| content |
HEADER HYDROLASE 10-MAR-23 8OE6
TITLE STRUCTURE OF HYPERSTABLE HALOALKANE DEHALOGENASE VARIANT DHAA231
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STRUCTURE OF HYPERSTABLE HALOALKANE DEHALOGENASE VARIANT
COMPND 3 DHAA231;
COMPND 4 CHAIN: A;
COMPND 5 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 ENGINEERED HALOALKANE DEHALOGENASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MAREK
REVDAT 1 17-JAN-24 8OE6 0
JRNL AUTH A.KUNKA,S.M.MARQUES,M.HAVLASEK,M.VASINA,N.VELATOVA,
JRNL AUTH 2 L.CENGELOVA,D.KOVAR,J.DAMBORSKY,M.MAREK,D.BEDNAR,Z.PROKOP
JRNL TITL ADVANCING ENZYME'S STABILITY AND CATALYTIC EFFICIENCY
JRNL TITL 2 THROUGH SYNERGY OF FORCE-FIELD CALCULATIONS, EVOLUTIONARY
JRNL TITL 3 ANALYSIS, AND MACHINE LEARNING.
JRNL REF ACS CATALYSIS V. 13 12506 2023
JRNL REFN ESSN 2155-5435
JRNL PMID 37822856
JRNL DOI 10.1021/ACSCATAL.3C02575
REMARK 2
REMARK 2 RESOLUTION. 1.31 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1-4487
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) : 1.31
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.48
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 90120
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.155
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.168
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.930
REMARK 3 FREE R VALUE TEST SET COUNT : 4440
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 45.4800 - 4.0542 1.00 3110 155 0.1497 0.1744
REMARK 3 2 4.0542 - 3.2182 1.00 3000 137 0.1430 0.1481
REMARK 3 3 3.2182 - 2.8115 1.00 2929 168 0.1540 0.1467
REMARK 3 4 2.8115 - 2.5545 1.00 2927 160 0.1543 0.1726
REMARK 3 5 2.5545 - 2.3714 1.00 2886 176 0.1545 0.1626
REMARK 3 6 2.3714 - 2.2316 1.00 2898 142 0.1514 0.1738
REMARK 3 7 2.2316 - 2.1198 1.00 2899 137 0.1471 0.1563
REMARK 3 8 2.1198 - 2.0275 1.00 2897 150 0.1465 0.1552
REMARK 3 9 2.0275 - 1.9495 1.00 2893 133 0.1491 0.1699
REMARK 3 10 1.9495 - 1.8822 1.00 2874 156 0.1444 0.1745
REMARK 3 11 1.8822 - 1.8234 1.00 2894 149 0.1484 0.1742
REMARK 3 12 1.8234 - 1.7712 1.00 2855 146 0.1456 0.1579
REMARK 3 13 1.7712 - 1.7246 1.00 2874 130 0.1458 0.1758
REMARK 3 14 1.7246 - 1.6825 1.00 2893 149 0.1446 0.1495
REMARK 3 15 1.6825 - 1.6443 1.00 2834 164 0.1418 0.1528
REMARK 3 16 1.6443 - 1.6093 1.00 2843 168 0.1404 0.1631
REMARK 3 17 1.6093 - 1.5771 1.00 2847 148 0.1395 0.1876
REMARK 3 18 1.5771 - 1.5473 1.00 2865 144 0.1465 0.1339
REMARK 3 19 1.5473 - 1.5197 1.00 2872 162 0.1505 0.1685
REMARK 3 20 1.5197 - 1.4939 1.00 2853 130 0.1568 0.1860
REMARK 3 21 1.4939 - 1.4698 1.00 2826 155 0.1662 0.1823
REMARK 3 22 1.4698 - 1.4472 1.00 2871 134 0.1786 0.2000
REMARK 3 23 1.4472 - 1.4259 1.00 2849 126 0.1814 0.2201
REMARK 3 24 1.4259 - 1.4058 1.00 2892 143 0.2045 0.2398
REMARK 3 25 1.4058 - 1.3868 1.00 2791 159 0.2208 0.2527
REMARK 3 26 1.3868 - 1.3688 1.00 2881 129 0.2497 0.2718
REMARK 3 27 1.3688 - 1.3517 0.98 2746 148 0.2599 0.2950
REMARK 3 28 1.3517 - 1.3354 0.97 2743 160 0.2798 0.2629
REMARK 3 29 1.3354 - 1.3199 0.94 2687 137 0.2937 0.2858
REMARK 3 30 1.3199 - 1.3100 0.88 2451 145 0.3187 0.3187
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) : 16.880
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.015 2525
REMARK 3 ANGLE : 1.366 3456
REMARK 3 CHIRALITY : 0.102 352
REMARK 3 PLANARITY : 0.012 456
REMARK 3 DIHEDRAL : 8.323 1528
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): 6.2308 -5.3269 -15.8813
REMARK 3 T TENSOR
REMARK 3 T11: 0.1423 T22: 0.1433
REMARK 3 T33: 0.1441 T12: -0.0041
REMARK 3 T13: -0.0094 T23: 0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 1.0885 L22: 1.0571
REMARK 3 L33: 1.2745 L12: -0.1084
REMARK 3 L13: 0.1939 L23: -0.4865
REMARK 3 S TENSOR
REMARK 3 S11: -0.0125 S12: 0.0263 S13: 0.0994
REMARK 3 S21: 0.0375 S22: -0.0308 S23: -0.0307
REMARK 3 S31: -0.1137 S32: 0.0685 S33: 0.0362
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 8OE6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-MAR-23.
REMARK 100 THE DEPOSITION ID IS D_1292129113.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-OCT-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.999
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 90219
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.310
REMARK 200 RESOLUTION RANGE LOW (A) : 45.480
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 11.70
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.31
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.33
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 : 1.100
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MAGNESIUM CHLORIDE, TRIS, PEG 8000, PH
REMARK 280 7, 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 22.21550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.18950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.99900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.18950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.21550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.99900
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 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 GLU A 3
REMARK 465 HIS A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
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 ARG A 80 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 146 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 146 NE - CZ - NH2 ANGL. DEV. = -3.5 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 PRO A 9 58.87 -90.28
REMARK 500 PRO A 42 45.88 -106.39
REMARK 500 THR A 43 -160.32 -103.70
REMARK 500 GLU A 98 -88.74 -105.18
REMARK 500 ASP A 106 -133.79 56.39
REMARK 500 VAL A 245 -77.22 -124.38
REMARK 500 LEU A 271 -96.79 -117.19
REMARK 500 ASN A 278 66.17 -150.03
REMARK 500 LEU A 293 8.59 -63.90
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 809 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH A 810 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH A 811 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH A 812 DISTANCE = 6.23 ANGSTROMS
REMARK 525 HOH A 813 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH A 814 DISTANCE = 6.57 ANGSTROMS
REMARK 525 HOH A 815 DISTANCE = 6.95 ANGSTROMS
REMARK 525 HOH A 816 DISTANCE = 7.44 ANGSTROMS
REMARK 525 HOH A 817 DISTANCE = 8.57 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 MG A 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 495 O
REMARK 620 2 HOH A 542 O 91.1
REMARK 620 3 HOH A 606 O 91.1 177.6
REMARK 620 4 HOH A 632 O 177.2 87.5 90.3
REMARK 620 5 HOH A 732 O 86.6 91.6 89.5 91.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 434 O
REMARK 620 2 HOH A 450 O 90.3
REMARK 620 3 HOH A 462 O 90.4 88.6
REMARK 620 4 HOH A 700 O 88.0 178.1 90.5
REMARK 620 5 HOH A 731 O 174.0 95.1 92.4 86.6
REMARK 620 6 HOH A 801 O 87.2 87.5 175.4 93.3 90.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 303 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 419 O
REMARK 620 2 HOH A 547 O 89.2
REMARK 620 3 HOH A 552 O 78.0 96.1
REMARK 620 4 HOH A 612 O 87.3 176.2 81.7
REMARK 620 5 HOH A 662 O 86.7 86.0 164.5 95.4
REMARK 620 6 HOH A 804 O 172.2 92.1 94.2 91.1 101.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 304 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 692 O
REMARK 620 2 HOH A 709 O 87.3
REMARK 620 3 HOH A 743 O 90.2 88.8
REMARK 620 4 HOH A 775 O 94.1 71.7 159.8
REMARK 620 5 HOH A 803 O 87.1 167.9 101.9 98.0
REMARK 620 N 1 2 3 4
DBREF 8OE6 A 1 299 PDB 8OE6 8OE6 1 299
SEQRES 1 A 299 MET SER GLU ILE GLY THR SER PHE PRO PHE ASP PRO HIS
SEQRES 2 A 299 TYR VAL GLU VAL LEU GLY SER ARG MET HIS TYR VAL ASP
SEQRES 3 A 299 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 A 299 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE
SEQRES 5 A 299 PRO HIS VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 A 299 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP
SEQRES 7 A 299 TYR ARG PHE GLU ASP HIS VAL ARG TYR LEU ASP ALA PHE
SEQRES 8 A 299 ILE GLU ALA LEU GLY LEU GLU ASP VAL VAL LEU VAL ILE
SEQRES 9 A 299 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA ARG
SEQRES 10 A 299 ARG ASN PRO GLU ARG VAL ARG GLY ILE ALA PHE MET GLU
SEQRES 11 A 299 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU
SEQRES 12 A 299 PHE ALA ARG GLU LEU PHE LYS ALA PHE ARG THR PRO GLY
SEQRES 13 A 299 VAL GLY ARG LYS MET ILE ILE GLU GLN ASN MET PHE ILE
SEQRES 14 A 299 GLU GLN ILE LEU PRO ALA PHE VAL VAL ARG PRO LEU THR
SEQRES 15 A 299 GLU GLU GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS
SEQRES 16 A 299 PRO GLU TRP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 A 299 LEU PRO ILE ALA GLY GLU PRO ALA ASP VAL TRP ALA LEU
SEQRES 18 A 299 VAL GLU ALA TYR MET ARG TRP LEU HIS GLN SER PRO VAL
SEQRES 19 A 299 PRO LYS LEU LEU PHE TRP GLY GLU PRO GLY VAL LEU ILE
SEQRES 20 A 299 PRO PRO GLU GLU ALA GLU ARG CYS ARG GLU SER LEU PRO
SEQRES 21 A 299 ASN LEU LYS THR VAL PHE ILE GLY PRO GLY LEU HIS TYR
SEQRES 22 A 299 LEU GLN GLU ASP ASN PRO ASP GLU ILE GLY SER GLU ILE
SEQRES 23 A 299 ALA ARG TRP LEU PRO ALA LEU HIS HIS HIS HIS HIS HIS
HET MG A 301 1
HET MG A 302 1
HET MG A 303 1
HET MG A 304 1
HET CL A 305 1
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
FORMUL 2 MG 4(MG 2+)
FORMUL 6 CL CL 1-
FORMUL 7 HOH *417(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 ALA A 145 ARG A 153 1 9
HELIX 7 AA7 GLY A 156 ILE A 163 1 8
HELIX 8 AA8 ASN A 166 GLN A 171 1 6
HELIX 9 AA9 GLN 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 ASN A 278 1 6
HELIX 17 AB8 ASN A 278 LEU A 290 1 13
HELIX 18 AB9 PRO A 291 HIS A 294 5 4
SHEET 1 AA1 8 HIS A 13 VAL A 17 0
SHEET 2 AA1 8 SER A 20 VAL A 27 -1 O MET A 22 N VAL A 15
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 VAL A 35 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
LINK MG MG A 301 O HOH A 495 1555 1555 2.00
LINK MG MG A 301 O HOH A 542 1555 1555 2.08
LINK MG MG A 301 O HOH A 606 1555 1555 2.01
LINK MG MG A 301 O HOH A 632 1555 1555 2.06
LINK MG MG A 301 O HOH A 732 1555 1555 2.04
LINK MG MG A 302 O HOH A 434 1555 1555 2.08
LINK MG MG A 302 O HOH A 450 1555 1555 2.06
LINK MG MG A 302 O HOH A 462 1555 1555 2.00
LINK MG MG A 302 O HOH A 700 1555 1555 2.12
LINK MG MG A 302 O HOH A 731 1555 1555 2.10
LINK MG MG A 302 O HOH A 801 1555 1555 2.07
LINK MG MG A 303 O HOH A 419 1555 1555 2.22
LINK MG MG A 303 O HOH A 547 1555 1555 2.10
LINK MG MG A 303 O HOH A 552 1555 1555 2.30
LINK MG MG A 303 O HOH A 612 1555 1555 1.91
LINK MG MG A 303 O HOH A 662 1555 1555 2.01
LINK MG MG A 303 O HOH A 804 1555 1555 2.10
LINK MG MG A 304 O HOH A 692 1555 1555 2.10
LINK MG MG A 304 O HOH A 709 1555 1555 2.32
LINK MG MG A 304 O HOH A 743 1555 1655 2.08
LINK MG MG A 304 O HOH A 775 1555 1555 2.15
LINK MG MG A 304 O HOH A 803 1555 1555 2.02
CISPEP 1 ASN A 41 PRO A 42 0 -1.86
CISPEP 2 GLU A 214 PRO A 215 0 -4.30
CISPEP 3 GLU A 242 PRO A 243 0 5.60
CRYST1 44.431 67.998 122.379 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 0.022507 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014706 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008171 0.00000
TER 2433 HIS A 294
MASTER 360 0 5 18 8 0 0 6 2821 1 28 23
END |