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HEADER HYDROLASE 16-MAR-17 5XB6
TITLE CRYSTAL STRUCTURE OF YCJY FROM E. COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN YCJY;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: YCJY, B1327, JW5804;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.F.CHEN,Z.Q.GAO,Q.S.LIU
REVDAT 1 11-APR-18 5XB6 0
JRNL AUTH C.F.CHEN,Z.Q.GAO,Q.S.LIU
JRNL TITL CRYSTAL STRUCTURE OF YCJY FROM E. COLI
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.1_1168
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.36
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.7
REMARK 3 NUMBER OF REFLECTIONS : 268967
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 13581
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 38.3706 - 6.2060 0.99 9759 515 0.1800 0.1947
REMARK 3 2 6.2060 - 4.9292 1.00 9533 484 0.1755 0.1963
REMARK 3 3 4.9292 - 4.3070 1.00 9389 512 0.1347 0.1542
REMARK 3 4 4.3070 - 3.9137 1.00 9406 477 0.1351 0.1551
REMARK 3 5 3.9137 - 3.6334 0.99 9325 484 0.1509 0.1776
REMARK 3 6 3.6334 - 3.4193 0.97 9096 439 0.1684 0.2079
REMARK 3 7 3.4193 - 3.2482 0.99 9143 515 0.1708 0.1971
REMARK 3 8 3.2482 - 3.1068 0.98 9088 528 0.1825 0.2283
REMARK 3 9 3.1068 - 2.9873 0.97 9006 490 0.1825 0.2247
REMARK 3 10 2.9873 - 2.8842 0.96 8907 474 0.1937 0.2359
REMARK 3 11 2.8842 - 2.7941 0.95 8834 455 0.1913 0.2419
REMARK 3 12 2.7941 - 2.7142 0.93 8669 458 0.1982 0.2381
REMARK 3 13 2.7142 - 2.6428 0.92 8453 464 0.1968 0.2405
REMARK 3 14 2.6428 - 2.5783 0.91 8405 472 0.1946 0.2262
REMARK 3 15 2.5783 - 2.5197 0.90 8325 430 0.1967 0.2415
REMARK 3 16 2.5197 - 2.4661 0.89 8236 432 0.1920 0.2391
REMARK 3 17 2.4661 - 2.4168 0.88 8164 399 0.1929 0.2504
REMARK 3 18 2.4168 - 2.3712 0.88 8141 425 0.1983 0.2527
REMARK 3 19 2.3712 - 2.3288 0.88 8101 438 0.2007 0.2455
REMARK 3 20 2.3288 - 2.2894 0.88 8059 423 0.2020 0.2617
REMARK 3 21 2.2894 - 2.2524 0.85 7845 410 0.2345 0.2898
REMARK 3 22 2.2524 - 2.2178 0.85 7802 379 0.2725 0.3377
REMARK 3 23 2.2178 - 2.1852 0.86 7976 419 0.2330 0.2932
REMARK 3 24 2.1852 - 2.1544 0.88 8061 407 0.2113 0.2704
REMARK 3 25 2.1544 - 2.1253 0.86 7909 456 0.2157 0.2728
REMARK 3 26 2.1253 - 2.0977 0.88 8012 431 0.2187 0.2657
REMARK 3 27 2.0977 - 2.0715 0.86 7938 445 0.2128 0.2580
REMARK 3 28 2.0715 - 2.0465 0.87 7917 441 0.2159 0.2754
REMARK 3 29 2.0465 - 2.0227 0.86 7936 464 0.2294 0.3048
REMARK 3 30 2.0227 - 2.0000 0.87 7951 415 0.2272 0.2660
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.790
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 29234
REMARK 3 ANGLE : 1.129 39779
REMARK 3 CHIRALITY : 0.077 4309
REMARK 3 PLANARITY : 0.005 5235
REMARK 3 DIHEDRAL : 13.305 10633
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 5XB6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1300003214.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-SEP-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 284153
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.960
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.4
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.09500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.99
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.60900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.250
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4 M AMMONIUM SULFATE 0.1 M BIS-TRIS
REMARK 280 PH 6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
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 38.79200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 129.41950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 108.20250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 129.41950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.79200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 108.20250
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, 5, 6
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET J 1
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 OH TYR K 263 O HOH K 401 1.80
REMARK 500 OD1 ASP G 283 O HOH G 401 1.80
REMARK 500 O HOH K 447 O HOH K 525 1.80
REMARK 500 N LYS J 27 O HOH J 401 1.84
REMARK 500 O HOH D 695 O HOH D 781 1.84
REMARK 500 O HOH A 453 O HOH B 666 1.85
REMARK 500 O HOH F 603 O HOH F 664 1.85
REMARK 500 O HOH B 655 O HOH B 660 1.86
REMARK 500 O HOH J 540 O HOH J 625 1.87
REMARK 500 O HOH K 699 O HOH L 587 1.88
REMARK 500 O HOH I 653 O HOH I 721 1.88
REMARK 500 O HOH B 621 O HOH B 638 1.89
REMARK 500 O THR C 305 O HOH C 401 1.89
REMARK 500 OE2 GLU B 60 O HOH B 401 1.90
REMARK 500 O HOH J 566 O HOH J 656 1.90
REMARK 500 OE1 GLU B 277 O HOH B 402 1.90
REMARK 500 O HOH C 611 O HOH C 650 1.90
REMARK 500 O HOH J 589 O HOH J 598 1.91
REMARK 500 O HOH E 562 O HOH E 595 1.92
REMARK 500 O LEU E 306 O HOH E 401 1.92
REMARK 500 O HOH J 598 O HOH J 616 1.92
REMARK 500 N MET F 1 O HOH F 401 1.92
REMARK 500 O HOH E 410 O HOH E 425 1.92
REMARK 500 O HOH H 644 O HOH H 686 1.92
REMARK 500 O HOH I 551 O HOH I 624 1.93
REMARK 500 OD1 ASN E 108 O HOH E 402 1.93
REMARK 500 O HOH F 676 O HOH F 711 1.93
REMARK 500 O HOH A 421 O HOH A 549 1.93
REMARK 500 O HOH F 564 O HOH F 647 1.94
REMARK 500 OD1 ASN B 155 O HOH B 403 1.94
REMARK 500 NZ LYS J 190 O HOH J 402 1.94
REMARK 500 O HOH D 626 O HOH D 768 1.94
REMARK 500 O HOH C 640 O HOH C 695 1.94
REMARK 500 O HOH E 581 O HOH E 627 1.94
REMARK 500 OG1 THR E 242 O HOH E 403 1.95
REMARK 500 O HOH E 633 O HOH E 647 1.95
REMARK 500 O HOH B 603 O HOH B 654 1.96
REMARK 500 NZ LYS J 190 O HOH J 403 1.96
REMARK 500 O HOH J 623 O HOH J 666 1.96
REMARK 500 O HOH J 422 O HOH J 498 1.97
REMARK 500 O PHE H 28 O HOH H 401 1.97
REMARK 500 O HOH K 402 O HOH K 505 1.97
REMARK 500 O HOH F 648 O HOH F 654 1.97
REMARK 500 OE1 GLU D 303 O HOH D 401 1.97
REMARK 500 O HOH J 544 O HOH J 655 1.97
REMARK 500 O HOH A 419 O HOH A 457 1.97
REMARK 500 O HOH I 691 O HOH I 742 1.98
REMARK 500 O HOH F 662 O HOH F 688 1.98
REMARK 500 O HOH I 661 O HOH I 716 1.98
REMARK 500 OD1 ASN D 154 O HOH D 402 1.98
REMARK 500
REMARK 500 THIS ENTRY HAS 210 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 F 590 O HOH I 407 4455 1.78
REMARK 500 O HOH F 586 O HOH G 686 3455 1.89
REMARK 500 O HOH E 455 O HOH J 489 4455 1.91
REMARK 500 O HOH F 543 O HOH I 696 4455 1.91
REMARK 500 O HOH F 749 O HOH I 729 4455 1.94
REMARK 500 O HOH I 585 O HOH K 752 2454 1.97
REMARK 500 O HOH G 515 O HOH K 687 1455 2.00
REMARK 500 O HOH G 629 O HOH I 676 2455 2.02
REMARK 500 O HOH G 791 O HOH K 744 1455 2.03
REMARK 500 O HOH G 659 O HOH K 619 1455 2.03
REMARK 500 O HOH I 549 O HOH K 720 2454 2.04
REMARK 500 O HOH D 479 O HOH K 489 4445 2.13
REMARK 500 O HOH I 650 O HOH K 752 2454 2.16
REMARK 500 O HOH F 576 O HOH I 527 4455 2.19
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 GLN A 49 -140.82 -92.38
REMARK 500 GLU A 84 61.97 -119.93
REMARK 500 CYS A 117 -131.18 61.94
REMARK 500 LEU A 186 -91.85 -101.54
REMARK 500 PRO A 209 0.23 -59.28
REMARK 500 ALA A 211 14.96 -157.34
REMARK 500 ASP A 286 -2.06 -153.22
REMARK 500 MET B 2 -48.51 -159.24
REMARK 500 ASN B 3 116.65 -160.74
REMARK 500 ASN B 13 87.47 -150.43
REMARK 500 GLN B 49 -143.82 -93.57
REMARK 500 TYR B 72 -1.45 73.80
REMARK 500 CYS B 117 -135.80 59.32
REMARK 500 SER B 140 46.93 39.50
REMARK 500 LEU B 186 -77.62 -97.89
REMARK 500 PRO B 209 -1.55 -57.61
REMARK 500 ALA B 211 17.05 -156.59
REMARK 500 SER B 268 130.09 -38.56
REMARK 500 ASN C 13 88.15 -150.93
REMARK 500 PRO C 42 170.41 -56.20
REMARK 500 GLN C 49 -145.54 -99.13
REMARK 500 CYS C 117 -130.26 58.68
REMARK 500 LEU C 186 -91.44 -101.51
REMARK 500 PRO C 209 2.44 -64.15
REMARK 500 ALA C 211 16.21 -149.25
REMARK 500 ASP C 270 76.57 -104.09
REMARK 500 ASP C 286 9.37 -150.20
REMARK 500 MET D 2 -67.59 -135.92
REMARK 500 ASN D 13 89.42 -153.31
REMARK 500 GLU D 30 -9.27 -58.49
REMARK 500 GLN D 49 -144.01 -93.15
REMARK 500 CYS D 117 -134.50 59.32
REMARK 500 LEU D 186 -80.08 -98.88
REMARK 500 PRO D 209 2.29 -62.84
REMARK 500 ALA D 211 23.33 -155.57
REMARK 500 SER D 268 131.75 -39.84
REMARK 500 ASN E 13 85.25 -155.39
REMARK 500 GLN E 49 -140.35 -90.47
REMARK 500 CYS E 117 -133.61 57.49
REMARK 500 LEU E 186 -88.08 -96.58
REMARK 500 ALA E 211 9.36 -159.43
REMARK 500 SER E 268 127.52 -31.87
REMARK 500 ASP E 286 6.14 -151.43
REMARK 500 GLU F 30 0.53 -68.96
REMARK 500 GLN F 49 -144.76 -96.56
REMARK 500 GLU F 84 61.95 -118.76
REMARK 500 CYS F 117 -137.19 59.62
REMARK 500 LEU F 186 -88.02 -103.68
REMARK 500 PRO F 209 4.66 -65.27
REMARK 500 ALA F 211 15.04 -160.93
REMARK 500
REMARK 500 THIS ENTRY HAS 101 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 A 716 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH A 717 DISTANCE = 6.81 ANGSTROMS
REMARK 525 HOH B 753 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH B 754 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH B 755 DISTANCE = 6.47 ANGSTROMS
REMARK 525 HOH B 756 DISTANCE = 6.87 ANGSTROMS
REMARK 525 HOH B 757 DISTANCE = 7.14 ANGSTROMS
REMARK 525 HOH B 758 DISTANCE = 7.43 ANGSTROMS
REMARK 525 HOH C 755 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH C 756 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH C 757 DISTANCE = 6.88 ANGSTROMS
REMARK 525 HOH C 758 DISTANCE = 6.95 ANGSTROMS
REMARK 525 HOH D 786 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH D 787 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH D 788 DISTANCE = 6.40 ANGSTROMS
REMARK 525 HOH D 789 DISTANCE = 6.70 ANGSTROMS
REMARK 525 HOH E 721 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH E 722 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH E 723 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH E 724 DISTANCE = 6.86 ANGSTROMS
REMARK 525 HOH E 725 DISTANCE = 7.41 ANGSTROMS
REMARK 525 HOH G 795 DISTANCE = 6.51 ANGSTROMS
REMARK 525 HOH H 721 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH H 722 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH H 723 DISTANCE = 6.51 ANGSTROMS
REMARK 525 HOH H 724 DISTANCE = 8.49 ANGSTROMS
REMARK 525 HOH I 747 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH J 731 DISTANCE = 6.52 ANGSTROMS
DBREF 5XB6 A 1 306 UNP P76049 YCJY_ECOLI 1 306
DBREF 5XB6 B 1 306 UNP P76049 YCJY_ECOLI 1 306
DBREF 5XB6 C 1 306 UNP P76049 YCJY_ECOLI 1 306
DBREF 5XB6 D 1 306 UNP P76049 YCJY_ECOLI 1 306
DBREF 5XB6 E 1 306 UNP P76049 YCJY_ECOLI 1 306
DBREF 5XB6 F 1 306 UNP P76049 YCJY_ECOLI 1 306
DBREF 5XB6 G 1 306 UNP P76049 YCJY_ECOLI 1 306
DBREF 5XB6 H 1 306 UNP P76049 YCJY_ECOLI 1 306
DBREF 5XB6 I 1 306 UNP P76049 YCJY_ECOLI 1 306
DBREF 5XB6 J 1 306 UNP P76049 YCJY_ECOLI 1 306
DBREF 5XB6 K 1 306 UNP P76049 YCJY_ECOLI 1 306
DBREF 5XB6 L 1 306 UNP P76049 YCJY_ECOLI 1 306
SEQRES 1 A 306 MET MET ASN ASN LYS VAL SER PHE THR ASN SER ASN ASN
SEQRES 2 A 306 PRO THR ILE SER LEU SER ALA VAL ILE TYR PHE PRO PRO
SEQRES 3 A 306 LYS PHE ASP GLU THR ARG GLN TYR GLN ALA ILE VAL LEU
SEQRES 4 A 306 SER HIS PRO GLY GLY GLY VAL LYS GLU GLN THR ALA GLY
SEQRES 5 A 306 THR TYR ALA LYS LYS LEU ALA GLU LYS GLY PHE VAL THR
SEQRES 6 A 306 ILE ALA TYR ASP ALA SER TYR GLN GLY GLU SER GLY GLY
SEQRES 7 A 306 GLU PRO ARG GLN LEU GLU ASN PRO TYR ILE ARG THR GLU
SEQRES 8 A 306 ASP ILE SER ALA VAL ILE ASP TYR LEU THR THR LEU SER
SEQRES 9 A 306 TYR VAL ASP ASN THR ARG ILE GLY ALA MET GLY ILE CYS
SEQRES 10 A 306 ALA GLY ALA GLY TYR THR ALA ASN ALA ALA ILE GLN ASP
SEQRES 11 A 306 ARG ARG ILE LYS ALA ILE GLY THR VAL SER ALA VAL ASN
SEQRES 12 A 306 ILE GLY SER ILE PHE ARG ASN GLY TRP GLU ASN ASN VAL
SEQRES 13 A 306 LYS SER ILE ASP ALA LEU PRO TYR VAL GLU ALA GLY SER
SEQRES 14 A 306 ASN ALA ARG THR SER ASP ILE SER SER GLY GLU TYR ALA
SEQRES 15 A 306 ILE MET PRO LEU ALA PRO MET LYS GLU SER ASP ALA PRO
SEQRES 16 A 306 ASN GLU GLU LEU ARG GLN ALA TRP GLU TYR TYR HIS THR
SEQRES 17 A 306 PRO ARG ALA GLN TYR PRO THR ALA PRO GLY TYR ALA THR
SEQRES 18 A 306 LEU ARG SER LEU ASN GLN ILE ILE THR TYR ASP ALA TYR
SEQRES 19 A 306 HIS MET ALA GLU VAL TYR LEU THR GLN PRO THR GLN ILE
SEQRES 20 A 306 VAL ALA GLY SER GLN ALA GLY SER LYS TRP MET SER ASP
SEQRES 21 A 306 ASP LEU TYR ASP ARG ALA SER SER GLN ASP LYS ARG TYR
SEQRES 22 A 306 HIS ILE VAL GLU GLY ALA ASN HIS MET ASP LEU TYR ASP
SEQRES 23 A 306 GLY LYS ALA TYR VAL ALA GLU ALA ILE SER VAL LEU ALA
SEQRES 24 A 306 PRO PHE PHE GLU GLU THR LEU
SEQRES 1 B 306 MET MET ASN ASN LYS VAL SER PHE THR ASN SER ASN ASN
SEQRES 2 B 306 PRO THR ILE SER LEU SER ALA VAL ILE TYR PHE PRO PRO
SEQRES 3 B 306 LYS PHE ASP GLU THR ARG GLN TYR GLN ALA ILE VAL LEU
SEQRES 4 B 306 SER HIS PRO GLY GLY GLY VAL LYS GLU GLN THR ALA GLY
SEQRES 5 B 306 THR TYR ALA LYS LYS LEU ALA GLU LYS GLY PHE VAL THR
SEQRES 6 B 306 ILE ALA TYR ASP ALA SER TYR GLN GLY GLU SER GLY GLY
SEQRES 7 B 306 GLU PRO ARG GLN LEU GLU ASN PRO TYR ILE ARG THR GLU
SEQRES 8 B 306 ASP ILE SER ALA VAL ILE ASP TYR LEU THR THR LEU SER
SEQRES 9 B 306 TYR VAL ASP ASN THR ARG ILE GLY ALA MET GLY ILE CYS
SEQRES 10 B 306 ALA GLY ALA GLY TYR THR ALA ASN ALA ALA ILE GLN ASP
SEQRES 11 B 306 ARG ARG ILE LYS ALA ILE GLY THR VAL SER ALA VAL ASN
SEQRES 12 B 306 ILE GLY SER ILE PHE ARG ASN GLY TRP GLU ASN ASN VAL
SEQRES 13 B 306 LYS SER ILE ASP ALA LEU PRO TYR VAL GLU ALA GLY SER
SEQRES 14 B 306 ASN ALA ARG THR SER ASP ILE SER SER GLY GLU TYR ALA
SEQRES 15 B 306 ILE MET PRO LEU ALA PRO MET LYS GLU SER ASP ALA PRO
SEQRES 16 B 306 ASN GLU GLU LEU ARG GLN ALA TRP GLU TYR TYR HIS THR
SEQRES 17 B 306 PRO ARG ALA GLN TYR PRO THR ALA PRO GLY TYR ALA THR
SEQRES 18 B 306 LEU ARG SER LEU ASN GLN ILE ILE THR TYR ASP ALA TYR
SEQRES 19 B 306 HIS MET ALA GLU VAL TYR LEU THR GLN PRO THR GLN ILE
SEQRES 20 B 306 VAL ALA GLY SER GLN ALA GLY SER LYS TRP MET SER ASP
SEQRES 21 B 306 ASP LEU TYR ASP ARG ALA SER SER GLN ASP LYS ARG TYR
SEQRES 22 B 306 HIS ILE VAL GLU GLY ALA ASN HIS MET ASP LEU TYR ASP
SEQRES 23 B 306 GLY LYS ALA TYR VAL ALA GLU ALA ILE SER VAL LEU ALA
SEQRES 24 B 306 PRO PHE PHE GLU GLU THR LEU
SEQRES 1 C 306 MET MET ASN ASN LYS VAL SER PHE THR ASN SER ASN ASN
SEQRES 2 C 306 PRO THR ILE SER LEU SER ALA VAL ILE TYR PHE PRO PRO
SEQRES 3 C 306 LYS PHE ASP GLU THR ARG GLN TYR GLN ALA ILE VAL LEU
SEQRES 4 C 306 SER HIS PRO GLY GLY GLY VAL LYS GLU GLN THR ALA GLY
SEQRES 5 C 306 THR TYR ALA LYS LYS LEU ALA GLU LYS GLY PHE VAL THR
SEQRES 6 C 306 ILE ALA TYR ASP ALA SER TYR GLN GLY GLU SER GLY GLY
SEQRES 7 C 306 GLU PRO ARG GLN LEU GLU ASN PRO TYR ILE ARG THR GLU
SEQRES 8 C 306 ASP ILE SER ALA VAL ILE ASP TYR LEU THR THR LEU SER
SEQRES 9 C 306 TYR VAL ASP ASN THR ARG ILE GLY ALA MET GLY ILE CYS
SEQRES 10 C 306 ALA GLY ALA GLY TYR THR ALA ASN ALA ALA ILE GLN ASP
SEQRES 11 C 306 ARG ARG ILE LYS ALA ILE GLY THR VAL SER ALA VAL ASN
SEQRES 12 C 306 ILE GLY SER ILE PHE ARG ASN GLY TRP GLU ASN ASN VAL
SEQRES 13 C 306 LYS SER ILE ASP ALA LEU PRO TYR VAL GLU ALA GLY SER
SEQRES 14 C 306 ASN ALA ARG THR SER ASP ILE SER SER GLY GLU TYR ALA
SEQRES 15 C 306 ILE MET PRO LEU ALA PRO MET LYS GLU SER ASP ALA PRO
SEQRES 16 C 306 ASN GLU GLU LEU ARG GLN ALA TRP GLU TYR TYR HIS THR
SEQRES 17 C 306 PRO ARG ALA GLN TYR PRO THR ALA PRO GLY TYR ALA THR
SEQRES 18 C 306 LEU ARG SER LEU ASN GLN ILE ILE THR TYR ASP ALA TYR
SEQRES 19 C 306 HIS MET ALA GLU VAL TYR LEU THR GLN PRO THR GLN ILE
SEQRES 20 C 306 VAL ALA GLY SER GLN ALA GLY SER LYS TRP MET SER ASP
SEQRES 21 C 306 ASP LEU TYR ASP ARG ALA SER SER GLN ASP LYS ARG TYR
SEQRES 22 C 306 HIS ILE VAL GLU GLY ALA ASN HIS MET ASP LEU TYR ASP
SEQRES 23 C 306 GLY LYS ALA TYR VAL ALA GLU ALA ILE SER VAL LEU ALA
SEQRES 24 C 306 PRO PHE PHE GLU GLU THR LEU
SEQRES 1 D 306 MET MET ASN ASN LYS VAL SER PHE THR ASN SER ASN ASN
SEQRES 2 D 306 PRO THR ILE SER LEU SER ALA VAL ILE TYR PHE PRO PRO
SEQRES 3 D 306 LYS PHE ASP GLU THR ARG GLN TYR GLN ALA ILE VAL LEU
SEQRES 4 D 306 SER HIS PRO GLY GLY GLY VAL LYS GLU GLN THR ALA GLY
SEQRES 5 D 306 THR TYR ALA LYS LYS LEU ALA GLU LYS GLY PHE VAL THR
SEQRES 6 D 306 ILE ALA TYR ASP ALA SER TYR GLN GLY GLU SER GLY GLY
SEQRES 7 D 306 GLU PRO ARG GLN LEU GLU ASN PRO TYR ILE ARG THR GLU
SEQRES 8 D 306 ASP ILE SER ALA VAL ILE ASP TYR LEU THR THR LEU SER
SEQRES 9 D 306 TYR VAL ASP ASN THR ARG ILE GLY ALA MET GLY ILE CYS
SEQRES 10 D 306 ALA GLY ALA GLY TYR THR ALA ASN ALA ALA ILE GLN ASP
SEQRES 11 D 306 ARG ARG ILE LYS ALA ILE GLY THR VAL SER ALA VAL ASN
SEQRES 12 D 306 ILE GLY SER ILE PHE ARG ASN GLY TRP GLU ASN ASN VAL
SEQRES 13 D 306 LYS SER ILE ASP ALA LEU PRO TYR VAL GLU ALA GLY SER
SEQRES 14 D 306 ASN ALA ARG THR SER ASP ILE SER SER GLY GLU TYR ALA
SEQRES 15 D 306 ILE MET PRO LEU ALA PRO MET LYS GLU SER ASP ALA PRO
SEQRES 16 D 306 ASN GLU GLU LEU ARG GLN ALA TRP GLU TYR TYR HIS THR
SEQRES 17 D 306 PRO ARG ALA GLN TYR PRO THR ALA PRO GLY TYR ALA THR
SEQRES 18 D 306 LEU ARG SER LEU ASN GLN ILE ILE THR TYR ASP ALA TYR
SEQRES 19 D 306 HIS MET ALA GLU VAL TYR LEU THR GLN PRO THR GLN ILE
SEQRES 20 D 306 VAL ALA GLY SER GLN ALA GLY SER LYS TRP MET SER ASP
SEQRES 21 D 306 ASP LEU TYR ASP ARG ALA SER SER GLN ASP LYS ARG TYR
SEQRES 22 D 306 HIS ILE VAL GLU GLY ALA ASN HIS MET ASP LEU TYR ASP
SEQRES 23 D 306 GLY LYS ALA TYR VAL ALA GLU ALA ILE SER VAL LEU ALA
SEQRES 24 D 306 PRO PHE PHE GLU GLU THR LEU
SEQRES 1 E 306 MET MET ASN ASN LYS VAL SER PHE THR ASN SER ASN ASN
SEQRES 2 E 306 PRO THR ILE SER LEU SER ALA VAL ILE TYR PHE PRO PRO
SEQRES 3 E 306 LYS PHE ASP GLU THR ARG GLN TYR GLN ALA ILE VAL LEU
SEQRES 4 E 306 SER HIS PRO GLY GLY GLY VAL LYS GLU GLN THR ALA GLY
SEQRES 5 E 306 THR TYR ALA LYS LYS LEU ALA GLU LYS GLY PHE VAL THR
SEQRES 6 E 306 ILE ALA TYR ASP ALA SER TYR GLN GLY GLU SER GLY GLY
SEQRES 7 E 306 GLU PRO ARG GLN LEU GLU ASN PRO TYR ILE ARG THR GLU
SEQRES 8 E 306 ASP ILE SER ALA VAL ILE ASP TYR LEU THR THR LEU SER
SEQRES 9 E 306 TYR VAL ASP ASN THR ARG ILE GLY ALA MET GLY ILE CYS
SEQRES 10 E 306 ALA GLY ALA GLY TYR THR ALA ASN ALA ALA ILE GLN ASP
SEQRES 11 E 306 ARG ARG ILE LYS ALA ILE GLY THR VAL SER ALA VAL ASN
SEQRES 12 E 306 ILE GLY SER ILE PHE ARG ASN GLY TRP GLU ASN ASN VAL
SEQRES 13 E 306 LYS SER ILE ASP ALA LEU PRO TYR VAL GLU ALA GLY SER
SEQRES 14 E 306 ASN ALA ARG THR SER ASP ILE SER SER GLY GLU TYR ALA
SEQRES 15 E 306 ILE MET PRO LEU ALA PRO MET LYS GLU SER ASP ALA PRO
SEQRES 16 E 306 ASN GLU GLU LEU ARG GLN ALA TRP GLU TYR TYR HIS THR
SEQRES 17 E 306 PRO ARG ALA GLN TYR PRO THR ALA PRO GLY TYR ALA THR
SEQRES 18 E 306 LEU ARG SER LEU ASN GLN ILE ILE THR TYR ASP ALA TYR
SEQRES 19 E 306 HIS MET ALA GLU VAL TYR LEU THR GLN PRO THR GLN ILE
SEQRES 20 E 306 VAL ALA GLY SER GLN ALA GLY SER LYS TRP MET SER ASP
SEQRES 21 E 306 ASP LEU TYR ASP ARG ALA SER SER GLN ASP LYS ARG TYR
SEQRES 22 E 306 HIS ILE VAL GLU GLY ALA ASN HIS MET ASP LEU TYR ASP
SEQRES 23 E 306 GLY LYS ALA TYR VAL ALA GLU ALA ILE SER VAL LEU ALA
SEQRES 24 E 306 PRO PHE PHE GLU GLU THR LEU
SEQRES 1 F 306 MET MET ASN ASN LYS VAL SER PHE THR ASN SER ASN ASN
SEQRES 2 F 306 PRO THR ILE SER LEU SER ALA VAL ILE TYR PHE PRO PRO
SEQRES 3 F 306 LYS PHE ASP GLU THR ARG GLN TYR GLN ALA ILE VAL LEU
SEQRES 4 F 306 SER HIS PRO GLY GLY GLY VAL LYS GLU GLN THR ALA GLY
SEQRES 5 F 306 THR TYR ALA LYS LYS LEU ALA GLU LYS GLY PHE VAL THR
SEQRES 6 F 306 ILE ALA TYR ASP ALA SER TYR GLN GLY GLU SER GLY GLY
SEQRES 7 F 306 GLU PRO ARG GLN LEU GLU ASN PRO TYR ILE ARG THR GLU
SEQRES 8 F 306 ASP ILE SER ALA VAL ILE ASP TYR LEU THR THR LEU SER
SEQRES 9 F 306 TYR VAL ASP ASN THR ARG ILE GLY ALA MET GLY ILE CYS
SEQRES 10 F 306 ALA GLY ALA GLY TYR THR ALA ASN ALA ALA ILE GLN ASP
SEQRES 11 F 306 ARG ARG ILE LYS ALA ILE GLY THR VAL SER ALA VAL ASN
SEQRES 12 F 306 ILE GLY SER ILE PHE ARG ASN GLY TRP GLU ASN ASN VAL
SEQRES 13 F 306 LYS SER ILE ASP ALA LEU PRO TYR VAL GLU ALA GLY SER
SEQRES 14 F 306 ASN ALA ARG THR SER ASP ILE SER SER GLY GLU TYR ALA
SEQRES 15 F 306 ILE MET PRO LEU ALA PRO MET LYS GLU SER ASP ALA PRO
SEQRES 16 F 306 ASN GLU GLU LEU ARG GLN ALA TRP GLU TYR TYR HIS THR
SEQRES 17 F 306 PRO ARG ALA GLN TYR PRO THR ALA PRO GLY TYR ALA THR
SEQRES 18 F 306 LEU ARG SER LEU ASN GLN ILE ILE THR TYR ASP ALA TYR
SEQRES 19 F 306 HIS MET ALA GLU VAL TYR LEU THR GLN PRO THR GLN ILE
SEQRES 20 F 306 VAL ALA GLY SER GLN ALA GLY SER LYS TRP MET SER ASP
SEQRES 21 F 306 ASP LEU TYR ASP ARG ALA SER SER GLN ASP LYS ARG TYR
SEQRES 22 F 306 HIS ILE VAL GLU GLY ALA ASN HIS MET ASP LEU TYR ASP
SEQRES 23 F 306 GLY LYS ALA TYR VAL ALA GLU ALA ILE SER VAL LEU ALA
SEQRES 24 F 306 PRO PHE PHE GLU GLU THR LEU
SEQRES 1 G 306 MET MET ASN ASN LYS VAL SER PHE THR ASN SER ASN ASN
SEQRES 2 G 306 PRO THR ILE SER LEU SER ALA VAL ILE TYR PHE PRO PRO
SEQRES 3 G 306 LYS PHE ASP GLU THR ARG GLN TYR GLN ALA ILE VAL LEU
SEQRES 4 G 306 SER HIS PRO GLY GLY GLY VAL LYS GLU GLN THR ALA GLY
SEQRES 5 G 306 THR TYR ALA LYS LYS LEU ALA GLU LYS GLY PHE VAL THR
SEQRES 6 G 306 ILE ALA TYR ASP ALA SER TYR GLN GLY GLU SER GLY GLY
SEQRES 7 G 306 GLU PRO ARG GLN LEU GLU ASN PRO TYR ILE ARG THR GLU
SEQRES 8 G 306 ASP ILE SER ALA VAL ILE ASP TYR LEU THR THR LEU SER
SEQRES 9 G 306 TYR VAL ASP ASN THR ARG ILE GLY ALA MET GLY ILE CYS
SEQRES 10 G 306 ALA GLY ALA GLY TYR THR ALA ASN ALA ALA ILE GLN ASP
SEQRES 11 G 306 ARG ARG ILE LYS ALA ILE GLY THR VAL SER ALA VAL ASN
SEQRES 12 G 306 ILE GLY SER ILE PHE ARG ASN GLY TRP GLU ASN ASN VAL
SEQRES 13 G 306 LYS SER ILE ASP ALA LEU PRO TYR VAL GLU ALA GLY SER
SEQRES 14 G 306 ASN ALA ARG THR SER ASP ILE SER SER GLY GLU TYR ALA
SEQRES 15 G 306 ILE MET PRO LEU ALA PRO MET LYS GLU SER ASP ALA PRO
SEQRES 16 G 306 ASN GLU GLU LEU ARG GLN ALA TRP GLU TYR TYR HIS THR
SEQRES 17 G 306 PRO ARG ALA GLN TYR PRO THR ALA PRO GLY TYR ALA THR
SEQRES 18 G 306 LEU ARG SER LEU ASN GLN ILE ILE THR TYR ASP ALA TYR
SEQRES 19 G 306 HIS MET ALA GLU VAL TYR LEU THR GLN PRO THR GLN ILE
SEQRES 20 G 306 VAL ALA GLY SER GLN ALA GLY SER LYS TRP MET SER ASP
SEQRES 21 G 306 ASP LEU TYR ASP ARG ALA SER SER GLN ASP LYS ARG TYR
SEQRES 22 G 306 HIS ILE VAL GLU GLY ALA ASN HIS MET ASP LEU TYR ASP
SEQRES 23 G 306 GLY LYS ALA TYR VAL ALA GLU ALA ILE SER VAL LEU ALA
SEQRES 24 G 306 PRO PHE PHE GLU GLU THR LEU
SEQRES 1 H 306 MET MET ASN ASN LYS VAL SER PHE THR ASN SER ASN ASN
SEQRES 2 H 306 PRO THR ILE SER LEU SER ALA VAL ILE TYR PHE PRO PRO
SEQRES 3 H 306 LYS PHE ASP GLU THR ARG GLN TYR GLN ALA ILE VAL LEU
SEQRES 4 H 306 SER HIS PRO GLY GLY GLY VAL LYS GLU GLN THR ALA GLY
SEQRES 5 H 306 THR TYR ALA LYS LYS LEU ALA GLU LYS GLY PHE VAL THR
SEQRES 6 H 306 ILE ALA TYR ASP ALA SER TYR GLN GLY GLU SER GLY GLY
SEQRES 7 H 306 GLU PRO ARG GLN LEU GLU ASN PRO TYR ILE ARG THR GLU
SEQRES 8 H 306 ASP ILE SER ALA VAL ILE ASP TYR LEU THR THR LEU SER
SEQRES 9 H 306 TYR VAL ASP ASN THR ARG ILE GLY ALA MET GLY ILE CYS
SEQRES 10 H 306 ALA GLY ALA GLY TYR THR ALA ASN ALA ALA ILE GLN ASP
SEQRES 11 H 306 ARG ARG ILE LYS ALA ILE GLY THR VAL SER ALA VAL ASN
SEQRES 12 H 306 ILE GLY SER ILE PHE ARG ASN GLY TRP GLU ASN ASN VAL
SEQRES 13 H 306 LYS SER ILE ASP ALA LEU PRO TYR VAL GLU ALA GLY SER
SEQRES 14 H 306 ASN ALA ARG THR SER ASP ILE SER SER GLY GLU TYR ALA
SEQRES 15 H 306 ILE MET PRO LEU ALA PRO MET LYS GLU SER ASP ALA PRO
SEQRES 16 H 306 ASN GLU GLU LEU ARG GLN ALA TRP GLU TYR TYR HIS THR
SEQRES 17 H 306 PRO ARG ALA GLN TYR PRO THR ALA PRO GLY TYR ALA THR
SEQRES 18 H 306 LEU ARG SER LEU ASN GLN ILE ILE THR TYR ASP ALA TYR
SEQRES 19 H 306 HIS MET ALA GLU VAL TYR LEU THR GLN PRO THR GLN ILE
SEQRES 20 H 306 VAL ALA GLY SER GLN ALA GLY SER LYS TRP MET SER ASP
SEQRES 21 H 306 ASP LEU TYR ASP ARG ALA SER SER GLN ASP LYS ARG TYR
SEQRES 22 H 306 HIS ILE VAL GLU GLY ALA ASN HIS MET ASP LEU TYR ASP
SEQRES 23 H 306 GLY LYS ALA TYR VAL ALA GLU ALA ILE SER VAL LEU ALA
SEQRES 24 H 306 PRO PHE PHE GLU GLU THR LEU
SEQRES 1 I 306 MET MET ASN ASN LYS VAL SER PHE THR ASN SER ASN ASN
SEQRES 2 I 306 PRO THR ILE SER LEU SER ALA VAL ILE TYR PHE PRO PRO
SEQRES 3 I 306 LYS PHE ASP GLU THR ARG GLN TYR GLN ALA ILE VAL LEU
SEQRES 4 I 306 SER HIS PRO GLY GLY GLY VAL LYS GLU GLN THR ALA GLY
SEQRES 5 I 306 THR TYR ALA LYS LYS LEU ALA GLU LYS GLY PHE VAL THR
SEQRES 6 I 306 ILE ALA TYR ASP ALA SER TYR GLN GLY GLU SER GLY GLY
SEQRES 7 I 306 GLU PRO ARG GLN LEU GLU ASN PRO TYR ILE ARG THR GLU
SEQRES 8 I 306 ASP ILE SER ALA VAL ILE ASP TYR LEU THR THR LEU SER
SEQRES 9 I 306 TYR VAL ASP ASN THR ARG ILE GLY ALA MET GLY ILE CYS
SEQRES 10 I 306 ALA GLY ALA GLY TYR THR ALA ASN ALA ALA ILE GLN ASP
SEQRES 11 I 306 ARG ARG ILE LYS ALA ILE GLY THR VAL SER ALA VAL ASN
SEQRES 12 I 306 ILE GLY SER ILE PHE ARG ASN GLY TRP GLU ASN ASN VAL
SEQRES 13 I 306 LYS SER ILE ASP ALA LEU PRO TYR VAL GLU ALA GLY SER
SEQRES 14 I 306 ASN ALA ARG THR SER ASP ILE SER SER GLY GLU TYR ALA
SEQRES 15 I 306 ILE MET PRO LEU ALA PRO MET LYS GLU SER ASP ALA PRO
SEQRES 16 I 306 ASN GLU GLU LEU ARG GLN ALA TRP GLU TYR TYR HIS THR
SEQRES 17 I 306 PRO ARG ALA GLN TYR PRO THR ALA PRO GLY TYR ALA THR
SEQRES 18 I 306 LEU ARG SER LEU ASN GLN ILE ILE THR TYR ASP ALA TYR
SEQRES 19 I 306 HIS MET ALA GLU VAL TYR LEU THR GLN PRO THR GLN ILE
SEQRES 20 I 306 VAL ALA GLY SER GLN ALA GLY SER LYS TRP MET SER ASP
SEQRES 21 I 306 ASP LEU TYR ASP ARG ALA SER SER GLN ASP LYS ARG TYR
SEQRES 22 I 306 HIS ILE VAL GLU GLY ALA ASN HIS MET ASP LEU TYR ASP
SEQRES 23 I 306 GLY LYS ALA TYR VAL ALA GLU ALA ILE SER VAL LEU ALA
SEQRES 24 I 306 PRO PHE PHE GLU GLU THR LEU
SEQRES 1 J 306 MET MET ASN ASN LYS VAL SER PHE THR ASN SER ASN ASN
SEQRES 2 J 306 PRO THR ILE SER LEU SER ALA VAL ILE TYR PHE PRO PRO
SEQRES 3 J 306 LYS PHE ASP GLU THR ARG GLN TYR GLN ALA ILE VAL LEU
SEQRES 4 J 306 SER HIS PRO GLY GLY GLY VAL LYS GLU GLN THR ALA GLY
SEQRES 5 J 306 THR TYR ALA LYS LYS LEU ALA GLU LYS GLY PHE VAL THR
SEQRES 6 J 306 ILE ALA TYR ASP ALA SER TYR GLN GLY GLU SER GLY GLY
SEQRES 7 J 306 GLU PRO ARG GLN LEU GLU ASN PRO TYR ILE ARG THR GLU
SEQRES 8 J 306 ASP ILE SER ALA VAL ILE ASP TYR LEU THR THR LEU SER
SEQRES 9 J 306 TYR VAL ASP ASN THR ARG ILE GLY ALA MET GLY ILE CYS
SEQRES 10 J 306 ALA GLY ALA GLY TYR THR ALA ASN ALA ALA ILE GLN ASP
SEQRES 11 J 306 ARG ARG ILE LYS ALA ILE GLY THR VAL SER ALA VAL ASN
SEQRES 12 J 306 ILE GLY SER ILE PHE ARG ASN GLY TRP GLU ASN ASN VAL
SEQRES 13 J 306 LYS SER ILE ASP ALA LEU PRO TYR VAL GLU ALA GLY SER
SEQRES 14 J 306 ASN ALA ARG THR SER ASP ILE SER SER GLY GLU TYR ALA
SEQRES 15 J 306 ILE MET PRO LEU ALA PRO MET LYS GLU SER ASP ALA PRO
SEQRES 16 J 306 ASN GLU GLU LEU ARG GLN ALA TRP GLU TYR TYR HIS THR
SEQRES 17 J 306 PRO ARG ALA GLN TYR PRO THR ALA PRO GLY TYR ALA THR
SEQRES 18 J 306 LEU ARG SER LEU ASN GLN ILE ILE THR TYR ASP ALA TYR
SEQRES 19 J 306 HIS MET ALA GLU VAL TYR LEU THR GLN PRO THR GLN ILE
SEQRES 20 J 306 VAL ALA GLY SER GLN ALA GLY SER LYS TRP MET SER ASP
SEQRES 21 J 306 ASP LEU TYR ASP ARG ALA SER SER GLN ASP LYS ARG TYR
SEQRES 22 J 306 HIS ILE VAL GLU GLY ALA ASN HIS MET ASP LEU TYR ASP
SEQRES 23 J 306 GLY LYS ALA TYR VAL ALA GLU ALA ILE SER VAL LEU ALA
SEQRES 24 J 306 PRO PHE PHE GLU GLU THR LEU
SEQRES 1 K 306 MET MET ASN ASN LYS VAL SER PHE THR ASN SER ASN ASN
SEQRES 2 K 306 PRO THR ILE SER LEU SER ALA VAL ILE TYR PHE PRO PRO
SEQRES 3 K 306 LYS PHE ASP GLU THR ARG GLN TYR GLN ALA ILE VAL LEU
SEQRES 4 K 306 SER HIS PRO GLY GLY GLY VAL LYS GLU GLN THR ALA GLY
SEQRES 5 K 306 THR TYR ALA LYS LYS LEU ALA GLU LYS GLY PHE VAL THR
SEQRES 6 K 306 ILE ALA TYR ASP ALA SER TYR GLN GLY GLU SER GLY GLY
SEQRES 7 K 306 GLU PRO ARG GLN LEU GLU ASN PRO TYR ILE ARG THR GLU
SEQRES 8 K 306 ASP ILE SER ALA VAL ILE ASP TYR LEU THR THR LEU SER
SEQRES 9 K 306 TYR VAL ASP ASN THR ARG ILE GLY ALA MET GLY ILE CYS
SEQRES 10 K 306 ALA GLY ALA GLY TYR THR ALA ASN ALA ALA ILE GLN ASP
SEQRES 11 K 306 ARG ARG ILE LYS ALA ILE GLY THR VAL SER ALA VAL ASN
SEQRES 12 K 306 ILE GLY SER ILE PHE ARG ASN GLY TRP GLU ASN ASN VAL
SEQRES 13 K 306 LYS SER ILE ASP ALA LEU PRO TYR VAL GLU ALA GLY SER
SEQRES 14 K 306 ASN ALA ARG THR SER ASP ILE SER SER GLY GLU TYR ALA
SEQRES 15 K 306 ILE MET PRO LEU ALA PRO MET LYS GLU SER ASP ALA PRO
SEQRES 16 K 306 ASN GLU GLU LEU ARG GLN ALA TRP GLU TYR TYR HIS THR
SEQRES 17 K 306 PRO ARG ALA GLN TYR PRO THR ALA PRO GLY TYR ALA THR
SEQRES 18 K 306 LEU ARG SER LEU ASN GLN ILE ILE THR TYR ASP ALA TYR
SEQRES 19 K 306 HIS MET ALA GLU VAL TYR LEU THR GLN PRO THR GLN ILE
SEQRES 20 K 306 VAL ALA GLY SER GLN ALA GLY SER LYS TRP MET SER ASP
SEQRES 21 K 306 ASP LEU TYR ASP ARG ALA SER SER GLN ASP LYS ARG TYR
SEQRES 22 K 306 HIS ILE VAL GLU GLY ALA ASN HIS MET ASP LEU TYR ASP
SEQRES 23 K 306 GLY LYS ALA TYR VAL ALA GLU ALA ILE SER VAL LEU ALA
SEQRES 24 K 306 PRO PHE PHE GLU GLU THR LEU
SEQRES 1 L 306 MET MET ASN ASN LYS VAL SER PHE THR ASN SER ASN ASN
SEQRES 2 L 306 PRO THR ILE SER LEU SER ALA VAL ILE TYR PHE PRO PRO
SEQRES 3 L 306 LYS PHE ASP GLU THR ARG GLN TYR GLN ALA ILE VAL LEU
SEQRES 4 L 306 SER HIS PRO GLY GLY GLY VAL LYS GLU GLN THR ALA GLY
SEQRES 5 L 306 THR TYR ALA LYS LYS LEU ALA GLU LYS GLY PHE VAL THR
SEQRES 6 L 306 ILE ALA TYR ASP ALA SER TYR GLN GLY GLU SER GLY GLY
SEQRES 7 L 306 GLU PRO ARG GLN LEU GLU ASN PRO TYR ILE ARG THR GLU
SEQRES 8 L 306 ASP ILE SER ALA VAL ILE ASP TYR LEU THR THR LEU SER
SEQRES 9 L 306 TYR VAL ASP ASN THR ARG ILE GLY ALA MET GLY ILE CYS
SEQRES 10 L 306 ALA GLY ALA GLY TYR THR ALA ASN ALA ALA ILE GLN ASP
SEQRES 11 L 306 ARG ARG ILE LYS ALA ILE GLY THR VAL SER ALA VAL ASN
SEQRES 12 L 306 ILE GLY SER ILE PHE ARG ASN GLY TRP GLU ASN ASN VAL
SEQRES 13 L 306 LYS SER ILE ASP ALA LEU PRO TYR VAL GLU ALA GLY SER
SEQRES 14 L 306 ASN ALA ARG THR SER ASP ILE SER SER GLY GLU TYR ALA
SEQRES 15 L 306 ILE MET PRO LEU ALA PRO MET LYS GLU SER ASP ALA PRO
SEQRES 16 L 306 ASN GLU GLU LEU ARG GLN ALA TRP GLU TYR TYR HIS THR
SEQRES 17 L 306 PRO ARG ALA GLN TYR PRO THR ALA PRO GLY TYR ALA THR
SEQRES 18 L 306 LEU ARG SER LEU ASN GLN ILE ILE THR TYR ASP ALA TYR
SEQRES 19 L 306 HIS MET ALA GLU VAL TYR LEU THR GLN PRO THR GLN ILE
SEQRES 20 L 306 VAL ALA GLY SER GLN ALA GLY SER LYS TRP MET SER ASP
SEQRES 21 L 306 ASP LEU TYR ASP ARG ALA SER SER GLN ASP LYS ARG TYR
SEQRES 22 L 306 HIS ILE VAL GLU GLY ALA ASN HIS MET ASP LEU TYR ASP
SEQRES 23 L 306 GLY LYS ALA TYR VAL ALA GLU ALA ILE SER VAL LEU ALA
SEQRES 24 L 306 PRO PHE PHE GLU GLU THR LEU
FORMUL 13 HOH *4102(H2 O)
HELIX 1 AA1 GLN A 49 LYS A 61 1 13
HELIX 2 AA2 ASN A 85 THR A 102 1 18
HELIX 3 AA3 ALA A 118 ASP A 130 1 13
HELIX 4 AA4 ASN A 143 GLY A 151 1 9
HELIX 5 AA5 LYS A 157 ASP A 160 5 4
HELIX 6 AA6 ALA A 161 GLY A 179 1 19
HELIX 7 AA7 LYS A 190 ALA A 194 5 5
HELIX 8 AA8 ASN A 196 THR A 208 1 13
HELIX 9 AA9 SER A 224 THR A 230 1 7
HELIX 10 AB1 MET A 236 LEU A 241 1 6
HELIX 11 AB2 SER A 255 ALA A 266 1 12
HELIX 12 AB3 MET A 282 GLY A 287 1 6
HELIX 13 AB4 GLY A 287 LEU A 306 1 20
HELIX 14 AB5 GLN B 49 LYS B 61 1 13
HELIX 15 AB6 ASN B 85 THR B 102 1 18
HELIX 16 AB7 ALA B 118 ASP B 130 1 13
HELIX 17 AB8 ASN B 143 GLY B 151 1 9
HELIX 18 AB9 LYS B 157 ASP B 160 5 4
HELIX 19 AC1 ALA B 161 GLY B 179 1 19
HELIX 20 AC2 LYS B 190 ALA B 194 5 5
HELIX 21 AC3 ASN B 196 THR B 208 1 13
HELIX 22 AC4 SER B 224 THR B 230 1 7
HELIX 23 AC5 MET B 236 LEU B 241 1 6
HELIX 24 AC6 SER B 255 ALA B 266 1 12
HELIX 25 AC7 MET B 282 GLY B 287 1 6
HELIX 26 AC8 GLY B 287 LEU B 306 1 20
HELIX 27 AC9 GLN C 49 LYS C 61 1 13
HELIX 28 AD1 ASN C 85 THR C 102 1 18
HELIX 29 AD2 CYS C 117 ASP C 130 1 14
HELIX 30 AD3 ASN C 143 GLY C 151 1 9
HELIX 31 AD4 LYS C 157 ASP C 160 5 4
HELIX 32 AD5 ALA C 161 GLY C 179 1 19
HELIX 33 AD6 LYS C 190 ALA C 194 5 5
HELIX 34 AD7 ASN C 196 THR C 208 1 13
HELIX 35 AD8 SER C 224 THR C 230 1 7
HELIX 36 AD9 MET C 236 LEU C 241 1 6
HELIX 37 AE1 SER C 255 ALA C 266 1 12
HELIX 38 AE2 MET C 282 GLY C 287 1 6
HELIX 39 AE3 GLY C 287 LEU C 306 1 20
HELIX 40 AE4 GLN D 49 LYS D 61 1 13
HELIX 41 AE5 ASN D 85 THR D 102 1 18
HELIX 42 AE6 ALA D 118 ASP D 130 1 13
HELIX 43 AE7 ASN D 143 GLY D 151 1 9
HELIX 44 AE8 LYS D 157 ASP D 160 5 4
HELIX 45 AE9 ALA D 161 GLY D 179 1 19
HELIX 46 AF1 LYS D 190 ALA D 194 5 5
HELIX 47 AF2 ASN D 196 THR D 208 1 13
HELIX 48 AF3 SER D 224 THR D 230 1 7
HELIX 49 AF4 MET D 236 LEU D 241 1 6
HELIX 50 AF5 SER D 255 ALA D 266 1 12
HELIX 51 AF6 MET D 282 GLY D 287 1 6
HELIX 52 AF7 GLY D 287 LEU D 306 1 20
HELIX 53 AF8 GLN E 49 LYS E 61 1 13
HELIX 54 AF9 ASN E 85 THR E 102 1 18
HELIX 55 AG1 ALA E 118 ASP E 130 1 13
HELIX 56 AG2 ASN E 143 GLY E 151 1 9
HELIX 57 AG3 LYS E 157 ASP E 160 5 4
HELIX 58 AG4 ALA E 161 GLY E 179 1 19
HELIX 59 AG5 LYS E 190 ALA E 194 5 5
HELIX 60 AG6 ASN E 196 THR E 208 1 13
HELIX 61 AG7 SER E 224 THR E 230 1 7
HELIX 62 AG8 MET E 236 LEU E 241 1 6
HELIX 63 AG9 SER E 255 ALA E 266 1 12
HELIX 64 AH1 MET E 282 GLY E 287 1 6
HELIX 65 AH2 GLY E 287 LEU E 306 1 20
HELIX 66 AH3 GLN F 49 LYS F 61 1 13
HELIX 67 AH4 ASN F 85 THR F 102 1 18
HELIX 68 AH5 ALA F 118 ASP F 130 1 13
HELIX 69 AH6 ASN F 143 ASN F 150 1 8
HELIX 70 AH7 LYS F 157 ASP F 160 5 4
HELIX 71 AH8 ALA F 161 GLY F 179 1 19
HELIX 72 AH9 LYS F 190 ALA F 194 5 5
HELIX 73 AI1 ASN F 196 THR F 208 1 13
HELIX 74 AI2 SER F 224 THR F 230 1 7
HELIX 75 AI3 MET F 236 LEU F 241 1 6
HELIX 76 AI4 SER F 255 ALA F 266 1 12
HELIX 77 AI5 MET F 282 GLY F 287 1 6
HELIX 78 AI6 GLY F 287 LEU F 306 1 20
HELIX 79 AI7 GLN G 49 GLU G 60 1 12
HELIX 80 AI8 ASN G 85 THR G 102 1 18
HELIX 81 AI9 ALA G 118 ASP G 130 1 13
HELIX 82 AJ1 ASN G 143 GLY G 151 1 9
HELIX 83 AJ2 LYS G 157 ASP G 160 5 4
HELIX 84 AJ3 ALA G 161 GLY G 179 1 19
HELIX 85 AJ4 LYS G 190 ALA G 194 5 5
HELIX 86 AJ5 ASN G 196 THR G 208 1 13
HELIX 87 AJ6 SER G 224 THR G 230 1 7
HELIX 88 AJ7 MET G 236 LEU G 241 1 6
HELIX 89 AJ8 SER G 255 ALA G 266 1 12
HELIX 90 AJ9 MET G 282 GLY G 287 1 6
HELIX 91 AK1 GLY G 287 LEU G 306 1 20
HELIX 92 AK2 GLN H 49 GLU H 60 1 12
HELIX 93 AK3 ASN H 85 THR H 102 1 18
HELIX 94 AK4 ALA H 118 ASP H 130 1 13
HELIX 95 AK5 ASN H 143 ASN H 150 1 8
HELIX 96 AK6 LYS H 157 ASP H 160 5 4
HELIX 97 AK7 ALA H 161 GLY H 179 1 19
HELIX 98 AK8 LYS H 190 ALA H 194 5 5
HELIX 99 AK9 ASN H 196 THR H 208 1 13
HELIX 100 AL1 SER H 224 THR H 230 1 7
HELIX 101 AL2 MET H 236 LEU H 241 1 6
HELIX 102 AL3 SER H 255 ALA H 266 1 12
HELIX 103 AL4 MET H 282 GLY H 287 1 6
HELIX 104 AL5 GLY H 287 LEU H 306 1 20
HELIX 105 AL6 GLN I 49 LYS I 61 1 13
HELIX 106 AL7 ASN I 85 THR I 102 1 18
HELIX 107 AL8 ALA I 118 ASP I 130 1 13
HELIX 108 AL9 ASN I 143 GLY I 151 1 9
HELIX 109 AM1 LYS I 157 ASP I 160 5 4
HELIX 110 AM2 ALA I 161 GLY I 179 1 19
HELIX 111 AM3 LYS I 190 ALA I 194 5 5
HELIX 112 AM4 ASN I 196 THR I 208 1 13
HELIX 113 AM5 SER I 224 THR I 230 1 7
HELIX 114 AM6 MET I 236 LEU I 241 1 6
HELIX 115 AM7 SER I 255 ALA I 266 1 12
HELIX 116 AM8 MET I 282 GLY I 287 1 6
HELIX 117 AM9 GLY I 287 LEU I 306 1 20
HELIX 118 AN1 GLN J 49 LYS J 61 1 13
HELIX 119 AN2 ASN J 85 THR J 102 1 18
HELIX 120 AN3 ALA J 118 ASP J 130 1 13
HELIX 121 AN4 ASN J 143 ASN J 150 1 8
HELIX 122 AN5 LYS J 157 ASP J 160 5 4
HELIX 123 AN6 ALA J 161 GLY J 179 1 19
HELIX 124 AN7 LYS J 190 ALA J 194 5 5
HELIX 125 AN8 ASN J 196 THR J 208 1 13
HELIX 126 AN9 SER J 224 THR J 230 1 7
HELIX 127 AO1 MET J 236 LEU J 241 1 6
HELIX 128 AO2 SER J 255 ALA J 266 1 12
HELIX 129 AO3 MET J 282 GLY J 287 1 6
HELIX 130 AO4 GLY J 287 LEU J 306 1 20
HELIX 131 AO5 GLN K 49 GLU K 60 1 12
HELIX 132 AO6 ASN K 85 THR K 102 1 18
HELIX 133 AO7 ALA K 118 ASP K 130 1 13
HELIX 134 AO8 ASN K 143 GLY K 151 1 9
HELIX 135 AO9 LYS K 157 ASP K 160 5 4
HELIX 136 AP1 ALA K 161 GLY K 179 1 19
HELIX 137 AP2 LYS K 190 ALA K 194 5 5
HELIX 138 AP3 ASN K 196 THR K 208 1 13
HELIX 139 AP4 SER K 224 THR K 230 1 7
HELIX 140 AP5 MET K 236 LEU K 241 1 6
HELIX 141 AP6 SER K 255 ALA K 266 1 12
HELIX 142 AP7 MET K 282 GLY K 287 1 6
HELIX 143 AP8 GLY K 287 LEU K 306 1 20
HELIX 144 AP9 GLN L 49 GLU L 60 1 12
HELIX 145 AQ1 ASN L 85 THR L 102 1 18
HELIX 146 AQ2 ALA L 118 ASP L 130 1 13
HELIX 147 AQ3 ASN L 143 GLY L 151 1 9
HELIX 148 AQ4 LYS L 157 ASP L 160 5 4
HELIX 149 AQ5 ALA L 161 GLY L 179 1 19
HELIX 150 AQ6 LYS L 190 ALA L 194 5 5
HELIX 151 AQ7 ASN L 196 THR L 208 1 13
HELIX 152 AQ8 SER L 224 THR L 230 1 7
HELIX 153 AQ9 MET L 236 LEU L 241 1 6
HELIX 154 AR1 SER L 255 ALA L 266 1 12
HELIX 155 AR2 MET L 282 GLY L 287 1 6
HELIX 156 AR3 GLY L 287 LEU L 306 1 20
SHEET 1 AA116 LYS A 271 VAL A 276 0
SHEET 2 AA116 THR A 245 GLY A 250 1 N ILE A 247 O HIS A 274
SHEET 3 AA116 ILE A 136 VAL A 139 1 N ILE A 136 O GLN A 246
SHEET 4 AA116 VAL A 106 ILE A 116 1 N GLY A 115 O VAL A 139
SHEET 5 AA116 TYR A 34 SER A 40 1 N ALA A 36 O GLY A 112
SHEET 6 AA116 VAL A 64 TYR A 68 1 O ILE A 66 N LEU A 39
SHEET 7 AA116 SER A 17 TYR A 23 -1 N VAL A 21 O ALA A 67
SHEET 8 AA116 ASN A 3 THR A 9 -1 N VAL A 6 O ALA A 20
SHEET 9 AA116 ASN C 3 THR C 9 -1 O ASN C 3 N LYS A 5
SHEET 10 AA116 SER C 17 TYR C 23 -1 O LEU C 18 N PHE C 8
SHEET 11 AA116 VAL C 64 TYR C 68 -1 O ALA C 67 N VAL C 21
SHEET 12 AA116 TYR C 34 SER C 40 1 N LEU C 39 O ILE C 66
SHEET 13 AA116 VAL C 106 ILE C 116 1 O GLY C 112 N ALA C 36
SHEET 14 AA116 ILE C 133 VAL C 139 1 O LYS C 134 N ILE C 111
SHEET 15 AA116 THR C 245 GLY C 250 1 O GLN C 246 N ILE C 136
SHEET 16 AA116 LYS C 271 VAL C 276 1 O ARG C 272 N THR C 245
SHEET 1 AA2 2 ILE A 183 PRO A 185 0
SHEET 2 AA2 2 TYR A 219 THR A 221 -1 O ALA A 220 N MET A 184
SHEET 1 AA3 8 ASN B 3 THR B 9 0
SHEET 2 AA3 8 SER B 17 TYR B 23 -1 O ILE B 22 N ASN B 4
SHEET 3 AA3 8 VAL B 64 TYR B 68 -1 O THR B 65 N TYR B 23
SHEET 4 AA3 8 TYR B 34 SER B 40 1 N LEU B 39 O ILE B 66
SHEET 5 AA3 8 VAL B 106 ILE B 116 1 O GLY B 112 N ALA B 36
SHEET 6 AA3 8 ILE B 136 VAL B 139 1 O VAL B 139 N GLY B 115
SHEET 7 AA3 8 THR B 245 GLY B 250 1 O GLN B 246 N ILE B 136
SHEET 8 AA3 8 LYS B 271 VAL B 276 1 O HIS B 274 N ILE B 247
SHEET 1 AA4 2 ILE B 183 PRO B 185 0
SHEET 2 AA4 2 TYR B 219 THR B 221 -1 O ALA B 220 N MET B 184
SHEET 1 AA5 2 ILE C 183 PRO C 185 0
SHEET 2 AA5 2 TYR C 219 THR C 221 -1 O ALA C 220 N MET C 184
SHEET 1 AA6 8 ASN D 3 THR D 9 0
SHEET 2 AA6 8 SER D 17 TYR D 23 -1 O LEU D 18 N PHE D 8
SHEET 3 AA6 8 VAL D 64 TYR D 68 -1 O THR D 65 N TYR D 23
SHEET 4 AA6 8 TYR D 34 SER D 40 1 N LEU D 39 O ILE D 66
SHEET 5 AA6 8 VAL D 106 ILE D 116 1 O MET D 114 N VAL D 38
SHEET 6 AA6 8 ILE D 136 VAL D 139 1 O VAL D 139 N GLY D 115
SHEET 7 AA6 8 THR D 245 GLY D 250 1 O GLN D 246 N ILE D 136
SHEET 8 AA6 8 LYS D 271 VAL D 276 1 O HIS D 274 N ILE D 247
SHEET 1 AA7 2 ILE D 183 PRO D 185 0
SHEET 2 AA7 2 TYR D 219 THR D 221 -1 O ALA D 220 N MET D 184
SHEET 1 AA816 LYS E 271 VAL E 276 0
SHEET 2 AA816 THR E 245 GLY E 250 1 N ILE E 247 O ARG E 272
SHEET 3 AA816 ILE E 136 VAL E 139 1 N ILE E 136 O GLN E 246
SHEET 4 AA816 VAL E 106 ILE E 116 1 N GLY E 115 O VAL E 139
SHEET 5 AA816 TYR E 34 SER E 40 1 N ALA E 36 O GLY E 112
SHEET 6 AA816 VAL E 64 TYR E 68 1 O ILE E 66 N LEU E 39
SHEET 7 AA816 SER E 17 TYR E 23 -1 N VAL E 21 O ALA E 67
SHEET 8 AA816 MET E 2 THR E 9 -1 N ASN E 4 O ILE E 22
SHEET 9 AA816 ASN J 3 THR J 9 -1 O ASN J 3 N ASN E 3
SHEET 10 AA816 SER J 17 TYR J 23 -1 O LEU J 18 N PHE J 8
SHEET 11 AA816 VAL J 64 TYR J 68 -1 O ALA J 67 N VAL J 21
SHEET 12 AA816 TYR J 34 SER J 40 1 N LEU J 39 O ILE J 66
SHEET 13 AA816 VAL J 106 ILE J 116 1 O GLY J 112 N ALA J 36
SHEET 14 AA816 ILE J 136 VAL J 139 1 O VAL J 139 N GLY J 115
SHEET 15 AA816 THR J 245 GLY J 250 1 O GLN J 246 N ILE J 136
SHEET 16 AA816 LYS J 271 VAL J 276 1 O HIS J 274 N ILE J 247
SHEET 1 AA9 2 ILE E 183 PRO E 185 0
SHEET 2 AA9 2 TYR E 219 THR E 221 -1 O ALA E 220 N MET E 184
SHEET 1 AB1 8 ASN F 3 THR F 9 0
SHEET 2 AB1 8 SER F 17 TYR F 23 -1 O ALA F 20 N VAL F 6
SHEET 3 AB1 8 VAL F 64 TYR F 68 -1 O ALA F 67 N VAL F 21
SHEET 4 AB1 8 TYR F 34 SER F 40 1 N LEU F 39 O ILE F 66
SHEET 5 AB1 8 VAL F 106 ILE F 116 1 O GLY F 112 N ALA F 36
SHEET 6 AB1 8 ILE F 136 VAL F 139 1 O VAL F 139 N GLY F 115
SHEET 7 AB1 8 THR F 245 GLY F 250 1 O GLN F 246 N ILE F 136
SHEET 8 AB1 8 LYS F 271 VAL F 276 1 O HIS F 274 N ILE F 247
SHEET 1 AB2 2 ILE F 183 PRO F 185 0
SHEET 2 AB2 2 TYR F 219 THR F 221 -1 O ALA F 220 N MET F 184
SHEET 1 AB3 8 ASN G 3 THR G 9 0
SHEET 2 AB3 8 SER G 17 TYR G 23 -1 O LEU G 18 N PHE G 8
SHEET 3 AB3 8 VAL G 64 TYR G 68 -1 O ALA G 67 N VAL G 21
SHEET 4 AB3 8 TYR G 34 SER G 40 1 N LEU G 39 O ILE G 66
SHEET 5 AB3 8 VAL G 106 ILE G 116 1 O GLY G 112 N ALA G 36
SHEET 6 AB3 8 ILE G 136 VAL G 139 1 O VAL G 139 N GLY G 115
SHEET 7 AB3 8 THR G 245 GLY G 250 1 O GLN G 246 N ILE G 136
SHEET 8 AB3 8 LYS G 271 VAL G 276 1 O HIS G 274 N ILE G 247
SHEET 1 AB4 2 ILE G 183 PRO G 185 0
SHEET 2 AB4 2 TYR G 219 THR G 221 -1 O ALA G 220 N MET G 184
SHEET 1 AB5 8 ASN H 3 THR H 9 0
SHEET 2 AB5 8 SER H 17 TYR H 23 -1 O LEU H 18 N PHE H 8
SHEET 3 AB5 8 VAL H 64 TYR H 68 -1 O THR H 65 N TYR H 23
SHEET 4 AB5 8 TYR H 34 SER H 40 1 N LEU H 39 O ILE H 66
SHEET 5 AB5 8 VAL H 106 ILE H 116 1 O MET H 114 N VAL H 38
SHEET 6 AB5 8 ILE H 136 VAL H 139 1 O VAL H 139 N GLY H 115
SHEET 7 AB5 8 THR H 245 GLY H 250 1 O GLN H 246 N ILE H 136
SHEET 8 AB5 8 LYS H 271 VAL H 276 1 O ARG H 272 N THR H 245
SHEET 1 AB6 2 ILE H 183 PRO H 185 0
SHEET 2 AB6 2 TYR H 219 THR H 221 -1 O ALA H 220 N MET H 184
SHEET 1 AB7 8 ASN I 3 THR I 9 0
SHEET 2 AB7 8 SER I 17 TYR I 23 -1 O ALA I 20 N VAL I 6
SHEET 3 AB7 8 VAL I 64 TYR I 68 -1 O ALA I 67 N VAL I 21
SHEET 4 AB7 8 TYR I 34 SER I 40 1 N LEU I 39 O ILE I 66
SHEET 5 AB7 8 VAL I 106 ILE I 116 1 O GLY I 112 N ALA I 36
SHEET 6 AB7 8 ILE I 136 VAL I 139 1 O VAL I 139 N GLY I 115
SHEET 7 AB7 8 THR I 245 GLY I 250 1 O GLN I 246 N ILE I 136
SHEET 8 AB7 8 LYS I 271 VAL I 276 1 O ARG I 272 N THR I 245
SHEET 1 AB8 2 ILE I 183 PRO I 185 0
SHEET 2 AB8 2 TYR I 219 THR I 221 -1 O ALA I 220 N MET I 184
SHEET 1 AB9 2 ILE J 183 PRO J 185 0
SHEET 2 AB9 2 TYR J 219 THR J 221 -1 O ALA J 220 N MET J 184
SHEET 1 AC1 8 ASN K 3 THR K 9 0
SHEET 2 AC1 8 SER K 17 TYR K 23 -1 O ALA K 20 N VAL K 6
SHEET 3 AC1 8 VAL K 64 TYR K 68 -1 O ALA K 67 N VAL K 21
SHEET 4 AC1 8 TYR K 34 SER K 40 1 N LEU K 39 O ILE K 66
SHEET 5 AC1 8 VAL K 106 ILE K 116 1 O GLY K 112 N ALA K 36
SHEET 6 AC1 8 ILE K 136 VAL K 139 1 O VAL K 139 N GLY K 115
SHEET 7 AC1 8 THR K 245 GLY K 250 1 O GLN K 246 N ILE K 136
SHEET 8 AC1 8 LYS K 271 VAL K 276 1 O ARG K 272 N THR K 245
SHEET 1 AC2 2 ILE K 183 PRO K 185 0
SHEET 2 AC2 2 TYR K 219 THR K 221 -1 O ALA K 220 N MET K 184
SHEET 1 AC3 8 ASN L 3 THR L 9 0
SHEET 2 AC3 8 SER L 17 TYR L 23 -1 O LEU L 18 N PHE L 8
SHEET 3 AC3 8 VAL L 64 TYR L 68 -1 O ALA L 67 N VAL L 21
SHEET 4 AC3 8 TYR L 34 SER L 40 1 N LEU L 39 O ILE L 66
SHEET 5 AC3 8 VAL L 106 CYS L 117 1 O MET L 114 N VAL L 38
SHEET 6 AC3 8 ILE L 136 ALA L 141 1 O VAL L 139 N GLY L 115
SHEET 7 AC3 8 THR L 245 GLY L 250 1 O GLN L 246 N ILE L 136
SHEET 8 AC3 8 LYS L 271 VAL L 276 1 O HIS L 274 N ILE L 247
SHEET 1 AC4 2 ILE L 183 PRO L 185 0
SHEET 2 AC4 2 TYR L 219 THR L 221 -1 O ALA L 220 N MET L 184
CISPEP 1 GLU A 79 PRO A 80 0 6.28
CISPEP 2 GLU B 79 PRO B 80 0 2.34
CISPEP 3 GLU C 79 PRO C 80 0 1.51
CISPEP 4 GLU D 79 PRO D 80 0 4.20
CISPEP 5 GLU E 79 PRO E 80 0 5.82
CISPEP 6 GLU F 79 PRO F 80 0 2.51
CISPEP 7 GLU G 79 PRO G 80 0 0.33
CISPEP 8 GLU H 79 PRO H 80 0 5.19
CISPEP 9 GLU I 79 PRO I 80 0 3.95
CISPEP 10 GLU J 79 PRO J 80 0 6.78
CISPEP 11 GLU K 79 PRO K 80 0 6.72
CISPEP 12 GLU L 79 PRO L 80 0 5.05
CRYST1 77.584 216.405 258.839 90.00 90.00 90.00 P 21 21 21 48
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 0.012889 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004621 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003863 0.00000
TER 2372 LEU A 306
TER 4753 LEU B 306
TER 7125 LEU C 306
TER 9506 LEU D 306
TER 11884 LEU E 306
TER 14265 LEU F 306
TER 16646 LEU G 306
TER 19027 LEU H 306
TER 21408 LEU I 306
TER 23781 LEU J 306
TER 26162 LEU K 306
TER 28534 LEU L 306
MASTER 491 0 0 156 120 0 0 632546 12 0 288
END |