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HEADER HYDROLASE 08-FEB-21 7NFZ
TITLE CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE LINB57 MUTANT (H272F)
TITLE 2 FROM SPHINGOBIUM JAPONICUM UT26
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 1,3,4,6-TETRACHLORO-1,4-CYCLOHEXADIENE HALIDOHYDROLASE,4-
COMPND 5 TCDN HALIDOHYDROLASE;
COMPND 6 EC: 3.8.1.5;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPHINGOBIUM JAPONICUM (STRAIN DSM 16413 / CCM
SOURCE 3 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S);
SOURCE 4 ORGANISM_TAXID: 452662;
SOURCE 5 STRAIN: DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 /
SOURCE 6 UT26S;
SOURCE 7 GENE: LINB, SJA_C1-19590;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HALOALKANE DEHALOGENASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MAREK
REVDAT 1 02-MAR-22 7NFZ 0
JRNL AUTH M.MAREK,J.DAMBORSKY
JRNL TITL CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE LINB57 MUTANT
JRNL TITL 2 (H272F) FROM SPHINGOBIUM JAPONICUM UT26
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.1-4122
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) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 44602
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.860
REMARK 3 FREE R VALUE TEST SET COUNT : 2168
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 44.7180 - 3.8245 1.00 3026 172 0.1689 0.1594
REMARK 3 2 3.8245 - 3.0359 1.00 2895 163 0.1370 0.1717
REMARK 3 3 3.0359 - 2.6522 1.00 2878 144 0.1492 0.1593
REMARK 3 4 2.6522 - 2.4097 1.00 2879 134 0.1558 0.1950
REMARK 3 5 2.4097 - 2.2370 1.00 2829 145 0.1503 0.1865
REMARK 3 6 2.2370 - 2.1051 1.00 2844 147 0.1461 0.1814
REMARK 3 7 2.1051 - 1.9997 1.00 2822 138 0.1515 0.1858
REMARK 3 8 1.9997 - 1.9126 1.00 2820 137 0.1603 0.2147
REMARK 3 9 1.9126 - 1.8390 0.99 2810 145 0.1845 0.2382
REMARK 3 10 1.8390 - 1.7755 0.99 2757 161 0.1820 0.2320
REMARK 3 11 1.7755 - 1.7200 0.99 2796 142 0.1903 0.1955
REMARK 3 12 1.7200 - 1.6708 0.99 2760 156 0.1926 0.2304
REMARK 3 13 1.6708 - 1.6269 0.99 2791 128 0.2097 0.2618
REMARK 3 14 1.6269 - 1.5872 0.98 2784 128 0.2318 0.2985
REMARK 3 15 1.5872 - 1.5511 0.98 2743 128 0.2588 0.2655
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) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.880
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.80
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 : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -19.0822 -0.1855 4.1442
REMARK 3 T TENSOR
REMARK 3 T11: 0.0801 T22: 0.0671
REMARK 3 T33: 0.0801 T12: 0.0039
REMARK 3 T13: 0.0004 T23: -0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 0.3358 L22: 0.3794
REMARK 3 L33: 1.0134 L12: -0.0547
REMARK 3 L13: -0.1567 L23: 0.0878
REMARK 3 S TENSOR
REMARK 3 S11: -0.0232 S12: 0.0004 S13: -0.0253
REMARK 3 S21: 0.0252 S22: -0.0037 S23: 0.0132
REMARK 3 S31: 0.2144 S32: -0.0071 S33: -0.0235
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 7NFZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-FEB-21.
REMARK 100 THE DEPOSITION ID IS D_1292113883.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAY-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 10.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44672
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 45.090
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 13.50
REMARK 200 R MERGE (I) : 0.19300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.90700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.400
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: 1MJ5
REMARK 200
REMARK 200 REMARK: PLATE-LIKE SHAPE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM DI-HYDROGEN PHOSPHATE, DI
REMARK 280 -POTASSIUM HYDROGEN PHOSPHATE, LITHIUM SULPHATE, CAPS, PH 10.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 25.74800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.08550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.72400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.08550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.74800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.72400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: 3090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 20.0 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 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 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
REMARK 465 HIS A 302
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 10 CB CG CD OE1 OE2
REMARK 470 ASP A 73 CG OD1 OD2
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 3 -169.53 -76.59
REMARK 500 PRO A 39 45.16 -103.18
REMARK 500 THR A 40 -160.21 -102.25
REMARK 500 TYR A 80 33.49 74.00
REMARK 500 ASP A 97 62.45 60.49
REMARK 500 ASP A 108 -132.53 60.25
REMARK 500 GLN A 172 -50.13 -125.04
REMARK 500 ALA A 271 -95.57 -104.33
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 A 745 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH A 746 DISTANCE = 8.72 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 410 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 2 O
REMARK 620 2 SER A 2 OG 70.5
REMARK 620 3 LEU A 3 O 65.7 70.3
REMARK 620 4 ASN A 47 OD1 74.3 140.4 79.1
REMARK 620 5 HOH A 619 O 130.6 149.9 134.4 69.3
REMARK 620 6 HOH A 652 O 66.7 84.4 131.2 98.1 86.3
REMARK 620 7 HOH A 710 O 141.0 104.8 76.2 91.2 72.6 152.3
REMARK 620 N 1 2 3 4 5 6
DBREF 7NFZ A 1 296 UNP D4Z2G1 LINB_SPHJU 1 296
SEQADV 7NFZ PHE A 272 UNP D4Z2G1 HIS 272 ENGINEERED MUTATION
SEQADV 7NFZ HIS A 297 UNP D4Z2G1 EXPRESSION TAG
SEQADV 7NFZ HIS A 298 UNP D4Z2G1 EXPRESSION TAG
SEQADV 7NFZ HIS A 299 UNP D4Z2G1 EXPRESSION TAG
SEQADV 7NFZ HIS A 300 UNP D4Z2G1 EXPRESSION TAG
SEQADV 7NFZ HIS A 301 UNP D4Z2G1 EXPRESSION TAG
SEQADV 7NFZ HIS A 302 UNP D4Z2G1 EXPRESSION TAG
SEQRES 1 A 302 MET SER LEU GLY ALA LYS PRO PHE GLY GLU LYS LYS PHE
SEQRES 2 A 302 ILE GLU ILE LYS GLY ARG ARG MET ALA TYR ILE ASP GLU
SEQRES 3 A 302 GLY THR GLY ASP PRO ILE LEU PHE GLN HIS GLY ASN PRO
SEQRES 4 A 302 THR SER SER TYR LEU TRP ARG ASN ILE MET PRO HIS CYS
SEQRES 5 A 302 ALA GLY LEU GLY ARG LEU ILE ALA CYS ASP LEU ILE GLY
SEQRES 6 A 302 MET GLY ASP SER ASP LYS LEU ASP PRO SER GLY PRO GLU
SEQRES 7 A 302 ARG TYR ALA TYR ALA GLU HIS ARG ASP TYR LEU ASP ALA
SEQRES 8 A 302 LEU TRP GLU ALA LEU ASP LEU GLY ASP ARG VAL VAL LEU
SEQRES 9 A 302 VAL VAL HIS ASP TRP GLY SER ALA LEU GLY PHE ASP TRP
SEQRES 10 A 302 ALA ARG ARG HIS ARG GLU ARG VAL GLN GLY ILE ALA TYR
SEQRES 11 A 302 MET GLU ALA ILE ALA MET PRO ILE GLU TRP ALA ASP PHE
SEQRES 12 A 302 PRO GLU GLN ASP ARG ASP LEU PHE GLN ALA PHE ARG SER
SEQRES 13 A 302 GLN ALA GLY GLU GLU LEU VAL LEU GLN ASP ASN VAL PHE
SEQRES 14 A 302 VAL GLU GLN VAL LEU PRO GLY LEU ILE LEU ARG PRO LEU
SEQRES 15 A 302 SER GLU ALA GLU MET ALA ALA TYR ARG GLU PRO PHE LEU
SEQRES 16 A 302 ALA ALA GLY GLU ALA ARG ARG PRO THR LEU SER TRP PRO
SEQRES 17 A 302 ARG GLN ILE PRO ILE ALA GLY THR PRO ALA ASP VAL VAL
SEQRES 18 A 302 ALA ILE ALA ARG ASP TYR ALA GLY TRP LEU SER GLU SER
SEQRES 19 A 302 PRO ILE PRO LYS LEU PHE ILE ASN ALA GLU PRO GLY ALA
SEQRES 20 A 302 LEU THR THR GLY ARG MET ARG ASP PHE CYS ARG THR TRP
SEQRES 21 A 302 PRO ASN GLN THR GLU ILE THR VAL ALA GLY ALA PHE PHE
SEQRES 22 A 302 ILE GLN GLU ASP SER PRO ASP GLU ILE GLY ALA ALA ILE
SEQRES 23 A 302 ALA ALA PHE VAL ARG ARG LEU ARG PRO ALA HIS HIS HIS
SEQRES 24 A 302 HIS HIS HIS
HET CXS A 401 14
HET CXS A 402 28
HET CXS A 403 14
HET CXS A 404 14
HET GOL A 405 6
HET GOL A 406 6
HET GOL A 407 6
HET TRS A 408 8
HET PO4 A 409 5
HET K A 410 1
HETNAM CXS 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID
HETNAM GOL GLYCEROL
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM PO4 PHOSPHATE ION
HETNAM K POTASSIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN TRS TRIS BUFFER
FORMUL 2 CXS 4(C9 H19 N O3 S)
FORMUL 6 GOL 3(C3 H8 O3)
FORMUL 9 TRS C4 H12 N O3 1+
FORMUL 10 PO4 O4 P 3-
FORMUL 11 K K 1+
FORMUL 12 HOH *246(H2 O)
HELIX 1 AA1 SER A 41 ARG A 46 5 6
HELIX 2 AA2 ILE A 48 ALA A 53 5 6
HELIX 3 AA3 ALA A 81 LEU A 96 1 16
HELIX 4 AA4 ASP A 108 HIS A 121 1 14
HELIX 5 AA5 GLU A 139 PHE A 143 5 5
HELIX 6 AA6 PRO A 144 ARG A 155 1 12
HELIX 7 AA7 ALA A 158 GLN A 165 1 8
HELIX 8 AA8 ASN A 167 GLN A 172 1 6
HELIX 9 AA9 GLN A 172 LEU A 177 1 6
HELIX 10 AB1 SER A 183 GLU A 192 1 10
HELIX 11 AB2 PRO A 193 LEU A 195 5 3
HELIX 12 AB3 GLY A 198 ALA A 200 5 3
HELIX 13 AB4 ARG A 201 TRP A 207 1 7
HELIX 14 AB5 PRO A 208 ILE A 211 5 4
HELIX 15 AB6 PRO A 217 SER A 234 1 18
HELIX 16 AB7 GLY A 251 ARG A 258 1 8
HELIX 17 AB8 PHE A 273 ASP A 277 5 5
HELIX 18 AB9 SER A 278 ARG A 294 1 17
SHEET 1 AA1 8 LYS A 12 ILE A 16 0
SHEET 2 AA1 8 ARG A 19 GLU A 26 -1 O ARG A 19 N ILE A 16
SHEET 3 AA1 8 ARG A 57 CYS A 61 -1 O LEU A 58 N GLU A 26
SHEET 4 AA1 8 PRO A 31 GLN A 35 1 N PHE A 34 O ILE A 59
SHEET 5 AA1 8 VAL A 102 HIS A 107 1 O VAL A 105 N LEU A 33
SHEET 6 AA1 8 VAL A 125 MET A 131 1 O ALA A 129 N LEU A 104
SHEET 7 AA1 8 LYS A 238 PRO A 245 1 O LEU A 239 N TYR A 130
SHEET 8 AA1 8 GLN A 263 GLY A 270 1 O THR A 264 N PHE A 240
LINK O SER A 2 K K A 410 1555 1555 2.87
LINK OG SER A 2 K K A 410 1555 1555 2.84
LINK O LEU A 3 K K A 410 1555 1555 2.94
LINK OD1 ASN A 47 K K A 410 1555 1555 2.69
LINK K K A 410 O HOH A 619 1555 1555 3.27
LINK K K A 410 O HOH A 652 1555 1555 2.96
LINK K K A 410 O HOH A 710 1555 1555 2.95
CISPEP 1 ASN A 38 PRO A 39 0 -6.88
CISPEP 2 ASP A 73 PRO A 74 0 -1.69
CISPEP 3 THR A 216 PRO A 217 0 -7.08
CISPEP 4 GLU A 244 PRO A 245 0 4.38
CRYST1 51.496 65.448 90.171 90.00 90.00 90.00 P 21 21 21 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 0.019419 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015279 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011090 0.00000
TER 2400 PRO A 295
MASTER 300 0 10 18 8 0 0 6 2649 1 110 24
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