAL SER LEU ALA LEU LEU LEU CYS LEU LEU
SEQRES 2 B 736 CYS LEU ALA GLY MET ALA GLN GLY GLN LYS ALA LEU ASP
SEQRES 3 B 736 LEU LYS ASP ILE THR SER GLY ARG PHE ARG PRO GLU ASN
SEQRES 4 B 736 ILE GLN GLY VAL ILE PRO MET PRO ASP GLY GLU HIS TYR
SEQRES 5 B 736 THR GLN MET SER ALA ASP GLY THR GLN ILE ILE LYS TYR
SEQRES 6 B 736 SER PHE ARG THR GLY GLU LYS VAL GLU VAL ILE PHE ASP
SEQRES 7 B 736 VAL ASN GLN ALA ARG GLU CYS ASP PHE LYS ASN PHE ASP
SEQRES 8 B 736 SER TYR GLN PHE SER PRO ASP GLY ASP LYS LEU LEU ILE
SEQRES 9 B 736 ALA THR ARG THR THR PRO ILE TYR ARG HIS SER TYR THR
SEQRES 10 B 736 ALA VAL HIS TYR ILE TYR PRO LEU LYS ARG ASN ASP LYS
SEQRES 11 B 736 GLY VAL THR THR ASN ASN ILE ILE GLU ARG LEU SER ASP
SEQRES 12 B 736 GLY GLY PRO GLN GLN VAL PRO VAL PHE SER PRO ASP GLY
SEQRES 13 B 736 THR MET ILE ALA PHE VAL ARG ASP ASN ASN ILE PHE LEU
SEQRES 14 B 736 VAL LYS LEU LEU TYR GLY ASN SER GLU SER GLN VAL THR
SEQRES 15 B 736 GLU ASP GLY LYS GLN ASN SER VAL LEU ASN GLY ILE PRO
SEQRES 16 B 736 ASP TRP VAL TYR GLU GLU GLU PHE GLY PHE ASN ARG ALA
SEQRES 17 B 736 LEU GLU PHE SER ALA ASP ASN THR MET ILE ALA PHE ILE
SEQRES 18 B 736 ARG PHE ASP GLU SER GLU VAL PRO SER TYR SER PHE PRO
SEQRES 19 B 736 MET PHE ALA GLY GLU ALA PRO GLN ILE THR PRO LEU LYS
SEQRES 20 B 736 ASP TYR PRO GLY GLU TYR THR TYR LYS TYR PRO LYS ALA
SEQRES 21 B 736 GLY TYR PRO ASN SER LYS VAL GLU VAL ARG THR TYR ASP
SEQRES 22 B 736 ILE LYS SER HIS VAL THR ARG THR MET LYS LEU PRO ILE
SEQRES 23 B 736 ASP ALA ASP GLY TYR ILE PRO ARG ILE ARG PHE THR LYS
SEQRES 24 B 736 ASP ALA SER LYS LEU ALA VAL MET THR LEU ASN ARG HIS
SEQRES 25 B 736 GLN ASP ARG PHE ASP LEU TYR PHE ALA ASP PRO ARG SER
SEQRES 26 B 736 THR LEU CYS LYS LEU VAL LEU ARG ASP GLU SER PRO TYR
SEQRES 27 B 736 TYR ILE LYS GLU ASN VAL PHE ASP ASN ILE LYS PHE TYR
SEQRES 28 B 736 PRO GLU THR PHE SER LEU LEU SER GLU ARG ASP GLY PHE
SEQRES 29 B 736 SER HIS LEU TYR TRP TYR SER MET GLY GLY ASN LEU ILE
SEQRES 30 B 736 LYS LYS VAL THR ASN GLY LYS TYR GLU VAL LYS ASP PHE
SEQRES 31 B 736 LEU GLY TYR ASP GLU ALA ASP GLY SER PHE TYR TYR THR
SEQRES 32 B 736 SER ASN GLU GLU SER PRO LEU ARG LYS ALA VAL TYR LYS
SEQRES 33 B 736 ILE ASP LYS LYS GLY LYS LYS LEU LYS LEU SER GLN ARG
SEQRES 34 B 736 GLU GLY THR ASN THR PRO LEU PHE SER GLN SER MET LYS
SEQRES 35 B 736 TYR TYR MET ASN LYS PHE SER ASN LEU ASP THR PRO MET
SEQRES 36 B 736 LEU VAL THR LEU ASN ASP ASN THR GLY LYS THR LEU LYS
SEQRES 37 B 736 THR LEU ILE ASN ASN ASP GLN LEU LYS GLN THR LEU SER
SEQRES 38 B 736 GLY TYR ALA ILE PRO GLN LYS GLU PHE PHE THR PHE GLN
SEQRES 39 B 736 THR THR ASP GLY VAL THR LEU ASN GLY TRP MET MET LYS
SEQRES 40 B 736 PRO ALA ASN PHE SER THR SER LYS LYS TYR PRO VAL LEU
SEQRES 41 B 736 MET TYR GLN TYR SER GLY PRO GLY SER GLN GLN VAL LEU
SEQRES 42 B 736 ASP THR TRP GLY ILE SER TRP GLU THR TYR MET ALA SER
SEQRES 43 B 736 LEU GLY TYR ILE VAL VAL CYS VAL ASP GLY ARG GLY THR
SEQRES 44 B 736 GLY GLY ARG GLY GLU ALA PHE GLU LYS CYS THR TYR LEU
SEQRES 45 B 736 LYS ILE GLY VAL LYS GLU ALA LYS ASP GLN VAL GLU THR
SEQRES 46 B 736 ALA LEU TYR LEU GLY LYS GLN PRO TYR VAL ASP LYS ASP
SEQRES 47 B 736 ARG ILE GLY ILE TRP GLY TRP SER TYR GLY GLY TYR MET
SEQRES 48 B 736 THR LEU MET SER MET SER GLU GLY THR PRO VAL PHE LYS
SEQRES 49 B 736 ALA GLY VAL ALA VAL ALA ALA PRO THR ASP TRP ARG PHE
SEQRES 50 B 736 TYR ASP THR ILE TYR THR GLU ARG PHE MET ARG THR PRO
SEQRES 51 B 736 LYS GLU ASN ALA GLU GLY TYR LYS GLU SER SER ALA PHE
SEQRES 52 B 736 THR ARG ALA ASP LYS LEU HIS GLY ASN LEU LEU LEU VAL
SEQRES 53 B 736 HIS GLY MET ALA ASP ASP ASN VAL HIS PHE GLN ASN CYS
SEQRES 54 B 736 ALA GLU TYR ALA GLU HIS LEU VAL GLN LEU GLY LYS GLN
SEQRES 55 B 736 PHE ASP MET GLN VAL TYR THR ASN ARG ASN HIS GLY ILE
SEQRES 56 B 736 TYR GLY GLY ASN THR ARG GLN HIS LEU TYR THR ARG LEU
SEQRES 57 B 736 THR ASN PHE PHE LEU ASN ASN LEU
SEQRES 1 C 736 MET ARG LYS VAL SER LEU ALA LEU LEU LEU CYS LEU LEU
SEQRES 2 C 736 CYS LEU ALA GLY MET ALA GLN GLY GLN LYS ALA LEU ASP
SEQRES 3 C 736 LEU LYS ASP ILE THR SER GLY ARG PHE ARG PRO GLU ASN
SEQRES 4 C 736 ILE GLN GLY VAL ILE PRO MET PRO ASP GLY GLU HIS TYR
SEQRES 5 C 736 THR GLN MET SER ALA ASP GLY THR GLN ILE ILE LYS TYR
SEQRES 6 C 736 SER PHE ARG THR GLY GLU LYS VAL GLU VAL ILE PHE ASP
SEQRES 7 C 736 VAL ASN GLN ALA ARG GLU CYS ASP PHE LYS ASN PHE ASP
SEQRES 8 C 736 SER TYR GLN PHE SER PRO ASP GLY ASP LYS LEU LEU ILE
SEQRES 9 C 736 ALA THR ARG THR THR PRO ILE TYR ARG HIS SER TYR THR
SEQRES 10 C 736 ALA VAL HIS TYR ILE TYR PRO LEU LYS ARG ASN ASP LYS
SEQRES 11 C 736 GLY VAL THR THR ASN ASN ILE ILE GLU ARG LEU SER ASP
SEQRES 12 C 736 GLY GLY PRO GLN GLN VAL PRO VAL PHE SER PRO ASP GLY
SEQRES 13 C 736 THR MET ILE ALA PHE VAL ARG ASP ASN ASN ILE PHE LEU
SEQRES 14 C 736 VAL LYS LEU LEU TYR GLY ASN SER GLU SER GLN VAL THR
SEQRES 15 C 736 GLU ASP GLY LYS GLN ASN SER VAL LEU ASN GLY ILE PRO
SEQRES 16 C 736 ASP TRP VAL TYR GLU GLU GLU PHE GLY PHE ASN ARG ALA
SEQRES 17 C 736 LEU GLU PHE SER ALA ASP ASN THR MET ILE ALA PHE ILE
SEQRES 18 C 736 ARG PHE ASP GLU SER GLU VAL PRO SER TYR SER PHE PRO
SEQRES 19 C 736 MET PHE ALA GLY GLU ALA PRO GLN ILE THR PRO LEU LYS
SEQRES 20 C 736 ASP TYR PRO GLY GLU TYR THR TYR LYS TYR PRO LYS ALA
SEQRES 21 C 736 GLY TYR PRO ASN SER LYS VAL GLU VAL ARG THR TYR ASP
SEQRES 22 C 736 ILE LYS SER HIS VAL THR ARG THR MET LYS LEU PRO ILE
SEQRES 23 C 736 ASP ALA ASP GLY TYR ILE PRO ARG ILE ARG PHE THR LYS
SEQRES 24 C 736 ASP ALA SER LYS LEU ALA VAL MET THR LEU ASN ARG HIS
SEQRES 25 C 736 GLN ASP ARG PHE ASP LEU TYR PHE ALA ASP PRO ARG SER
SEQRES 26 C 736 THR LEU CYS LYS LEU VAL LEU ARG ASP GLU SER PRO TYR
SEQRES 27 C 736 TYR ILE LYS GLU ASN VAL PHE ASP ASN ILE LYS PHE TYR
SEQRES 28 C 736 PRO GLU THR PHE SER LEU LEU SER GLU ARG ASP GLY PHE
SEQRES 29 C 736 SER HIS LEU TYR TRP TYR SER MET GLY GLY ASN LEU ILE
SEQRES 30 C 736 LYS LYS VAL THR ASN GLY LYS TYR GLU VAL LYS ASP PHE
SEQRES 31 C 736 LEU GLY TYR ASP GLU ALA ASP GLY SER PHE TYR TYR THR
SEQRES 32 C 736 SER ASN GLU GLU SER PRO LEU ARG LYS ALA VAL TYR LYS
SEQRES 33 C 736 ILE ASP LYS LYS GLY LYS LYS LEU LYS LEU SER GLN ARG
SEQRES 34 C 736 GLU GLY THR ASN THR PRO LEU PHE SER GLN SER MET LYS
SEQRES 35 C 736 TYR TYR MET ASN LYS PHE SER ASN LEU ASP THR PRO MET
SEQRES 36 C 736 LEU VAL THR LEU ASN ASP ASN THR GLY LYS THR LEU LYS
SEQRES 37 C 736 THR LEU ILE ASN ASN ASP GLN LEU LYS GLN THR LEU SER
SEQRES 38 C 736 GLY TYR ALA ILE PRO GLN LYS GLU PHE PHE THR PHE GLN
SEQRES 39 C 736 THR THR ASP GLY VAL THR LEU ASN GLY TRP MET MET LYS
SEQRES 40 C 736 PRO ALA ASN PHE SER THR SER LYS LYS TYR PRO VAL LEU
SEQRES 41 C 736 MET TYR GLN TYR SER GLY PRO GLY SER GLN GLN VAL LEU
SEQRES 42 C 736 ASP THR TRP GLY ILE SER TRP GLU THR TYR MET ALA SER
SEQRES 43 C 736 LEU GLY TYR ILE VAL VAL CYS VAL ASP GLY ARG GLY THR
SEQRES 44 C 736 GLY GLY ARG GLY GLU ALA PHE GLU LYS CYS THR TYR LEU
SEQRES 45 C 736 LYS ILE GLY VAL LYS GLU ALA LYS ASP GLN VAL GLU THR
SEQRES 46 C 736 ALA LEU TYR LEU GLY LYS GLN PRO TYR VAL ASP LYS ASP
SEQRES 47 C 736 ARG ILE GLY ILE TRP GLY TRP SER TYR GLY GLY TYR MET
SEQRES 48 C 736 THR LEU MET SER MET SER GLU GLY THR PRO VAL PHE LYS
SEQRES 49 C 736 ALA GLY VAL ALA VAL ALA ALA PRO THR ASP TRP ARG PHE
SEQRES 50 C 736 TYR ASP THR ILE TYR THR GLU ARG PHE MET ARG THR PRO
SEQRES 51 C 736 LYS GLU ASN ALA GLU GLY TYR LYS GLU SER SER ALA PHE
SEQRES 52 C 736 THR ARG ALA ASP LYS LEU HIS GLY ASN LEU LEU LEU VAL
SEQRES 53 C 736 HIS GLY MET ALA ASP ASP ASN VAL HIS PHE GLN ASN CYS
SEQRES 54 C 736 ALA GLU TYR ALA GLU HIS LEU VAL GLN LEU GLY LYS GLN
SEQRES 55 C 736 PHE ASP MET GLN VAL TYR THR ASN ARG ASN HIS GLY ILE
SEQRES 56 C 736 TYR GLY GLY ASN THR ARG GLN HIS LEU TYR THR ARG LEU
SEQRES 57 C 736 THR ASN PHE PHE LEU ASN ASN LEU
SEQRES 1 D 736 MET ARG LYS VAL SER LEU ALA LEU LEU LEU CYS LEU LEU
SEQRES 2 D 736 CYS LEU ALA GLY MET ALA GLN GLY GLN LYS ALA LEU ASP
SEQRES 3 D 736 LEU LYS ASP ILE THR SER GLY ARG PHE ARG PRO GLU ASN
SEQRES 4 D 736 ILE GLN GLY VAL ILE PRO MET PRO ASP GLY GLU HIS TYR
SEQRES 5 D 736 THR GLN MET SER ALA ASP GLY THR GLN ILE ILE LYS TYR
SEQRES 6 D 736 SER PHE ARG THR GLY GLU LYS VAL GLU VAL ILE PHE ASP
SEQRES 7 D 736 VAL ASN GLN ALA ARG GLU CYS ASP PHE LYS ASN PHE ASP
SEQRES 8 D 736 SER TYR GLN PHE SER PRO ASP GLY ASP LYS LEU LEU ILE
SEQRES 9 D 736 ALA THR ARG THR THR PRO ILE TYR ARG HIS SER TYR THR
SEQRES 10 D 736 ALA VAL HIS TYR ILE TYR PRO LEU LYS ARG ASN ASP LYS
SEQRES 11 D 736 GLY VAL THR THR ASN ASN ILE ILE GLU ARG LEU SER ASP
SEQRES 12 D 736 GLY GLY PRO GLN GLN VAL PRO VAL PHE SER PRO ASP GLY
SEQRES 13 D 736 THR MET ILE ALA PHE VAL ARG ASP ASN ASN ILE PHE LEU
SEQRES 14 D 736 VAL LYS LEU LEU TYR GLY ASN SER GLU SER GLN VAL THR
SEQRES 15 D 736 GLU ASP GLY LYS GLN ASN SER VAL LEU ASN GLY ILE PRO
SEQRES 16 D 736 ASP TRP VAL TYR GLU GLU GLU PHE GLY PHE ASN ARG ALA
SEQRES 17 D 736 LEU GLU PHE SER ALA ASP ASN THR MET ILE ALA PHE ILE
SEQRES 18 D 736 ARG PHE ASP GLU SER GLU VAL PRO SER TYR SER PHE PRO
SEQRES 19 D 736 MET PHE ALA GLY GLU ALA PRO GLN ILE THR PRO LEU LYS
SEQRES 20 D 736 ASP TYR PRO GLY GLU TYR THR TYR LYS TYR PRO LYS ALA
SEQRES 21 D 736 GLY TYR PRO ASN SER LYS VAL GLU VAL ARG THR TYR ASP
SEQRES 22 D 736 ILE LYS SER HIS VAL THR ARG THR MET LYS LEU PRO ILE
SEQRES 23 D 736 ASP ALA ASP GLY TYR ILE PRO ARG ILE ARG PHE THR LYS
SEQRES 24 D 736 ASP ALA SER LYS LEU ALA VAL MET THR LEU ASN ARG HIS
SEQRES 25 D 736 GLN ASP ARG PHE ASP LEU TYR PHE ALA ASP PRO ARG SER
SEQRES 26 D 736 THR LEU CYS LYS LEU VAL LEU ARG ASP GLU SER PRO TYR
SEQRES 27 D 736 TYR ILE LYS GLU ASN VAL PHE ASP ASN ILE LYS PHE TYR
SEQRES 28 D 736 PRO GLU THR PHE SER LEU LEU SER GLU ARG ASP GLY PHE
SEQRES 29 D 736 SER HIS LEU TYR TRP TYR SER MET GLY GLY ASN LEU ILE
SEQRES 30 D 736 LYS LYS VAL THR ASN GLY LYS TYR GLU VAL LYS ASP PHE
SEQRES 31 D 736 LEU GLY TYR ASP GLU ALA ASP GLY SER PHE TYR TYR THR
SEQRES 32 D 736 SER ASN GLU GLU SER PRO LEU ARG LYS ALA VAL TYR LYS
SEQRES 33 D 736 ILE ASP LYS LYS GLY LYS LYS LEU LYS LEU SER GLN ARG
SEQRES 34 D 736 GLU GLY THR ASN THR PRO LEU PHE SER GLN SER MET LYS
SEQRES 35 D 736 TYR TYR MET ASN LYS PHE SER ASN LEU ASP THR PRO MET
SEQRES 36 D 736 LEU VAL THR LEU ASN ASP ASN THR GLY LYS THR LEU LYS
SEQRES 37 D 736 THR LEU ILE ASN ASN ASP GLN LEU LYS GLN THR LEU SER
SEQRES 38 D 736 GLY TYR ALA ILE PRO GLN LYS GLU PHE PHE THR PHE GLN
SEQRES 39 D 736 THR THR ASP GLY VAL THR LEU ASN GLY TRP MET MET LYS
SEQRES 40 D 736 PRO ALA ASN PHE SER THR SER LYS LYS TYR PRO VAL LEU
SEQRES 41 D 736 MET TYR GLN TYR SER GLY PRO GLY SER GLN GLN VAL LEU
SEQRES 42 D 736 ASP THR TRP GLY ILE SER TRP GLU THR TYR MET ALA SER
SEQRES 43 D 736 LEU GLY TYR ILE VAL VAL CYS VAL ASP GLY ARG GLY THR
SEQRES 44 D 736 GLY GLY ARG GLY GLU ALA PHE GLU LYS CYS THR TYR LEU
SEQRES 45 D 736 LYS ILE GLY VAL LYS GLU ALA LYS ASP GLN VAL GLU THR
SEQRES 46 D 736 ALA LEU TYR LEU GLY LYS GLN PRO TYR VAL ASP LYS ASP
SEQRES 47 D 736 ARG ILE GLY ILE TRP GLY TRP SER TYR GLY GLY TYR MET
SEQRES 48 D 736 THR LEU MET SER MET SER GLU GLY THR PRO VAL PHE LYS
SEQRES 49 D 736 ALA GLY VAL ALA VAL ALA ALA PRO THR ASP TRP ARG PHE
SEQRES 50 D 736 TYR ASP THR ILE TYR THR GLU ARG PHE MET ARG THR PRO
SEQRES 51 D 736 LYS GLU ASN ALA GLU GLY TYR LYS GLU SER SER ALA PHE
SEQRES 52 D 736 THR ARG ALA ASP LYS LEU HIS GLY ASN LEU LEU LEU VAL
SEQRES 53 D 736 HIS GLY MET ALA ASP ASP ASN VAL HIS PHE GLN ASN CYS
SEQRES 54 D 736 ALA GLU TYR ALA GLU HIS LEU VAL GLN LEU GLY LYS GLN
SEQRES 55 D 736 PHE ASP MET GLN VAL TYR THR ASN ARG ASN HIS GLY ILE
SEQRES 56 D 736 TYR GLY GLY ASN THR ARG GLN HIS LEU TYR THR ARG LEU
SEQRES 57 D 736 THR ASN PHE PHE LEU ASN ASN LEU
FORMUL 5 HOH *2802(H2 O)
HELIX 1 AA1 ASP A 26 SER A 32 1 7
HELIX 2 AA2 ASP A 196 PHE A 203 1 8
HELIX 3 AA3 ILE A 243 LYS A 247 5 5
HELIX 4 AA4 LYS A 341 ILE A 348 5 8
HELIX 5 AA5 ASN A 473 GLY A 482 1 10
HELIX 6 AA6 SER A 539 LEU A 547 1 9
HELIX 7 AA7 GLY A 563 CYS A 569 1 7
HELIX 8 AA8 GLY A 575 GLN A 592 1 18
HELIX 9 AA9 SER A 606 SER A 617 1 12
HELIX 10 AB1 ASP A 634 TYR A 638 5 5
HELIX 11 AB2 ASP A 639 ARG A 648 1 10
HELIX 12 AB3 ASN A 653 SER A 661 1 9
HELIX 13 AB4 ARG A 665 LEU A 669 5 5
HELIX 14 AB5 HIS A 685 GLY A 700 1 16
HELIX 15 AB6 ASN A 719 LEU A 736 1 18
HELIX 16 AB7 ASP B 196 GLY B 204 1 9
HELIX 17 AB8 ILE B 243 LYS B 247 5 5
HELIX 18 AB9 LYS B 341 ILE B 348 5 8
HELIX 19 AC1 ASN B 473 GLY B 482 1 10
HELIX 20 AC2 SER B 539 LEU B 547 1 9
HELIX 21 AC3 GLY B 563 CYS B 569 1 7
HELIX 22 AC4 GLY B 575 LYS B 591 1 17
HELIX 23 AC5 SER B 606 SER B 617 1 12
HELIX 24 AC6 ASP B 634 TYR B 638 5 5
HELIX 25 AC7 ASP B 639 ARG B 648 1 10
HELIX 26 AC8 ASN B 653 SER B 661 1 9
HELIX 27 AC9 ARG B 665 LEU B 669 5 5
HELIX 28 AD1 HIS B 685 GLY B 700 1 16
HELIX 29 AD2 ASN B 719 LEU B 736 1 18
HELIX 30 AD3 ASP C 26 SER C 32 1 7
HELIX 31 AD4 LEU C 173 GLY C 175 5 3
HELIX 32 AD5 ASP C 196 GLY C 204 1 9
HELIX 33 AD6 ILE C 243 LYS C 247 5 5
HELIX 34 AD7 LYS C 341 ILE C 348 5 8
HELIX 35 AD8 ASN C 473 GLY C 482 1 10
HELIX 36 AD9 SER C 539 LEU C 547 1 9
HELIX 37 AE1 GLY C 563 LYS C 568 1 6
HELIX 38 AE2 CYS C 569 TYR C 571 5 3
HELIX 39 AE3 GLY C 575 LYS C 591 1 17
HELIX 40 AE4 SER C 606 SER C 617 1 12
HELIX 41 AE5 ASP C 634 TYR C 638 5 5
HELIX 42 AE6 ASP C 639 ARG C 648 1 10
HELIX 43 AE7 ASN C 653 SER C 661 1 9
HELIX 44 AE8 ARG C 665 LEU C 669 5 5
HELIX 45 AE9 PHE C 686 GLY C 700 1 15
HELIX 46 AF1 ASN C 719 LEU C 736 1 18
HELIX 47 AF2 ASP D 26 GLY D 33 1 8
HELIX 48 AF3 ASP D 196 PHE D 203 1 8
HELIX 49 AF4 ILE D 243 LYS D 247 5 5
HELIX 50 AF5 LYS D 341 ILE D 348 5 8
HELIX 51 AF6 ASN D 473 GLY D 482 1 10
HELIX 52 AF7 SER D 539 LEU D 547 1 9
HELIX 53 AF8 GLY D 563 CYS D 569 1 7
HELIX 54 AF9 GLY D 575 LYS D 591 1 17
HELIX 55 AG1 SER D 606 SER D 617 1 12
HELIX 56 AG2 ASP D 634 TYR D 638 5 5
HELIX 57 AG3 ASP D 639 ARG D 648 1 10
HELIX 58 AG4 ASN D 653 SER D 661 1 9
HELIX 59 AG5 ARG D 665 LEU D 669 5 5
HELIX 60 AG6 HIS D 685 GLY D 700 1 16
HELIX 61 AG7 ASN D 719 LEU D 736 1 18
SHEET 1 AA1 4 ILE A 44 PRO A 45 0
SHEET 2 AA1 4 HIS A 51 MET A 55 -1 O THR A 53 N ILE A 44
SHEET 3 AA1 4 GLN A 61 SER A 66 -1 O TYR A 65 N TYR A 52
SHEET 4 AA1 4 LYS A 72 ASP A 78 -1 O GLU A 74 N LYS A 64
SHEET 1 AA2 4 SER A 92 PHE A 95 0
SHEET 2 AA2 4 LYS A 101 PRO A 110 -1 O ALA A 105 N SER A 92
SHEET 3 AA2 4 TYR A 116 PRO A 124 -1 O THR A 117 N THR A 109
SHEET 4 AA2 4 GLU A 139 ARG A 140 -1 O GLU A 139 N ILE A 122
SHEET 1 AA3 4 GLN A 148 PHE A 152 0
SHEET 2 AA3 4 MET A 158 ARG A 163 -1 O VAL A 162 N GLN A 148
SHEET 3 AA3 4 ASN A 166 LYS A 171 -1 O VAL A 170 N ILE A 159
SHEET 4 AA3 4 SER A 177 GLN A 180 -1 O SER A 179 N LEU A 169
SHEET 1 AA4 3 VAL A 190 ASN A 192 0
SHEET 2 AA4 3 MET A 217 ASP A 224 -1 O PHE A 223 N LEU A 191
SHEET 3 AA4 3 LEU A 209 PHE A 211 -1 N GLU A 210 O ALA A 219
SHEET 1 AA5 4 VAL A 190 ASN A 192 0
SHEET 2 AA5 4 MET A 217 ASP A 224 -1 O PHE A 223 N LEU A 191
SHEET 3 AA5 4 LYS A 266 ASP A 273 -1 O LYS A 266 N ASP A 224
SHEET 4 AA5 4 THR A 279 THR A 281 -1 O ARG A 280 N THR A 271
SHEET 1 AA6 2 SER A 230 MET A 235 0
SHEET 2 AA6 2 GLY A 251 LYS A 256 -1 O GLY A 251 N MET A 235
SHEET 1 AA7 4 TYR A 291 PHE A 297 0
SHEET 2 AA7 4 LEU A 304 LEU A 309 -1 O LEU A 309 N TYR A 291
SHEET 3 AA7 4 ARG A 315 ALA A 321 -1 O ALA A 321 N LEU A 304
SHEET 4 AA7 4 CYS A 328 GLU A 335 -1 O VAL A 331 N LEU A 318
SHEET 1 AA8 3 THR A 354 SER A 359 0
SHEET 2 AA8 3 HIS A 366 SER A 371 -1 O TYR A 368 N LEU A 357
SHEET 3 AA8 3 LEU A 376 LYS A 379 -1 O ILE A 377 N TRP A 369
SHEET 1 AA9 4 VAL A 387 TYR A 393 0
SHEET 2 AA9 4 PHE A 400 SER A 404 -1 O THR A 403 N LYS A 388
SHEET 3 AA9 4 ALA A 413 ILE A 417 -1 O ILE A 417 N PHE A 400
SHEET 4 AA9 4 LYS A 423 LYS A 425 -1 O LEU A 424 N LYS A 416
SHEET 1 AB1 4 THR A 432 PHE A 437 0
SHEET 2 AB1 4 TYR A 443 ASN A 450 -1 O MET A 445 N LEU A 436
SHEET 3 AB1 4 THR A 453 ASP A 461 -1 O THR A 458 N ASN A 446
SHEET 4 AB1 4 THR A 466 ILE A 471 -1 O LEU A 467 N LEU A 459
SHEET 1 AB2 8 GLN A 487 GLN A 494 0
SHEET 2 AB2 8 THR A 500 LYS A 507 -1 O LEU A 501 N PHE A 493
SHEET 3 AB2 8 ILE A 550 ASP A 555 -1 O VAL A 551 N MET A 506
SHEET 4 AB2 8 TYR A 517 TYR A 522 1 N TYR A 522 O VAL A 552
SHEET 5 AB2 8 VAL A 595 TRP A 605 1 O GLY A 601 N MET A 521
SHEET 6 AB2 8 ALA A 625 VAL A 629 1 O VAL A 629 N GLY A 604
SHEET 7 AB2 8 ASN A 672 GLY A 678 1 O VAL A 676 N ALA A 628
SHEET 8 AB2 8 ASP A 704 TYR A 708 1 O ASP A 704 N LEU A 673
SHEET 1 AB3 4 GLN B 41 PRO B 45 0
SHEET 2 AB3 4 HIS B 51 MET B 55 -1 O MET B 55 N GLN B 41
SHEET 3 AB3 4 GLN B 61 SER B 66 -1 O TYR B 65 N TYR B 52
SHEET 4 AB3 4 LYS B 72 ASP B 78 -1 O VAL B 73 N LYS B 64
SHEET 1 AB4 4 SER B 92 PHE B 95 0
SHEET 2 AB4 4 LYS B 101 PRO B 110 -1 O ALA B 105 N SER B 92
SHEET 3 AB4 4 TYR B 116 PRO B 124 -1 O VAL B 119 N THR B 106
SHEET 4 AB4 4 GLU B 139 ARG B 140 -1 O GLU B 139 N ILE B 122
SHEET 1 AB5 4 GLN B 148 PHE B 152 0
SHEET 2 AB5 4 MET B 158 ARG B 163 -1 O VAL B 162 N GLN B 148
SHEET 3 AB5 4 ASN B 166 LYS B 171 -1 O PHE B 168 N PHE B 161
SHEET 4 AB5 4 GLU B 178 GLN B 180 -1 O SER B 179 N LEU B 169
SHEET 1 AB6 3 VAL B 190 ASN B 192 0
SHEET 2 AB6 3 MET B 217 ASP B 224 -1 O PHE B 223 N LEU B 191
SHEET 3 AB6 3 LEU B 209 PHE B 211 -1 N GLU B 210 O ALA B 219
SHEET 1 AB7 4 VAL B 190 ASN B 192 0
SHEET 2 AB7 4 MET B 217 ASP B 224 -1 O PHE B 223 N LEU B 191
SHEET 3 AB7 4 LYS B 266 ASP B 273 -1 O LYS B 266 N ASP B 224
SHEET 4 AB7 4 THR B 279 THR B 281 -1 O ARG B 280 N THR B 271
SHEET 1 AB8 2 SER B 230 MET B 235 0
SHEET 2 AB8 2 GLY B 251 LYS B 256 -1 O TYR B 255 N TYR B 231
SHEET 1 AB9 4 TYR B 291 PHE B 297 0
SHEET 2 AB9 4 LEU B 304 LEU B 309 -1 O ALA B 305 N ARG B 296
SHEET 3 AB9 4 ARG B 315 ALA B 321 -1 O ALA B 321 N LEU B 304
SHEET 4 AB9 4 CYS B 328 GLU B 335 -1 O VAL B 331 N LEU B 318
SHEET 1 AC1 3 THR B 354 SER B 359 0
SHEET 2 AC1 3 HIS B 366 SER B 371 -1 O TYR B 368 N LEU B 357
SHEET 3 AC1 3 LEU B 376 LYS B 379 -1 O ILE B 377 N TRP B 369
SHEET 1 AC2 4 VAL B 387 ASP B 394 0
SHEET 2 AC2 4 SER B 399 SER B 404 -1 O SER B 399 N ASP B 394
SHEET 3 AC2 4 ALA B 413 ILE B 417 -1 O ILE B 417 N PHE B 400
SHEET 4 AC2 4 LYS B 423 LYS B 425 -1 O LEU B 424 N LYS B 416
SHEET 1 AC3 4 THR B 432 PHE B 437 0
SHEET 2 AC3 4 TYR B 443 ASN B 450 -1 O SER B 449 N THR B 432
SHEET 3 AC3 4 THR B 453 ASP B 461 -1 O THR B 458 N ASN B 446
SHEET 4 AC3 4 THR B 466 ILE B 471 -1 O LEU B 467 N LEU B 459
SHEET 1 AC4 8 GLN B 487 GLN B 494 0
SHEET 2 AC4 8 THR B 500 LYS B 507 -1 O LEU B 501 N PHE B 493
SHEET 3 AC4 8 ILE B 550 ASP B 555 -1 O VAL B 551 N MET B 506
SHEET 4 AC4 8 TYR B 517 TYR B 522 1 N TYR B 522 O VAL B 552
SHEET 5 AC4 8 VAL B 595 TRP B 605 1 O GLY B 601 N VAL B 519
SHEET 6 AC4 8 ALA B 625 VAL B 629 1 O VAL B 629 N GLY B 604
SHEET 7 AC4 8 ASN B 672 GLY B 678 1 O VAL B 676 N ALA B 628
SHEET 8 AC4 8 ASP B 704 TYR B 708 1 O ASP B 704 N LEU B 673
SHEET 1 AC5 4 ILE C 44 PRO C 45 0
SHEET 2 AC5 4 HIS C 51 MET C 55 -1 O THR C 53 N ILE C 44
SHEET 3 AC5 4 GLN C 61 SER C 66 -1 O TYR C 65 N TYR C 52
SHEET 4 AC5 4 LYS C 72 ASP C 78 -1 O VAL C 73 N LYS C 64
SHEET 1 AC6 4 SER C 92 PHE C 95 0
SHEET 2 AC6 4 LYS C 101 PRO C 110 -1 O ALA C 105 N SER C 92
SHEET 3 AC6 4 TYR C 116 PRO C 124 -1 O VAL C 119 N THR C 106
SHEET 4 AC6 4 GLU C 139 ARG C 140 -1 O GLU C 139 N ILE C 122
SHEET 1 AC7 4 GLN C 148 PHE C 152 0
SHEET 2 AC7 4 MET C 158 ARG C 163 -1 O VAL C 162 N GLN C 148
SHEET 3 AC7 4 ASN C 166 LYS C 171 -1 O PHE C 168 N PHE C 161
SHEET 4 AC7 4 GLU C 178 GLN C 180 -1 O SER C 179 N LEU C 169
SHEET 1 AC8 3 VAL C 190 ASN C 192 0
SHEET 2 AC8 3 MET C 217 ASP C 224 -1 O PHE C 223 N LEU C 191
SHEET 3 AC8 3 LEU C 209 PHE C 211 -1 N GLU C 210 O ALA C 219
SHEET 1 AC9 4 VAL C 190 ASN C 192 0
SHEET 2 AC9 4 MET C 217 ASP C 224 -1 O PHE C 223 N LEU C 191
SHEET 3 AC9 4 LYS C 266 ASP C 273 -1 O LYS C 266 N ASP C 224
SHEET 4 AC9 4 THR C 279 THR C 281 -1 O ARG C 280 N THR C 271
SHEET 1 AD1 2 SER C 230 MET C 235 0
SHEET 2 AD1 2 GLY C 251 LYS C 256 -1 O TYR C 255 N TYR C 231
SHEET 1 AD2 4 TYR C 291 PHE C 297 0
SHEET 2 AD2 4 LEU C 304 LEU C 309 -1 O LEU C 309 N TYR C 291
SHEET 3 AD2 4 ARG C 315 ALA C 321 -1 O ALA C 321 N LEU C 304
SHEET 4 AD2 4 CYS C 328 GLU C 335 -1 O VAL C 331 N LEU C 318
SHEET 1 AD3 3 THR C 354 SER C 359 0
SHEET 2 AD3 3 HIS C 366 SER C 371 -1 O TYR C 368 N LEU C 357
SHEET 3 AD3 3 LEU C 376 LYS C 379 -1 O ILE C 377 N TRP C 369
SHEET 1 AD4 4 VAL C 387 ASP C 394 0
SHEET 2 AD4 4 SER C 399 SER C 404 -1 O SER C 399 N ASP C 394
SHEET 3 AD4 4 ALA C 413 ILE C 417 -1 O TYR C 415 N TYR C 402
SHEET 4 AD4 4 LYS C 423 LYS C 425 -1 O LEU C 424 N LYS C 416
SHEET 1 AD5 4 THR C 432 PHE C 437 0
SHEET 2 AD5 4 TYR C 443 ASN C 450 -1 O SER C 449 N THR C 432
SHEET 3 AD5 4 THR C 453 ASP C 461 -1 O THR C 458 N ASN C 446
SHEET 4 AD5 4 THR C 466 ILE C 471 -1 O LEU C 467 N LEU C 459
SHEET 1 AD6 8 LYS C 488 GLN C 494 0
SHEET 2 AD6 8 THR C 500 MET C 506 -1 O LEU C 501 N PHE C 493
SHEET 3 AD6 8 ILE C 550 ASP C 555 -1 O VAL C 551 N MET C 506
SHEET 4 AD6 8 TYR C 517 TYR C 522 1 N TYR C 522 O VAL C 552
SHEET 5 AD6 8 VAL C 595 TRP C 605 1 O GLY C 601 N VAL C 519
SHEET 6 AD6 8 ALA C 625 VAL C 629 1 O VAL C 629 N GLY C 604
SHEET 7 AD6 8 ASN C 672 GLY C 678 1 O VAL C 676 N ALA C 628
SHEET 8 AD6 8 ASP C 704 TYR C 708 1 O ASP C 704 N LEU C 675
SHEET 1 AD7 4 ILE D 44 PRO D 45 0
SHEET 2 AD7 4 HIS D 51 MET D 55 -1 O THR D 53 N ILE D 44
SHEET 3 AD7 4 GLN D 61 SER D 66 -1 O TYR D 65 N TYR D 52
SHEET 4 AD7 4 LYS D 72 ASP D 78 -1 O VAL D 73 N LYS D 64
SHEET 1 AD8 4 SER D 92 PHE D 95 0
SHEET 2 AD8 4 LYS D 101 PRO D 110 -1 O ALA D 105 N SER D 92
SHEET 3 AD8 4 TYR D 116 PRO D 124 -1 O THR D 117 N THR D 109
SHEET 4 AD8 4 GLU D 139 ARG D 140 -1 O GLU D 139 N ILE D 122
SHEET 1 AD9 4 GLN D 148 PHE D 152 0
SHEET 2 AD9 4 MET D 158 ARG D 163 -1 O VAL D 162 N GLN D 148
SHEET 3 AD9 4 ASN D 166 LYS D 171 -1 O PHE D 168 N PHE D 161
SHEET 4 AD9 4 SER D 177 GLN D 180 -1 O SER D 179 N LEU D 169
SHEET 1 AE1 3 VAL D 190 ASN D 192 0
SHEET 2 AE1 3 MET D 217 ASP D 224 -1 O PHE D 223 N LEU D 191
SHEET 3 AE1 3 LEU D 209 PHE D 211 -1 N GLU D 210 O ALA D 219
SHEET 1 AE2 4 VAL D 190 ASN D 192 0
SHEET 2 AE2 4 MET D 217 ASP D 224 -1 O PHE D 223 N LEU D 191
SHEET 3 AE2 4 LYS D 266 ASP D 273 -1 O GLU D 268 N ARG D 222
SHEET 4 AE2 4 THR D 279 THR D 281 -1 O ARG D 280 N THR D 271
SHEET 1 AE3 2 SER D 230 MET D 235 0
SHEET 2 AE3 2 GLY D 251 LYS D 256 -1 O GLY D 251 N MET D 235
SHEET 1 AE4 4 TYR D 291 PHE D 297 0
SHEET 2 AE4 4 LEU D 304 LEU D 309 -1 O LEU D 309 N TYR D 291
SHEET 3 AE4 4 ARG D 315 ALA D 321 -1 O ALA D 321 N LEU D 304
SHEET 4 AE4 4 CYS D 328 GLU D 335 -1 O VAL D 331 N LEU D 318
SHEET 1 AE5 4 PHE D 350 TYR D 351 0
SHEET 2 AE5 4 THR D 354 SER D 359 -1 O THR D 354 N TYR D 351
SHEET 3 AE5 4 HIS D 366 SER D 371 -1 O TYR D 370 N PHE D 355
SHEET 4 AE5 4 LEU D 376 LYS D 379 -1 O LYS D 378 N TRP D 369
SHEET 1 AE6 4 VAL D 387 TYR D 393 0
SHEET 2 AE6 4 PHE D 400 SER D 404 -1 O TYR D 401 N GLY D 392
SHEET 3 AE6 4 ALA D 413 ILE D 417 -1 O ILE D 417 N PHE D 400
SHEET 4 AE6 4 LYS D 423 LYS D 425 -1 O LEU D 424 N LYS D 416
SHEET 1 AE7 4 THR D 432 PHE D 437 0
SHEET 2 AE7 4 TYR D 443 ASN D 450 -1 O SER D 449 N THR D 432
SHEET 3 AE7 4 THR D 453 ASP D 461 -1 O ASN D 460 N TYR D 444
SHEET 4 AE7 4 THR D 466 ILE D 471 -1 O LEU D 467 N LEU D 459
SHEET 1 AE8 8 LYS D 488 GLN D 494 0
SHEET 2 AE8 8 THR D 500 MET D 506 -1 O MET D 505 N GLU D 489
SHEET 3 AE8 8 ILE D 550 ASP D 555 -1 O VAL D 551 N MET D 506
SHEET 4 AE8 8 TYR D 517 TYR D 522 1 N TYR D 522 O VAL D 552
SHEET 5 AE8 8 VAL D 595 TRP D 605 1 O ASP D 596 N TYR D 517
SHEET 6 AE8 8 ALA D 625 VAL D 629 1 O VAL D 629 N GLY D 604
SHEET 7 AE8 8 ASN D 672 GLY D 678 1 O ASN D 672 N GLY D 626
SHEET 8 AE8 8 ASP D 704 TYR D 708 1 O TYR D 708 N HIS D 677
CISPEP 1 ALA A 240 PRO A 241 0 2.56
CISPEP 2 ALA B 240 PRO B 241 0 0.90
CISPEP 3 ALA C 240 PRO C 241 0 2.62
CISPEP 4 ALA D 240 PRO D 241 0 -0.69
CRYST1 95.800 148.857 137.125 90.00 104.02 90.00 P 1 21 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 0.010438 0.000000 0.002605 0.00000
SCALE2 0.000000 0.006718 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007516 0.00000
TER 5771 LEU A 736
TER 11542 LEU B 736
TER 17313 LEU C 736
TER 23084 LEU D 736
MASTER 505 0 0 61 177 0 0 625882 4 0 228
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