5z7w-pdb | HEADER HYDROLASE 30-JAN-18 5Z7W
TITLE CRYSTAL STRUCTURE OF STRIGA HERMONTHICA HTL1 (SHHTL1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOSENSITIVE TO LIGHT 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HYDROLASE, ALPHA/BETA FOLD FAMILY PROTEIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STRIGA HERMONTHICA;
SOURCE 3 ORGANISM_COMMON: PURPLE WITCHWEED;
SOURCE 4 ORGANISM_TAXID: 68872;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS HYDROLASE ACTIVITY, PUTATIVE RECEPTOR OF KARRIKIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.XU,T.MIYAKAWA,A.NAKAMURA,M.TANOKURA
REVDAT 1 29-AUG-18 5Z7W 0
JRNL AUTH Y.XU,T.MIYAKAWA,S.NOSAKI,A.NAKAMURA,Y.LYU,H.NAKAMURA,U.OHTO,
JRNL AUTH 2 H.ISHIDA,T.SHIMIZU,T.ASAMI,M.TANOKURA
JRNL TITL COMPREHENSIVE STRUCTURAL STUDIES REVEAL EVOLUTION OF
JRNL TITL 2 STRIGOLACTONE/KARRIKIN SELECTIVITY OF HTL AND D14 PROTEINS
JRNL TITL 3 IN STRIGA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.66 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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) : 1.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.95
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 127260
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 6415
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 38.9640 - 5.1450 1.00 4080 197 0.1654 0.2051
REMARK 3 2 5.1450 - 4.0851 1.00 4045 218 0.1382 0.1604
REMARK 3 3 4.0851 - 3.5692 1.00 4019 244 0.1418 0.1678
REMARK 3 4 3.5692 - 3.2430 1.00 4048 219 0.1507 0.1836
REMARK 3 5 3.2430 - 3.0107 1.00 4082 186 0.1495 0.1640
REMARK 3 6 3.0107 - 2.8332 1.00 4048 212 0.1562 0.1623
REMARK 3 7 2.8332 - 2.6914 1.00 4044 242 0.1668 0.1958
REMARK 3 8 2.6914 - 2.5742 1.00 3997 223 0.1707 0.2035
REMARK 3 9 2.5742 - 2.4751 1.00 4005 262 0.1635 0.1971
REMARK 3 10 2.4751 - 2.3897 1.00 4063 228 0.1664 0.1913
REMARK 3 11 2.3897 - 2.3150 1.00 4066 216 0.1661 0.2137
REMARK 3 12 2.3150 - 2.2489 1.00 4023 211 0.1698 0.2014
REMARK 3 13 2.2489 - 2.1897 1.00 4074 230 0.1636 0.2178
REMARK 3 14 2.1897 - 2.1362 1.00 4011 204 0.1694 0.1812
REMARK 3 15 2.1362 - 2.0877 1.00 4078 243 0.1762 0.2102
REMARK 3 16 2.0877 - 2.0433 1.00 4084 183 0.1778 0.2556
REMARK 3 17 2.0433 - 2.0024 1.00 4111 178 0.1884 0.2235
REMARK 3 18 2.0024 - 1.9646 1.00 4005 236 0.1946 0.2082
REMARK 3 19 1.9646 - 1.9295 1.00 4086 185 0.2040 0.2538
REMARK 3 20 1.9295 - 1.8968 1.00 4023 203 0.2048 0.2181
REMARK 3 21 1.8968 - 1.8662 1.00 4079 214 0.1939 0.2284
REMARK 3 22 1.8662 - 1.8375 1.00 4048 238 0.1978 0.2445
REMARK 3 23 1.8375 - 1.8105 1.00 4022 220 0.2190 0.2879
REMARK 3 24 1.8105 - 1.7850 1.00 4045 223 0.2153 0.2594
REMARK 3 25 1.7850 - 1.7609 1.00 4030 202 0.2288 0.2616
REMARK 3 26 1.7609 - 1.7380 1.00 4077 223 0.2337 0.2429
REMARK 3 27 1.7380 - 1.7163 0.99 4010 226 0.2480 0.2828
REMARK 3 28 1.7163 - 1.6956 0.98 3957 174 0.2527 0.3008
REMARK 3 29 1.6956 - 1.6759 0.97 4045 153 0.2678 0.2566
REMARK 3 30 1.6759 - 1.6570 0.89 3540 222 0.2798 0.3105
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.150
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 : 0.004 4316
REMARK 3 ANGLE : 0.657 5890
REMARK 3 CHIRALITY : 0.050 678
REMARK 3 PLANARITY : 0.005 757
REMARK 3 DIHEDRAL : 12.723 2544
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): 14.6835 25.3781 15.3325
REMARK 3 T TENSOR
REMARK 3 T11: 0.0867 T22: 0.0860
REMARK 3 T33: 0.0571 T12: -0.0017
REMARK 3 T13: 0.0059 T23: 0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 0.2793 L22: 0.2991
REMARK 3 L33: 0.0174 L12: -0.0576
REMARK 3 L13: -0.0115 L23: 0.0606
REMARK 3 S TENSOR
REMARK 3 S11: 0.0004 S12: 0.0070 S13: -0.0296
REMARK 3 S21: 0.0105 S22: -0.0069 S23: -0.0124
REMARK 3 S31: -0.0110 S32: -0.0007 S33: 0.0000
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 5Z7W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1300006457.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-FEB-17
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-5A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 127266
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.657
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 (%) : 99.4
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 4JYP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL (PH 8.5), 200MM MGCL2,
REMARK 280 30% (W/V) PEG 4000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 40.58500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 69.38500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.58500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 69.38500
REMARK 290 SMTRY3 4 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 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 631 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 644 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 710 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 730 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 733 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 777 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 GLY A -4
REMARK 465 PRO A -3
REMARK 465 LEU A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 PRO A 271
REMARK 465 ASN A 272
REMARK 465 GLY B -4
REMARK 465 PRO B -3
REMARK 465 LEU B -2
REMARK 465 ARG B 270
REMARK 465 PRO B 271
REMARK 465 ASN B 272
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 THR A 28 -161.44 -121.12
REMARK 500 PHE A 62 121.82 -39.45
REMARK 500 SER A 95 -119.46 49.09
REMARK 500 ARG A 123 123.98 -171.29
REMARK 500 LEU A 247 55.86 -119.45
REMARK 500 MET B 1 35.62 -83.80
REMARK 500 THR B 28 -163.65 -121.62
REMARK 500 PRO B 59 12.48 -64.03
REMARK 500 SER B 95 -119.48 53.04
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 792 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH A 793 DISTANCE = 6.08 ANGSTROMS
REMARK 525 HOH A 794 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH A 795 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH A 796 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH A 797 DISTANCE = 6.50 ANGSTROMS
REMARK 525 HOH A 798 DISTANCE = 6.56 ANGSTROMS
REMARK 525 HOH A 799 DISTANCE = 6.88 ANGSTROMS
REMARK 525 HOH A 800 DISTANCE = 6.90 ANGSTROMS
REMARK 525 HOH A 801 DISTANCE = 7.10 ANGSTROMS
REMARK 525 HOH B 801 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH B 802 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH B 803 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH B 804 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH B 805 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH B 806 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH B 807 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH B 808 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH B 809 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH B 810 DISTANCE = 6.34 ANGSTROMS
REMARK 525 HOH B 811 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH B 812 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH B 813 DISTANCE = 6.79 ANGSTROMS
REMARK 525 HOH B 814 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH B 815 DISTANCE = 7.41 ANGSTROMS
REMARK 525 HOH B 816 DISTANCE = 7.49 ANGSTROMS
REMARK 525 HOH B 817 DISTANCE = 8.14 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 NA A 303 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRO A 109 O
REMARK 620 2 PHE A 112 O 87.2
REMARK 620 3 HOH A 647 O 86.5 173.7
REMARK 620 4 HOH A 651 O 110.9 88.6 93.3
REMARK 620 5 HOH A 658 O 138.8 94.3 90.7 110.2
REMARK 620 N 1 2 3 4
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 ASP A 129 OD2
REMARK 620 2 HOH A 611 O 92.9
REMARK 620 3 HOH A 700 O 159.4 105.7
REMARK 620 4 HOH A 655 O 101.5 104.3 82.6
REMARK 620 5 HOH B 421 O 82.7 96.3 86.4 158.6
REMARK 620 6 HOH B 487 O 71.9 164.2 88.8 83.3 78.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 303 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRO B 109 O
REMARK 620 2 PHE B 112 O 69.4
REMARK 620 3 HOH B 655 O 152.7 85.0
REMARK 620 4 HOH B 728 O 109.5 156.5 90.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 302 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 503 O
REMARK 620 2 HOH B 706 O 49.5
REMARK 620 3 HOH B 401 O 53.4 62.3
REMARK 620 4 GLU A 141 OE2 59.0 30.3 38.9
REMARK 620 5 HOH A 670 O 59.4 108.8 74.1 107.3
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 304
DBREF1 5Z7W A 1 272 UNP A0A0M4AV81_STRHE
DBREF2 5Z7W A A0A0M4AV81 1 272
DBREF1 5Z7W B 1 272 UNP A0A0M4AV81_STRHE
DBREF2 5Z7W B A0A0M4AV81 1 272
SEQADV 5Z7W GLY A -4 UNP A0A0M4AV8 EXPRESSION TAG
SEQADV 5Z7W PRO A -3 UNP A0A0M4AV8 EXPRESSION TAG
SEQADV 5Z7W LEU A -2 UNP A0A0M4AV8 EXPRESSION TAG
SEQADV 5Z7W GLY A -1 UNP A0A0M4AV8 EXPRESSION TAG
SEQADV 5Z7W SER A 0 UNP A0A0M4AV8 EXPRESSION TAG
SEQADV 5Z7W GLY B -4 UNP A0A0M4AV8 EXPRESSION TAG
SEQADV 5Z7W PRO B -3 UNP A0A0M4AV8 EXPRESSION TAG
SEQADV 5Z7W LEU B -2 UNP A0A0M4AV8 EXPRESSION TAG
SEQADV 5Z7W GLY B -1 UNP A0A0M4AV8 EXPRESSION TAG
SEQADV 5Z7W SER B 0 UNP A0A0M4AV8 EXPRESSION TAG
SEQRES 1 A 277 GLY PRO LEU GLY SER MET GLY LEU ALA GLN GLU ALA HIS
SEQRES 2 A 277 ASN VAL ARG VAL LEU GLY SER GLY PRO GLN THR VAL VAL
SEQRES 3 A 277 LEU ALA HIS GLY PHE GLY THR ASP GLN SER VAL TRP LYS
SEQRES 4 A 277 TYR LEU VAL PRO HIS LEU VAL GLU ASP TYR ARG VAL VAL
SEQRES 5 A 277 LEU PHE ASP ILE MET GLY ALA GLY THR THR ASN PRO THR
SEQRES 6 A 277 TYR PHE ASN PHE GLU ARG TYR SER SER LEU GLU GLY TYR
SEQRES 7 A 277 ALA GLY ASP VAL ILE ALA ILE LEU GLU GLU LEU GLN ILE
SEQRES 8 A 277 SER SER CYS VAL TYR VAL GLY HIS SER VAL SER ALA MET
SEQRES 9 A 277 ILE GLY VAL ILE ALA SER VAL THR ARG PRO ASP LEU PHE
SEQRES 10 A 277 THR LYS LEU VAL THR VAL ALA GLY SER PRO ARG TYR LEU
SEQRES 11 A 277 ASN ASP PRO ASP TYR PHE GLY GLY PHE ASP LEU ASP GLU
SEQRES 12 A 277 LEU HIS GLU LEU PHE GLU ALA MET LYS GLU ASN TYR LYS
SEQRES 13 A 277 ALA TRP CYS SER GLY PHE ALA PRO LEU CYS VAL GLY ALA
SEQRES 14 A 277 ASP MET GLU SER LEU ALA VAL GLN GLU PHE SER ARG THR
SEQRES 15 A 277 LEU PHE ASN MET ARG PRO ASP ILE ALA LEU SER ILE LEU
SEQRES 16 A 277 GLN THR ILE PHE TYR SER ASP VAL ARG PRO LEU LEU PRO
SEQRES 17 A 277 HIS VAL THR VAL PRO CYS HIS ILE ILE GLN SER VAL LYS
SEQRES 18 A 277 ASP LEU ALA VAL PRO VAL ALA VAL SER GLU TYR ILE HIS
SEQRES 19 A 277 GLN SER LEU GLY GLY GLU SER ILE LEU GLU VAL MET ALA
SEQRES 20 A 277 THR GLU GLY HIS LEU PRO GLN LEU SER SER PRO ASP VAL
SEQRES 21 A 277 VAL VAL PRO VAL LEU LEU ARG HIS ILE ARG TYR ALA ILE
SEQRES 22 A 277 ALA ARG PRO ASN
SEQRES 1 B 277 GLY PRO LEU GLY SER MET GLY LEU ALA GLN GLU ALA HIS
SEQRES 2 B 277 ASN VAL ARG VAL LEU GLY SER GLY PRO GLN THR VAL VAL
SEQRES 3 B 277 LEU ALA HIS GLY PHE GLY THR ASP GLN SER VAL TRP LYS
SEQRES 4 B 277 TYR LEU VAL PRO HIS LEU VAL GLU ASP TYR ARG VAL VAL
SEQRES 5 B 277 LEU PHE ASP ILE MET GLY ALA GLY THR THR ASN PRO THR
SEQRES 6 B 277 TYR PHE ASN PHE GLU ARG TYR SER SER LEU GLU GLY TYR
SEQRES 7 B 277 ALA GLY ASP VAL ILE ALA ILE LEU GLU GLU LEU GLN ILE
SEQRES 8 B 277 SER SER CYS VAL TYR VAL GLY HIS SER VAL SER ALA MET
SEQRES 9 B 277 ILE GLY VAL ILE ALA SER VAL THR ARG PRO ASP LEU PHE
SEQRES 10 B 277 THR LYS LEU VAL THR VAL ALA GLY SER PRO ARG TYR LEU
SEQRES 11 B 277 ASN ASP PRO ASP TYR PHE GLY GLY PHE ASP LEU ASP GLU
SEQRES 12 B 277 LEU HIS GLU LEU PHE GLU ALA MET LYS GLU ASN TYR LYS
SEQRES 13 B 277 ALA TRP CYS SER GLY PHE ALA PRO LEU CYS VAL GLY ALA
SEQRES 14 B 277 ASP MET GLU SER LEU ALA VAL GLN GLU PHE SER ARG THR
SEQRES 15 B 277 LEU PHE ASN MET ARG PRO ASP ILE ALA LEU SER ILE LEU
SEQRES 16 B 277 GLN THR ILE PHE TYR SER ASP VAL ARG PRO LEU LEU PRO
SEQRES 17 B 277 HIS VAL THR VAL PRO CYS HIS ILE ILE GLN SER VAL LYS
SEQRES 18 B 277 ASP LEU ALA VAL PRO VAL ALA VAL SER GLU TYR ILE HIS
SEQRES 19 B 277 GLN SER LEU GLY GLY GLU SER ILE LEU GLU VAL MET ALA
SEQRES 20 B 277 THR GLU GLY HIS LEU PRO GLN LEU SER SER PRO ASP VAL
SEQRES 21 B 277 VAL VAL PRO VAL LEU LEU ARG HIS ILE ARG TYR ALA ILE
SEQRES 22 B 277 ALA ARG PRO ASN
HET MG A 301 1
HET MG A 302 1
HET NA A 303 1
HET GOL A 304 6
HET MG B 301 1
HET NA B 302 1
HET NA B 303 1
HET GOL B 304 6
HETNAM MG MAGNESIUM ION
HETNAM NA SODIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 MG 3(MG 2+)
FORMUL 5 NA 3(NA 1+)
FORMUL 6 GOL 2(C3 H8 O3)
FORMUL 11 HOH *818(H2 O)
HELIX 1 AA1 GLY A 2 HIS A 8 1 7
HELIX 2 AA2 ASP A 29 LYS A 34 5 6
HELIX 3 AA3 LEU A 36 LEU A 40 5 5
HELIX 4 AA4 GLU A 65 SER A 68 5 4
HELIX 5 AA5 SER A 69 LEU A 84 1 16
HELIX 6 AA6 SER A 95 ARG A 108 1 14
HELIX 7 AA7 ASP A 135 ASN A 149 1 15
HELIX 8 AA8 ASN A 149 GLY A 163 1 15
HELIX 9 AA9 SER A 168 ASN A 180 1 13
HELIX 10 AB1 ARG A 182 TYR A 195 1 14
HELIX 11 AB2 VAL A 198 VAL A 205 5 8
HELIX 12 AB3 PRO A 221 LEU A 232 1 12
HELIX 13 AB4 LEU A 247 SER A 252 1 6
HELIX 14 AB5 SER A 252 TYR A 266 1 15
HELIX 15 AB6 GLY B 2 HIS B 8 1 7
HELIX 16 AB7 ASP B 29 LYS B 34 5 6
HELIX 17 AB8 LEU B 36 LEU B 40 5 5
HELIX 18 AB9 GLU B 65 SER B 68 5 4
HELIX 19 AC1 SER B 69 LEU B 84 1 16
HELIX 20 AC2 SER B 95 ARG B 108 1 14
HELIX 21 AC3 ASP B 135 ASN B 149 1 15
HELIX 22 AC4 ASN B 149 GLY B 163 1 15
HELIX 23 AC5 SER B 168 ASN B 180 1 13
HELIX 24 AC6 ARG B 182 TYR B 195 1 14
HELIX 25 AC7 VAL B 198 VAL B 205 5 8
HELIX 26 AC8 PRO B 221 LEU B 232 1 12
HELIX 27 AC9 LEU B 247 SER B 252 1 6
HELIX 28 AD1 SER B 252 TYR B 266 1 15
SHEET 1 AA1 7 ARG A 11 GLY A 14 0
SHEET 2 AA1 7 ARG A 45 PHE A 49 -1 O LEU A 48 N ARG A 11
SHEET 3 AA1 7 THR A 19 ALA A 23 1 N VAL A 20 O ARG A 45
SHEET 4 AA1 7 CYS A 89 HIS A 94 1 O VAL A 90 N VAL A 21
SHEET 5 AA1 7 PHE A 112 VAL A 118 1 O VAL A 116 N GLY A 93
SHEET 6 AA1 7 CYS A 209 LYS A 216 1 O HIS A 210 N LEU A 115
SHEET 7 AA1 7 SER A 236 GLU A 244 1 O ILE A 237 N ILE A 211
SHEET 1 AA2 7 ARG B 11 GLY B 14 0
SHEET 2 AA2 7 ARG B 45 PHE B 49 -1 O VAL B 46 N LEU B 13
SHEET 3 AA2 7 THR B 19 ALA B 23 1 N VAL B 20 O ARG B 45
SHEET 4 AA2 7 CYS B 89 HIS B 94 1 O VAL B 92 N VAL B 21
SHEET 5 AA2 7 PHE B 112 VAL B 118 1 O VAL B 116 N TYR B 91
SHEET 6 AA2 7 CYS B 209 LYS B 216 1 O HIS B 210 N LEU B 115
SHEET 7 AA2 7 SER B 236 GLU B 244 1 O MET B 241 N GLN B 213
LINK OG SER A 95 MG MG A 302 1555 1555 2.83
LINK O PRO A 109 NA NA A 303 1555 1555 2.38
LINK O PHE A 112 NA NA A 303 1555 1555 2.32
LINK OD2 ASP A 129 MG MG A 301 1555 1555 2.05
LINK OG SER B 95 MG MG B 301 1555 1555 2.86
LINK O PRO B 109 NA NA B 303 1555 1555 2.64
LINK O PHE B 112 NA NA B 303 1555 1555 2.63
LINK MG MG A 301 O HOH A 611 1555 1555 2.13
LINK NA NA A 303 O HOH A 647 1555 1555 2.43
LINK NA NA A 303 O HOH A 651 1555 1555 2.46
LINK NA NA A 303 O HOH A 658 1555 1555 2.34
LINK NA NA B 302 O HOH B 503 1555 1555 3.18
LINK NA NA B 302 O HOH B 706 1555 1555 2.75
LINK NA NA B 302 O HOH B 401 1555 1555 2.73
LINK NA NA B 303 O HOH B 655 1555 1555 2.45
LINK NA NA B 303 O HOH B 728 1555 1555 2.42
LINK OE2 GLU A 141 NA NA B 302 1555 3546 2.98
LINK MG MG A 301 O HOH A 700 1555 2655 2.58
LINK MG MG A 301 O HOH A 655 1555 2655 2.05
LINK MG MG A 301 O HOH B 421 1555 3546 2.49
LINK MG MG A 301 O HOH B 487 1555 3546 2.63
LINK NA NA B 302 O HOH A 670 1555 3556 2.41
SITE 1 AC1 6 ASP A 129 HOH A 611 HOH A 655 HOH A 700
SITE 2 AC1 6 HOH B 421 HOH B 487
SITE 1 AC2 4 PHE A 26 SER A 95 VAL A 96 GOL A 304
SITE 1 AC3 5 PRO A 109 PHE A 112 HOH A 647 HOH A 651
SITE 2 AC3 5 HOH A 658
SITE 1 AC4 6 SER A 95 PHE A 157 ILE A 193 HIS A 246
SITE 2 AC4 6 MG A 302 HOH A 414
SITE 1 AC5 4 PHE B 26 SER B 95 VAL B 96 GOL B 304
SITE 1 AC6 4 GLU A 141 HOH A 670 HOH B 401 HOH B 706
SITE 1 AC7 5 PRO B 109 PHE B 112 VAL B 207 HOH B 655
SITE 2 AC7 5 HOH B 728
SITE 1 AC8 6 SER B 95 PHE B 157 ALA B 219 HIS B 246
SITE 2 AC8 6 MG B 301 HOH B 521
CRYST1 81.170 138.770 49.410 90.00 90.00 90.00 P 21 21 2 8
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 0.012320 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007206 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020239 0.00000
TER 2106 ARG A 270
TER 4201 ALA B 269
MASTER 415 0 8 28 14 0 13 6 5017 2 35 44
END
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