| 5egn-pdb | HEADER HYDROLASE 27-OCT-15 5EGN
TITLE EST816 AS AN N-ACYL HOMOSERINE LACTONE DEGRADING ENZYME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 FRAGMENT: UNP RESIDUES 1-261;
COMPND 5 SYNONYM: AHL-LACTONASE 816;
COMPND 6 EC: 3.1.1.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 GENE: EST816;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS N-ACYL-HOMOSERINE LACTONE, LACTONASE, QUORUM-SENSING,
KEYWDS 2 THERMOSTABILITY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.XIE,X.LIU,L.CAO,Y.LIU
REVDAT 1 02-NOV-16 5EGN 0
JRNL AUTH W.XIE,X.LIU,L.CAO,Y.LIU
JRNL TITL EST816 AS AN N-ACYL HOMOSERINE LACTONE DEGRADING ENZYME
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.64 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.64
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.82
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 57279
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.222
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 2981
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 44.8237 - 7.2633 0.97 2653 144 0.1768 0.1979
REMARK 3 2 7.2633 - 5.7690 0.98 2594 157 0.2137 0.2510
REMARK 3 3 5.7690 - 5.0409 1.00 2641 134 0.1964 0.2053
REMARK 3 4 5.0409 - 4.5805 0.99 2632 136 0.1800 0.2175
REMARK 3 5 4.5805 - 4.2524 1.00 2641 118 0.1795 0.2316
REMARK 3 6 4.2524 - 4.0019 0.99 2611 142 0.1862 0.2734
REMARK 3 7 4.0019 - 3.8016 0.99 2614 132 0.2014 0.2563
REMARK 3 8 3.8016 - 3.6362 0.99 2592 143 0.2075 0.2675
REMARK 3 9 3.6362 - 3.4962 0.99 2624 132 0.2164 0.2422
REMARK 3 10 3.4962 - 3.3756 0.99 2562 137 0.2274 0.3095
REMARK 3 11 3.3756 - 3.2701 0.99 2573 170 0.2345 0.2623
REMARK 3 12 3.2701 - 3.1767 0.99 2606 146 0.2431 0.2851
REMARK 3 13 3.1767 - 3.0931 0.99 2534 184 0.2490 0.2882
REMARK 3 14 3.0931 - 3.0176 0.99 2572 131 0.2542 0.2977
REMARK 3 15 3.0176 - 2.9490 0.99 2605 133 0.2550 0.3260
REMARK 3 16 2.9490 - 2.8863 0.99 2562 144 0.2685 0.2900
REMARK 3 17 2.8863 - 2.8286 0.99 2577 125 0.2742 0.3081
REMARK 3 18 2.8286 - 2.7752 0.98 2580 137 0.2698 0.2775
REMARK 3 19 2.7752 - 2.7256 0.99 2554 159 0.2787 0.3176
REMARK 3 20 2.7256 - 2.6794 0.99 2534 148 0.2917 0.3425
REMARK 3 21 2.6794 - 2.6362 0.93 2437 129 0.3028 0.3637
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) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.060
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 : 0.003 16175
REMARK 3 ANGLE : 0.729 22017
REMARK 3 CHIRALITY : 0.028 2425
REMARK 3 PLANARITY : 0.004 2938
REMARK 3 DIHEDRAL : 13.882 5712
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 5EGN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000214679.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57955
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.630
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.63
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.51800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: 2XUA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG 3350, 0.1M SODIUM ACETATE PH
REMARK 280 5.6, 0.2M SODIUM CHLORIDE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
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 39.27250
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
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: 2670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 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: 2670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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: 2590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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: 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: 2630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 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 ALA A 262
REMARK 465 ALA A 263
REMARK 465 LEU A 264
REMARK 465 GLU A 265
REMARK 465 HIS A 266
REMARK 465 HIS A 267
REMARK 465 HIS A 268
REMARK 465 HIS A 269
REMARK 465 HIS A 270
REMARK 465 HIS A 271
REMARK 465 MET B 1
REMARK 465 ALA B 262
REMARK 465 ALA B 263
REMARK 465 LEU B 264
REMARK 465 GLU B 265
REMARK 465 HIS B 266
REMARK 465 HIS B 267
REMARK 465 HIS B 268
REMARK 465 HIS B 269
REMARK 465 HIS B 270
REMARK 465 HIS B 271
REMARK 465 MET C 1
REMARK 465 ALA C 261
REMARK 465 ALA C 262
REMARK 465 ALA C 263
REMARK 465 LEU C 264
REMARK 465 GLU C 265
REMARK 465 HIS C 266
REMARK 465 HIS C 267
REMARK 465 HIS C 268
REMARK 465 HIS C 269
REMARK 465 HIS C 270
REMARK 465 HIS C 271
REMARK 465 MET D 1
REMARK 465 ALA D 261
REMARK 465 ALA D 262
REMARK 465 ALA D 263
REMARK 465 LEU D 264
REMARK 465 GLU D 265
REMARK 465 HIS D 266
REMARK 465 HIS D 267
REMARK 465 HIS D 268
REMARK 465 HIS D 269
REMARK 465 HIS D 270
REMARK 465 HIS D 271
REMARK 465 MET E 1
REMARK 465 ALA E 261
REMARK 465 ALA E 262
REMARK 465 ALA E 263
REMARK 465 LEU E 264
REMARK 465 GLU E 265
REMARK 465 HIS E 266
REMARK 465 HIS E 267
REMARK 465 HIS E 268
REMARK 465 HIS E 269
REMARK 465 HIS E 270
REMARK 465 HIS E 271
REMARK 465 MET F 1
REMARK 465 ALA F 262
REMARK 465 ALA F 263
REMARK 465 LEU F 264
REMARK 465 GLU F 265
REMARK 465 HIS F 266
REMARK 465 HIS F 267
REMARK 465 HIS F 268
REMARK 465 HIS F 269
REMARK 465 HIS F 270
REMARK 465 HIS F 271
REMARK 465 MET G 1
REMARK 465 ALA G 261
REMARK 465 ALA G 262
REMARK 465 ALA G 263
REMARK 465 LEU G 264
REMARK 465 GLU G 265
REMARK 465 HIS G 266
REMARK 465 HIS G 267
REMARK 465 HIS G 268
REMARK 465 HIS G 269
REMARK 465 HIS G 270
REMARK 465 HIS G 271
REMARK 465 MET H 1
REMARK 465 VAL H 260
REMARK 465 ALA H 261
REMARK 465 ALA H 262
REMARK 465 ALA H 263
REMARK 465 LEU H 264
REMARK 465 GLU H 265
REMARK 465 HIS H 266
REMARK 465 HIS H 267
REMARK 465 HIS H 268
REMARK 465 HIS H 269
REMARK 465 HIS H 270
REMARK 465 HIS H 271
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 129 CG CD OE1 OE2
REMARK 470 GLN A 135 CG CD OE1 NE2
REMARK 470 PHE D 259 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE E 134 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PRO F 128 CG CD
REMARK 470 GLU F 129 CG CD OE1 OE2
REMARK 470 PHE F 259 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PRO G 127 CG CD
REMARK 470 GLN G 135 CG CD OE1 NE2
REMARK 470 ASN G 136 CG OD1 ND2
REMARK 470 LYS G 177 CG CD CE NZ
REMARK 470 PHE G 180 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PRO G 187 CG CD
REMARK 470 ASN G 188 CG OD1 ND2
REMARK 470 ARG G 198 CG CD NE CZ NH1 NH2
REMARK 470 ARG G 257 CG CD NE CZ NH1 NH2
REMARK 470 LYS H 83 CG CD CE NZ
REMARK 470 GLN H 108 CG CD OE1 NE2
REMARK 470 GLU H 124 CG CD OE1 OE2
REMARK 470 PRO H 127 CG CD
REMARK 470 GLU H 233 CG CD OE1 OE2
REMARK 470 ARG H 248 CG CD NE CZ NH1 NH2
REMARK 470 GLU H 251 CG CD OE1 OE2
REMARK 470 GLU H 254 CG CD OE1 OE2
REMARK 470 ARG H 257 CG CD NE CZ NH1 NH2
REMARK 470 PHE H 259 CG CD1 CD2 CE1 CE2 CZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O GLY G 55 O HOH G 301 1.91
REMARK 500 O ASN G 174 O HOH G 301 2.04
REMARK 500 OD1 ASP E 80 NH2 ARG E 109 2.14
REMARK 500 O LEU D 256 O HOH D 301 2.14
REMARK 500 NZ LYS G 61 O SER G 173 2.15
REMARK 500 OE1 GLU A 251 O HOH A 301 2.17
REMARK 500 OD1 ASP F 80 NH2 ARG F 109 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OG1 THR D 64 ND2 ASN D 238 2547 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 29 -4.81 72.66
REMARK 500 THR A 30 -157.10 -103.36
REMARK 500 SER A 93 -107.59 53.40
REMARK 500 VAL A 260 -48.45 -133.48
REMARK 500 SER B 29 -4.95 74.47
REMARK 500 THR B 30 -158.33 -105.72
REMARK 500 SER B 93 -106.28 53.42
REMARK 500 VAL B 260 89.46 -60.88
REMARK 500 SER C 29 -8.36 73.85
REMARK 500 THR C 30 -157.45 -105.13
REMARK 500 SER C 93 -108.70 55.32
REMARK 500 GLN C 135 -73.03 -45.94
REMARK 500 PHE C 243 68.06 -119.19
REMARK 500 SER D 29 -5.68 72.63
REMARK 500 THR D 30 -159.07 -104.68
REMARK 500 SER D 93 -112.98 55.70
REMARK 500 PHE D 243 71.90 -119.54
REMARK 500 SER E 29 -7.67 75.27
REMARK 500 THR E 30 -158.88 -111.31
REMARK 500 SER E 93 -103.25 50.77
REMARK 500 SER F 29 -4.60 73.72
REMARK 500 THR F 30 -157.46 -105.25
REMARK 500 SER F 93 -107.11 53.42
REMARK 500 THR G 30 -159.56 -103.20
REMARK 500 ASP G 85 -79.93 -81.08
REMARK 500 SER G 93 -110.81 53.95
REMARK 500 PHE G 259 -70.37 -85.24
REMARK 500 SER H 29 -3.56 73.60
REMARK 500 THR H 30 -156.72 -104.21
REMARK 500 SER H 93 -106.73 51.99
REMARK 500 ASP H 197 -94.78 -17.33
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 H 336 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH H 337 DISTANCE = 6.93 ANGSTROMS
DBREF 5EGN A 1 261 UNP I6YRG4 I6YRG4_9BACT 1 261
DBREF 5EGN B 1 261 UNP I6YRG4 I6YRG4_9BACT 1 261
DBREF 5EGN C 1 261 UNP I6YRG4 I6YRG4_9BACT 1 261
DBREF 5EGN D 1 261 UNP I6YRG4 I6YRG4_9BACT 1 261
DBREF 5EGN E 1 261 UNP I6YRG4 I6YRG4_9BACT 1 261
DBREF 5EGN F 1 261 UNP I6YRG4 I6YRG4_9BACT 1 261
DBREF 5EGN G 1 261 UNP I6YRG4 I6YRG4_9BACT 1 261
DBREF 5EGN H 1 261 UNP I6YRG4 I6YRG4_9BACT 1 261
SEQADV 5EGN VAL A 216 UNP I6YRG4 ALA 216 ENGINEERED MUTATION
SEQADV 5EGN ASN A 238 UNP I6YRG4 LYS 238 ENGINEERED MUTATION
SEQADV 5EGN ALA A 262 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN ALA A 263 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN LEU A 264 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN GLU A 265 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS A 266 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS A 267 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS A 268 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS A 269 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS A 270 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS A 271 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN VAL B 216 UNP I6YRG4 ALA 216 ENGINEERED MUTATION
SEQADV 5EGN ASN B 238 UNP I6YRG4 LYS 238 ENGINEERED MUTATION
SEQADV 5EGN ALA B 262 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN ALA B 263 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN LEU B 264 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN GLU B 265 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS B 266 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS B 267 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS B 268 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS B 269 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS B 270 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS B 271 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN VAL C 216 UNP I6YRG4 ALA 216 ENGINEERED MUTATION
SEQADV 5EGN ASN C 238 UNP I6YRG4 LYS 238 ENGINEERED MUTATION
SEQADV 5EGN ALA C 262 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN ALA C 263 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN LEU C 264 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN GLU C 265 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS C 266 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS C 267 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS C 268 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS C 269 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS C 270 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS C 271 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN VAL D 216 UNP I6YRG4 ALA 216 ENGINEERED MUTATION
SEQADV 5EGN ASN D 238 UNP I6YRG4 LYS 238 ENGINEERED MUTATION
SEQADV 5EGN ALA D 262 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN ALA D 263 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN LEU D 264 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN GLU D 265 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS D 266 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS D 267 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS D 268 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS D 269 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS D 270 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS D 271 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN VAL E 216 UNP I6YRG4 ALA 216 ENGINEERED MUTATION
SEQADV 5EGN ASN E 238 UNP I6YRG4 LYS 238 ENGINEERED MUTATION
SEQADV 5EGN ALA E 262 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN ALA E 263 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN LEU E 264 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN GLU E 265 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS E 266 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS E 267 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS E 268 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS E 269 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS E 270 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS E 271 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN VAL F 216 UNP I6YRG4 ALA 216 ENGINEERED MUTATION
SEQADV 5EGN ASN F 238 UNP I6YRG4 LYS 238 ENGINEERED MUTATION
SEQADV 5EGN ALA F 262 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN ALA F 263 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN LEU F 264 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN GLU F 265 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS F 266 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS F 267 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS F 268 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS F 269 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS F 270 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS F 271 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN VAL G 216 UNP I6YRG4 ALA 216 ENGINEERED MUTATION
SEQADV 5EGN ASN G 238 UNP I6YRG4 LYS 238 ENGINEERED MUTATION
SEQADV 5EGN ALA G 262 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN ALA G 263 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN LEU G 264 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN GLU G 265 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS G 266 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS G 267 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS G 268 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS G 269 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS G 270 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS G 271 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN VAL H 216 UNP I6YRG4 ALA 216 ENGINEERED MUTATION
SEQADV 5EGN ASN H 238 UNP I6YRG4 LYS 238 ENGINEERED MUTATION
SEQADV 5EGN ALA H 262 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN ALA H 263 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN LEU H 264 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN GLU H 265 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS H 266 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS H 267 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS H 268 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS H 269 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS H 270 UNP I6YRG4 EXPRESSION TAG
SEQADV 5EGN HIS H 271 UNP I6YRG4 EXPRESSION TAG
SEQRES 1 A 271 MET PRO HIS VAL GLU ASN ASP GLY VAL LYS ILE TYR TYR
SEQRES 2 A 271 ASP SER TYR GLY GLU GLY VAL PRO ILE VAL PHE LEU HIS
SEQRES 3 A 271 PRO PHE SER THR ASN GLY GLY ILE TRP TYR PHE GLN THR
SEQRES 4 A 271 PHE PRO PHE ALA GLN THR ASN HIS VAL ILE VAL ILE ASP
SEQRES 5 A 271 HIS ARG GLY HIS GLY ARG SER ASP LYS PRO ALA THR GLY
SEQRES 6 A 271 TYR SER ILE MET GLU HIS ALA ASP ASP VAL VAL ALA VAL
SEQRES 7 A 271 LEU ASP ALA LEU LYS VAL ASP ARG ALA VAL PHE VAL GLY
SEQRES 8 A 271 ASN SER ILE GLY GLY MET ILE ALA MET GLN LEU ASN LEU
SEQRES 9 A 271 ASP HIS PRO GLN ARG VAL ILE GLY ASN LEU ILE LEU SER
SEQRES 10 A 271 SER GLY THR GLY LEU GLY GLU GLY MET PRO PRO GLU ALA
SEQRES 11 A 271 GLY ALA ALA PHE GLN ASN ASP TYR ILE GLY ALA PHE GLY
SEQRES 12 A 271 GLY LEU LEU GLU GLY ALA VAL SER ALA ARG SER LYS ARG
SEQRES 13 A 271 GLU ARG PRO GLU ILE LEU ALA VAL MET LYS ALA HIS PHE
SEQRES 14 A 271 SER VAL PRO SER ASN PHE PRO LYS HIS VAL PHE ASP ALA
SEQRES 15 A 271 ALA THR ALA ASP PRO ASN GLY VAL PHE ALA TRP ASN ILE
SEQRES 16 A 271 LYS ASP ARG LEU SER SER ILE GLN ALA PRO THR LEU VAL
SEQRES 17 A 271 VAL ALA GLY GLU GLU ASP LEU VAL THR THR VAL ALA ASN
SEQRES 18 A 271 ASN GLN LEU LEU ALA ASP ASN ILE PRO GLY ALA GLU LEU
SEQRES 19 A 271 ARG VAL ILE ASN ASP VAL GLY HIS PHE TYR GLN LEU GLU
SEQRES 20 A 271 ARG PRO SER GLU PHE ASN GLU LEU LEU ARG GLY PHE VAL
SEQRES 21 A 271 ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 271 MET PRO HIS VAL GLU ASN ASP GLY VAL LYS ILE TYR TYR
SEQRES 2 B 271 ASP SER TYR GLY GLU GLY VAL PRO ILE VAL PHE LEU HIS
SEQRES 3 B 271 PRO PHE SER THR ASN GLY GLY ILE TRP TYR PHE GLN THR
SEQRES 4 B 271 PHE PRO PHE ALA GLN THR ASN HIS VAL ILE VAL ILE ASP
SEQRES 5 B 271 HIS ARG GLY HIS GLY ARG SER ASP LYS PRO ALA THR GLY
SEQRES 6 B 271 TYR SER ILE MET GLU HIS ALA ASP ASP VAL VAL ALA VAL
SEQRES 7 B 271 LEU ASP ALA LEU LYS VAL ASP ARG ALA VAL PHE VAL GLY
SEQRES 8 B 271 ASN SER ILE GLY GLY MET ILE ALA MET GLN LEU ASN LEU
SEQRES 9 B 271 ASP HIS PRO GLN ARG VAL ILE GLY ASN LEU ILE LEU SER
SEQRES 10 B 271 SER GLY THR GLY LEU GLY GLU GLY MET PRO PRO GLU ALA
SEQRES 11 B 271 GLY ALA ALA PHE GLN ASN ASP TYR ILE GLY ALA PHE GLY
SEQRES 12 B 271 GLY LEU LEU GLU GLY ALA VAL SER ALA ARG SER LYS ARG
SEQRES 13 B 271 GLU ARG PRO GLU ILE LEU ALA VAL MET LYS ALA HIS PHE
SEQRES 14 B 271 SER VAL PRO SER ASN PHE PRO LYS HIS VAL PHE ASP ALA
SEQRES 15 B 271 ALA THR ALA ASP PRO ASN GLY VAL PHE ALA TRP ASN ILE
SEQRES 16 B 271 LYS ASP ARG LEU SER SER ILE GLN ALA PRO THR LEU VAL
SEQRES 17 B 271 VAL ALA GLY GLU GLU ASP LEU VAL THR THR VAL ALA ASN
SEQRES 18 B 271 ASN GLN LEU LEU ALA ASP ASN ILE PRO GLY ALA GLU LEU
SEQRES 19 B 271 ARG VAL ILE ASN ASP VAL GLY HIS PHE TYR GLN LEU GLU
SEQRES 20 B 271 ARG PRO SER GLU PHE ASN GLU LEU LEU ARG GLY PHE VAL
SEQRES 21 B 271 ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 271 MET PRO HIS VAL GLU ASN ASP GLY VAL LYS ILE TYR TYR
SEQRES 2 C 271 ASP SER TYR GLY GLU GLY VAL PRO ILE VAL PHE LEU HIS
SEQRES 3 C 271 PRO PHE SER THR ASN GLY GLY ILE TRP TYR PHE GLN THR
SEQRES 4 C 271 PHE PRO PHE ALA GLN THR ASN HIS VAL ILE VAL ILE ASP
SEQRES 5 C 271 HIS ARG GLY HIS GLY ARG SER ASP LYS PRO ALA THR GLY
SEQRES 6 C 271 TYR SER ILE MET GLU HIS ALA ASP ASP VAL VAL ALA VAL
SEQRES 7 C 271 LEU ASP ALA LEU LYS VAL ASP ARG ALA VAL PHE VAL GLY
SEQRES 8 C 271 ASN SER ILE GLY GLY MET ILE ALA MET GLN LEU ASN LEU
SEQRES 9 C 271 ASP HIS PRO GLN ARG VAL ILE GLY ASN LEU ILE LEU SER
SEQRES 10 C 271 SER GLY THR GLY LEU GLY GLU GLY MET PRO PRO GLU ALA
SEQRES 11 C 271 GLY ALA ALA PHE GLN ASN ASP TYR ILE GLY ALA PHE GLY
SEQRES 12 C 271 GLY LEU LEU GLU GLY ALA VAL SER ALA ARG SER LYS ARG
SEQRES 13 C 271 GLU ARG PRO GLU ILE LEU ALA VAL MET LYS ALA HIS PHE
SEQRES 14 C 271 SER VAL PRO SER ASN PHE PRO LYS HIS VAL PHE ASP ALA
SEQRES 15 C 271 ALA THR ALA ASP PRO ASN GLY VAL PHE ALA TRP ASN ILE
SEQRES 16 C 271 LYS ASP ARG LEU SER SER ILE GLN ALA PRO THR LEU VAL
SEQRES 17 C 271 VAL ALA GLY GLU GLU ASP LEU VAL THR THR VAL ALA ASN
SEQRES 18 C 271 ASN GLN LEU LEU ALA ASP ASN ILE PRO GLY ALA GLU LEU
SEQRES 19 C 271 ARG VAL ILE ASN ASP VAL GLY HIS PHE TYR GLN LEU GLU
SEQRES 20 C 271 ARG PRO SER GLU PHE ASN GLU LEU LEU ARG GLY PHE VAL
SEQRES 21 C 271 ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 271 MET PRO HIS VAL GLU ASN ASP GLY VAL LYS ILE TYR TYR
SEQRES 2 D 271 ASP SER TYR GLY GLU GLY VAL PRO ILE VAL PHE LEU HIS
SEQRES 3 D 271 PRO PHE SER THR ASN GLY GLY ILE TRP TYR PHE GLN THR
SEQRES 4 D 271 PHE PRO PHE ALA GLN THR ASN HIS VAL ILE VAL ILE ASP
SEQRES 5 D 271 HIS ARG GLY HIS GLY ARG SER ASP LYS PRO ALA THR GLY
SEQRES 6 D 271 TYR SER ILE MET GLU HIS ALA ASP ASP VAL VAL ALA VAL
SEQRES 7 D 271 LEU ASP ALA LEU LYS VAL ASP ARG ALA VAL PHE VAL GLY
SEQRES 8 D 271 ASN SER ILE GLY GLY MET ILE ALA MET GLN LEU ASN LEU
SEQRES 9 D 271 ASP HIS PRO GLN ARG VAL ILE GLY ASN LEU ILE LEU SER
SEQRES 10 D 271 SER GLY THR GLY LEU GLY GLU GLY MET PRO PRO GLU ALA
SEQRES 11 D 271 GLY ALA ALA PHE GLN ASN ASP TYR ILE GLY ALA PHE GLY
SEQRES 12 D 271 GLY LEU LEU GLU GLY ALA VAL SER ALA ARG SER LYS ARG
SEQRES 13 D 271 GLU ARG PRO GLU ILE LEU ALA VAL MET LYS ALA HIS PHE
SEQRES 14 D 271 SER VAL PRO SER ASN PHE PRO LYS HIS VAL PHE ASP ALA
SEQRES 15 D 271 ALA THR ALA ASP PRO ASN GLY VAL PHE ALA TRP ASN ILE
SEQRES 16 D 271 LYS ASP ARG LEU SER SER ILE GLN ALA PRO THR LEU VAL
SEQRES 17 D 271 VAL ALA GLY GLU GLU ASP LEU VAL THR THR VAL ALA ASN
SEQRES 18 D 271 ASN GLN LEU LEU ALA ASP ASN ILE PRO GLY ALA GLU LEU
SEQRES 19 D 271 ARG VAL ILE ASN ASP VAL GLY HIS PHE TYR GLN LEU GLU
SEQRES 20 D 271 ARG PRO SER GLU PHE ASN GLU LEU LEU ARG GLY PHE VAL
SEQRES 21 D 271 ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 E 271 MET PRO HIS VAL GLU ASN ASP GLY VAL LYS ILE TYR TYR
SEQRES 2 E 271 ASP SER TYR GLY GLU GLY VAL PRO ILE VAL PHE LEU HIS
SEQRES 3 E 271 PRO PHE SER THR ASN GLY GLY ILE TRP TYR PHE GLN THR
SEQRES 4 E 271 PHE PRO PHE ALA GLN THR ASN HIS VAL ILE VAL ILE ASP
SEQRES 5 E 271 HIS ARG GLY HIS GLY ARG SER ASP LYS PRO ALA THR GLY
SEQRES 6 E 271 TYR SER ILE MET GLU HIS ALA ASP ASP VAL VAL ALA VAL
SEQRES 7 E 271 LEU ASP ALA LEU LYS VAL ASP ARG ALA VAL PHE VAL GLY
SEQRES 8 E 271 ASN SER ILE GLY GLY MET ILE ALA MET GLN LEU ASN LEU
SEQRES 9 E 271 ASP HIS PRO GLN ARG VAL ILE GLY ASN LEU ILE LEU SER
SEQRES 10 E 271 SER GLY THR GLY LEU GLY GLU GLY MET PRO PRO GLU ALA
SEQRES 11 E 271 GLY ALA ALA PHE GLN ASN ASP TYR ILE GLY ALA PHE GLY
SEQRES 12 E 271 GLY LEU LEU GLU GLY ALA VAL SER ALA ARG SER LYS ARG
SEQRES 13 E 271 GLU ARG PRO GLU ILE LEU ALA VAL MET LYS ALA HIS PHE
SEQRES 14 E 271 SER VAL PRO SER ASN PHE PRO LYS HIS VAL PHE ASP ALA
SEQRES 15 E 271 ALA THR ALA ASP PRO ASN GLY VAL PHE ALA TRP ASN ILE
SEQRES 16 E 271 LYS ASP ARG LEU SER SER ILE GLN ALA PRO THR LEU VAL
SEQRES 17 E 271 VAL ALA GLY GLU GLU ASP LEU VAL THR THR VAL ALA ASN
SEQRES 18 E 271 ASN GLN LEU LEU ALA ASP ASN ILE PRO GLY ALA GLU LEU
SEQRES 19 E 271 ARG VAL ILE ASN ASP VAL GLY HIS PHE TYR GLN LEU GLU
SEQRES 20 E 271 ARG PRO SER GLU PHE ASN GLU LEU LEU ARG GLY PHE VAL
SEQRES 21 E 271 ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 F 271 MET PRO HIS VAL GLU ASN ASP GLY VAL LYS ILE TYR TYR
SEQRES 2 F 271 ASP SER TYR GLY GLU GLY VAL PRO ILE VAL PHE LEU HIS
SEQRES 3 F 271 PRO PHE SER THR ASN GLY GLY ILE TRP TYR PHE GLN THR
SEQRES 4 F 271 PHE PRO PHE ALA GLN THR ASN HIS VAL ILE VAL ILE ASP
SEQRES 5 F 271 HIS ARG GLY HIS GLY ARG SER ASP LYS PRO ALA THR GLY
SEQRES 6 F 271 TYR SER ILE MET GLU HIS ALA ASP ASP VAL VAL ALA VAL
SEQRES 7 F 271 LEU ASP ALA LEU LYS VAL ASP ARG ALA VAL PHE VAL GLY
SEQRES 8 F 271 ASN SER ILE GLY GLY MET ILE ALA MET GLN LEU ASN LEU
SEQRES 9 F 271 ASP HIS PRO GLN ARG VAL ILE GLY ASN LEU ILE LEU SER
SEQRES 10 F 271 SER GLY THR GLY LEU GLY GLU GLY MET PRO PRO GLU ALA
SEQRES 11 F 271 GLY ALA ALA PHE GLN ASN ASP TYR ILE GLY ALA PHE GLY
SEQRES 12 F 271 GLY LEU LEU GLU GLY ALA VAL SER ALA ARG SER LYS ARG
SEQRES 13 F 271 GLU ARG PRO GLU ILE LEU ALA VAL MET LYS ALA HIS PHE
SEQRES 14 F 271 SER VAL PRO SER ASN PHE PRO LYS HIS VAL PHE ASP ALA
SEQRES 15 F 271 ALA THR ALA ASP PRO ASN GLY VAL PHE ALA TRP ASN ILE
SEQRES 16 F 271 LYS ASP ARG LEU SER SER ILE GLN ALA PRO THR LEU VAL
SEQRES 17 F 271 VAL ALA GLY GLU GLU ASP LEU VAL THR THR VAL ALA ASN
SEQRES 18 F 271 ASN GLN LEU LEU ALA ASP ASN ILE PRO GLY ALA GLU LEU
SEQRES 19 F 271 ARG VAL ILE ASN ASP VAL GLY HIS PHE TYR GLN LEU GLU
SEQRES 20 F 271 ARG PRO SER GLU PHE ASN GLU LEU LEU ARG GLY PHE VAL
SEQRES 21 F 271 ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 G 271 MET PRO HIS VAL GLU ASN ASP GLY VAL LYS ILE TYR TYR
SEQRES 2 G 271 ASP SER TYR GLY GLU GLY VAL PRO ILE VAL PHE LEU HIS
SEQRES 3 G 271 PRO PHE SER THR ASN GLY GLY ILE TRP TYR PHE GLN THR
SEQRES 4 G 271 PHE PRO PHE ALA GLN THR ASN HIS VAL ILE VAL ILE ASP
SEQRES 5 G 271 HIS ARG GLY HIS GLY ARG SER ASP LYS PRO ALA THR GLY
SEQRES 6 G 271 TYR SER ILE MET GLU HIS ALA ASP ASP VAL VAL ALA VAL
SEQRES 7 G 271 LEU ASP ALA LEU LYS VAL ASP ARG ALA VAL PHE VAL GLY
SEQRES 8 G 271 ASN SER ILE GLY GLY MET ILE ALA MET GLN LEU ASN LEU
SEQRES 9 G 271 ASP HIS PRO GLN ARG VAL ILE GLY ASN LEU ILE LEU SER
SEQRES 10 G 271 SER GLY THR GLY LEU GLY GLU GLY MET PRO PRO GLU ALA
SEQRES 11 G 271 GLY ALA ALA PHE GLN ASN ASP TYR ILE GLY ALA PHE GLY
SEQRES 12 G 271 GLY LEU LEU GLU GLY ALA VAL SER ALA ARG SER LYS ARG
SEQRES 13 G 271 GLU ARG PRO GLU ILE LEU ALA VAL MET LYS ALA HIS PHE
SEQRES 14 G 271 SER VAL PRO SER ASN PHE PRO LYS HIS VAL PHE ASP ALA
SEQRES 15 G 271 ALA THR ALA ASP PRO ASN GLY VAL PHE ALA TRP ASN ILE
SEQRES 16 G 271 LYS ASP ARG LEU SER SER ILE GLN ALA PRO THR LEU VAL
SEQRES 17 G 271 VAL ALA GLY GLU GLU ASP LEU VAL THR THR VAL ALA ASN
SEQRES 18 G 271 ASN GLN LEU LEU ALA ASP ASN ILE PRO GLY ALA GLU LEU
SEQRES 19 G 271 ARG VAL ILE ASN ASP VAL GLY HIS PHE TYR GLN LEU GLU
SEQRES 20 G 271 ARG PRO SER GLU PHE ASN GLU LEU LEU ARG GLY PHE VAL
SEQRES 21 G 271 ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 H 271 MET PRO HIS VAL GLU ASN ASP GLY VAL LYS ILE TYR TYR
SEQRES 2 H 271 ASP SER TYR GLY GLU GLY VAL PRO ILE VAL PHE LEU HIS
SEQRES 3 H 271 PRO PHE SER THR ASN GLY GLY ILE TRP TYR PHE GLN THR
SEQRES 4 H 271 PHE PRO PHE ALA GLN THR ASN HIS VAL ILE VAL ILE ASP
SEQRES 5 H 271 HIS ARG GLY HIS GLY ARG SER ASP LYS PRO ALA THR GLY
SEQRES 6 H 271 TYR SER ILE MET GLU HIS ALA ASP ASP VAL VAL ALA VAL
SEQRES 7 H 271 LEU ASP ALA LEU LYS VAL ASP ARG ALA VAL PHE VAL GLY
SEQRES 8 H 271 ASN SER ILE GLY GLY MET ILE ALA MET GLN LEU ASN LEU
SEQRES 9 H 271 ASP HIS PRO GLN ARG VAL ILE GLY ASN LEU ILE LEU SER
SEQRES 10 H 271 SER GLY THR GLY LEU GLY GLU GLY MET PRO PRO GLU ALA
SEQRES 11 H 271 GLY ALA ALA PHE GLN ASN ASP TYR ILE GLY ALA PHE GLY
SEQRES 12 H 271 GLY LEU LEU GLU GLY ALA VAL SER ALA ARG SER LYS ARG
SEQRES 13 H 271 GLU ARG PRO GLU ILE LEU ALA VAL MET LYS ALA HIS PHE
SEQRES 14 H 271 SER VAL PRO SER ASN PHE PRO LYS HIS VAL PHE ASP ALA
SEQRES 15 H 271 ALA THR ALA ASP PRO ASN GLY VAL PHE ALA TRP ASN ILE
SEQRES 16 H 271 LYS ASP ARG LEU SER SER ILE GLN ALA PRO THR LEU VAL
SEQRES 17 H 271 VAL ALA GLY GLU GLU ASP LEU VAL THR THR VAL ALA ASN
SEQRES 18 H 271 ASN GLN LEU LEU ALA ASP ASN ILE PRO GLY ALA GLU LEU
SEQRES 19 H 271 ARG VAL ILE ASN ASP VAL GLY HIS PHE TYR GLN LEU GLU
SEQRES 20 H 271 ARG PRO SER GLU PHE ASN GLU LEU LEU ARG GLY PHE VAL
SEQRES 21 H 271 ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
FORMUL 9 HOH *400(H2 O)
HELIX 1 AA1 ASN A 31 ILE A 34 5 4
HELIX 2 AA2 TRP A 35 PHE A 40 1 6
HELIX 3 AA3 SER A 67 LEU A 82 1 16
HELIX 4 AA4 SER A 93 HIS A 106 1 14
HELIX 5 AA5 GLY A 121 MET A 126 1 6
HELIX 6 AA6 PRO A 127 ASP A 137 1 11
HELIX 7 AA7 ASP A 137 GLU A 147 1 11
HELIX 8 AA8 SER A 151 ARG A 158 1 8
HELIX 9 AA9 PRO A 159 PHE A 169 1 11
HELIX 10 AB1 PRO A 176 ASP A 186 1 11
HELIX 11 AB2 ILE A 195 ILE A 202 5 8
HELIX 12 AB3 THR A 218 ILE A 229 1 12
HELIX 13 AB4 PHE A 243 ARG A 248 1 6
HELIX 14 AB5 ARG A 248 GLY A 258 1 11
HELIX 15 AB6 ASN B 31 ILE B 34 5 4
HELIX 16 AB7 TRP B 35 PHE B 40 1 6
HELIX 17 AB8 SER B 67 LEU B 82 1 16
HELIX 18 AB9 SER B 93 HIS B 106 1 14
HELIX 19 AC1 LEU B 122 MET B 126 5 5
HELIX 20 AC2 GLU B 129 ASP B 137 1 9
HELIX 21 AC3 ASP B 137 GLU B 147 1 11
HELIX 22 AC4 SER B 151 ARG B 158 1 8
HELIX 23 AC5 ARG B 158 VAL B 171 1 14
HELIX 24 AC6 PRO B 176 ASP B 186 1 11
HELIX 25 AC7 ARG B 198 ILE B 202 5 5
HELIX 26 AC8 THR B 218 ILE B 229 1 12
HELIX 27 AC9 PHE B 243 ARG B 248 1 6
HELIX 28 AD1 ARG B 248 VAL B 260 1 13
HELIX 29 AD2 ASN C 31 ILE C 34 5 4
HELIX 30 AD3 TRP C 35 PHE C 40 1 6
HELIX 31 AD4 PRO C 41 THR C 45 5 5
HELIX 32 AD5 SER C 67 LEU C 82 1 16
HELIX 33 AD6 SER C 93 HIS C 106 1 14
HELIX 34 AD7 GLY C 121 MET C 126 5 6
HELIX 35 AD8 PRO C 127 GLU C 129 5 3
HELIX 36 AD9 ALA C 130 ASP C 137 1 8
HELIX 37 AE1 ASP C 137 GLU C 147 1 11
HELIX 38 AE2 SER C 151 ARG C 158 1 8
HELIX 39 AE3 PRO C 159 VAL C 171 1 13
HELIX 40 AE4 PRO C 176 ASP C 186 1 11
HELIX 41 AE5 ILE C 195 ILE C 202 5 8
HELIX 42 AE6 THR C 218 ILE C 229 1 12
HELIX 43 AE7 PHE C 243 ARG C 248 1 6
HELIX 44 AE8 ARG C 248 PHE C 259 1 12
HELIX 45 AE9 ASN D 31 ILE D 34 5 4
HELIX 46 AF1 TRP D 35 ALA D 43 1 9
HELIX 47 AF2 SER D 67 LEU D 82 1 16
HELIX 48 AF3 SER D 93 HIS D 106 1 14
HELIX 49 AF4 LEU D 122 MET D 126 5 5
HELIX 50 AF5 PRO D 127 ASP D 137 1 11
HELIX 51 AF6 ASP D 137 GLU D 147 1 11
HELIX 52 AF7 SER D 151 ARG D 158 1 8
HELIX 53 AF8 PRO D 159 PHE D 169 1 11
HELIX 54 AF9 PRO D 176 ASP D 186 1 11
HELIX 55 AG1 ARG D 198 ILE D 202 5 5
HELIX 56 AG2 THR D 218 ILE D 229 1 12
HELIX 57 AG3 PHE D 243 ARG D 248 1 6
HELIX 58 AG4 ARG D 248 VAL D 260 1 13
HELIX 59 AG5 ASN E 31 ILE E 34 5 4
HELIX 60 AG6 TRP E 35 PHE E 40 1 6
HELIX 61 AG7 SER E 67 LEU E 82 1 16
HELIX 62 AG8 SER E 93 HIS E 106 1 14
HELIX 63 AG9 GLY E 121 MET E 126 1 6
HELIX 64 AH1 PRO E 127 ASP E 137 1 11
HELIX 65 AH2 ASP E 137 GLU E 147 1 11
HELIX 66 AH3 SER E 151 ARG E 158 1 8
HELIX 67 AH4 PRO E 159 VAL E 171 1 13
HELIX 68 AH5 PRO E 176 ASP E 186 1 11
HELIX 69 AH6 ILE E 195 ILE E 202 5 8
HELIX 70 AH7 THR E 218 ILE E 229 1 12
HELIX 71 AH8 PHE E 243 ARG E 248 1 6
HELIX 72 AH9 ARG E 248 GLY E 258 1 11
HELIX 73 AI1 ASN F 31 ILE F 34 5 4
HELIX 74 AI2 TRP F 35 PHE F 40 1 6
HELIX 75 AI3 SER F 67 LEU F 82 1 16
HELIX 76 AI4 SER F 93 HIS F 106 1 14
HELIX 77 AI5 GLY F 121 MET F 126 1 6
HELIX 78 AI6 GLU F 129 ASP F 137 1 9
HELIX 79 AI7 ASP F 137 GLU F 147 1 11
HELIX 80 AI8 SER F 151 ARG F 158 1 8
HELIX 81 AI9 PRO F 159 PHE F 169 1 11
HELIX 82 AJ1 PRO F 176 ASP F 186 1 11
HELIX 83 AJ2 ILE F 195 ILE F 202 5 8
HELIX 84 AJ3 THR F 218 ILE F 229 1 12
HELIX 85 AJ4 PHE F 243 ARG F 248 1 6
HELIX 86 AJ5 ARG F 248 GLY F 258 1 11
HELIX 87 AJ6 ASN G 31 ILE G 34 5 4
HELIX 88 AJ7 TRP G 35 PHE G 40 1 6
HELIX 89 AJ8 PRO G 41 GLN G 44 5 4
HELIX 90 AJ9 SER G 67 LEU G 82 1 16
HELIX 91 AK1 SER G 93 HIS G 106 1 14
HELIX 92 AK2 GLY G 121 MET G 126 5 6
HELIX 93 AK3 PRO G 127 ASP G 137 1 11
HELIX 94 AK4 ASP G 137 GLY G 148 1 12
HELIX 95 AK5 SER G 151 ARG G 158 1 8
HELIX 96 AK6 PRO G 159 VAL G 171 1 13
HELIX 97 AK7 PRO G 176 ASP G 186 1 11
HELIX 98 AK8 ILE G 195 SER G 200 1 6
HELIX 99 AK9 THR G 218 ILE G 229 1 12
HELIX 100 AL1 PHE G 243 ARG G 248 1 6
HELIX 101 AL2 ARG G 248 GLY G 258 1 11
HELIX 102 AL3 ASN H 31 ILE H 34 5 4
HELIX 103 AL4 TRP H 35 PHE H 40 1 6
HELIX 104 AL5 SER H 67 LEU H 82 1 16
HELIX 105 AL6 SER H 93 HIS H 106 1 14
HELIX 106 AL7 GLY H 121 MET H 126 1 6
HELIX 107 AL8 PRO H 127 ASP H 137 1 11
HELIX 108 AL9 ASP H 137 GLY H 148 1 12
HELIX 109 AM1 SER H 151 ARG H 158 1 8
HELIX 110 AM2 ARG H 158 VAL H 171 1 14
HELIX 111 AM3 PRO H 176 ASP H 186 1 11
HELIX 112 AM4 ILE H 195 SER H 200 1 6
HELIX 113 AM5 THR H 218 ASN H 228 1 11
HELIX 114 AM6 PHE H 243 ARG H 248 1 6
HELIX 115 AM7 ARG H 248 GLY H 258 1 11
SHEET 1 AA1 8 HIS A 3 ASN A 6 0
SHEET 2 AA1 8 VAL A 9 TYR A 16 -1 O ILE A 11 N VAL A 4
SHEET 3 AA1 8 HIS A 47 ILE A 51 -1 O VAL A 50 N ASP A 14
SHEET 4 AA1 8 PRO A 21 LEU A 25 1 N PHE A 24 O ILE A 49
SHEET 5 AA1 8 ALA A 87 ASN A 92 1 O VAL A 88 N VAL A 23
SHEET 6 AA1 8 VAL A 110 LEU A 116 1 O LEU A 116 N GLY A 91
SHEET 7 AA1 8 THR A 206 GLY A 211 1 O VAL A 209 N ILE A 115
SHEET 8 AA1 8 GLU A 233 ILE A 237 1 O ILE A 237 N ALA A 210
SHEET 1 AA2 8 HIS B 3 ASN B 6 0
SHEET 2 AA2 8 VAL B 9 TYR B 16 -1 O ILE B 11 N VAL B 4
SHEET 3 AA2 8 HIS B 47 ILE B 51 -1 O VAL B 48 N TYR B 16
SHEET 4 AA2 8 PRO B 21 LEU B 25 1 N ILE B 22 O ILE B 49
SHEET 5 AA2 8 ALA B 87 ASN B 92 1 O VAL B 90 N LEU B 25
SHEET 6 AA2 8 VAL B 110 LEU B 116 1 O LEU B 114 N PHE B 89
SHEET 7 AA2 8 THR B 206 GLY B 211 1 O VAL B 209 N ILE B 115
SHEET 8 AA2 8 GLU B 233 ILE B 237 1 O ILE B 237 N ALA B 210
SHEET 1 AA3 8 HIS C 3 ASN C 6 0
SHEET 2 AA3 8 VAL C 9 TYR C 16 -1 O ILE C 11 N VAL C 4
SHEET 3 AA3 8 HIS C 47 ILE C 51 -1 O VAL C 48 N TYR C 16
SHEET 4 AA3 8 PRO C 21 LEU C 25 1 N ILE C 22 O ILE C 49
SHEET 5 AA3 8 ALA C 87 ASN C 92 1 O VAL C 88 N VAL C 23
SHEET 6 AA3 8 VAL C 110 LEU C 116 1 O LEU C 114 N PHE C 89
SHEET 7 AA3 8 THR C 206 GLY C 211 1 O LEU C 207 N ASN C 113
SHEET 8 AA3 8 GLU C 233 ILE C 237 1 O ILE C 237 N ALA C 210
SHEET 1 AA4 8 HIS D 3 ASN D 6 0
SHEET 2 AA4 8 VAL D 9 TYR D 16 -1 O ILE D 11 N VAL D 4
SHEET 3 AA4 8 ASN D 46 ILE D 51 -1 O VAL D 50 N ASP D 14
SHEET 4 AA4 8 VAL D 20 LEU D 25 1 N ILE D 22 O ILE D 49
SHEET 5 AA4 8 ALA D 87 ASN D 92 1 O VAL D 90 N LEU D 25
SHEET 6 AA4 8 VAL D 110 LEU D 116 1 O LEU D 114 N PHE D 89
SHEET 7 AA4 8 THR D 206 GLY D 211 1 O VAL D 209 N ILE D 115
SHEET 8 AA4 8 GLU D 233 ILE D 237 1 O ILE D 237 N ALA D 210
SHEET 1 AA5 8 HIS E 3 ASN E 6 0
SHEET 2 AA5 8 VAL E 9 TYR E 16 -1 O ILE E 11 N VAL E 4
SHEET 3 AA5 8 HIS E 47 ILE E 51 -1 O VAL E 48 N TYR E 16
SHEET 4 AA5 8 PRO E 21 LEU E 25 1 N ILE E 22 O ILE E 49
SHEET 5 AA5 8 ALA E 87 ASN E 92 1 O VAL E 90 N VAL E 23
SHEET 6 AA5 8 VAL E 110 LEU E 116 1 O LEU E 116 N GLY E 91
SHEET 7 AA5 8 THR E 206 GLY E 211 1 O LEU E 207 N ASN E 113
SHEET 8 AA5 8 GLU E 233 ILE E 237 1 O GLU E 233 N VAL E 208
SHEET 1 AA6 8 HIS F 3 ASN F 6 0
SHEET 2 AA6 8 VAL F 9 TYR F 16 -1 O ILE F 11 N VAL F 4
SHEET 3 AA6 8 HIS F 47 ILE F 51 -1 O VAL F 48 N TYR F 16
SHEET 4 AA6 8 PRO F 21 LEU F 25 1 N ILE F 22 O ILE F 49
SHEET 5 AA6 8 ALA F 87 ASN F 92 1 O VAL F 88 N VAL F 23
SHEET 6 AA6 8 VAL F 110 LEU F 116 1 O LEU F 114 N PHE F 89
SHEET 7 AA6 8 THR F 206 GLY F 211 1 O LEU F 207 N ASN F 113
SHEET 8 AA6 8 GLU F 233 ILE F 237 1 O ILE F 237 N ALA F 210
SHEET 1 AA7 8 HIS G 3 ASN G 6 0
SHEET 2 AA7 8 VAL G 9 TYR G 16 -1 O VAL G 9 N ASN G 6
SHEET 3 AA7 8 ASN G 46 ILE G 51 -1 O VAL G 50 N ASP G 14
SHEET 4 AA7 8 VAL G 20 LEU G 25 1 N ILE G 22 O ILE G 49
SHEET 5 AA7 8 ALA G 87 ASN G 92 1 O VAL G 90 N LEU G 25
SHEET 6 AA7 8 VAL G 110 LEU G 116 1 O LEU G 116 N GLY G 91
SHEET 7 AA7 8 THR G 206 GLY G 211 1 O VAL G 209 N ILE G 115
SHEET 8 AA7 8 GLU G 233 ILE G 237 1 O GLU G 233 N VAL G 208
SHEET 1 AA8 8 HIS H 3 ASN H 6 0
SHEET 2 AA8 8 VAL H 9 TYR H 16 -1 O ILE H 11 N VAL H 4
SHEET 3 AA8 8 HIS H 47 ILE H 51 -1 O VAL H 50 N ASP H 14
SHEET 4 AA8 8 PRO H 21 LEU H 25 1 N PHE H 24 O ILE H 49
SHEET 5 AA8 8 ALA H 87 ASN H 92 1 O VAL H 88 N PRO H 21
SHEET 6 AA8 8 VAL H 110 LEU H 116 1 O LEU H 116 N GLY H 91
SHEET 7 AA8 8 THR H 206 GLY H 211 1 O VAL H 209 N ILE H 115
SHEET 8 AA8 8 GLU H 233 ILE H 237 1 O ILE H 237 N ALA H 210
CISPEP 1 ASN B 238 ASP B 239 0 -21.54
CISPEP 2 GLU C 18 GLY C 19 0 -4.91
CISPEP 3 THR D 64 GLY D 65 0 -4.22
CISPEP 4 THR E 64 GLY E 65 0 -7.43
CISPEP 5 THR F 64 GLY F 65 0 -6.51
CISPEP 6 THR G 64 GLY G 65 0 -6.92
CISPEP 7 THR H 64 GLY H 65 0 -4.19
CRYST1 109.806 78.545 116.472 90.00 99.37 90.00 P 1 21 1 16
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 0.009107 0.000000 0.001503 0.00000
SCALE2 0.000000 0.012732 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008702 0.00000
TER 1984 ALA A 261
TER 3976 ALA B 261
TER 5963 VAL C 260
TER 7944 VAL D 260
TER 9925 VAL E 260
TER 11905 ALA F 261
TER 13856 VAL G 260
TER 15792 PHE H 259
MASTER 471 0 0 115 64 0 0 616184 8 0 168
END
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