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HEADER HYDROLASE 22-APR-24 8Z91
TITLE SOIL METAGENOMIC-DERIVED ESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: SEQUENCE REFERENCE FOR SOIL METAGENOME (410658) IS NOT
COMPND 6 AVAILABLE IN UNIPROT AT THE TIME OF BIOCURATION. CURRENT SEQUENCE
COMPND 7 REFERENCE IS FROM UNIPROT ID A0A8F6XWV1.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SOIL METAGENOME;
SOURCE 3 ORGANISM_TAXID: 410658;
SOURCE 4 GENE: ESTSC4;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ESTERASE, PET DEGRADATION ACTIVITY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.Q.LI,S.W.SUN
REVDAT 1 25-DEC-24 8Z91 0
JRNL AUTH W.LI
JRNL TITL DISCOVERY AND CHARACTERIZATION OF A NOVEL BOTTLE-GRADE PET
JRNL TITL 2 DEPOLYMERASE WITH A BON DOMAIN-CONTAINING PROTEIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.73 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX V1.0
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) : 1.73
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.68
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 79430
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 3936
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 31.6800 - 5.2400 1.00 2971 146 0.1737 0.1956
REMARK 3 2 5.2300 - 4.1600 1.00 2889 119 0.1322 0.1499
REMARK 3 3 4.1600 - 3.6300 1.00 2802 167 0.1441 0.1775
REMARK 3 4 3.6300 - 3.3000 1.00 2764 168 0.1612 0.2094
REMARK 3 5 3.3000 - 3.0700 1.00 2785 147 0.1773 0.1948
REMARK 3 6 3.0700 - 2.8900 1.00 2759 164 0.1914 0.2346
REMARK 3 7 2.8800 - 2.7400 1.00 2783 125 0.1828 0.2378
REMARK 3 8 2.7400 - 2.6200 1.00 2776 138 0.1936 0.2413
REMARK 3 9 2.6200 - 2.5200 1.00 2758 139 0.1835 0.2446
REMARK 3 10 2.5200 - 2.4300 1.00 2737 156 0.1812 0.2212
REMARK 3 11 2.4300 - 2.3600 1.00 2796 117 0.1772 0.2184
REMARK 3 12 2.3600 - 2.2900 1.00 2767 126 0.1843 0.1894
REMARK 3 13 2.2900 - 2.2300 0.89 2409 138 0.3648 0.4105
REMARK 3 14 2.2300 - 2.1800 0.99 2698 157 0.2087 0.2724
REMARK 3 15 2.1800 - 2.1300 1.00 2759 111 0.1890 0.2391
REMARK 3 16 2.1300 - 2.0800 1.00 2739 134 0.1890 0.2163
REMARK 3 17 2.0800 - 2.0400 1.00 2745 154 0.1924 0.2297
REMARK 3 18 2.0400 - 2.0000 1.00 2700 154 0.2039 0.2455
REMARK 3 19 2.0000 - 1.9600 1.00 2761 132 0.2152 0.2785
REMARK 3 20 1.9600 - 1.9300 1.00 2752 115 0.2475 0.2675
REMARK 3 21 1.9300 - 1.9000 0.84 2278 115 0.5221 0.6379
REMARK 3 22 1.9000 - 1.8700 0.69 1856 101 0.2456 0.2864
REMARK 3 23 1.8700 - 1.8400 1.00 2753 157 0.2671 0.3316
REMARK 3 24 1.8400 - 1.8200 1.00 2708 151 0.2788 0.2913
REMARK 3 25 1.8200 - 1.7900 1.00 2701 140 0.2908 0.2967
REMARK 3 26 1.7900 - 1.7700 1.00 2708 170 0.3150 0.3445
REMARK 3 27 1.7700 - 1.7500 1.00 2686 141 0.3124 0.3156
REMARK 3 28 1.7500 - 1.7300 0.98 2654 154 0.3487 0.3653
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.320
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 : 0.008 5574
REMARK 3 ANGLE : 0.933 7538
REMARK 3 CHIRALITY : 0.061 798
REMARK 3 PLANARITY : 0.007 976
REMARK 3 DIHEDRAL : 8.407 772
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 32 THROUGH 210 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.6132 35.8611 -20.3222
REMARK 3 T TENSOR
REMARK 3 T11: 0.1675 T22: 0.2683
REMARK 3 T33: 0.1828 T12: -0.0005
REMARK 3 T13: -0.0140 T23: -0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 0.6698 L22: 1.5634
REMARK 3 L33: 1.4817 L12: -0.3125
REMARK 3 L13: -0.1149 L23: 0.1321
REMARK 3 S TENSOR
REMARK 3 S11: -0.0370 S12: -0.0598 S13: 0.0402
REMARK 3 S21: 0.2139 S22: 0.0444 S23: 0.0009
REMARK 3 S31: 0.0464 S32: -0.0566 S33: -0.0073
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 211 THROUGH 281 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.0333 17.1016 -14.2390
REMARK 3 T TENSOR
REMARK 3 T11: 0.5282 T22: 0.4929
REMARK 3 T33: 0.3726 T12: 0.1753
REMARK 3 T13: -0.0272 T23: 0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 2.1828 L22: 1.4177
REMARK 3 L33: 2.4319 L12: 0.2684
REMARK 3 L13: -0.6142 L23: -0.0163
REMARK 3 S TENSOR
REMARK 3 S11: -0.1876 S12: -0.4194 S13: -0.1749
REMARK 3 S21: 0.1990 S22: 0.1365 S23: -0.5070
REMARK 3 S31: 0.6780 S32: 0.7034 S33: 0.0294
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 282 THROUGH 352 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.1452 27.2352 -34.8550
REMARK 3 T TENSOR
REMARK 3 T11: 0.1708 T22: 0.2371
REMARK 3 T33: 0.1917 T12: 0.0011
REMARK 3 T13: -0.0091 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 1.2058 L22: 1.7562
REMARK 3 L33: 1.7122 L12: -0.0958
REMARK 3 L13: 0.0781 L23: -0.0488
REMARK 3 S TENSOR
REMARK 3 S11: 0.0412 S12: -0.0980 S13: -0.0033
REMARK 3 S21: -0.0032 S22: -0.0188 S23: -0.1351
REMARK 3 S31: 0.1048 S32: 0.0883 S33: -0.0167
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 353 THROUGH 378 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.6233 36.9729 -36.9503
REMARK 3 T TENSOR
REMARK 3 T11: 0.2262 T22: 0.5067
REMARK 3 T33: 0.3180 T12: -0.0049
REMARK 3 T13: -0.0657 T23: -0.0551
REMARK 3 L TENSOR
REMARK 3 L11: 0.2637 L22: 0.8243
REMARK 3 L33: 0.2056 L12: -0.4698
REMARK 3 L13: 0.2328 L23: -0.4127
REMARK 3 S TENSOR
REMARK 3 S11: 0.0780 S12: 0.3648 S13: -0.1881
REMARK 3 S21: -0.3208 S22: -0.0826 S23: 0.4618
REMARK 3 S31: 0.1556 S32: -0.5245 S33: 0.0459
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 32 THROUGH 161 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.8117 41.8595 -66.8287
REMARK 3 T TENSOR
REMARK 3 T11: 0.1823 T22: 0.2671
REMARK 3 T33: 0.1913 T12: -0.0438
REMARK 3 T13: -0.0025 T23: 0.0399
REMARK 3 L TENSOR
REMARK 3 L11: 1.0184 L22: 1.4569
REMARK 3 L33: 1.2824 L12: 0.1984
REMARK 3 L13: 0.2857 L23: 0.0469
REMARK 3 S TENSOR
REMARK 3 S11: -0.0573 S12: 0.1708 S13: 0.1273
REMARK 3 S21: -0.1082 S22: 0.0420 S23: -0.0425
REMARK 3 S31: -0.1559 S32: 0.1360 S33: 0.0251
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 162 THROUGH 281 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.2632 18.6305 -66.8485
REMARK 3 T TENSOR
REMARK 3 T11: 0.2449 T22: 0.2827
REMARK 3 T33: 0.2720 T12: 0.0137
REMARK 3 T13: 0.0107 T23: -0.0766
REMARK 3 L TENSOR
REMARK 3 L11: 1.7829 L22: 1.5156
REMARK 3 L33: 1.3993 L12: 0.5957
REMARK 3 L13: 0.1620 L23: -0.2010
REMARK 3 S TENSOR
REMARK 3 S11: -0.0181 S12: 0.3452 S13: -0.4251
REMARK 3 S21: -0.2822 S22: 0.0727 S23: -0.1516
REMARK 3 S31: 0.3618 S32: 0.1272 S33: -0.0190
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 282 THROUGH 366 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.2206 30.2435 -50.6764
REMARK 3 T TENSOR
REMARK 3 T11: 0.1626 T22: 0.2494
REMARK 3 T33: 0.1957 T12: -0.0140
REMARK 3 T13: 0.0032 T23: -0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 0.8181 L22: 1.4966
REMARK 3 L33: 1.3683 L12: 0.2092
REMARK 3 L13: 0.3044 L23: 0.0783
REMARK 3 S TENSOR
REMARK 3 S11: 0.0349 S12: 0.0470 S13: 0.0078
REMARK 3 S21: 0.0241 S22: -0.0060 S23: -0.0572
REMARK 3 S31: -0.0331 S32: 0.1274 S33: -0.0271
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 8Z91 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 26-APR-24.
REMARK 100 THE DEPOSITION ID IS D_1300047188.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-23
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL10U2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
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 : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79430
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.727
REMARK 200 RESOLUTION RANGE LOW (A) : 75.993
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 1.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 1.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.73
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.41
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: SAD
REMARK 200 SOFTWARE USED: PHENIX V1.0
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1MHEPES (PH7.5), 2.0M AMMONIUM
REMARK 280 SULFATE, 2% POLYETHYLENE GLYCOL 400; 2.0M AMMONIUM SULFATE, 5%
REMARK 280 (V/V) 2-PROPANOL; 0.1M AMMONIUM CITRATE, 0.2M POTASSIUM SODIUM
REMARK 280 TARTRATE, 2M AMMONIUM SULFATE; 0.1M MES (PH 6.5), 0.01M COBALT
REMARK 280 CHLORIDE, 1.8M AMMONIUM SULFATE, LIQUID DIFFUSION, TEMPERATURE
REMARK 280 320.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 57.39800
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 114.79600
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 114.79600
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 57.39800
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 51370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -93.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -114.79600
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 ASN B 367
REMARK 465 ALA B 368
REMARK 465 ALA B 369
REMARK 465 ALA B 370
REMARK 465 LEU B 371
REMARK 465 GLU B 372
REMARK 465 HIS B 373
REMARK 465 HIS B 374
REMARK 465 HIS B 375
REMARK 465 HIS B 376
REMARK 465 HIS B 377
REMARK 465 HIS B 378
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 ARG A 229 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 264 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 272 CG CD OE1 OE2
REMARK 470 HIS A 374 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 375 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 376 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 378 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 219 CG CD CE NZ
REMARK 470 THR B 251 OG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 513 O HOH B 743 2.15
REMARK 500 O HOH A 653 O HOH A 743 2.16
REMARK 500 O HOH A 505 O HOH A 591 2.17
REMARK 500 O HOH B 707 O HOH B 726 2.18
REMARK 500 O HOH B 698 O HOH B 755 2.18
REMARK 500 O HOH B 769 O HOH B 794 2.19
REMARK 500 O HOH B 729 O HOH B 784 2.19
REMARK 500 O HOH A 726 O HOH A 752 2.19
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 THR A 85 -2.76 65.77
REMARK 500 ALA A 96 -133.69 -97.09
REMARK 500 ARG A 146 -72.61 -106.84
REMARK 500 SER A 171 -108.97 51.25
REMARK 500 HIS A 184 56.17 -143.03
REMARK 500 SER A 195 58.75 39.96
REMARK 500 ASP A 265 -20.59 74.92
REMARK 500 ARG A 352 -60.42 -136.45
REMARK 500 THR B 85 -1.15 69.61
REMARK 500 ALA B 96 -126.02 -116.62
REMARK 500 LYS B 127 15.45 80.18
REMARK 500 ARG B 146 -74.10 -106.09
REMARK 500 SER B 171 -123.51 62.94
REMARK 500 HIS B 184 54.75 -144.45
REMARK 500 SER B 195 59.92 38.48
REMARK 500 LEU B 250 -5.26 -57.43
REMARK 500 ARG B 352 -57.71 -137.09
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 8Z91 A 32 367 UNP A0A8F6XWV1_9BACT
DBREF2 8Z91 A A0A8F6XWV1 32 367
DBREF1 8Z91 B 32 367 UNP A0A8F6XWV1_9BACT
DBREF2 8Z91 B A0A8F6XWV1 32 367
SEQADV 8Z91 ALA A 368 UNP A0A8F6XWV EXPRESSION TAG
SEQADV 8Z91 ALA A 369 UNP A0A8F6XWV EXPRESSION TAG
SEQADV 8Z91 ALA A 370 UNP A0A8F6XWV EXPRESSION TAG
SEQADV 8Z91 LEU A 371 UNP A0A8F6XWV EXPRESSION TAG
SEQADV 8Z91 GLU A 372 UNP A0A8F6XWV EXPRESSION TAG
SEQADV 8Z91 HIS A 373 UNP A0A8F6XWV EXPRESSION TAG
SEQADV 8Z91 HIS A 374 UNP A0A8F6XWV EXPRESSION TAG
SEQADV 8Z91 HIS A 375 UNP A0A8F6XWV EXPRESSION TAG
SEQADV 8Z91 HIS A 376 UNP A0A8F6XWV EXPRESSION TAG
SEQADV 8Z91 HIS A 377 UNP A0A8F6XWV EXPRESSION TAG
SEQADV 8Z91 HIS A 378 UNP A0A8F6XWV EXPRESSION TAG
SEQADV 8Z91 ALA B 368 UNP A0A8F6XWV EXPRESSION TAG
SEQADV 8Z91 ALA B 369 UNP A0A8F6XWV EXPRESSION TAG
SEQADV 8Z91 ALA B 370 UNP A0A8F6XWV EXPRESSION TAG
SEQADV 8Z91 LEU B 371 UNP A0A8F6XWV EXPRESSION TAG
SEQADV 8Z91 GLU B 372 UNP A0A8F6XWV EXPRESSION TAG
SEQADV 8Z91 HIS B 373 UNP A0A8F6XWV EXPRESSION TAG
SEQADV 8Z91 HIS B 374 UNP A0A8F6XWV EXPRESSION TAG
SEQADV 8Z91 HIS B 375 UNP A0A8F6XWV EXPRESSION TAG
SEQADV 8Z91 HIS B 376 UNP A0A8F6XWV EXPRESSION TAG
SEQADV 8Z91 HIS B 377 UNP A0A8F6XWV EXPRESSION TAG
SEQADV 8Z91 HIS B 378 UNP A0A8F6XWV EXPRESSION TAG
SEQRES 1 A 347 HIS ALA GLY ARG LEU ILE GLU VAL LYS ILE PRO ALA PRO
SEQRES 2 A 347 SER LEU LYS GLY ASN LEU LEU GLY ASP PRO THR GLU GLN
SEQRES 3 A 347 SER ILE ALA VAL TYR LEU PRO ALA SER TYR GLU SER ALA
SEQRES 4 A 347 PRO ALA LYS ARG TYR PRO THR LEU TYR LEU LEU HIS GLY
SEQRES 5 A 347 TYR THR GLY THR ASN LYS THR TRP THR SER PRO GLU ALA
SEQRES 6 A 347 MET ASN ILE ARG ALA MET MET ASP GLU MET ILE LYS SER
SEQRES 7 A 347 GLY ARG VAL GLN GLU MET ILE VAL VAL ALA PRO ASN GLY
SEQRES 8 A 347 TRP ASN ALA TYR LYS GLY ALA PHE TYR THR ASN SER ALA
SEQRES 9 A 347 VAL THR GLY ASN TRP GLU ASP TYR ILE TYR ARG ASP LEU
SEQRES 10 A 347 VAL GLN TYR VAL ASP ALA ASN TYR ARG THR ILE THR ARG
SEQRES 11 A 347 ALA GLU SER ARG GLY ILE ALA GLY HIS SER MET GLY GLY
SEQRES 12 A 347 TYR GLY ALA LEU THR LEU ALA MET ASN HIS ALA ASP VAL
SEQRES 13 A 347 PHE SER ALA VAL TYR ALA LEU SER PRO CYS CYS LEU GLY
SEQRES 14 A 347 MET GLU GLY ASP PHE THR ALA GLU ASN SER ALA TRP LEU
SEQRES 15 A 347 LYS THR LEU ARG LEU LYS SER LYS GLU GLN ILE SER ALA
SEQRES 16 A 347 ARG PRO ARG SER LEU GLU GLU PHE TYR GLN ASN ALA PHE
SEQRES 17 A 347 VAL ALA LEU SER ALA ALA PHE SER PRO ASN LEU THR ARG
SEQRES 18 A 347 ALA PRO PHE PHE VAL ASP PHE PRO TYR GLN GLU ARG ASP
SEQRES 19 A 347 GLY VAL VAL GLU LYS ASN GLU PRO ALA PHE ALA LYS TRP
SEQRES 20 A 347 ARG SER LYS MET PRO LEU TYR MET ILE GLY GLU LYS LYS
SEQRES 21 A 347 ALA ASP ILE LEU LYS LEU ARG GLY ILE ALA ILE ASP VAL
SEQRES 22 A 347 GLY GLU LYS GLU GLU PHE SER HIS ILE ARG ILE THR THR
SEQRES 23 A 347 GLY GLN PHE SER LYS ALA LEU SER GLU GLN ASN ILE PRO
SEQRES 24 A 347 HIS MET PHE GLU ILE TYR GLN GLY GLY THR HIS ASN ASN
SEQRES 25 A 347 LYS VAL ARG GLN ARG LEU GLU THR ARG LEU LEU GLN PHE
SEQRES 26 A 347 PHE SER GLU LYS LEU ASP PHE THR ASN PRO ASN ALA ALA
SEQRES 27 A 347 ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 347 HIS ALA GLY ARG LEU ILE GLU VAL LYS ILE PRO ALA PRO
SEQRES 2 B 347 SER LEU LYS GLY ASN LEU LEU GLY ASP PRO THR GLU GLN
SEQRES 3 B 347 SER ILE ALA VAL TYR LEU PRO ALA SER TYR GLU SER ALA
SEQRES 4 B 347 PRO ALA LYS ARG TYR PRO THR LEU TYR LEU LEU HIS GLY
SEQRES 5 B 347 TYR THR GLY THR ASN LYS THR TRP THR SER PRO GLU ALA
SEQRES 6 B 347 MET ASN ILE ARG ALA MET MET ASP GLU MET ILE LYS SER
SEQRES 7 B 347 GLY ARG VAL GLN GLU MET ILE VAL VAL ALA PRO ASN GLY
SEQRES 8 B 347 TRP ASN ALA TYR LYS GLY ALA PHE TYR THR ASN SER ALA
SEQRES 9 B 347 VAL THR GLY ASN TRP GLU ASP TYR ILE TYR ARG ASP LEU
SEQRES 10 B 347 VAL GLN TYR VAL ASP ALA ASN TYR ARG THR ILE THR ARG
SEQRES 11 B 347 ALA GLU SER ARG GLY ILE ALA GLY HIS SER MET GLY GLY
SEQRES 12 B 347 TYR GLY ALA LEU THR LEU ALA MET ASN HIS ALA ASP VAL
SEQRES 13 B 347 PHE SER ALA VAL TYR ALA LEU SER PRO CYS CYS LEU GLY
SEQRES 14 B 347 MET GLU GLY ASP PHE THR ALA GLU ASN SER ALA TRP LEU
SEQRES 15 B 347 LYS THR LEU ARG LEU LYS SER LYS GLU GLN ILE SER ALA
SEQRES 16 B 347 ARG PRO ARG SER LEU GLU GLU PHE TYR GLN ASN ALA PHE
SEQRES 17 B 347 VAL ALA LEU SER ALA ALA PHE SER PRO ASN LEU THR ARG
SEQRES 18 B 347 ALA PRO PHE PHE VAL ASP PHE PRO TYR GLN GLU ARG ASP
SEQRES 19 B 347 GLY VAL VAL GLU LYS ASN GLU PRO ALA PHE ALA LYS TRP
SEQRES 20 B 347 ARG SER LYS MET PRO LEU TYR MET ILE GLY GLU LYS LYS
SEQRES 21 B 347 ALA ASP ILE LEU LYS LEU ARG GLY ILE ALA ILE ASP VAL
SEQRES 22 B 347 GLY GLU LYS GLU GLU PHE SER HIS ILE ARG ILE THR THR
SEQRES 23 B 347 GLY GLN PHE SER LYS ALA LEU SER GLU GLN ASN ILE PRO
SEQRES 24 B 347 HIS MET PHE GLU ILE TYR GLN GLY GLY THR HIS ASN ASN
SEQRES 25 B 347 LYS VAL ARG GLN ARG LEU GLU THR ARG LEU LEU GLN PHE
SEQRES 26 B 347 PHE SER GLU LYS LEU ASP PHE THR ASN PRO ASN ALA ALA
SEQRES 27 B 347 ALA LEU GLU HIS HIS HIS HIS HIS HIS
HET ACT A 401 4
HET PEG A 402 7
HET PEG A 403 7
HET 1PE A 404 16
HET SO4 A 405 5
HET SO4 A 406 5
HET ACT B 401 4
HET PEG B 402 7
HET SO4 B 403 5
HETNAM ACT ACETATE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM SO4 SULFATE ION
HETSYN 1PE PEG400
FORMUL 3 ACT 2(C2 H3 O2 1-)
FORMUL 4 PEG 3(C4 H10 O3)
FORMUL 6 1PE C10 H22 O6
FORMUL 7 SO4 3(O4 S 2-)
FORMUL 12 HOH *550(H2 O)
HELIX 1 AA1 PRO A 44 LYS A 47 5 4
HELIX 2 AA2 PRO A 64 GLU A 68 5 5
HELIX 3 AA3 ASN A 88 SER A 93 1 6
HELIX 4 AA4 ASN A 98 SER A 109 1 12
HELIX 5 AA5 TRP A 140 ARG A 146 1 7
HELIX 6 AA6 ARG A 146 TYR A 156 1 11
HELIX 7 AA7 ARG A 161 GLU A 163 5 3
HELIX 8 AA8 SER A 171 HIS A 184 1 14
HELIX 9 AA9 GLU A 202 THR A 206 5 5
HELIX 10 AB1 SER A 210 ARG A 217 1 8
HELIX 11 AB2 SER A 220 SER A 225 5 6
HELIX 12 AB3 SER A 230 SER A 247 1 18
HELIX 13 AB4 ASN A 271 LYS A 281 1 11
HELIX 14 AB5 MET A 282 MET A 286 5 5
HELIX 15 AB6 LYS A 290 LEU A 295 1 6
HELIX 16 AB7 PHE A 310 GLN A 327 1 18
HELIX 17 AB8 LYS A 344 ARG A 352 1 9
HELIX 18 AB9 ARG A 352 LEU A 361 1 10
HELIX 19 AC1 ASN A 367 HIS A 374 1 8
HELIX 20 AC2 PRO B 44 LYS B 47 5 4
HELIX 21 AC3 ASN B 88 SER B 93 1 6
HELIX 22 AC4 ASN B 98 SER B 109 1 12
HELIX 23 AC5 TRP B 140 ARG B 146 1 7
HELIX 24 AC6 ARG B 146 TYR B 156 1 11
HELIX 25 AC7 ARG B 161 GLU B 163 5 3
HELIX 26 AC8 SER B 171 HIS B 184 1 14
HELIX 27 AC9 GLU B 202 THR B 206 5 5
HELIX 28 AD1 SER B 210 ARG B 217 1 8
HELIX 29 AD2 SER B 220 ILE B 224 5 5
HELIX 30 AD3 SER B 230 SER B 247 1 18
HELIX 31 AD4 ASN B 271 LYS B 281 1 11
HELIX 32 AD5 MET B 282 TYR B 285 5 4
HELIX 33 AD6 MET B 286 LEU B 295 1 10
HELIX 34 AD7 PHE B 310 GLN B 327 1 18
HELIX 35 AD8 LYS B 344 ARG B 352 1 9
HELIX 36 AD9 ARG B 352 LEU B 361 1 10
SHEET 1 AA116 ARG A 35 PRO A 42 0
SHEET 2 AA116 GLU A 56 LEU A 63 -1 O VAL A 61 N ILE A 37
SHEET 3 AA116 ILE A 116 PRO A 120 -1 O VAL A 117 N TYR A 62
SHEET 4 AA116 THR A 77 LEU A 81 1 N LEU A 78 O ILE A 116
SHEET 5 AA116 ARG A 165 HIS A 170 1 O GLY A 166 N THR A 77
SHEET 6 AA116 ALA A 190 LEU A 194 1 O LEU A 194 N GLY A 169
SHEET 7 AA116 GLY A 299 GLY A 305 1 O ALA A 301 N ALA A 193
SHEET 8 AA116 HIS A 331 TYR A 336 1 O MET A 332 N ILE A 300
SHEET 9 AA116 HIS B 331 TYR B 336 -1 O PHE B 333 N PHE A 333
SHEET 10 AA116 GLY B 299 GLY B 305 1 N ILE B 300 O MET B 332
SHEET 11 AA116 ALA B 190 LEU B 194 1 N ALA B 193 O ALA B 301
SHEET 12 AA116 ARG B 165 HIS B 170 1 N GLY B 169 O LEU B 194
SHEET 13 AA116 THR B 77 LEU B 81 1 N TYR B 79 O ALA B 168
SHEET 14 AA116 ILE B 116 PRO B 120 1 O VAL B 118 N LEU B 80
SHEET 15 AA116 GLU B 56 LEU B 63 -1 N TYR B 62 O VAL B 117
SHEET 16 AA116 ARG B 35 PRO B 42 -1 N ILE B 41 O GLN B 57
SHEET 1 AA2 2 ASN A 133 SER A 134 0
SHEET 2 AA2 2 GLY A 138 ASN A 139 -1 O GLY A 138 N SER A 134
SHEET 1 AA3 2 TYR A 261 ARG A 264 0
SHEET 2 AA3 2 VAL A 267 LYS A 270 -1 O GLU A 269 N GLN A 262
SHEET 1 AA4 2 ASN B 133 SER B 134 0
SHEET 2 AA4 2 GLY B 138 ASN B 139 -1 O GLY B 138 N SER B 134
SHEET 1 AA5 2 TYR B 261 ARG B 264 0
SHEET 2 AA5 2 VAL B 267 LYS B 270 -1 O GLU B 269 N GLN B 262
CISPEP 1 ALA A 253 PRO A 254 0 7.08
CISPEP 2 ALA B 253 PRO B 254 0 2.23
CRYST1 87.749 87.749 172.194 90.00 90.00 120.00 P 31 2 1 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 0.011396 0.006580 0.000000 0.00000
SCALE2 0.000000 0.013159 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005807 0.00000
TER 2728 HIS A 378
TER 5389 PRO B 366
MASTER 424 0 9 36 24 0 0 6 5988 2 60 54
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