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HEADER HYDROLASE 22-NOV-22 8BRA
TITLE POLYESTER HYDROLASE LEIPZIG 7 (PHL7) BOUND TO TEREPHTHALIC ACID (TPA)
TITLE 2 AND MG2+
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, MG2+, MAGNESIUM
EXPDTA X-RAY DIFFRACTION
AUTHOR P.K.RICHTER,N.STRATER
REVDAT 1 19-APR-23 8BRA 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) : 21.46
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 63957
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.131
REMARK 3 R VALUE (WORKING SET) : 0.130
REMARK 3 FREE R VALUE : 0.161
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.510
REMARK 3 FREE R VALUE TEST SET COUNT : 2885
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 21.4600 - 4.6800 1.00 2996 166 0.1405 0.1450
REMARK 3 2 4.6700 - 3.7200 1.00 2942 134 0.1088 0.1283
REMARK 3 3 3.7200 - 3.2500 1.00 2943 141 0.1250 0.1608
REMARK 3 4 3.2500 - 2.9500 1.00 2900 137 0.1308 0.1806
REMARK 3 5 2.9500 - 2.7400 1.00 2906 135 0.1259 0.1426
REMARK 3 6 2.7400 - 2.5800 1.00 2921 139 0.1193 0.1461
REMARK 3 7 2.5800 - 2.4500 1.00 2918 130 0.1189 0.1398
REMARK 3 8 2.4500 - 2.3400 1.00 2890 137 0.1160 0.1510
REMARK 3 9 2.3400 - 2.2500 1.00 2917 107 0.1185 0.1599
REMARK 3 10 2.2500 - 2.1800 1.00 2929 125 0.1207 0.1405
REMARK 3 11 2.1800 - 2.1100 1.00 2928 127 0.1244 0.1707
REMARK 3 12 2.1100 - 2.0500 1.00 2849 176 0.1298 0.1656
REMARK 3 13 2.0500 - 1.9900 1.00 2913 136 0.1298 0.1746
REMARK 3 14 1.9900 - 1.9500 1.00 2869 140 0.1363 0.1714
REMARK 3 15 1.9500 - 1.9000 1.00 2943 109 0.1396 0.2108
REMARK 3 16 1.9000 - 1.8600 1.00 2886 113 0.1467 0.1800
REMARK 3 17 1.8600 - 1.8200 1.00 2909 136 0.1476 0.1679
REMARK 3 18 1.8200 - 1.7900 1.00 2904 127 0.1539 0.2092
REMARK 3 19 1.7900 - 1.7600 1.00 2884 169 0.1639 0.1860
REMARK 3 20 1.7600 - 1.7300 1.00 2902 149 0.1699 0.2087
REMARK 3 21 1.7300 - 1.7000 1.00 2823 152 0.1753 0.2173
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) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 13.740
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 4127
REMARK 3 ANGLE : 0.956 5654
REMARK 3 CHIRALITY : 0.056 631
REMARK 3 PLANARITY : 0.012 762
REMARK 3 DIHEDRAL : 12.434 1513
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): 13.1316 3.1582 42.8477
REMARK 3 T TENSOR
REMARK 3 T11: 0.0375 T22: 0.0623
REMARK 3 T33: 0.0517 T12: 0.0052
REMARK 3 T13: -0.0093 T23: -0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 0.4273 L22: 1.2569
REMARK 3 L33: 0.7514 L12: -0.0461
REMARK 3 L13: -0.0093 L23: -0.4595
REMARK 3 S TENSOR
REMARK 3 S11: -0.0114 S12: 0.0027 S13: 0.0062
REMARK 3 S21: -0.0284 S22: 0.0417 S23: 0.1287
REMARK 3 S31: 0.0079 S32: -0.0878 S33: 0.0144
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN 'B' AND RESID 2 THROUGH 260)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.6536 -4.6878 7.1370
REMARK 3 T TENSOR
REMARK 3 T11: 0.0419 T22: 0.0482
REMARK 3 T33: 0.0349 T12: -0.0058
REMARK 3 T13: 0.0045 T23: -0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 0.5544 L22: 1.1221
REMARK 3 L33: 0.8711 L12: 0.0547
REMARK 3 L13: -0.0407 L23: -0.4185
REMARK 3 S TENSOR
REMARK 3 S11: -0.0092 S12: -0.0209 S13: 0.0142
REMARK 3 S21: -0.0596 S22: 0.0272 S23: 0.0830
REMARK 3 S31: 0.0410 S32: -0.0664 S33: 0.0112
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 8BRA 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_1292126875.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAY-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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 : 63959
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 21.460
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.05707
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.8100
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.33890
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.020
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 (%): 51.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM TRIS 100 MM KCL 30 % (V/V) PEG
REMARK 280 400 10 MM MGCL2, PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 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 28.03450
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 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 HD22 ASN A 213 O HOH A 401 1.45
REMARK 500 HD21 ASN B 123 O HOH B 403 1.48
REMARK 500 O HOH B 427 O HOH B 538 1.95
REMARK 500 O HOH B 730 O HOH B 770 1.95
REMARK 500 O HOH B 536 O HOH B 733 2.01
REMARK 500 O HOH A 680 O HOH A 731 2.02
REMARK 500 O HOH A 551 O HOH A 652 2.02
REMARK 500 O HOH A 451 O HOH A 699 2.03
REMARK 500 O HOH B 647 O HOH B 732 2.03
REMARK 500 O HOH B 669 O HOH B 722 2.06
REMARK 500 O HOH A 675 O HOH A 725 2.06
REMARK 500 O HOH B 403 O HOH B 518 2.07
REMARK 500 O HOH A 494 O HOH A 625 2.09
REMARK 500 O HOH B 582 O HOH B 794 2.09
REMARK 500 O HOH B 541 O HOH B 613 2.10
REMARK 500 O HOH A 711 O HOH A 726 2.11
REMARK 500 O HOH A 407 O HOH A 649 2.11
REMARK 500 O HOH B 531 O HOH B 748 2.11
REMARK 500 O HOH A 724 O HOH A 733 2.12
REMARK 500 O HOH B 665 O HOH B 737 2.12
REMARK 500 ND2 ASN A 213 O HOH A 401 2.13
REMARK 500 O HOH B 776 O HOH B 788 2.16
REMARK 500 O HOH B 572 O HOH B 760 2.18
REMARK 500 O HOH B 759 O HOH B 760 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 528 O HOH A 681 2646 1.80
REMARK 500 O HOH B 528 O HOH B 666 2655 2.13
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 -123.57 64.13
REMARK 500 HIS A 185 -97.51 -117.75
REMARK 500 PRO A 243 -169.27 -73.29
REMARK 500 THR B 64 -2.85 72.12
REMARK 500 ALA B 131 -123.23 65.30
REMARK 500 HIS B 185 -97.76 -119.72
REMARK 500 PRO B 243 -169.44 -74.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ILE B 87 ASP B 88 149.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 99 0.09 SIDE CHAIN
REMARK 500 ARG B 99 0.09 SIDE CHAIN
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 794 DISTANCE = 6.51 ANGSTROMS
REMARK 525 HOH A 795 DISTANCE = 6.68 ANGSTROMS
REMARK 525 HOH B 828 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH B 829 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH B 830 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH B 831 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH B 832 DISTANCE = 6.54 ANGSTROMS
REMARK 525 HOH B 833 DISTANCE = 6.70 ANGSTROMS
REMARK 525 HOH B 834 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH B 835 DISTANCE = 7.14 ANGSTROMS
REMARK 525 HOH B 836 DISTANCE = 7.16 ANGSTROMS
REMARK 525 HOH B 837 DISTANCE = 7.54 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 ASP A 246 OD1
REMARK 620 2 HOH A 423 O 89.3
REMARK 620 3 HOH A 424 O 87.8 170.6
REMARK 620 4 HOH A 463 O 175.2 93.8 88.6
REMARK 620 5 HOH A 501 O 83.1 87.4 83.4 93.3
REMARK 620 6 HOH A 610 O 92.9 92.4 96.7 90.7 176.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 246 OD1
REMARK 620 2 HOH B 422 O 84.2
REMARK 620 3 HOH B 428 O 171.8 87.7
REMARK 620 4 HOH B 444 O 77.3 76.0 101.3
REMARK 620 5 HOH B 482 O 90.8 162.0 97.2 86.0
REMARK 620 6 HOH B 658 O 92.5 99.7 88.3 169.2 97.9
REMARK 620 N 1 2 3 4 5
DBREF 8BRA A 1 267 PDB 8BRA 8BRA 1 267
DBREF 8BRA B 1 267 PDB 8BRA 8BRA 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 MG A 301 1
HET UB7 B 301 18
HET MG B 302 1
HETNAM MG MAGNESIUM ION
HETNAM UB7 TEREPHTHALIC ACID
HETSYN UB7 BENZENE-1,4-DICARBOXYLIC ACID
FORMUL 3 MG 2(MG 2+)
FORMUL 4 UB7 C8 H6 O4
FORMUL 6 HOH *832(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 SER A 208 THR A 214 5 7
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 VAL B 116 ASN B 118 5 3
HELIX 17 AB8 ALA B 131 ASN B 143 1 13
HELIX 18 AB9 HIS B 185 LEU B 193 1 9
HELIX 19 AC1 SER B 208 THR B 214 5 7
HELIX 20 AC2 ASP B 216 ASP B 232 1 17
HELIX 21 AC3 ASP B 234 ARG B 236 5 3
HELIX 22 AC4 TYR B 237 CYS B 242 1 6
SHEET 1 AA1 6 VAL A 25 VAL A 30 0
SHEET 2 AA1 6 GLY A 41 PRO A 46 -1 O ILE A 43 N THR A 28
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 MET A 128 N ALA A 58
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 GLU A 252 N GLU A 203
SHEET 1 AA3 6 VAL B 25 VAL B 30 0
SHEET 2 AA3 6 GLY B 41 PRO B 46 -1 O GLY B 41 N VAL B 30
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 ALA B 200 N VAL B 171
SHEET 3 AA4 3 ILE B 250 SER B 255 -1 O GLU B 252 N GLU B 203
SSBOND 1 CYS A 242 CYS A 257 1555 1555 2.03
SSBOND 2 CYS B 242 CYS B 257 1555 1555 2.04
LINK OD1 ASP A 246 MG MG A 301 1555 1555 2.13
LINK MG MG A 301 O HOH A 423 1555 1555 2.04
LINK MG MG A 301 O HOH A 424 1555 1555 2.13
LINK MG MG A 301 O HOH A 463 1555 1555 2.06
LINK MG MG A 301 O HOH A 501 1555 1555 1.98
LINK MG MG A 301 O HOH A 610 1555 1555 1.97
LINK OD1 ASP B 246 MG MG B 302 1555 1555 2.19
LINK MG MG B 302 O HOH B 422 1555 1555 2.16
LINK MG MG B 302 O HOH B 428 1555 1555 2.07
LINK MG MG B 302 O HOH B 444 1555 1555 2.00
LINK MG MG B 302 O HOH B 482 1555 1555 2.05
LINK MG MG B 302 O HOH B 658 1555 1555 2.07
CISPEP 1 CYS A 242 PRO A 243 0 -2.59
CISPEP 2 CYS A 257 PRO A 258 0 -2.79
CISPEP 3 CYS B 242 PRO B 243 0 -3.98
CISPEP 4 CYS B 257 PRO B 258 0 -2.38
CRYST1 52.352 56.069 100.442 90.00 94.01 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 0.019101 0.000000 0.001339 0.00000
SCALE2 0.000000 0.017835 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009980 0.00000
TER 3967 LEU A 260
TER 7889 LEU B 260
MASTER 416 0 3 22 18 0 0 6 4782 2 38 42
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