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HEADER HYDROLASE 30-AUG-19 6SP5
TITLE STRUCTURE OF HYPERSTABLE HALOALKANE DEHALOGENASE VARIANT DHAA115
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS RHODOCHROUS;
SOURCE 3 ORGANISM_TAXID: 1829;
SOURCE 4 GENE: DHAA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HALOALKANE DEHALOGENASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.CHMELOVA,K.MARKOVA,J.DAMBORSKY,M.MAREK
REVDAT 1 18-NOV-20 6SP5 0
JRNL AUTH K.MARKOVA,K.CHMELOVA,S.M.MARQUES,P.CARPENTIER,D.BEDNAR,
JRNL AUTH 2 J.DAMBORSKY,M.MAREK
JRNL TITL DECODING THE INTRICATE NETWORK OF MOLECULAR INTERACTIONS OF
JRNL TITL 2 A HYPERSTABLE ENGINEERED BIOCATALYST
JRNL REF CHEM SCI 2020
JRNL REFN ESSN 2041-6539
JRNL DOI 10.1039/D0SC03367G
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.07
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 99049
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.178
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880
REMARK 3 FREE R VALUE TEST SET COUNT : 4830
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 48.0740 - 4.9699 0.96 3209 154 0.1590 0.1708
REMARK 3 2 4.9699 - 3.9453 0.99 3233 158 0.1279 0.1355
REMARK 3 3 3.9453 - 3.4468 0.99 3210 179 0.1460 0.1521
REMARK 3 4 3.4468 - 3.1317 0.98 3149 155 0.1540 0.1817
REMARK 3 5 3.1317 - 2.9073 0.95 3045 169 0.1643 0.1867
REMARK 3 6 2.9073 - 2.7359 0.99 3140 190 0.1614 0.1863
REMARK 3 7 2.7359 - 2.5989 0.99 3179 154 0.1635 0.1726
REMARK 3 8 2.5989 - 2.4857 0.99 3164 175 0.1584 0.1756
REMARK 3 9 2.4857 - 2.3900 0.99 3209 141 0.1557 0.1774
REMARK 3 10 2.3900 - 2.3076 0.99 3183 155 0.1474 0.1674
REMARK 3 11 2.3076 - 2.2354 1.00 3219 150 0.1519 0.1800
REMARK 3 12 2.2354 - 2.1715 0.99 3152 152 0.1531 0.1921
REMARK 3 13 2.1715 - 2.1144 0.95 3033 153 0.1578 0.1663
REMARK 3 14 2.1144 - 2.0628 0.97 3106 159 0.1483 0.1804
REMARK 3 15 2.0628 - 2.0159 0.99 3135 164 0.1561 0.1985
REMARK 3 16 2.0159 - 1.9730 0.99 3167 151 0.1483 0.1830
REMARK 3 17 1.9730 - 1.9335 0.99 3171 172 0.1531 0.1743
REMARK 3 18 1.9335 - 1.8970 0.99 3121 162 0.1521 0.2029
REMARK 3 19 1.8970 - 1.8631 0.99 3145 183 0.1538 0.1822
REMARK 3 20 1.8631 - 1.8316 0.99 3156 166 0.1590 0.1893
REMARK 3 21 1.8316 - 1.8020 0.99 3127 175 0.1622 0.2093
REMARK 3 22 1.8020 - 1.7743 0.99 3169 148 0.1725 0.1950
REMARK 3 23 1.7743 - 1.7482 0.99 3114 171 0.1761 0.2098
REMARK 3 24 1.7482 - 1.7236 0.98 3184 164 0.1876 0.2082
REMARK 3 25 1.7236 - 1.7003 0.98 3150 162 0.1951 0.2213
REMARK 3 26 1.7003 - 1.6782 0.95 2977 153 0.2061 0.2452
REMARK 3 27 1.6782 - 1.6572 0.96 3094 159 0.2145 0.2242
REMARK 3 28 1.6572 - 1.6372 0.97 3068 165 0.2272 0.2383
REMARK 3 29 1.6372 - 1.6182 0.98 3122 144 0.2429 0.2303
REMARK 3 30 1.6182 - 1.6000 0.97 3088 147 0.2729 0.2962
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) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.590
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.10
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 : 0.006 5078
REMARK 3 ANGLE : 0.844 6955
REMARK 3 CHIRALITY : 0.057 719
REMARK 3 PLANARITY : 0.007 906
REMARK 3 DIHEDRAL : 7.368 4105
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 6SP5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-AUG-19.
REMARK 100 THE DEPOSITION ID IS D_1292104088.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUL-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.860999
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.6.2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 99102
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 48.074
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : 0.63200
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: 4HZG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, POTASSIUM ISOTHIOCYANATE, BIS
REMARK 280 -TRIS PROPANE, 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 34.06050
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 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 PRO A 9 56.40 -91.95
REMARK 500 ASP A 31 -168.73 -114.26
REMARK 500 PRO A 42 50.36 -107.24
REMARK 500 THR A 43 -158.39 -105.43
REMARK 500 SER A 44 -168.58 -161.96
REMARK 500 GLU A 98 -87.32 -106.14
REMARK 500 ASP A 106 -133.10 55.48
REMARK 500 ASP A 156 -56.34 72.31
REMARK 500 VAL A 245 -72.38 -131.01
REMARK 500 LEU A 271 -96.81 -110.34
REMARK 500 PRO B 9 58.10 -92.89
REMARK 500 ASP B 31 -166.54 -118.60
REMARK 500 PRO B 42 50.52 -106.94
REMARK 500 THR B 43 -159.28 -103.64
REMARK 500 SER B 44 -169.64 -160.53
REMARK 500 GLU B 98 -88.23 -105.81
REMARK 500 ASP B 106 -133.08 53.04
REMARK 500 ASP B 156 -53.23 68.82
REMARK 500 VAL B 245 -69.94 -128.29
REMARK 500 LEU B 271 -93.90 -112.77
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 B 676 DISTANCE = 6.30 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue B3P A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue B3P B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN B 305
DBREF 6SP5 A 3 293 UNP P0A3G2 DHAA_RHORH 3 293
DBREF 6SP5 B 3 293 UNP P0A3G2 DHAA_RHORH 3 293
SEQADV 6SP5 SER A 20 UNP P0A3G2 GLU 20 CONFLICT
SEQADV 6SP5 ARG A 80 UNP P0A3G2 PHE 80 CONFLICT
SEQADV 6SP5 PHE A 128 UNP P0A3G2 CYS 128 CONFLICT
SEQADV 6SP5 LEU A 148 UNP P0A3G2 THR 148 CONFLICT
SEQADV 6SP5 PRO A 155 UNP P0A3G2 ALA 155 CONFLICT
SEQADV 6SP5 ILE A 172 UNP P0A3G2 ALA 172 CONFLICT
SEQADV 6SP5 PHE A 176 UNP P0A3G2 CYS 176 CONFLICT
SEQADV 6SP5 TRP A 198 UNP P0A3G2 ASP 198 CONFLICT
SEQADV 6SP5 TRP A 219 UNP P0A3G2 VAL 219 CONFLICT
SEQADV 6SP5 LEU A 262 UNP P0A3G2 CYS 262 CONFLICT
SEQADV 6SP5 PHE A 266 UNP P0A3G2 ASP 266 CONFLICT
SEQADV 6SP5 SER B 20 UNP P0A3G2 GLU 20 CONFLICT
SEQADV 6SP5 ARG B 80 UNP P0A3G2 PHE 80 CONFLICT
SEQADV 6SP5 PHE B 128 UNP P0A3G2 CYS 128 CONFLICT
SEQADV 6SP5 LEU B 148 UNP P0A3G2 THR 148 CONFLICT
SEQADV 6SP5 PRO B 155 UNP P0A3G2 ALA 155 CONFLICT
SEQADV 6SP5 ILE B 172 UNP P0A3G2 ALA 172 CONFLICT
SEQADV 6SP5 PHE B 176 UNP P0A3G2 CYS 176 CONFLICT
SEQADV 6SP5 TRP B 198 UNP P0A3G2 ASP 198 CONFLICT
SEQADV 6SP5 TRP B 219 UNP P0A3G2 VAL 219 CONFLICT
SEQADV 6SP5 LEU B 262 UNP P0A3G2 CYS 262 CONFLICT
SEQADV 6SP5 PHE B 266 UNP P0A3G2 ASP 266 CONFLICT
SEQRES 1 A 291 GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 2 A 291 GLU VAL LEU GLY SER ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 3 A 291 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 4 A 291 PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE PRO HIS
SEQRES 5 A 291 VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 6 A 291 GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP TYR ARG
SEQRES 7 A 291 PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE GLU
SEQRES 8 A 291 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 9 A 291 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 10 A 291 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 11 A 291 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 12 A 291 ARG GLU LEU PHE GLN ALA PHE ARG THR PRO ASP VAL GLY
SEQRES 13 A 291 ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE GLU GLY
SEQRES 14 A 291 ILE LEU PRO LYS PHE VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 15 A 291 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS PRO VAL
SEQRES 16 A 291 TRP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 17 A 291 ILE ALA GLY GLU PRO ALA ASN ILE TRP ALA LEU VAL GLU
SEQRES 18 A 291 ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 19 A 291 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 20 A 291 ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO ASN LEU
SEQRES 21 A 291 LYS THR VAL PHE ILE GLY PRO GLY LEU HIS TYR LEU GLN
SEQRES 22 A 291 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 23 A 291 TRP LEU PRO ALA LEU
SEQRES 1 B 291 GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 2 B 291 GLU VAL LEU GLY SER ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 3 B 291 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 4 B 291 PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE PRO HIS
SEQRES 5 B 291 VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 6 B 291 GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP TYR ARG
SEQRES 7 B 291 PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE GLU
SEQRES 8 B 291 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 9 B 291 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 10 B 291 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 11 B 291 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 12 B 291 ARG GLU LEU PHE GLN ALA PHE ARG THR PRO ASP VAL GLY
SEQRES 13 B 291 ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE GLU GLY
SEQRES 14 B 291 ILE LEU PRO LYS PHE VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 15 B 291 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS PRO VAL
SEQRES 16 B 291 TRP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 17 B 291 ILE ALA GLY GLU PRO ALA ASN ILE TRP ALA LEU VAL GLU
SEQRES 18 B 291 ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 19 B 291 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 20 B 291 ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO ASN LEU
SEQRES 21 B 291 LYS THR VAL PHE ILE GLY PRO GLY LEU HIS TYR LEU GLN
SEQRES 22 B 291 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 23 B 291 TRP LEU PRO ALA LEU
HET B3P A 301 19
HET SCN A 302 3
HET SCN A 303 3
HET SCN A 304 3
HET B3P B 301 19
HET GOL B 302 6
HET SCN B 303 3
HET SCN B 304 3
HET SCN B 305 3
HETNAM B3P 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-
HETNAM 2 B3P PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM SCN THIOCYANATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 B3P 2(C11 H26 N2 O6)
FORMUL 4 SCN 6(C N S 1-)
FORMUL 8 GOL C3 H8 O3
FORMUL 12 HOH *564(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 GLY A 171 1 6
HELIX 9 AA9 GLY 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 LEU A 209 1 11
HELIX 14 AB5 PRO A 215 SER A 232 1 18
HELIX 15 AB6 PRO A 248 LEU A 259 1 12
HELIX 16 AB7 TYR A 273 ASP A 277 5 5
HELIX 17 AB8 ASN A 278 LEU A 290 1 13
HELIX 18 AB9 PRO A 291 LEU A 293 5 3
HELIX 19 AC1 SER B 44 ARG B 49 5 6
HELIX 20 AC2 ILE B 51 ALA B 56 1 6
HELIX 21 AC3 ARG B 80 LEU B 95 1 16
HELIX 22 AC4 ASP B 106 ASN B 119 1 14
HELIX 23 AC5 THR B 137 TRP B 141 5 5
HELIX 24 AC6 PRO B 142 ARG B 153 1 12
HELIX 25 AC7 ASP B 156 ILE B 163 1 8
HELIX 26 AC8 ASN B 166 GLY B 171 1 6
HELIX 27 AC9 GLY B 171 PHE B 176 1 6
HELIX 28 AD1 THR B 182 GLU B 191 1 10
HELIX 29 AD2 PRO B 192 LEU B 194 5 3
HELIX 30 AD3 LYS B 195 TRP B 198 5 4
HELIX 31 AD4 ARG B 199 LEU B 209 1 11
HELIX 32 AD5 PRO B 215 SER B 232 1 18
HELIX 33 AD6 PRO B 248 LEU B 259 1 12
HELIX 34 AD7 TYR B 273 ASN B 278 1 6
HELIX 35 AD8 ASN B 278 LEU B 290 1 13
HELIX 36 AD9 PRO B 291 LEU B 293 5 3
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 ALA B 127 N LEU B 102
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 LYS B 263 N LEU B 238
CISPEP 1 ASN A 41 PRO A 42 0 -4.14
CISPEP 2 GLU A 214 PRO A 215 0 -3.55
CISPEP 3 THR A 242 PRO A 243 0 6.17
CISPEP 4 ASN B 41 PRO B 42 0 -4.83
CISPEP 5 GLU B 214 PRO B 215 0 -4.04
CISPEP 6 THR B 242 PRO B 243 0 6.90
SITE 1 AC1 12 ASP A 76 LEU A 77 ASP A 78 GLU A 200
SITE 2 AC1 12 ARG A 204 HOH A 401 HOH A 419 HOH A 424
SITE 3 AC1 12 HOH A 435 HOH A 519 HOH A 561 HOH A 566
SITE 1 AC2 6 ASN A 41 ASP A 106 TRP A 107 PHE A 168
SITE 2 AC2 6 PHE A 205 PRO A 206
SITE 1 AC3 1 HOH A 510
SITE 1 AC4 1 PRO A 269
SITE 1 AC5 11 ASP B 76 LEU B 77 ASP B 78 GLU B 200
SITE 2 AC5 11 ARG B 204 HOH B 401 HOH B 422 HOH B 433
SITE 3 AC5 11 HOH B 443 HOH B 453 HOH B 532
SITE 1 AC6 5 LYS B 74 GLU B 191 TRP B 198 HOH B 413
SITE 2 AC6 5 HOH B 558
SITE 1 AC7 2 HIS B 13 TYR B 14
SITE 1 AC8 2 PRO B 53 HOH B 522
SITE 1 AC9 5 ASN B 41 ASP B 106 TRP B 107 PHE B 205
SITE 2 AC9 5 PRO B 206
CRYST1 70.188 68.121 83.916 90.00 104.82 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 0.014247 0.000000 0.003770 0.00000
SCALE2 0.000000 0.014680 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012327 0.00000
TER 2426 LEU A 293
TER 4839 LEU B 293
MASTER 302 0 9 36 16 0 16 6 5364 2 62 46
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