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HEADER HYDROLASE 09-MAR-20 6Y9F
TITLE CRYSTAL STRUCTURE OF PUTATIVE ANCESTRAL HALOALKANE DEHALOGENASE
TITLE 2 ANCHLD3 (NODE 3)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANCESTRAL HALOALKANE DEHALOGENASE ANCHLD3;
COMPND 3 CHAIN: A;
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 6Y9F 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. 1.26 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.18.1-3865
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) : 1.26
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 61.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 92503
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.148
REMARK 3 R VALUE (WORKING SET) : 0.147
REMARK 3 FREE R VALUE : 0.169
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 4591
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 61.8520 - 3.9148 1.00 3317 158 0.1619 0.1803
REMARK 3 2 3.9148 - 3.1073 1.00 3062 180 0.1431 0.1567
REMARK 3 3 3.1073 - 2.7145 1.00 3054 156 0.1692 0.1920
REMARK 3 4 2.7145 - 2.4663 1.00 2995 156 0.1667 0.1875
REMARK 3 5 2.4663 - 2.2895 1.00 2970 175 0.1455 0.1634
REMARK 3 6 2.2895 - 2.1546 1.00 2971 157 0.1303 0.1484
REMARK 3 7 2.1546 - 2.0466 1.00 2937 159 0.1257 0.1257
REMARK 3 8 2.0466 - 1.9575 1.00 2957 163 0.1242 0.1524
REMARK 3 9 1.9575 - 1.8822 1.00 2929 138 0.1217 0.1620
REMARK 3 10 1.8822 - 1.8172 1.00 2924 172 0.1248 0.1449
REMARK 3 11 1.8172 - 1.7604 1.00 2956 153 0.1198 0.1520
REMARK 3 12 1.7604 - 1.7101 1.00 2886 172 0.1171 0.1437
REMARK 3 13 1.7101 - 1.6651 1.00 2922 146 0.1130 0.1333
REMARK 3 14 1.6651 - 1.6244 1.00 2923 140 0.1113 0.1577
REMARK 3 15 1.6244 - 1.5875 1.00 2891 156 0.1127 0.1448
REMARK 3 16 1.5875 - 1.5537 1.00 2928 155 0.1112 0.1311
REMARK 3 17 1.5537 - 1.5226 1.00 2919 126 0.1145 0.1435
REMARK 3 18 1.5226 - 1.4939 1.00 2943 131 0.1221 0.1748
REMARK 3 19 1.4939 - 1.4672 1.00 2880 164 0.1332 0.1648
REMARK 3 20 1.4672 - 1.4423 1.00 2914 134 0.1384 0.1913
REMARK 3 21 1.4423 - 1.4191 1.00 2898 148 0.1440 0.1640
REMARK 3 22 1.4191 - 1.3972 1.00 2906 148 0.1417 0.1849
REMARK 3 23 1.3972 - 1.3767 1.00 2846 157 0.1472 0.2080
REMARK 3 24 1.3767 - 1.3573 1.00 2892 168 0.1663 0.2076
REMARK 3 25 1.3573 - 1.3390 1.00 2906 145 0.1780 0.2003
REMARK 3 26 1.3390 - 1.3216 1.00 2846 144 0.1965 0.2384
REMARK 3 27 1.3216 - 1.3050 0.99 2912 151 0.2181 0.2652
REMARK 3 28 1.3050 - 1.2893 0.99 2854 142 0.2440 0.2804
REMARK 3 29 1.2893 - 1.2743 0.98 2770 136 0.2581 0.3208
REMARK 3 30 1.2743 - 1.2600 0.97 2804 161 0.2886 0.2909
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) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.590
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.80
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 6Y9F 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_1292107180.
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 : 9.5
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 : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 92642
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.260
REMARK 200 RESOLUTION RANGE LOW (A) : 61.852
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 17.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 25.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.26
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.29
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 (%): 49.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE TRIBASIC, CHES, PH 9.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 150.50667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 75.25333
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 112.88000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 37.62667
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 188.13333
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 150.50667
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 75.25333
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 37.62667
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 112.88000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 188.13333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 9.0 KCAL/MOL
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 532 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 726 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 771 LIES ON A SPECIAL POSITION.
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 ALA A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 294
REMARK 465 ALA A 295
REMARK 465 SER A 296
REMARK 465 ARG A 297
REMARK 465 THR A 298
REMARK 465 ALA A 299
REMARK 465 GLU A 300
REMARK 465 ALA A 301
REMARK 465 HIS A 302
REMARK 465 HIS A 303
REMARK 465 HIS A 304
REMARK 465 HIS A 305
REMARK 465 HIS A 306
REMARK 465 HIS A 307
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 LEU A 15 -120.07 50.58
REMARK 500 SER A 17 -153.82 -153.12
REMARK 500 PRO A 39 55.08 -109.56
REMARK 500 THR A 40 -154.35 -102.25
REMARK 500 GLN A 95 -103.13 -120.04
REMARK 500 ASP A 103 -137.14 59.10
REMARK 500 HIS A 139 -168.08 63.99
REMARK 500 ALA A 244 -73.33 -138.68
REMARK 500 LEU A 270 -124.12 -117.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NHE A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NHE A 401
DBREF 6Y9F A 1 307 PDB 6Y9F 6Y9F 1 307
SEQRES 1 A 307 MET SER ALA ALA ALA ALA ILE GLU ARG ARG HIS VAL ALA
SEQRES 2 A 307 VAL LEU ASP SER THR MET SER TYR VAL GLU THR GLY ALA
SEQRES 3 A 307 SER ASP GLY PRO THR VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 A 307 THR SER SER TYR ILE TRP ARG ASN ILE ILE PRO HIS VAL
SEQRES 5 A 307 ALA PRO LEU GLY ARG CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 6 A 307 PHE GLY GLN SER GLY LYS PRO ASP ILE ASP TYR ARG PHE
SEQRES 7 A 307 PHE ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE ASP ALA
SEQRES 8 A 307 LEU GLY ILE GLN ASP VAL VAL LEU VAL ALA GLN ASP TRP
SEQRES 9 A 307 GLY THR ALA LEU ALA PHE HIS LEU ALA ALA ARG ARG PRO
SEQRES 10 A 307 ASP ARG VAL ARG GLY LEU ALA PHE MET GLU PHE ILE ARG
SEQRES 11 A 307 PRO MET PRO THR TRP ASP ASP PHE HIS GLN ARG PRO GLN
SEQRES 12 A 307 ALA ARG GLU MET PHE LYS ALA PHE ARG THR PRO GLY VAL
SEQRES 13 A 307 GLY GLU LYS MET ILE LEU GLU ASP ASN VAL PHE VAL GLU
SEQRES 14 A 307 LYS VAL LEU PRO GLY SER VAL LEU ARG THR LEU SER GLU
SEQRES 15 A 307 GLU GLU MET ALA VAL TYR ARG ALA PRO PHE PRO THR PRO
SEQRES 16 A 307 GLU SER ARG LYS PRO VAL LEU ARG PHE PRO ARG GLU LEU
SEQRES 17 A 307 PRO ILE GLU GLY GLU PRO ALA ASP VAL ALA ALA ILE LEU
SEQRES 18 A 307 GLU SER ALA HIS ARG ALA LEU ALA ALA SER THR TYR PRO
SEQRES 19 A 307 LYS LEU LEU PHE ALA GLY ASP PRO GLY ALA LEU ILE SER
SEQRES 20 A 307 PRO GLN ALA ALA GLU ARG PHE ALA ALA ASN LEU LYS ASN
SEQRES 21 A 307 CYS ARG LEU ILE ASN LEU GLY PRO GLY LEU HIS TYR LEU
SEQRES 22 A 307 GLN GLU ASP HIS PRO ASP ALA ILE GLY ARG THR ILE ALA
SEQRES 23 A 307 GLY TRP LEU PRO GLU ILE ALA ALA ALA SER ARG THR ALA
SEQRES 24 A 307 GLU ALA HIS HIS HIS HIS HIS HIS
HET NHE A 400 13
HET NHE A 401 13
HETNAM NHE 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID
HETSYN NHE N-CYCLOHEXYLTAURINE; CHES
FORMUL 2 NHE 2(C8 H17 N O3 S)
FORMUL 4 HOH *271(H2 O)
HELIX 1 AA1 SER A 41 ARG A 46 5 6
HELIX 2 AA2 ILE A 48 ALA A 53 1 6
HELIX 3 AA3 ARG A 77 GLY A 93 1 17
HELIX 4 AA4 ASP A 103 ARG A 116 1 14
HELIX 5 AA5 THR A 134 PHE A 138 5 5
HELIX 6 AA6 ARG A 141 ARG A 152 1 12
HELIX 7 AA7 GLY A 155 LEU A 162 1 8
HELIX 8 AA8 ASN A 165 LYS A 170 1 6
HELIX 9 AA9 LYS A 170 SER A 175 1 6
HELIX 10 AB1 SER A 181 ALA A 190 1 10
HELIX 11 AB2 PRO A 195 SER A 197 5 3
HELIX 12 AB3 ARG A 198 LEU A 208 1 11
HELIX 13 AB4 PRO A 214 SER A 231 1 18
HELIX 14 AB5 SER A 247 LEU A 258 1 12
HELIX 15 AB6 TYR A 272 HIS A 277 1 6
HELIX 16 AB7 HIS A 277 ALA A 293 1 17
SHEET 1 AA1 8 GLU A 8 VAL A 14 0
SHEET 2 AA1 8 SER A 17 GLU A 23 -1 O TYR A 21 N ARG A 10
SHEET 3 AA1 8 ARG A 57 PRO A 61 -1 O ALA A 60 N VAL A 22
SHEET 4 AA1 8 THR A 31 LEU A 35 1 N VAL A 32 O ARG A 57
SHEET 5 AA1 8 VAL A 97 GLN A 102 1 O VAL A 100 N LEU A 35
SHEET 6 AA1 8 VAL A 120 MET A 126 1 O ARG A 121 N VAL A 97
SHEET 7 AA1 8 LYS A 235 PRO A 242 1 O LEU A 236 N PHE A 125
SHEET 8 AA1 8 CYS A 261 GLY A 269 1 O ILE A 264 N LEU A 237
CISPEP 1 ASN A 38 PRO A 39 0 -5.24
CISPEP 2 GLU A 213 PRO A 214 0 -2.07
CISPEP 3 ASP A 241 PRO A 242 0 7.35
SITE 1 AC1 11 ASN A 38 ASP A 103 TRP A 104 PHE A 148
SITE 2 AC1 11 PHE A 167 VAL A 171 PHE A 204 PRO A 205
SITE 3 AC1 11 LEU A 208 HIS A 271 TYR A 272
SITE 1 AC2 6 ILE A 7 VAL A 22 SER A 42 ARG A 46
SITE 2 AC2 6 ILE A 49 HOH A 530
CRYST1 71.420 71.420 225.760 90.00 90.00 120.00 P 65 2 2 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 0.014002 0.008084 0.000000 0.00000
SCALE2 0.000000 0.016168 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004429 0.00000
TER 2317 ALA A 293
MASTER 324 0 2 16 8 0 5 6 2559 1 26 24
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