| content |
HEADER HYDROLASE 14-JUN-19 6S06
TITLE CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE LINB D147C+L177C MUTANT
TITLE 2 (LINB73) 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;
COMPND 8 MUTATION: 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, PROTEIN ENGINEERING, MUTANT, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.IERMAK,J.R.MESTERS,O.DEGTJARIK,R.CHALOUPKOVA,I.KUTA SMATANOVA
REVDAT 1 15-JUL-20 6S06 0
JRNL AUTH P.HAVLICKOVA,I.IERMAK,O.DEGTJARIK,T.PRUDNIKOVA,J.R.MESTERS,
JRNL AUTH 2 R.CHALOUPKOVA,J.DAMBORSKY,M.KUTY,I.KUTA SMATANOVA
JRNL TITL COMPUTATIONAL AND EXPERIMENTAL DESIGN OF TRANSPORT TUNNEL IN
JRNL TITL 2 HLD LINB73 FROM SPHINGOBIUM JAPONICUM UT26
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL VERSION 2014/7
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2272
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 233
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : NULL
REMARK 3 NUMBER OF RESTRAINTS : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.013
REMARK 3 ANGLE DISTANCES (A) : 205.0
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.004
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 84.00
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 2.000
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.026
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.000
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.046
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : NULL
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: LEAST SQUARES ANISOTROPIC REFINEMENT
REMARK 3 REDUCED FREE R (NO CUTOFF)
REMARK 4
REMARK 4 6S06 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-JUN-19.
REMARK 100 THE DEPOSITION ID IS D_1292102603.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-MAR-14
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 : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918409
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 JANUARY 10, 2014
REMARK 200 DATA SCALING SOFTWARE : XDS JANUARY 10, 2014
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 88614
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.150
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 (%) : 99.6
REMARK 200 DATA REDUNDANCY : 6.210
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.9300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.22
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
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: MOLREP 11.2.08
REMARK 200 STARTING MODEL: 1CV2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 32.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM CHLORIDE, 20% W/V PEG
REMARK 280 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295.0K
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 22.36200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.30700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.35450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.30700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.36200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.35450
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: 310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11000 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 SER A 2
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 LYS A 6 CG CD CE NZ
REMARK 470 LYS A 17 CE NZ
REMARK 470 GLU A 78 CG CD OE1 OE2
REMARK 470 GLU A 94 CG CD OE1 OE2
REMARK 470 GLU A 145 CB CG CD OE1 OE2
REMARK 470 GLN A 146 CB CG CD OE1 NE2
REMARK 470 ARG A 148 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 233 CD OE1 OE2
REMARK 470 ARG A 252 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 292 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 MET A 253 CG - SD - CE ANGL. DEV. = -16.2 DEGREES
REMARK 500 ARG A 291 CD - NE - CZ ANGL. DEV. = 12.1 DEGREES
REMARK 500 ARG A 291 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
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 ASP A 25 86.48 -150.52
REMARK 500 PRO A 39 50.37 -101.10
REMARK 500 THR A 40 -160.45 -103.86
REMARK 500 ASP A 108 -132.99 56.78
REMARK 500 ALA A 247 -69.33 -144.69
REMARK 500 ALA A 271 -100.25 -100.18
REMARK 500
REMARK 500 REMARK: NULL
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 MG A 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 541 O
REMARK 620 2 HOH A 509 O 86.3
REMARK 620 3 HOH A 550 O 176.6 90.4
REMARK 620 4 HOH A 594 O 89.6 88.1 89.1
REMARK 620 5 HOH A 713 O 92.2 91.4 89.1 178.1
REMARK 620 6 HOH A 691 O 88.9 174.5 94.4 94.8 85.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 510 O
REMARK 620 2 HOH A 512 O 89.6
REMARK 620 3 HOH A 536 O 82.5 92.0
REMARK 620 4 HOH A 689 O 170.2 82.5 91.9
REMARK 620 5 HOH A 732 O 84.5 82.8 166.0 100.3
REMARK 620 6 HOH A 705 O 94.9 171.4 95.8 93.7 90.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 404 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 520 O
REMARK 620 2 HOH A 688 O 90.1
REMARK 620 3 HOH A 700 O 88.7 81.0
REMARK 620 4 HOH A 730 O 172.2 92.1 84.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 404
DBREF 6S06 A 1 296 UNP D4Z2G1 LINB_SPHJU 1 296
SEQADV 6S06 CYS A 147 UNP D4Z2G1 ASP 147 ENGINEERED MUTATION
SEQADV 6S06 CYS A 177 UNP D4Z2G1 LEU 177 ENGINEERED MUTATION
SEQADV 6S06 HIS A 297 UNP D4Z2G1 EXPRESSION TAG
SEQADV 6S06 HIS A 298 UNP D4Z2G1 EXPRESSION TAG
SEQADV 6S06 HIS A 299 UNP D4Z2G1 EXPRESSION TAG
SEQADV 6S06 HIS A 300 UNP D4Z2G1 EXPRESSION TAG
SEQADV 6S06 HIS A 301 UNP D4Z2G1 EXPRESSION TAG
SEQADV 6S06 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 CYS 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 CYS 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 HIS 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 CL A 401 1
HET MG A 402 1
HET MG A 403 1
HET MG A 404 1
HETNAM CL CHLORIDE ION
HETNAM MG MAGNESIUM ION
FORMUL 2 CL CL 1-
FORMUL 3 MG 3(MG 2+)
FORMUL 6 HOH *233(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 GLN A 146 5 3
HELIX 7 AA7 CYS A 147 SER A 156 1 10
HELIX 8 AA8 ALA A 158 GLN A 165 1 8
HELIX 9 AA9 ASN A 167 GLN A 172 1 6
HELIX 10 AB1 GLN A 172 CYS A 177 1 6
HELIX 11 AB2 SER A 183 GLU A 192 1 10
HELIX 12 AB3 PRO A 193 LEU A 195 5 3
HELIX 13 AB4 GLY A 198 ALA A 200 5 3
HELIX 14 AB5 ARG A 201 ILE A 211 1 11
HELIX 15 AB6 PRO A 217 SER A 232 1 16
HELIX 16 AB7 THR A 250 ARG A 258 1 9
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 11 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 103 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 ILE A 241 N TYR A 130
SHEET 8 AA1 8 GLN A 263 GLY A 270 1 O THR A 264 N PHE A 240
LINK MG MG A 402 O HOH A 541 1555 1555 2.10
LINK MG MG A 403 O HOH A 510 1555 1555 2.26
LINK MG MG A 403 O HOH A 512 1555 1555 2.20
LINK MG MG A 403 O HOH A 536 1555 1555 2.01
LINK MG MG A 404 O HOH A 520 1555 1555 1.98
LINK MG MG A 404 O HOH A 688 1555 1555 2.09
LINK MG MG A 404 O HOH A 700 1555 1555 2.23
LINK MG MG A 402 O HOH A 509 1555 4545 2.14
LINK MG MG A 402 O HOH A 550 1555 4545 2.04
LINK MG MG A 402 O HOH A 594 1555 4545 2.11
LINK MG MG A 402 O HOH A 713 1555 4545 2.10
LINK MG MG A 402 O HOH A 691 1555 4545 2.08
LINK MG MG A 403 O HOH A 689 1555 3544 2.20
LINK MG MG A 403 O HOH A 732 1555 1455 2.22
LINK MG MG A 403 O HOH A 705 1555 3544 2.05
LINK MG MG A 404 O HOH A 730 1555 4455 2.12
CISPEP 1 ASN A 38 PRO A 39 0 -11.47
CISPEP 2 ASP A 73 PRO A 74 0 17.43
CISPEP 3 THR A 216 PRO A 217 0 -5.66
CISPEP 4 GLU A 244 PRO A 245 0 -1.14
SITE 1 AC1 3 ASN A 38 TRP A 109 PRO A 208
SITE 1 AC2 6 HOH A 509 HOH A 541 HOH A 550 HOH A 594
SITE 2 AC2 6 HOH A 691 HOH A 713
SITE 1 AC3 6 HOH A 510 HOH A 512 HOH A 536 HOH A 689
SITE 2 AC3 6 HOH A 705 HOH A 732
SITE 1 AC4 4 HOH A 520 HOH A 688 HOH A 700 HOH A 730
CRYST1 44.724 68.709 80.614 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 0.022359 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014554 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012405 0.00000
TER 2295 ALA A 296
MASTER 308 0 4 18 8 0 6 6 2509 1 10 24
END |