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HEADER HYDROLASE 10-MAR-23 8OE2
TITLE STRUCTURE OF HYPERSTABLE HALOALKANE DEHALOGENASE VARIANT DHAA223
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 3 ORGANISM_TAXID: 32630;
SOURCE 4 GENE: DHAA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ENGINEERED HALOALKANE DEHALOGENASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MAREK
REVDAT 1 17-JAN-24 8OE2 0
JRNL AUTH A.KUNKA,S.M.MARQUES,M.HAVLASEK,M.VASINA,N.VELATOVA,
JRNL AUTH 2 L.CENGELOVA,D.KOVAR,J.DAMBORSKY,M.MAREK,D.BEDNAR,Z.PROKOP
JRNL TITL ADVANCING ENZYME'S STABILITY AND CATALYTIC EFFICIENCY
JRNL TITL 2 THROUGH SYNERGY OF FORCE-FIELD CALCULATIONS, EVOLUTIONARY
JRNL TITL 3 ANALYSIS, AND MACHINE LEARNING.
JRNL REF ACS CATALYSIS V. 13 12506 2023
JRNL REFN ESSN 2155-5435
JRNL PMID 37822856
JRNL DOI 10.1021/ACSCATAL.3C02575
REMARK 2
REMARK 2 RESOLUTION. 1.51 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1-4487
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) : 1.51
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 295797
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 14654
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 47.7200 - 4.6781 0.96 9293 516 0.1686 0.1858
REMARK 3 2 4.6781 - 3.7136 0.98 9380 490 0.1377 0.1519
REMARK 3 3 3.7136 - 3.2443 0.98 9398 450 0.1494 0.1707
REMARK 3 4 3.2443 - 2.9477 0.99 9486 503 0.1576 0.1733
REMARK 3 5 2.9477 - 2.7364 0.99 9425 479 0.1555 0.1940
REMARK 3 6 2.7364 - 2.5751 0.96 9222 489 0.1587 0.1756
REMARK 3 7 2.5751 - 2.4462 0.98 9309 493 0.1553 0.1889
REMARK 3 8 2.4462 - 2.3397 0.98 9391 516 0.1573 0.1886
REMARK 3 9 2.3397 - 2.2496 0.98 9342 502 0.1544 0.1806
REMARK 3 10 2.2496 - 2.1720 0.98 9406 447 0.1540 0.1824
REMARK 3 11 2.1720 - 2.1041 0.99 9459 493 0.1519 0.1781
REMARK 3 12 2.1041 - 2.0439 0.99 9408 518 0.1541 0.1915
REMARK 3 13 2.0439 - 1.9901 0.99 9542 505 0.1522 0.1897
REMARK 3 14 1.9901 - 1.9416 0.99 9467 462 0.1546 0.1809
REMARK 3 15 1.9416 - 1.8974 0.98 9366 489 0.1722 0.1971
REMARK 3 16 1.8974 - 1.8570 0.97 9232 460 0.1686 0.2042
REMARK 3 17 1.8570 - 1.8199 0.96 9202 488 0.1766 0.2140
REMARK 3 18 1.8199 - 1.7855 0.98 9334 471 0.1784 0.2180
REMARK 3 19 1.7855 - 1.7537 0.99 9510 430 0.1875 0.2374
REMARK 3 20 1.7537 - 1.7239 0.99 9327 506 0.1920 0.2254
REMARK 3 21 1.7239 - 1.6961 0.99 9464 525 0.2006 0.2364
REMARK 3 22 1.6961 - 1.6700 0.99 9455 444 0.2036 0.2272
REMARK 3 23 1.6700 - 1.6455 0.99 9445 468 0.2109 0.2293
REMARK 3 24 1.6455 - 1.6223 0.99 9368 564 0.2182 0.2617
REMARK 3 25 1.6223 - 1.6004 0.99 9452 500 0.2216 0.2520
REMARK 3 26 1.6004 - 1.5796 0.99 9449 501 0.2363 0.2678
REMARK 3 27 1.5796 - 1.5598 0.99 9350 515 0.2474 0.2881
REMARK 3 28 1.5598 - 1.5410 0.98 9429 482 0.2691 0.2910
REMARK 3 29 1.5410 - 1.5231 0.97 9197 465 0.2902 0.3107
REMARK 3 30 1.5231 - 1.5100 0.95 9035 483 0.3143 0.3354
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.440
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 : 0.017 15185
REMARK 3 ANGLE : 1.427 20766
REMARK 3 CHIRALITY : 0.093 2130
REMARK 3 PLANARITY : 0.012 2700
REMARK 3 DIHEDRAL : 7.303 12351
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 21.1346 23.7350 -20.4705
REMARK 3 T TENSOR
REMARK 3 T11: 0.0916 T22: 0.0946
REMARK 3 T33: 0.1086 T12: 0.0008
REMARK 3 T13: 0.0031 T23: -0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 0.0191 L22: 0.0196
REMARK 3 L33: 0.0202 L12: 0.0037
REMARK 3 L13: 0.0002 L23: -0.0062
REMARK 3 S TENSOR
REMARK 3 S11: -0.0041 S12: -0.0068 S13: 0.0026
REMARK 3 S21: 0.0011 S22: 0.0015 S23: 0.0027
REMARK 3 S31: 0.0018 S32: 0.0023 S33: -0.0000
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 8OE2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-MAR-23.
REMARK 100 THE DEPOSITION ID IS D_1292129110.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-OCT-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.999
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 296214
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.510
REMARK 200 RESOLUTION RANGE LOW (A) : 47.720
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.51
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
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 : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, BIS-TRIS, PEG 3350,
REMARK 280 PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
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 71.57200
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, 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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 SER A 2
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 MET B 1
REMARK 465 ALA B 292
REMARK 465 LEU B 293
REMARK 465 HIS B 294
REMARK 465 HIS B 295
REMARK 465 HIS B 296
REMARK 465 HIS B 297
REMARK 465 HIS B 298
REMARK 465 HIS B 299
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 HIS C 295
REMARK 465 HIS C 296
REMARK 465 HIS C 297
REMARK 465 HIS C 298
REMARK 465 HIS C 299
REMARK 465 MET D 1
REMARK 465 HIS D 295
REMARK 465 HIS D 296
REMARK 465 HIS D 297
REMARK 465 HIS D 298
REMARK 465 HIS D 299
REMARK 465 MET E 1
REMARK 465 SER E 2
REMARK 465 ALA E 292
REMARK 465 LEU E 293
REMARK 465 HIS E 294
REMARK 465 HIS E 295
REMARK 465 HIS E 296
REMARK 465 HIS E 297
REMARK 465 HIS E 298
REMARK 465 HIS E 299
REMARK 465 MET F 1
REMARK 465 SER F 2
REMARK 465 HIS F 294
REMARK 465 HIS F 295
REMARK 465 HIS F 296
REMARK 465 HIS F 297
REMARK 465 HIS F 298
REMARK 465 HIS F 299
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 SER D 232 C PRO D 233 N 0.123
REMARK 500 TYR F 165 CE2 TYR F 165 CD2 0.124
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 ASP A 217 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP B 217 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG F 30 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG F 199 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP F 217 CB - CG - OD1 ANGL. DEV. = 5.8 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 ASP A 31 -163.04 -126.48
REMARK 500 PRO A 42 45.04 -107.25
REMARK 500 THR A 43 -156.51 -101.70
REMARK 500 SER A 44 -169.40 -164.26
REMARK 500 GLU A 98 -83.92 -103.11
REMARK 500 ASP A 106 -134.49 52.78
REMARK 500 ASP A 156 -53.17 71.01
REMARK 500 VAL A 245 -68.51 -134.47
REMARK 500 LEU A 271 -91.58 -116.06
REMARK 500 ASP B 31 -164.96 -126.45
REMARK 500 PRO B 42 47.78 -104.46
REMARK 500 THR B 43 -158.34 -105.05
REMARK 500 SER B 44 -168.43 -161.97
REMARK 500 GLU B 98 -93.16 -107.58
REMARK 500 ASP B 106 -133.62 53.27
REMARK 500 ASP B 156 -52.64 68.79
REMARK 500 VAL B 245 -65.51 -134.37
REMARK 500 LEU B 271 -95.36 -117.39
REMARK 500 ASP C 31 -160.49 -122.27
REMARK 500 PRO C 42 45.00 -107.13
REMARK 500 THR C 43 -158.45 -102.05
REMARK 500 SER C 44 -164.13 -162.26
REMARK 500 GLU C 98 -86.43 -107.80
REMARK 500 ASP C 106 -135.55 53.12
REMARK 500 ASP C 156 -52.24 67.79
REMARK 500 VAL C 245 -68.36 -132.64
REMARK 500 LEU C 271 -94.33 -115.50
REMARK 500 ASP D 31 -164.84 -127.71
REMARK 500 PRO D 42 46.50 -107.13
REMARK 500 THR D 43 -154.32 -103.66
REMARK 500 GLU D 98 -87.51 -104.99
REMARK 500 ASP D 106 -134.04 53.93
REMARK 500 ASP D 156 -53.39 69.40
REMARK 500 VAL D 245 -70.11 -133.48
REMARK 500 LEU D 271 -94.51 -116.17
REMARK 500 LEU D 293 9.16 -68.49
REMARK 500 ASP E 31 -162.91 -127.07
REMARK 500 PRO E 42 44.79 -103.41
REMARK 500 THR E 43 -152.28 -104.00
REMARK 500 GLU E 98 -89.14 -104.94
REMARK 500 ASP E 106 -134.57 51.16
REMARK 500 ASP E 156 -54.98 71.15
REMARK 500 ILE E 171 -61.49 -104.75
REMARK 500 VAL E 245 -67.11 -129.57
REMARK 500 LEU E 271 -98.97 -113.96
REMARK 500 PRO F 42 44.60 -101.97
REMARK 500 THR F 43 -155.38 -105.41
REMARK 500 GLU F 98 -92.86 -112.44
REMARK 500 ASP F 106 -133.70 53.24
REMARK 500 ASP F 156 -54.34 71.52
REMARK 500
REMARK 500 THIS ENTRY HAS 52 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 760 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A 761 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH A 762 DISTANCE = 6.36 ANGSTROMS
REMARK 525 HOH A 763 DISTANCE = 6.53 ANGSTROMS
REMARK 525 HOH A 764 DISTANCE = 6.54 ANGSTROMS
REMARK 525 HOH A 765 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH A 766 DISTANCE = 6.93 ANGSTROMS
REMARK 525 HOH B 712 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH B 713 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH B 714 DISTANCE = 7.11 ANGSTROMS
REMARK 525 HOH B 715 DISTANCE = 8.76 ANGSTROMS
REMARK 525 HOH C 711 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH C 712 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH C 713 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH C 714 DISTANCE = 6.23 ANGSTROMS
REMARK 525 HOH C 715 DISTANCE = 6.54 ANGSTROMS
REMARK 525 HOH D 680 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH D 681 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH D 682 DISTANCE = 6.53 ANGSTROMS
REMARK 525 HOH D 683 DISTANCE = 6.86 ANGSTROMS
REMARK 525 HOH E 708 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH F 666 DISTANCE = 6.34 ANGSTROMS
DBREF 8OE2 A 1 293 UNP P0A3G4 DHAA_PSEPV 1 293
DBREF 8OE2 B 1 293 UNP P0A3G4 DHAA_PSEPV 1 293
DBREF 8OE2 C 1 293 UNP P0A3G4 DHAA_PSEPV 1 293
DBREF 8OE2 D 1 293 UNP P0A3G4 DHAA_PSEPV 1 293
DBREF 8OE2 E 1 293 UNP P0A3G4 DHAA_PSEPV 1 293
DBREF 8OE2 F 1 293 UNP P0A3G4 DHAA_PSEPV 1 293
SEQADV 8OE2 SER A 20 UNP P0A3G4 GLU 20 CONFLICT
SEQADV 8OE2 ARG A 80 UNP P0A3G4 PHE 80 CONFLICT
SEQADV 8OE2 PHE A 128 UNP P0A3G4 CYS 128 CONFLICT
SEQADV 8OE2 LEU A 148 UNP P0A3G4 THR 148 CONFLICT
SEQADV 8OE2 PRO A 155 UNP P0A3G4 ALA 155 CONFLICT
SEQADV 8OE2 TYR A 165 UNP P0A3G4 GLN 165 CONFLICT
SEQADV 8OE2 ILE A 171 UNP P0A3G4 GLY 171 CONFLICT
SEQADV 8OE2 ILE A 172 UNP P0A3G4 ALA 172 CONFLICT
SEQADV 8OE2 PHE A 176 UNP P0A3G4 CYS 176 CONFLICT
SEQADV 8OE2 GLU A 184 UNP P0A3G4 VAL 184 CONFLICT
SEQADV 8OE2 GLU A 197 UNP P0A3G4 VAL 197 CONFLICT
SEQADV 8OE2 TRP A 198 UNP P0A3G4 ASP 198 CONFLICT
SEQADV 8OE2 ASN A 212 UNP P0A3G4 ALA 212 CONFLICT
SEQADV 8OE2 ASP A 217 UNP P0A3G4 ASN 217 CONFLICT
SEQADV 8OE2 TRP A 219 UNP P0A3G4 VAL 219 CONFLICT
SEQADV 8OE2 LEU A 262 UNP P0A3G4 CYS 262 CONFLICT
SEQADV 8OE2 PHE A 266 UNP P0A3G4 ASP 266 CONFLICT
SEQADV 8OE2 HIS A 294 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS A 295 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS A 296 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS A 297 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS A 298 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS A 299 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 SER B 20 UNP P0A3G4 GLU 20 CONFLICT
SEQADV 8OE2 ARG B 80 UNP P0A3G4 PHE 80 CONFLICT
SEQADV 8OE2 PHE B 128 UNP P0A3G4 CYS 128 CONFLICT
SEQADV 8OE2 LEU B 148 UNP P0A3G4 THR 148 CONFLICT
SEQADV 8OE2 PRO B 155 UNP P0A3G4 ALA 155 CONFLICT
SEQADV 8OE2 TYR B 165 UNP P0A3G4 GLN 165 CONFLICT
SEQADV 8OE2 ILE B 171 UNP P0A3G4 GLY 171 CONFLICT
SEQADV 8OE2 ILE B 172 UNP P0A3G4 ALA 172 CONFLICT
SEQADV 8OE2 PHE B 176 UNP P0A3G4 CYS 176 CONFLICT
SEQADV 8OE2 GLU B 184 UNP P0A3G4 VAL 184 CONFLICT
SEQADV 8OE2 GLU B 197 UNP P0A3G4 VAL 197 CONFLICT
SEQADV 8OE2 TRP B 198 UNP P0A3G4 ASP 198 CONFLICT
SEQADV 8OE2 ASN B 212 UNP P0A3G4 ALA 212 CONFLICT
SEQADV 8OE2 ASP B 217 UNP P0A3G4 ASN 217 CONFLICT
SEQADV 8OE2 TRP B 219 UNP P0A3G4 VAL 219 CONFLICT
SEQADV 8OE2 LEU B 262 UNP P0A3G4 CYS 262 CONFLICT
SEQADV 8OE2 PHE B 266 UNP P0A3G4 ASP 266 CONFLICT
SEQADV 8OE2 HIS B 294 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS B 295 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS B 296 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS B 297 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS B 298 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS B 299 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 SER C 20 UNP P0A3G4 GLU 20 CONFLICT
SEQADV 8OE2 ARG C 80 UNP P0A3G4 PHE 80 CONFLICT
SEQADV 8OE2 PHE C 128 UNP P0A3G4 CYS 128 CONFLICT
SEQADV 8OE2 LEU C 148 UNP P0A3G4 THR 148 CONFLICT
SEQADV 8OE2 PRO C 155 UNP P0A3G4 ALA 155 CONFLICT
SEQADV 8OE2 TYR C 165 UNP P0A3G4 GLN 165 CONFLICT
SEQADV 8OE2 ILE C 171 UNP P0A3G4 GLY 171 CONFLICT
SEQADV 8OE2 ILE C 172 UNP P0A3G4 ALA 172 CONFLICT
SEQADV 8OE2 PHE C 176 UNP P0A3G4 CYS 176 CONFLICT
SEQADV 8OE2 GLU C 184 UNP P0A3G4 VAL 184 CONFLICT
SEQADV 8OE2 GLU C 197 UNP P0A3G4 VAL 197 CONFLICT
SEQADV 8OE2 TRP C 198 UNP P0A3G4 ASP 198 CONFLICT
SEQADV 8OE2 ASN C 212 UNP P0A3G4 ALA 212 CONFLICT
SEQADV 8OE2 ASP C 217 UNP P0A3G4 ASN 217 CONFLICT
SEQADV 8OE2 TRP C 219 UNP P0A3G4 VAL 219 CONFLICT
SEQADV 8OE2 LEU C 262 UNP P0A3G4 CYS 262 CONFLICT
SEQADV 8OE2 PHE C 266 UNP P0A3G4 ASP 266 CONFLICT
SEQADV 8OE2 HIS C 294 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS C 295 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS C 296 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS C 297 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS C 298 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS C 299 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 SER D 20 UNP P0A3G4 GLU 20 CONFLICT
SEQADV 8OE2 ARG D 80 UNP P0A3G4 PHE 80 CONFLICT
SEQADV 8OE2 PHE D 128 UNP P0A3G4 CYS 128 CONFLICT
SEQADV 8OE2 LEU D 148 UNP P0A3G4 THR 148 CONFLICT
SEQADV 8OE2 PRO D 155 UNP P0A3G4 ALA 155 CONFLICT
SEQADV 8OE2 TYR D 165 UNP P0A3G4 GLN 165 CONFLICT
SEQADV 8OE2 ILE D 171 UNP P0A3G4 GLY 171 CONFLICT
SEQADV 8OE2 ILE D 172 UNP P0A3G4 ALA 172 CONFLICT
SEQADV 8OE2 PHE D 176 UNP P0A3G4 CYS 176 CONFLICT
SEQADV 8OE2 GLU D 184 UNP P0A3G4 VAL 184 CONFLICT
SEQADV 8OE2 GLU D 197 UNP P0A3G4 VAL 197 CONFLICT
SEQADV 8OE2 TRP D 198 UNP P0A3G4 ASP 198 CONFLICT
SEQADV 8OE2 ASN D 212 UNP P0A3G4 ALA 212 CONFLICT
SEQADV 8OE2 ASP D 217 UNP P0A3G4 ASN 217 CONFLICT
SEQADV 8OE2 TRP D 219 UNP P0A3G4 VAL 219 CONFLICT
SEQADV 8OE2 LEU D 262 UNP P0A3G4 CYS 262 CONFLICT
SEQADV 8OE2 PHE D 266 UNP P0A3G4 ASP 266 CONFLICT
SEQADV 8OE2 HIS D 294 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS D 295 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS D 296 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS D 297 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS D 298 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS D 299 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 SER E 20 UNP P0A3G4 GLU 20 CONFLICT
SEQADV 8OE2 ARG E 80 UNP P0A3G4 PHE 80 CONFLICT
SEQADV 8OE2 PHE E 128 UNP P0A3G4 CYS 128 CONFLICT
SEQADV 8OE2 LEU E 148 UNP P0A3G4 THR 148 CONFLICT
SEQADV 8OE2 PRO E 155 UNP P0A3G4 ALA 155 CONFLICT
SEQADV 8OE2 TYR E 165 UNP P0A3G4 GLN 165 CONFLICT
SEQADV 8OE2 ILE E 171 UNP P0A3G4 GLY 171 CONFLICT
SEQADV 8OE2 ILE E 172 UNP P0A3G4 ALA 172 CONFLICT
SEQADV 8OE2 PHE E 176 UNP P0A3G4 CYS 176 CONFLICT
SEQADV 8OE2 GLU E 184 UNP P0A3G4 VAL 184 CONFLICT
SEQADV 8OE2 GLU E 197 UNP P0A3G4 VAL 197 CONFLICT
SEQADV 8OE2 TRP E 198 UNP P0A3G4 ASP 198 CONFLICT
SEQADV 8OE2 ASN E 212 UNP P0A3G4 ALA 212 CONFLICT
SEQADV 8OE2 ASP E 217 UNP P0A3G4 ASN 217 CONFLICT
SEQADV 8OE2 TRP E 219 UNP P0A3G4 VAL 219 CONFLICT
SEQADV 8OE2 LEU E 262 UNP P0A3G4 CYS 262 CONFLICT
SEQADV 8OE2 PHE E 266 UNP P0A3G4 ASP 266 CONFLICT
SEQADV 8OE2 HIS E 294 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS E 295 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS E 296 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS E 297 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS E 298 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS E 299 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 SER F 20 UNP P0A3G4 GLU 20 CONFLICT
SEQADV 8OE2 ARG F 80 UNP P0A3G4 PHE 80 CONFLICT
SEQADV 8OE2 PHE F 128 UNP P0A3G4 CYS 128 CONFLICT
SEQADV 8OE2 LEU F 148 UNP P0A3G4 THR 148 CONFLICT
SEQADV 8OE2 PRO F 155 UNP P0A3G4 ALA 155 CONFLICT
SEQADV 8OE2 TYR F 165 UNP P0A3G4 GLN 165 CONFLICT
SEQADV 8OE2 ILE F 171 UNP P0A3G4 GLY 171 CONFLICT
SEQADV 8OE2 ILE F 172 UNP P0A3G4 ALA 172 CONFLICT
SEQADV 8OE2 PHE F 176 UNP P0A3G4 CYS 176 CONFLICT
SEQADV 8OE2 GLU F 184 UNP P0A3G4 VAL 184 CONFLICT
SEQADV 8OE2 GLU F 197 UNP P0A3G4 VAL 197 CONFLICT
SEQADV 8OE2 TRP F 198 UNP P0A3G4 ASP 198 CONFLICT
SEQADV 8OE2 ASN F 212 UNP P0A3G4 ALA 212 CONFLICT
SEQADV 8OE2 ASP F 217 UNP P0A3G4 ASN 217 CONFLICT
SEQADV 8OE2 TRP F 219 UNP P0A3G4 VAL 219 CONFLICT
SEQADV 8OE2 LEU F 262 UNP P0A3G4 CYS 262 CONFLICT
SEQADV 8OE2 PHE F 266 UNP P0A3G4 ASP 266 CONFLICT
SEQADV 8OE2 HIS F 294 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS F 295 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS F 296 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS F 297 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS F 298 UNP P0A3G4 EXPRESSION TAG
SEQADV 8OE2 HIS F 299 UNP P0A3G4 EXPRESSION TAG
SEQRES 1 A 299 MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 A 299 TYR VAL GLU VAL LEU GLY SER ARG MET HIS TYR VAL ASP
SEQRES 3 A 299 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 A 299 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE
SEQRES 5 A 299 PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 A 299 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP
SEQRES 7 A 299 TYR ARG PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE
SEQRES 8 A 299 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 A 299 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 A 299 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU
SEQRES 11 A 299 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU
SEQRES 12 A 299 PHE ALA ARG GLU LEU PHE GLN ALA PHE ARG THR PRO ASP
SEQRES 13 A 299 VAL GLY ARG GLU LEU ILE ILE ASP TYR ASN ALA PHE ILE
SEQRES 14 A 299 GLU ILE ILE LEU PRO LYS PHE VAL VAL ARG PRO LEU THR
SEQRES 15 A 299 GLU GLU GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS
SEQRES 16 A 299 PRO GLU TRP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 A 299 LEU PRO ILE ASN GLY GLU PRO ALA ASP ILE TRP ALA LEU
SEQRES 18 A 299 VAL GLU ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL
SEQRES 19 A 299 PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE
SEQRES 20 A 299 PRO PRO ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO
SEQRES 21 A 299 ASN LEU LYS THR VAL PHE ILE GLY PRO GLY LEU HIS TYR
SEQRES 22 A 299 LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE
SEQRES 23 A 299 ALA ARG TRP LEU PRO ALA LEU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 299 MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 B 299 TYR VAL GLU VAL LEU GLY SER ARG MET HIS TYR VAL ASP
SEQRES 3 B 299 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 B 299 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE
SEQRES 5 B 299 PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 B 299 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP
SEQRES 7 B 299 TYR ARG PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE
SEQRES 8 B 299 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 B 299 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 B 299 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU
SEQRES 11 B 299 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU
SEQRES 12 B 299 PHE ALA ARG GLU LEU PHE GLN ALA PHE ARG THR PRO ASP
SEQRES 13 B 299 VAL GLY ARG GLU LEU ILE ILE ASP TYR ASN ALA PHE ILE
SEQRES 14 B 299 GLU ILE ILE LEU PRO LYS PHE VAL VAL ARG PRO LEU THR
SEQRES 15 B 299 GLU GLU GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS
SEQRES 16 B 299 PRO GLU TRP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 B 299 LEU PRO ILE ASN GLY GLU PRO ALA ASP ILE TRP ALA LEU
SEQRES 18 B 299 VAL GLU ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL
SEQRES 19 B 299 PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE
SEQRES 20 B 299 PRO PRO ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO
SEQRES 21 B 299 ASN LEU LYS THR VAL PHE ILE GLY PRO GLY LEU HIS TYR
SEQRES 22 B 299 LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE
SEQRES 23 B 299 ALA ARG TRP LEU PRO ALA LEU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 299 MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 C 299 TYR VAL GLU VAL LEU GLY SER ARG MET HIS TYR VAL ASP
SEQRES 3 C 299 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 C 299 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE
SEQRES 5 C 299 PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 C 299 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP
SEQRES 7 C 299 TYR ARG PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE
SEQRES 8 C 299 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 C 299 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 C 299 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU
SEQRES 11 C 299 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU
SEQRES 12 C 299 PHE ALA ARG GLU LEU PHE GLN ALA PHE ARG THR PRO ASP
SEQRES 13 C 299 VAL GLY ARG GLU LEU ILE ILE ASP TYR ASN ALA PHE ILE
SEQRES 14 C 299 GLU ILE ILE LEU PRO LYS PHE VAL VAL ARG PRO LEU THR
SEQRES 15 C 299 GLU GLU GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS
SEQRES 16 C 299 PRO GLU TRP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 C 299 LEU PRO ILE ASN GLY GLU PRO ALA ASP ILE TRP ALA LEU
SEQRES 18 C 299 VAL GLU ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL
SEQRES 19 C 299 PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE
SEQRES 20 C 299 PRO PRO ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO
SEQRES 21 C 299 ASN LEU LYS THR VAL PHE ILE GLY PRO GLY LEU HIS TYR
SEQRES 22 C 299 LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE
SEQRES 23 C 299 ALA ARG TRP LEU PRO ALA LEU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 299 MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 D 299 TYR VAL GLU VAL LEU GLY SER ARG MET HIS TYR VAL ASP
SEQRES 3 D 299 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 D 299 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE
SEQRES 5 D 299 PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 D 299 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP
SEQRES 7 D 299 TYR ARG PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE
SEQRES 8 D 299 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 D 299 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 D 299 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU
SEQRES 11 D 299 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU
SEQRES 12 D 299 PHE ALA ARG GLU LEU PHE GLN ALA PHE ARG THR PRO ASP
SEQRES 13 D 299 VAL GLY ARG GLU LEU ILE ILE ASP TYR ASN ALA PHE ILE
SEQRES 14 D 299 GLU ILE ILE LEU PRO LYS PHE VAL VAL ARG PRO LEU THR
SEQRES 15 D 299 GLU GLU GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS
SEQRES 16 D 299 PRO GLU TRP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 D 299 LEU PRO ILE ASN GLY GLU PRO ALA ASP ILE TRP ALA LEU
SEQRES 18 D 299 VAL GLU ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL
SEQRES 19 D 299 PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE
SEQRES 20 D 299 PRO PRO ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO
SEQRES 21 D 299 ASN LEU LYS THR VAL PHE ILE GLY PRO GLY LEU HIS TYR
SEQRES 22 D 299 LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE
SEQRES 23 D 299 ALA ARG TRP LEU PRO ALA LEU HIS HIS HIS HIS HIS HIS
SEQRES 1 E 299 MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 E 299 TYR VAL GLU VAL LEU GLY SER ARG MET HIS TYR VAL ASP
SEQRES 3 E 299 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 E 299 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE
SEQRES 5 E 299 PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 E 299 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP
SEQRES 7 E 299 TYR ARG PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE
SEQRES 8 E 299 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 E 299 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 E 299 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU
SEQRES 11 E 299 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU
SEQRES 12 E 299 PHE ALA ARG GLU LEU PHE GLN ALA PHE ARG THR PRO ASP
SEQRES 13 E 299 VAL GLY ARG GLU LEU ILE ILE ASP TYR ASN ALA PHE ILE
SEQRES 14 E 299 GLU ILE ILE LEU PRO LYS PHE VAL VAL ARG PRO LEU THR
SEQRES 15 E 299 GLU GLU GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS
SEQRES 16 E 299 PRO GLU TRP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 E 299 LEU PRO ILE ASN GLY GLU PRO ALA ASP ILE TRP ALA LEU
SEQRES 18 E 299 VAL GLU ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL
SEQRES 19 E 299 PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE
SEQRES 20 E 299 PRO PRO ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO
SEQRES 21 E 299 ASN LEU LYS THR VAL PHE ILE GLY PRO GLY LEU HIS TYR
SEQRES 22 E 299 LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE
SEQRES 23 E 299 ALA ARG TRP LEU PRO ALA LEU HIS HIS HIS HIS HIS HIS
SEQRES 1 F 299 MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 F 299 TYR VAL GLU VAL LEU GLY SER ARG MET HIS TYR VAL ASP
SEQRES 3 F 299 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 F 299 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE
SEQRES 5 F 299 PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 F 299 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP
SEQRES 7 F 299 TYR ARG PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE
SEQRES 8 F 299 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 F 299 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 F 299 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU
SEQRES 11 F 299 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU
SEQRES 12 F 299 PHE ALA ARG GLU LEU PHE GLN ALA PHE ARG THR PRO ASP
SEQRES 13 F 299 VAL GLY ARG GLU LEU ILE ILE ASP TYR ASN ALA PHE ILE
SEQRES 14 F 299 GLU ILE ILE LEU PRO LYS PHE VAL VAL ARG PRO LEU THR
SEQRES 15 F 299 GLU GLU GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS
SEQRES 16 F 299 PRO GLU TRP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 F 299 LEU PRO ILE ASN GLY GLU PRO ALA ASP ILE TRP ALA LEU
SEQRES 18 F 299 VAL GLU ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL
SEQRES 19 F 299 PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE
SEQRES 20 F 299 PRO PRO ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO
SEQRES 21 F 299 ASN LEU LYS THR VAL PHE ILE GLY PRO GLY LEU HIS TYR
SEQRES 22 F 299 LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE
SEQRES 23 F 299 ALA ARG TRP LEU PRO ALA LEU HIS HIS HIS HIS HIS HIS
HET CL A 301 1
HET SO4 A 302 5
HET PG4 A 303 13
HET GOL A 304 6
HET GOL A 305 6
HET TRS A 306 8
HET GOL A 307 6
HET GOL A 308 6
HET CL B 301 1
HET SO4 B 302 5
HET GOL B 303 6
HET GOL B 304 6
HET CL C 301 1
HET SO4 C 302 5
HET SO4 C 303 5
HET GOL C 304 6
HET CL D 301 1
HET SO4 D 302 5
HET SO4 D 303 5
HET PG4 D 304 13
HET GOL D 305 6
HET CL E 301 1
HET SO4 E 302 5
HET GOL E 303 6
HET GOL E 304 6
HET PG4 E 305 13
HET GOL E 306 6
HET CL F 301 1
HET GOL F 302 6
HETNAM CL CHLORIDE ION
HETNAM SO4 SULFATE ION
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM GOL GLYCEROL
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN TRS TRIS BUFFER
FORMUL 7 CL 6(CL 1-)
FORMUL 8 SO4 7(O4 S 2-)
FORMUL 9 PG4 3(C8 H18 O5)
FORMUL 10 GOL 12(C3 H8 O3)
FORMUL 12 TRS C4 H12 N O3 1+
FORMUL 36 HOH *1853(H2 O)
HELIX 1 AA1 SER A 44 ARG A 49 5 6
HELIX 2 AA2 ILE A 51 ALA A 56 1 6
HELIX 3 AA3 ARG A 80 LEU A 95 1 16
HELIX 4 AA4 ASP A 106 ASN A 119 1 14
HELIX 5 AA5 THR A 137 TRP A 141 5 5
HELIX 6 AA6 PRO A 142 ARG A 153 1 12
HELIX 7 AA7 ASP A 156 ILE A 163 1 8
HELIX 8 AA8 ASN A 166 ILE A 171 1 6
HELIX 9 AA9 ILE A 171 PHE A 176 1 6
HELIX 10 AB1 THR A 182 GLU A 191 1 10
HELIX 11 AB2 PRO A 192 LEU A 194 5 3
HELIX 12 AB3 LYS A 195 TRP A 198 5 4
HELIX 13 AB4 ARG A 199 PHE A 205 1 7
HELIX 14 AB5 PRO A 206 LEU A 209 5 4
HELIX 15 AB6 PRO A 215 SER A 232 1 18
HELIX 16 AB7 PRO A 248 LEU A 259 1 12
HELIX 17 AB8 TYR A 273 ASP A 277 5 5
HELIX 18 AB9 ASN A 278 LEU A 290 1 13
HELIX 19 AC1 PRO A 291 HIS A 294 5 4
HELIX 20 AC2 SER B 44 ARG B 49 5 6
HELIX 21 AC3 ILE B 51 ALA B 56 1 6
HELIX 22 AC4 ARG B 80 LEU B 95 1 16
HELIX 23 AC5 ASP B 106 ASN B 119 1 14
HELIX 24 AC6 THR B 137 TRP B 141 5 5
HELIX 25 AC7 PRO B 142 ARG B 153 1 12
HELIX 26 AC8 ASP B 156 ASP B 164 1 9
HELIX 27 AC9 ASN B 166 ILE B 171 1 6
HELIX 28 AD1 ILE B 171 PHE B 176 1 6
HELIX 29 AD2 THR B 182 GLU B 191 1 10
HELIX 30 AD3 PRO B 192 LEU B 194 5 3
HELIX 31 AD4 LYS B 195 TRP B 198 5 4
HELIX 32 AD5 ARG B 199 LEU B 209 1 11
HELIX 33 AD6 PRO B 215 SER B 232 1 18
HELIX 34 AD7 PRO B 248 LEU B 259 1 12
HELIX 35 AD8 TYR B 273 ASN B 278 1 6
HELIX 36 AD9 ASN B 278 LEU B 290 1 13
HELIX 37 AE1 SER C 44 ARG C 49 5 6
HELIX 38 AE2 ILE C 51 ALA C 56 1 6
HELIX 39 AE3 ARG C 80 GLY C 96 1 17
HELIX 40 AE4 ASP C 106 ASN C 119 1 14
HELIX 41 AE5 THR C 137 TRP C 141 5 5
HELIX 42 AE6 PRO C 142 ARG C 153 1 12
HELIX 43 AE7 ASP C 156 ILE C 163 1 8
HELIX 44 AE8 ASN C 166 ILE C 171 1 6
HELIX 45 AE9 ILE C 171 PHE C 176 1 6
HELIX 46 AF1 THR C 182 GLU C 191 1 10
HELIX 47 AF2 PRO C 192 LEU C 194 5 3
HELIX 48 AF3 LYS C 195 TRP C 198 5 4
HELIX 49 AF4 ARG C 199 LEU C 209 1 11
HELIX 50 AF5 PRO C 215 SER C 232 1 18
HELIX 51 AF6 PRO C 248 LEU C 259 1 12
HELIX 52 AF7 TYR C 273 ASN C 278 1 6
HELIX 53 AF8 ASN C 278 LEU C 290 1 13
HELIX 54 AF9 PRO C 291 HIS C 294 5 4
HELIX 55 AG1 SER D 44 ARG D 49 5 6
HELIX 56 AG2 ILE D 51 ALA D 56 1 6
HELIX 57 AG3 ARG D 80 LEU D 95 1 16
HELIX 58 AG4 ASP D 106 ASN D 119 1 14
HELIX 59 AG5 THR D 137 TRP D 141 5 5
HELIX 60 AG6 PRO D 142 ARG D 153 1 12
HELIX 61 AG7 ASP D 156 ILE D 163 1 8
HELIX 62 AG8 ASN D 166 ILE D 171 1 6
HELIX 63 AG9 ILE D 171 PHE D 176 1 6
HELIX 64 AH1 THR D 182 GLU D 191 1 10
HELIX 65 AH2 PRO D 192 LEU D 194 5 3
HELIX 66 AH3 LYS D 195 TRP D 198 5 4
HELIX 67 AH4 ARG D 199 LEU D 209 1 11
HELIX 68 AH5 PRO D 215 SER D 232 1 18
HELIX 69 AH6 PRO D 248 LEU D 259 1 12
HELIX 70 AH7 TYR D 273 ASP D 277 5 5
HELIX 71 AH8 ASN D 278 LEU D 290 1 13
HELIX 72 AH9 PRO D 291 HIS D 294 5 4
HELIX 73 AI1 SER E 44 ARG E 49 5 6
HELIX 74 AI2 ILE E 51 ALA E 56 1 6
HELIX 75 AI3 ARG E 80 GLY E 96 1 17
HELIX 76 AI4 ASP E 106 ASN E 119 1 14
HELIX 77 AI5 THR E 137 TRP E 141 5 5
HELIX 78 AI6 PRO E 142 ARG E 153 1 12
HELIX 79 AI7 ASP E 156 ILE E 163 1 8
HELIX 80 AI8 ASN E 166 ILE E 171 1 6
HELIX 81 AI9 ILE E 171 PHE E 176 1 6
HELIX 82 AJ1 THR E 182 GLU E 191 1 10
HELIX 83 AJ2 PRO E 192 LEU E 194 5 3
HELIX 84 AJ3 LYS E 195 TRP E 198 5 4
HELIX 85 AJ4 ARG E 199 LEU E 209 1 11
HELIX 86 AJ5 PRO E 215 SER E 232 1 18
HELIX 87 AJ6 PRO E 248 LEU E 259 1 12
HELIX 88 AJ7 TYR E 273 ASN E 278 1 6
HELIX 89 AJ8 ASN E 278 LEU E 290 1 13
HELIX 90 AJ9 SER F 44 ARG F 49 5 6
HELIX 91 AK1 ILE F 51 ALA F 56 1 6
HELIX 92 AK2 ARG F 80 LEU F 95 1 16
HELIX 93 AK3 ASP F 106 ASN F 119 1 14
HELIX 94 AK4 THR F 137 TRP F 141 5 5
HELIX 95 AK5 PRO F 142 ARG F 153 1 12
HELIX 96 AK6 ASP F 156 ILE F 163 1 8
HELIX 97 AK7 ASN F 166 ILE F 171 1 6
HELIX 98 AK8 ILE F 171 PHE F 176 1 6
HELIX 99 AK9 THR F 182 GLU F 191 1 10
HELIX 100 AL1 PRO F 192 LEU F 194 5 3
HELIX 101 AL2 LYS F 195 TRP F 198 5 4
HELIX 102 AL3 ARG F 199 LEU F 209 1 11
HELIX 103 AL4 PRO F 215 SER F 232 1 18
HELIX 104 AL5 PRO F 248 LEU F 259 1 12
HELIX 105 AL6 TYR F 273 ASP F 277 5 5
HELIX 106 AL7 ASN F 278 LEU F 290 1 13
SHEET 1 AA1 8 HIS A 13 VAL A 17 0
SHEET 2 AA1 8 SER A 20 VAL A 27 -1 O SER A 20 N VAL A 17
SHEET 3 AA1 8 CYS A 61 PRO A 64 -1 O CYS A 61 N VAL A 27
SHEET 4 AA1 8 VAL A 35 LEU A 38 1 N PHE A 37 O ILE A 62
SHEET 5 AA1 8 VAL A 100 HIS A 105 1 O VAL A 101 N LEU A 36
SHEET 6 AA1 8 VAL A 123 MET A 129 1 O ALA A 127 N LEU A 102
SHEET 7 AA1 8 LYS A 236 PRO A 243 1 O LEU A 237 N PHE A 128
SHEET 8 AA1 8 LEU A 262 GLY A 270 1 O ILE A 267 N TRP A 240
SHEET 1 AA2 8 HIS B 13 VAL B 17 0
SHEET 2 AA2 8 SER B 20 VAL B 27 -1 O SER B 20 N VAL B 17
SHEET 3 AA2 8 CYS B 61 PRO B 64 -1 O CYS B 61 N VAL B 27
SHEET 4 AA2 8 VAL B 35 LEU B 38 1 N VAL B 35 O ILE B 62
SHEET 5 AA2 8 VAL B 100 HIS B 105 1 O VAL B 101 N LEU B 36
SHEET 6 AA2 8 VAL B 123 MET B 129 1 O LYS B 124 N VAL B 100
SHEET 7 AA2 8 LYS B 236 PRO B 243 1 O LEU B 237 N PHE B 128
SHEET 8 AA2 8 LEU B 262 GLY B 270 1 O ILE B 267 N TRP B 240
SHEET 1 AA3 8 HIS C 13 VAL C 17 0
SHEET 2 AA3 8 SER C 20 VAL C 27 -1 O SER C 20 N VAL C 17
SHEET 3 AA3 8 CYS C 61 PRO C 64 -1 O CYS C 61 N VAL C 27
SHEET 4 AA3 8 VAL C 35 LEU C 38 1 N VAL C 35 O ILE C 62
SHEET 5 AA3 8 VAL C 100 HIS C 105 1 O VAL C 101 N LEU C 36
SHEET 6 AA3 8 VAL C 123 MET C 129 1 O ALA C 127 N LEU C 102
SHEET 7 AA3 8 LYS C 236 PRO C 243 1 O LEU C 237 N PHE C 128
SHEET 8 AA3 8 LEU C 262 GLY C 270 1 O VAL C 265 N LEU C 238
SHEET 1 AA4 8 HIS D 13 VAL D 17 0
SHEET 2 AA4 8 SER D 20 VAL D 27 -1 O SER D 20 N VAL D 17
SHEET 3 AA4 8 CYS D 61 PRO D 64 -1 O CYS D 61 N VAL D 27
SHEET 4 AA4 8 VAL D 35 LEU D 38 1 N VAL D 35 O ILE D 62
SHEET 5 AA4 8 VAL D 100 HIS D 105 1 O VAL D 101 N LEU D 36
SHEET 6 AA4 8 VAL D 123 MET D 129 1 O ALA D 127 N LEU D 102
SHEET 7 AA4 8 LYS D 236 PRO D 243 1 O LEU D 237 N PHE D 128
SHEET 8 AA4 8 LEU D 262 GLY D 270 1 O ILE D 267 N TRP D 240
SHEET 1 AA5 8 HIS E 13 VAL E 17 0
SHEET 2 AA5 8 SER E 20 VAL E 27 -1 O SER E 20 N VAL E 17
SHEET 3 AA5 8 CYS E 61 PRO E 64 -1 O CYS E 61 N VAL E 27
SHEET 4 AA5 8 VAL E 35 LEU E 38 1 N PHE E 37 O ILE E 62
SHEET 5 AA5 8 VAL E 100 HIS E 105 1 O VAL E 101 N LEU E 36
SHEET 6 AA5 8 VAL E 123 MET E 129 1 O ALA E 127 N LEU E 102
SHEET 7 AA5 8 LYS E 236 PRO E 243 1 O LEU E 237 N PHE E 128
SHEET 8 AA5 8 LEU E 262 GLY E 270 1 O VAL E 265 N LEU E 238
SHEET 1 AA6 8 HIS F 13 VAL F 17 0
SHEET 2 AA6 8 SER F 20 VAL F 27 -1 O SER F 20 N VAL F 17
SHEET 3 AA6 8 CYS F 61 PRO F 64 -1 O CYS F 61 N VAL F 27
SHEET 4 AA6 8 VAL F 35 LEU F 38 1 N PHE F 37 O ILE F 62
SHEET 5 AA6 8 VAL F 100 HIS F 105 1 O VAL F 101 N LEU F 36
SHEET 6 AA6 8 VAL F 123 MET F 129 1 O ALA F 127 N LEU F 102
SHEET 7 AA6 8 LYS F 236 PRO F 243 1 O LEU F 237 N PHE F 128
SHEET 8 AA6 8 LEU F 262 GLY F 270 1 O ILE F 267 N TRP F 240
CISPEP 1 ASN A 41 PRO A 42 0 -3.51
CISPEP 2 GLU A 214 PRO A 215 0 -2.06
CISPEP 3 THR A 242 PRO A 243 0 7.09
CISPEP 4 ASN B 41 PRO B 42 0 -7.39
CISPEP 5 GLU B 214 PRO B 215 0 -5.02
CISPEP 6 THR B 242 PRO B 243 0 4.26
CISPEP 7 ASN C 41 PRO C 42 0 -4.44
CISPEP 8 GLU C 214 PRO C 215 0 -7.95
CISPEP 9 THR C 242 PRO C 243 0 1.38
CISPEP 10 ASN D 41 PRO D 42 0 -3.35
CISPEP 11 GLU D 214 PRO D 215 0 -0.82
CISPEP 12 THR D 242 PRO D 243 0 2.41
CISPEP 13 ASN E 41 PRO E 42 0 -6.59
CISPEP 14 GLU E 214 PRO E 215 0 -1.41
CISPEP 15 THR E 242 PRO E 243 0 1.59
CISPEP 16 ASN F 41 PRO F 42 0 -6.24
CISPEP 17 GLU F 214 PRO F 215 0 -3.18
CISPEP 18 THR F 242 PRO F 243 0 6.02
CRYST1 67.350 143.144 106.676 90.00 108.38 90.00 P 1 21 1 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014848 0.000000 0.004933 0.00000
SCALE2 0.000000 0.006986 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009878 0.00000
TER 2461 HIS A 295
TER 4844 PRO B 291
TER 7261 HIS C 294
TER 9676 HIS D 294
TER 12063 PRO E 291
TER 14463 LEU F 293
MASTER 457 0 29 106 48 0 0 616337 6 154 138
END |