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HEADER HYDROLASE 22-NOV-22 8BRB
TITLE POLYESTER HYDROLASE LEIPZIG 7 (PHL7) BOUND TO TEREPHTHALIC ACID (TPA)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYESTER HYDROLASE LEIPZIG 7 (PHL-7), CATALYSIS-DEFICIENT
COMPND 3 S131A MUTANT;
COMPND 4 CHAIN: A, B;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNIDENTIFIED;
SOURCE 3 ORGANISM_TAXID: 32644;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PETASE, CUTINASE, POLYETHYLENE TEREPHTHALATE, HYDROLASE, TEREPHTHALIC
KEYWDS 2 ACID, TPA, POLYESTER HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.K.RICHTER,N.STRATER
REVDAT 1 19-APR-23 8BRB 0
JRNL AUTH P.K.RICHTER,P.BLAZQUEZ-SANCHEZ,Z.ZHAO,F.ENGELBERGER,
JRNL AUTH 2 C.WIEBELER,G.KUNZE,R.FRANK,D.KRINKE,E.FREZZOTTI,Y.LIHANOVA,
JRNL AUTH 3 P.FALKENSTEIN,J.MATYSIK,W.ZIMMERMANN,N.STRATER,
JRNL AUTH 4 C.SONNENDECKER
JRNL TITL STRUCTURE AND FUNCTION OF THE METAGENOMIC PLASTIC-DEGRADING
JRNL TITL 2 POLYESTER HYDROLASE PHL7 BOUND TO ITS PRODUCT.
JRNL REF NAT COMMUN V. 14 1905 2023
JRNL REFN ESSN 2041-1723
JRNL PMID 37019924
JRNL DOI 10.1038/S41467-023-37415-X
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 21.57
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 66048
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.510
REMARK 3 FREE R VALUE TEST SET COUNT : 2978
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 21.5700 - 4.6800 1.00 3090 170 0.1559 0.1783
REMARK 3 2 4.6700 - 3.7200 1.00 3040 141 0.1288 0.1755
REMARK 3 3 3.7200 - 3.2500 1.00 3036 136 0.1430 0.1858
REMARK 3 4 3.2500 - 2.9500 1.00 3010 146 0.1513 0.2090
REMARK 3 5 2.9500 - 2.7400 1.00 3021 150 0.1458 0.1801
REMARK 3 6 2.7400 - 2.5800 1.00 3002 128 0.1374 0.1916
REMARK 3 7 2.5800 - 2.4500 1.00 3002 142 0.1449 0.1966
REMARK 3 8 2.4500 - 2.3400 1.00 3005 144 0.1490 0.2067
REMARK 3 9 2.3400 - 2.2500 1.00 3019 106 0.1846 0.2400
REMARK 3 10 2.2500 - 2.1800 0.99 2993 126 0.1975 0.2557
REMARK 3 11 2.1800 - 2.1100 1.00 2962 162 0.1469 0.1936
REMARK 3 12 2.1100 - 2.0500 1.00 2983 158 0.1547 0.2098
REMARK 3 13 2.0500 - 1.9900 1.00 3018 136 0.1570 0.2178
REMARK 3 14 1.9900 - 1.9500 1.00 2962 137 0.1743 0.2113
REMARK 3 15 1.9500 - 1.9000 1.00 3030 119 0.2343 0.2884
REMARK 3 16 1.9000 - 1.8600 1.00 3018 125 0.2289 0.2602
REMARK 3 17 1.8600 - 1.8200 1.00 2989 121 0.1811 0.2546
REMARK 3 18 1.8200 - 1.7900 1.00 2971 163 0.1851 0.2188
REMARK 3 19 1.7900 - 1.7600 1.00 2930 159 0.1929 0.2412
REMARK 3 20 1.7600 - 1.7300 1.00 3009 167 0.1977 0.2700
REMARK 3 21 1.7300 - 1.7000 1.00 2980 142 0.1967 0.2290
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.350
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.27
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 4181
REMARK 3 ANGLE : 0.773 5731
REMARK 3 CHIRALITY : 0.048 634
REMARK 3 PLANARITY : 0.009 781
REMARK 3 DIHEDRAL : 12.021 1540
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN 'A' AND RESID 2 THROUGH 260)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.2030 3.4187 43.6593
REMARK 3 T TENSOR
REMARK 3 T11: 0.0674 T22: 0.0949
REMARK 3 T33: 0.0634 T12: -0.0128
REMARK 3 T13: -0.0187 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 0.5283 L22: 0.8441
REMARK 3 L33: 0.8971 L12: -0.0874
REMARK 3 L13: -0.0248 L23: -0.3082
REMARK 3 S TENSOR
REMARK 3 S11: 0.0088 S12: -0.0087 S13: -0.0154
REMARK 3 S21: 0.0560 S22: 0.0090 S23: 0.0016
REMARK 3 S31: 0.0174 S32: -0.1283 S33: 0.0519
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN 'B' AND RESID 2 THROUGH 260)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.8424 -5.0448 7.0768
REMARK 3 T TENSOR
REMARK 3 T11: 0.0547 T22: 0.0546
REMARK 3 T33: 0.0599 T12: 0.0015
REMARK 3 T13: 0.0225 T23: -0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 0.9430 L22: 0.6374
REMARK 3 L33: 0.6867 L12: 0.1697
REMARK 3 L13: 0.0815 L23: -0.1018
REMARK 3 S TENSOR
REMARK 3 S11: 0.0105 S12: -0.0959 S13: -0.0018
REMARK 3 S21: -0.0881 S22: -0.0124 S23: -0.0441
REMARK 3 S31: 0.0333 S32: -0.0502 S33: -0.0521
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 8BRB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-NOV-22.
REMARK 100 THE DEPOSITION ID IS D_1292126874.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-NOV-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU PHOTONJET-R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5406
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : RIGAKU HYPIX-6000HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSALISPRO 171.41.112A
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.7
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66097
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 21.570
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.07515
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.3300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.47920
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 7NEI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CITRATE 20 % (W/V) PEG
REMARK 280 4,000 5 % (V/V) 2-PROPANOL, PH 5.6, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 28.25500
REMARK 290 SMTRY3 2 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 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 GLU A 261
REMARK 465 HIS A 262
REMARK 465 HIS A 263
REMARK 465 HIS A 264
REMARK 465 HIS A 265
REMARK 465 HIS A 266
REMARK 465 HIS A 267
REMARK 465 MET B 1
REMARK 465 GLU B 261
REMARK 465 HIS B 262
REMARK 465 HIS B 263
REMARK 465 HIS B 264
REMARK 465 HIS B 265
REMARK 465 HIS B 266
REMARK 465 HIS B 267
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 LEU B 33 CG CD1 CD2
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 HH22 ARG B 111 O HOH B 406 1.56
REMARK 500 OE2 GLU A 68 O HOH A 401 1.79
REMARK 500 O HOH B 530 O HOH B 775 1.95
REMARK 500 O HOH B 622 O HOH B 766 2.00
REMARK 500 O HOH A 401 O HOH A 704 2.02
REMARK 500 O HOH A 467 O HOH A 630 2.02
REMARK 500 O HOH B 800 O HOH B 822 2.03
REMARK 500 O HOH B 834 O HOH B 840 2.03
REMARK 500 O HOH A 715 O HOH B 758 2.04
REMARK 500 O HOH B 465 O HOH B 663 2.06
REMARK 500 O HOH A 757 O HOH A 761 2.06
REMARK 500 O HOH A 700 O HOH A 711 2.06
REMARK 500 O HOH B 409 O HOH B 716 2.07
REMARK 500 O HOH A 660 O HOH A 718 2.08
REMARK 500 O HOH B 619 O HOH B 642 2.09
REMARK 500 OE2 GLU A 68 O HOH A 402 2.11
REMARK 500 O HOH A 719 O HOH B 790 2.12
REMARK 500 O HOH A 408 O HOH A 627 2.12
REMARK 500 O HOH A 759 O HOH A 839 2.13
REMARK 500 OE1 GLU A 68 O HOH A 403 2.13
REMARK 500 O HOH A 788 O HOH A 794 2.13
REMARK 500 O HOH B 826 O HOH B 847 2.13
REMARK 500 O HOH A 620 O HOH A 658 2.13
REMARK 500 O PHE A 259 O HOH A 404 2.14
REMARK 500 O HOH B 408 O HOH B 557 2.14
REMARK 500 O HOH A 842 O HOH B 817 2.15
REMARK 500 O HOH A 796 O HOH A 799 2.17
REMARK 500 O HOH B 598 O HOH B 674 2.17
REMARK 500 O HOH B 464 O HOH B 706 2.17
REMARK 500 O HOH A 660 O HOH A 690 2.17
REMARK 500 O HOH A 597 O HOH A 725 2.18
REMARK 500 O HOH B 583 O HOH B 739 2.18
REMARK 500 O HOH B 579 O HOH B 753 2.18
REMARK 500 O HOH B 620 O HOH B 690 2.19
REMARK 500 O HOH A 631 O HOH A 692 2.19
REMARK 500 O HOH B 655 O HOH B 802 2.19
REMARK 500 O HOH B 407 O HOH B 582 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 430 O HOH A 689 2646 1.95
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 ALA A 131 -125.11 63.49
REMARK 500 HIS A 185 -94.72 -118.13
REMARK 500 PRO A 243 -158.40 -85.14
REMARK 500 ALA B 131 -123.61 62.99
REMARK 500 HIS B 185 -95.97 -119.17
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 841 DISTANCE = 6.08 ANGSTROMS
REMARK 525 HOH A 842 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH A 843 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH A 844 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH A 845 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH A 846 DISTANCE = 6.44 ANGSTROMS
REMARK 525 HOH A 847 DISTANCE = 6.52 ANGSTROMS
REMARK 525 HOH A 848 DISTANCE = 6.58 ANGSTROMS
REMARK 525 HOH A 849 DISTANCE = 6.79 ANGSTROMS
REMARK 525 HOH A 850 DISTANCE = 6.87 ANGSTROMS
REMARK 525 HOH A 851 DISTANCE = 7.99 ANGSTROMS
REMARK 525 HOH A 852 DISTANCE = 8.09 ANGSTROMS
REMARK 525 HOH A 853 DISTANCE = 9.17 ANGSTROMS
REMARK 525 HOH B 843 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH B 844 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH B 845 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH B 846 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH B 847 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH B 848 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH B 849 DISTANCE = 6.36 ANGSTROMS
REMARK 525 HOH B 850 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH B 851 DISTANCE = 6.93 ANGSTROMS
REMARK 525 HOH B 852 DISTANCE = 7.00 ANGSTROMS
REMARK 525 HOH B 853 DISTANCE = 7.22 ANGSTROMS
REMARK 525 HOH B 854 DISTANCE = 7.24 ANGSTROMS
REMARK 525 HOH B 855 DISTANCE = 7.27 ANGSTROMS
REMARK 525 HOH B 856 DISTANCE = 7.35 ANGSTROMS
REMARK 525 HOH B 857 DISTANCE = 7.41 ANGSTROMS
DBREF 8BRB A 1 267 PDB 8BRB 8BRB 1 267
DBREF 8BRB B 1 267 PDB 8BRB 8BRB 1 267
SEQRES 1 A 267 MET ALA ASN PRO TYR GLU ARG GLY PRO ASP PRO THR GLU
SEQRES 2 A 267 SER SER ILE GLU ALA VAL ARG GLY PRO PHE ALA VAL ALA
SEQRES 3 A 267 GLN THR THR VAL SER ARG LEU GLN ALA ASP GLY PHE GLY
SEQRES 4 A 267 GLY GLY THR ILE TYR TYR PRO THR ASP THR SER GLN GLY
SEQRES 5 A 267 THR PHE GLY ALA VAL ALA ILE SER PRO GLY PHE THR ALA
SEQRES 6 A 267 GLY GLN GLU SER ILE ALA TRP LEU GLY PRO ARG ILE ALA
SEQRES 7 A 267 SER GLN GLY PHE VAL VAL ILE THR ILE ASP THR ILE THR
SEQRES 8 A 267 ARG LEU ASP GLN PRO ASP SER ARG GLY ARG GLN LEU GLN
SEQRES 9 A 267 ALA ALA LEU ASP HIS LEU ARG THR ASN SER VAL VAL ARG
SEQRES 10 A 267 ASN ARG ILE ASP PRO ASN ARG MET ALA VAL MET GLY HIS
SEQRES 11 A 267 ALA MET GLY GLY GLY GLY ALA LEU SER ALA ALA ALA ASN
SEQRES 12 A 267 ASN THR SER LEU GLU ALA ALA ILE PRO LEU GLN GLY TRP
SEQRES 13 A 267 HIS THR ARG LYS ASN TRP SER SER VAL ARG THR PRO THR
SEQRES 14 A 267 LEU VAL VAL GLY ALA GLN LEU ASP THR ILE ALA PRO VAL
SEQRES 15 A 267 SER SER HIS SER GLU ALA PHE TYR ASN SER LEU PRO SER
SEQRES 16 A 267 ASP LEU ASP LYS ALA TYR MET GLU LEU ARG GLY ALA SER
SEQRES 17 A 267 HIS LEU VAL SER ASN THR PRO ASP THR THR THR ALA LYS
SEQRES 18 A 267 TYR SER ILE ALA TRP LEU LYS ARG PHE VAL ASP ASP ASP
SEQRES 19 A 267 LEU ARG TYR GLU GLN PHE LEU CYS PRO ALA PRO ASP ASP
SEQRES 20 A 267 PHE ALA ILE SER GLU TYR ARG SER THR CYS PRO PHE LEU
SEQRES 21 A 267 GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 267 MET ALA ASN PRO TYR GLU ARG GLY PRO ASP PRO THR GLU
SEQRES 2 B 267 SER SER ILE GLU ALA VAL ARG GLY PRO PHE ALA VAL ALA
SEQRES 3 B 267 GLN THR THR VAL SER ARG LEU GLN ALA ASP GLY PHE GLY
SEQRES 4 B 267 GLY GLY THR ILE TYR TYR PRO THR ASP THR SER GLN GLY
SEQRES 5 B 267 THR PHE GLY ALA VAL ALA ILE SER PRO GLY PHE THR ALA
SEQRES 6 B 267 GLY GLN GLU SER ILE ALA TRP LEU GLY PRO ARG ILE ALA
SEQRES 7 B 267 SER GLN GLY PHE VAL VAL ILE THR ILE ASP THR ILE THR
SEQRES 8 B 267 ARG LEU ASP GLN PRO ASP SER ARG GLY ARG GLN LEU GLN
SEQRES 9 B 267 ALA ALA LEU ASP HIS LEU ARG THR ASN SER VAL VAL ARG
SEQRES 10 B 267 ASN ARG ILE ASP PRO ASN ARG MET ALA VAL MET GLY HIS
SEQRES 11 B 267 ALA MET GLY GLY GLY GLY ALA LEU SER ALA ALA ALA ASN
SEQRES 12 B 267 ASN THR SER LEU GLU ALA ALA ILE PRO LEU GLN GLY TRP
SEQRES 13 B 267 HIS THR ARG LYS ASN TRP SER SER VAL ARG THR PRO THR
SEQRES 14 B 267 LEU VAL VAL GLY ALA GLN LEU ASP THR ILE ALA PRO VAL
SEQRES 15 B 267 SER SER HIS SER GLU ALA PHE TYR ASN SER LEU PRO SER
SEQRES 16 B 267 ASP LEU ASP LYS ALA TYR MET GLU LEU ARG GLY ALA SER
SEQRES 17 B 267 HIS LEU VAL SER ASN THR PRO ASP THR THR THR ALA LYS
SEQRES 18 B 267 TYR SER ILE ALA TRP LEU LYS ARG PHE VAL ASP ASP ASP
SEQRES 19 B 267 LEU ARG TYR GLU GLN PHE LEU CYS PRO ALA PRO ASP ASP
SEQRES 20 B 267 PHE ALA ILE SER GLU TYR ARG SER THR CYS PRO PHE LEU
SEQRES 21 B 267 GLU HIS HIS HIS HIS HIS HIS
HET UB7 A 301 18
HET DMS A 302 10
HET UB7 B 301 18
HET DMS B 302 10
HETNAM UB7 TEREPHTHALIC ACID
HETNAM DMS DIMETHYL SULFOXIDE
HETSYN UB7 BENZENE-1,4-DICARBOXYLIC ACID
FORMUL 3 UB7 2(C8 H6 O4)
FORMUL 4 DMS 2(C2 H6 O S)
FORMUL 7 HOH *910(H2 O)
HELIX 1 AA1 THR A 12 ALA A 18 1 7
HELIX 2 AA2 GLY A 66 ALA A 71 5 6
HELIX 3 AA3 TRP A 72 SER A 79 1 8
HELIX 4 AA4 GLN A 95 ASN A 113 1 19
HELIX 5 AA5 VAL A 116 ASN A 118 5 3
HELIX 6 AA6 ALA A 131 ASN A 143 1 13
HELIX 7 AA7 HIS A 185 LEU A 193 1 9
HELIX 8 AA8 LEU A 210 THR A 214 5 5
HELIX 9 AA9 ASP A 216 ASP A 232 1 17
HELIX 10 AB1 ASP A 234 ARG A 236 5 3
HELIX 11 AB2 TYR A 237 CYS A 242 1 6
HELIX 12 AB3 THR B 12 ALA B 18 1 7
HELIX 13 AB4 GLY B 66 ALA B 71 5 6
HELIX 14 AB5 TRP B 72 SER B 79 1 8
HELIX 15 AB6 GLN B 95 ASN B 113 1 19
HELIX 16 AB7 ALA B 131 ASN B 143 1 13
HELIX 17 AB8 HIS B 185 LEU B 193 1 9
HELIX 18 AB9 SER B 208 THR B 214 5 7
HELIX 19 AC1 ASP B 216 ASP B 232 1 17
HELIX 20 AC2 ASP B 234 LEU B 241 5 8
SHEET 1 AA1 6 VAL A 25 VAL A 30 0
SHEET 2 AA1 6 GLY A 41 PRO A 46 -1 O GLY A 41 N VAL A 30
SHEET 3 AA1 6 VAL A 83 ILE A 87 -1 O VAL A 84 N TYR A 44
SHEET 4 AA1 6 PHE A 54 SER A 60 1 N VAL A 57 O ILE A 85
SHEET 5 AA1 6 ILE A 120 HIS A 130 1 O ARG A 124 N ALA A 56
SHEET 6 AA1 6 ALA A 149 LEU A 153 1 O LEU A 153 N GLY A 129
SHEET 1 AA2 3 THR A 169 ALA A 174 0
SHEET 2 AA2 3 LYS A 199 LEU A 204 1 O ALA A 200 N VAL A 171
SHEET 3 AA2 3 ILE A 250 SER A 255 -1 O ARG A 254 N TYR A 201
SHEET 1 AA3 6 VAL B 25 VAL B 30 0
SHEET 2 AA3 6 GLY B 41 PRO B 46 -1 O ILE B 43 N THR B 28
SHEET 3 AA3 6 VAL B 83 ILE B 87 -1 O VAL B 84 N TYR B 44
SHEET 4 AA3 6 PHE B 54 SER B 60 1 N VAL B 57 O ILE B 85
SHEET 5 AA3 6 ILE B 120 HIS B 130 1 O ASP B 121 N PHE B 54
SHEET 6 AA3 6 ALA B 149 LEU B 153 1 O LEU B 153 N GLY B 129
SHEET 1 AA4 3 THR B 169 ALA B 174 0
SHEET 2 AA4 3 LYS B 199 LEU B 204 1 O LEU B 204 N GLY B 173
SHEET 3 AA4 3 ILE B 250 SER B 255 -1 O ARG B 254 N TYR B 201
SSBOND 1 CYS A 242 CYS A 257 1555 1555 2.03
SSBOND 2 CYS B 242 CYS B 257 1555 1555 2.03
CISPEP 1 CYS A 242 PRO A 243 0 0.07
CISPEP 2 CYS A 257 PRO A 258 0 -6.07
CISPEP 3 CYS B 242 PRO B 243 0 -0.22
CISPEP 4 CYS B 257 PRO B 258 0 -6.63
CRYST1 52.912 56.510 101.744 90.00 94.11 90.00 P 1 21 1 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 0.018899 0.000000 0.001358 0.00000
SCALE2 0.000000 0.017696 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009854 0.00000
TER 3985 LEU A 260
TER 7959 LEU B 260
MASTER 394 0 4 20 18 0 0 6 4875 2 60 42
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