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HEADER HYDROLASE 09-MAR-20 6Y9G
TITLE CRYSTAL STRUCTURE OF PUTATIVE ANCESTRAL HALOALKANE DEHALOGENASE
TITLE 2 ANCHLD5 (NODE 5)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANCESTRAL HALOALKANE DEHALOGENASE ANCHLD5;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 3 ORGANISM_TAXID: 32630;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HALOALKANE DEHALOGENASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.CHALOUPKOVA,J.DAMBORSKY,M.MAREK
REVDAT 1 18-NOV-20 6Y9G 0
JRNL AUTH P.BABKOVA,Z.DUNAJOVA,R.CHALOUPKOVA,J.DAMBORSKY,D.BEDNAR,
JRNL AUTH 2 M.MAREK
JRNL TITL STRUCTURES OF HYPERSTABLE ANCESTRAL HALOALKANE DEHALOGENASES
JRNL TITL 2 SHOW RESTRICTED CONFORMATIONAL DYNAMICS.
JRNL REF COMPUT STRUCT BIOTECHNOL J V. 18 1497 2020
JRNL REFN ISSN 2001-0370
JRNL PMID 32637047
JRNL DOI 10.1016/J.CSBJ.2020.06.021
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14-3260
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.99
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 50921
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 2528
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 39.9880 - 4.5795 0.97 2746 131 0.1885 0.2047
REMARK 3 2 4.5795 - 3.6357 0.97 2675 148 0.1644 0.1874
REMARK 3 3 3.6357 - 3.1763 0.98 2680 152 0.1710 0.1939
REMARK 3 4 3.1763 - 2.8860 0.99 2718 133 0.1838 0.2062
REMARK 3 5 2.8860 - 2.6792 0.99 2704 137 0.1884 0.2219
REMARK 3 6 2.6792 - 2.5213 1.00 2730 131 0.1822 0.2188
REMARK 3 7 2.5213 - 2.3950 1.00 2671 164 0.1829 0.2425
REMARK 3 8 2.3950 - 2.2908 1.00 2706 130 0.1809 0.2294
REMARK 3 9 2.2908 - 2.2026 0.99 2687 137 0.1793 0.2154
REMARK 3 10 2.2026 - 2.1266 1.00 2700 161 0.1686 0.2136
REMARK 3 11 2.1266 - 2.0601 1.00 2661 163 0.1818 0.2299
REMARK 3 12 2.0601 - 2.0012 1.00 2722 130 0.1825 0.2506
REMARK 3 13 2.0012 - 1.9485 1.00 2701 132 0.1784 0.2032
REMARK 3 14 1.9485 - 1.9010 0.99 2682 136 0.2013 0.2540
REMARK 3 15 1.9010 - 1.8578 0.99 2722 140 0.1994 0.2575
REMARK 3 16 1.8578 - 1.8182 1.00 2682 147 0.2200 0.2731
REMARK 3 17 1.8182 - 1.7819 1.00 2702 141 0.2361 0.2896
REMARK 3 18 1.7819 - 1.7482 0.93 2504 115 0.2710 0.2779
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.780
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.01
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6Y9G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-MAR-20.
REMARK 100 THE DEPOSITION ID IS D_1292106785.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50947
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.748
REMARK 200 RESOLUTION RANGE LOW (A) : 47.060
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4K2A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, MAGNESIUM CHLORIDE, TRIS
REMARK 280 BASE, PH 8.5, 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 25.68250
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 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 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 THR A 3
REMARK 465 GLN A 4
REMARK 465 ILE A 5
REMARK 465 SER A 6
REMARK 465 ALA A 7
REMARK 465 GLU A 8
REMARK 465 PHE A 9
REMARK 465 ASN A 166
REMARK 465 MET A 167
REMARK 465 SER A 297
REMARK 465 SER A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
REMARK 465 HIS A 302
REMARK 465 HIS A 303
REMARK 465 HIS A 304
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 THR B 3
REMARK 465 GLN B 4
REMARK 465 ILE B 5
REMARK 465 SER B 6
REMARK 465 ALA B 7
REMARK 465 GLU B 8
REMARK 465 PHE B 9
REMARK 465 SER B 295
REMARK 465 ARG B 296
REMARK 465 SER B 297
REMARK 465 SER B 298
REMARK 465 HIS B 299
REMARK 465 HIS B 300
REMARK 465 HIS B 301
REMARK 465 HIS B 302
REMARK 465 HIS B 303
REMARK 465 HIS B 304
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 21 -158.00 -120.24
REMARK 500 PRO A 41 55.15 -103.73
REMARK 500 THR A 42 -159.36 -107.80
REMARK 500 ASP A 105 -131.73 59.06
REMARK 500 LEU A 163 -78.26 -84.92
REMARK 500 GLU A 164 48.53 -72.37
REMARK 500 ALA A 245 -73.88 -145.64
REMARK 500 LEU A 271 -143.61 -116.02
REMARK 500 PHE B 11 140.83 65.84
REMARK 500 SER B 21 -151.59 -119.06
REMARK 500 PRO B 41 52.83 -108.69
REMARK 500 THR B 42 -156.87 -103.27
REMARK 500 ASP B 105 -129.55 56.05
REMARK 500 LYS B 171 -46.89 -130.29
REMARK 500 ALA B 245 -77.53 -146.28
REMARK 500 LEU B 271 -109.40 -108.85
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6Y9G A 1 304 PDB 6Y9G 6Y9G 1 304
DBREF 6Y9G B 1 304 PDB 6Y9G 6Y9G 1 304
SEQRES 1 A 304 MET SER THR GLN ILE SER ALA GLU PHE PRO PHE GLU ARG
SEQRES 2 A 304 ARG HIS VAL GLU VAL LEU GLY SER THR MET HIS TYR VAL
SEQRES 3 A 304 GLU THR GLY GLU GLY PRO PRO VAL LEU PHE LEU HIS GLY
SEQRES 4 A 304 ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE PRO
SEQRES 5 A 304 HIS VAL ALA ASP HIS GLY ARG CYS ILE ALA PRO ASP LEU
SEQRES 6 A 304 ILE GLY MET GLY GLN SER GLY LYS PRO ASP ILE ASP TYR
SEQRES 7 A 304 ARG PHE ALA ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE
SEQRES 8 A 304 ASP ALA LEU GLY LEU ASP ASP VAL THR LEU VAL VAL HIS
SEQRES 9 A 304 ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA ARG ARG
SEQRES 10 A 304 HIS PRO ASP ARG VAL LYS GLY ILE ALA PHE MET GLU ALA
SEQRES 11 A 304 ILE VAL ARG PRO MET PRO SER TRP ASP ASP PHE PRO PRO
SEQRES 12 A 304 GLN ALA ARG GLU LEU PHE GLN ALA LEU ARG THR PRO GLY
SEQRES 13 A 304 VAL GLY GLU LYS MET ILE LEU GLU GLN ASN MET PHE ILE
SEQRES 14 A 304 GLU LYS ILE LEU PRO GLY SER VAL LEU ARG PRO LEU SER
SEQRES 15 A 304 GLU GLU GLU MET ASP ALA TYR ARG ALA PRO PHE PRO THR
SEQRES 16 A 304 PRO GLU SER ARG LYS PRO VAL LEU GLN TRP PRO ARG GLU
SEQRES 17 A 304 LEU PRO ILE ASP GLY GLU PRO ALA ASP VAL VAL ALA ILE
SEQRES 18 A 304 VAL GLU ALA TYR ALA GLU TRP LEU ALA THR SER ASP VAL
SEQRES 19 A 304 PRO LYS LEU LEU PHE TYR ALA GLU PRO GLY ALA LEU ILE
SEQRES 20 A 304 SER PRO GLU GLN VAL GLU TRP CYS ARG GLU ASN LEU PRO
SEQRES 21 A 304 ASN LEU GLU VAL VAL HIS VAL GLY PRO GLY LEU HIS PHE
SEQRES 22 A 304 LEU GLN GLU ASP GLN PRO ASP ALA ILE GLY GLN ALA ILE
SEQRES 23 A 304 ALA ASP TRP LEU GLN ARG LEU ALA SER ARG SER SER HIS
SEQRES 24 A 304 HIS HIS HIS HIS HIS
SEQRES 1 B 304 MET SER THR GLN ILE SER ALA GLU PHE PRO PHE GLU ARG
SEQRES 2 B 304 ARG HIS VAL GLU VAL LEU GLY SER THR MET HIS TYR VAL
SEQRES 3 B 304 GLU THR GLY GLU GLY PRO PRO VAL LEU PHE LEU HIS GLY
SEQRES 4 B 304 ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE PRO
SEQRES 5 B 304 HIS VAL ALA ASP HIS GLY ARG CYS ILE ALA PRO ASP LEU
SEQRES 6 B 304 ILE GLY MET GLY GLN SER GLY LYS PRO ASP ILE ASP TYR
SEQRES 7 B 304 ARG PHE ALA ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE
SEQRES 8 B 304 ASP ALA LEU GLY LEU ASP ASP VAL THR LEU VAL VAL HIS
SEQRES 9 B 304 ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA ARG ARG
SEQRES 10 B 304 HIS PRO ASP ARG VAL LYS GLY ILE ALA PHE MET GLU ALA
SEQRES 11 B 304 ILE VAL ARG PRO MET PRO SER TRP ASP ASP PHE PRO PRO
SEQRES 12 B 304 GLN ALA ARG GLU LEU PHE GLN ALA LEU ARG THR PRO GLY
SEQRES 13 B 304 VAL GLY GLU LYS MET ILE LEU GLU GLN ASN MET PHE ILE
SEQRES 14 B 304 GLU LYS ILE LEU PRO GLY SER VAL LEU ARG PRO LEU SER
SEQRES 15 B 304 GLU GLU GLU MET ASP ALA TYR ARG ALA PRO PHE PRO THR
SEQRES 16 B 304 PRO GLU SER ARG LYS PRO VAL LEU GLN TRP PRO ARG GLU
SEQRES 17 B 304 LEU PRO ILE ASP GLY GLU PRO ALA ASP VAL VAL ALA ILE
SEQRES 18 B 304 VAL GLU ALA TYR ALA GLU TRP LEU ALA THR SER ASP VAL
SEQRES 19 B 304 PRO LYS LEU LEU PHE TYR ALA GLU PRO GLY ALA LEU ILE
SEQRES 20 B 304 SER PRO GLU GLN VAL GLU TRP CYS ARG GLU ASN LEU PRO
SEQRES 21 B 304 ASN LEU GLU VAL VAL HIS VAL GLY PRO GLY LEU HIS PHE
SEQRES 22 B 304 LEU GLN GLU ASP GLN PRO ASP ALA ILE GLY GLN ALA ILE
SEQRES 23 B 304 ALA ASP TRP LEU GLN ARG LEU ALA SER ARG SER SER HIS
SEQRES 24 B 304 HIS HIS HIS HIS HIS
FORMUL 3 HOH *176(H2 O)
HELIX 1 AA1 SER A 43 ARG A 48 5 6
HELIX 2 AA2 ILE A 50 ALA A 55 1 6
HELIX 3 AA3 ARG A 79 GLY A 95 1 17
HELIX 4 AA4 ASP A 105 HIS A 118 1 14
HELIX 5 AA5 SER A 137 PHE A 141 5 5
HELIX 6 AA6 PRO A 142 ARG A 153 1 12
HELIX 7 AA7 GLY A 156 LEU A 163 1 8
HELIX 8 AA8 ILE A 169 SER A 176 1 8
HELIX 9 AA9 SER A 182 ALA A 191 1 10
HELIX 10 AB1 PRO A 196 SER A 198 5 3
HELIX 11 AB2 ARG A 199 GLU A 208 1 10
HELIX 12 AB3 PRO A 215 SER A 232 1 18
HELIX 13 AB4 SER A 248 LEU A 259 1 12
HELIX 14 AB5 PHE A 273 ASP A 277 5 5
HELIX 15 AB6 GLN A 278 SER A 295 1 18
HELIX 16 AB7 SER B 43 ARG B 48 5 6
HELIX 17 AB8 ILE B 50 ALA B 55 1 6
HELIX 18 AB9 ARG B 79 GLY B 95 1 17
HELIX 19 AC1 ASP B 105 HIS B 118 1 14
HELIX 20 AC2 SER B 137 PHE B 141 5 5
HELIX 21 AC3 PRO B 142 GLN B 144 5 3
HELIX 22 AC4 ALA B 145 ARG B 153 1 9
HELIX 23 AC5 GLY B 156 LEU B 163 1 8
HELIX 24 AC6 ASN B 166 LYS B 171 1 6
HELIX 25 AC7 LYS B 171 SER B 176 1 6
HELIX 26 AC8 SER B 182 ALA B 191 1 10
HELIX 27 AC9 PRO B 196 SER B 198 5 3
HELIX 28 AD1 ARG B 199 LEU B 209 1 11
HELIX 29 AD2 PRO B 215 SER B 232 1 18
HELIX 30 AD3 SER B 248 LEU B 259 1 12
HELIX 31 AD4 PHE B 273 ASP B 277 5 5
HELIX 32 AD5 GLN B 278 ALA B 294 1 17
SHEET 1 AA1 8 GLU A 12 VAL A 18 0
SHEET 2 AA1 8 SER A 21 THR A 28 -1 O SER A 21 N VAL A 18
SHEET 3 AA1 8 ARG A 59 PRO A 63 -1 O CYS A 60 N THR A 28
SHEET 4 AA1 8 PRO A 33 LEU A 37 1 N VAL A 34 O ILE A 61
SHEET 5 AA1 8 VAL A 99 HIS A 104 1 O VAL A 102 N LEU A 35
SHEET 6 AA1 8 VAL A 122 MET A 128 1 O LYS A 123 N VAL A 99
SHEET 7 AA1 8 LYS A 236 PRO A 243 1 O LEU A 237 N PHE A 127
SHEET 8 AA1 8 LEU A 262 GLY A 270 1 O GLU A 263 N LEU A 238
SHEET 1 AA2 8 GLU B 12 VAL B 18 0
SHEET 2 AA2 8 SER B 21 THR B 28 -1 O SER B 21 N VAL B 18
SHEET 3 AA2 8 ARG B 59 PRO B 63 -1 O CYS B 60 N THR B 28
SHEET 4 AA2 8 PRO B 33 LEU B 37 1 N VAL B 34 O ILE B 61
SHEET 5 AA2 8 VAL B 99 HIS B 104 1 O THR B 100 N LEU B 35
SHEET 6 AA2 8 VAL B 122 MET B 128 1 O LYS B 123 N VAL B 99
SHEET 7 AA2 8 LYS B 236 PRO B 243 1 O LEU B 237 N PHE B 127
SHEET 8 AA2 8 LEU B 262 GLY B 270 1 O GLU B 263 N LEU B 238
CISPEP 1 ASN A 40 PRO A 41 0 -7.01
CISPEP 2 GLU A 214 PRO A 215 0 -8.32
CISPEP 3 GLU A 242 PRO A 243 0 1.17
CISPEP 4 ASN B 40 PRO B 41 0 -1.84
CISPEP 5 GLU B 214 PRO B 215 0 -1.97
CISPEP 6 GLU B 242 PRO B 243 0 0.79
CRYST1 63.871 51.365 78.419 90.00 94.07 90.00 P 1 21 1 4
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 0.015657 0.000000 0.001113 0.00000
SCALE2 0.000000 0.019469 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012784 0.00000
TER 2281 ARG A 296
TER 4554 ALA B 294
MASTER 281 0 0 32 16 0 0 6 4721 2 0 48
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