HEADER METAL TRANSPORT 22-JAN-13 3ZK7
TITLE CRYSTAL STRUCTURE OF PNEUMOCOCCAL SURFACE ANTIGEN PSAA IN THE METAL-
TITLE 2 FREE, OPEN STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MANGANESE ABC TRANSPORTER SUBSTRATE-BINDING LIPOPROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 23-309;
COMPND 5 SYNONYM: PNEUMOCOCCAL SURFACE ADHESIN A, PSAA;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE 3 ORGANISM_COMMON: PNEUMOCOCCUS;
SOURCE 4 ORGANISM_TAXID: 1313;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS METAL TRANSPORT, ATP-BINDING CASSETTE TRANSPORTERS, LIPOPROTEIN,
KEYWDS 2 MEMBRANE TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.M.COUNAGO,M.P.WEEN,M.BAJAJ,J.ZUEGG,M.A.COOPER,A.G.MCEWAN,J.C.PATON,
AUTHOR 2 B.KOBE,C.A.MCDEVITT
REVDAT 7 20-DEC-23 3ZK7 1 REMARK
REVDAT 6 06-MAR-19 3ZK7 1 REMARK
REVDAT 5 28-MAR-18 3ZK7 1 JRNL ATOM
REVDAT 4 08-JAN-14 3ZK7 1 JRNL
REVDAT 3 20-NOV-13 3ZK7 1 JRNL
REVDAT 2 13-NOV-13 3ZK7 1 JRNL
REVDAT 1 06-NOV-13 3ZK7 0
JRNL AUTH R.M.COUNAGO,M.P.WEEN,S.L.BEGG,M.BAJAJ,J.ZUEGG,M.L.O'MARA,
JRNL AUTH 2 M.A.COOPER,A.G.MCEWAN,J.C.PATON,B.KOBE,C.A.MCDEVITT
JRNL TITL IMPERFECT COORDINATION CHEMISTRY FACILITATES METAL ION
JRNL TITL 2 RELEASE IN THE PSA PERMEASE.
JRNL REF NAT. CHEM. BIOL. V. 10 35 2014
JRNL REFN ESSN 1552-4469
JRNL PMID 24212134
JRNL DOI 10.1038/NCHEMBIO.1382
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.C.LAWRENCE,P.A.PILLING,V.C.EPA,A.M.BERRY,A.D.OGUNNIYI,
REMARK 1 AUTH 2 J.C.PATON
REMARK 1 TITL THE CRYSTAL STRUCTURE OF PNEUMOCOCCAL SURFACE ANTIGEN PSAA
REMARK 1 TITL 2 REVEALS A METAL-BINDING SITE AND A NOVEL STRUCTURE FOR A
REMARK 1 TITL 3 PUTATIVE ABC-TYPE BINDING PROTEIN.
REMARK 1 REF STRUCTURE V. 6 1553 1998
REMARK 1 REFN ISSN 0969-2126
REMARK 1 PMID 9862808
REMARK 1 DOI 10.1016/S0969-2126(98)00153-1
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.A.MCDEVITT,A.D.OGUNNIYI,E.VALKOV,M.C.LAWRENCE,B.KOBE,
REMARK 1 AUTH 2 A.G.MCEWAN,J.C.PATON
REMARK 1 TITL A MOLECULAR MECHANISM FOR BACTERIAL SUSCEPTIBILITY TO ZINC.
REMARK 1 REF PLOS PATHOG. V. 7 02357 2011
REMARK 1 REFN ISSN 1553-7366
REMARK 1 PMID 22072971
REMARK 1 DOI 10.1371/JOURNAL.PPAT.1002357
REMARK 2
REMARK 2 RESOLUTION. 1.69 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 17.04
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 57796
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 2930
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.69
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.73
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.56
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 4069
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2041
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3861
REMARK 3 BIN R VALUE (WORKING SET) : 0.2031
REMARK 3 BIN FREE R VALUE : 0.2241
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.11
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 208
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4432
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 667
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.88
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.05
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.77460
REMARK 3 B22 (A**2) : 0.29820
REMARK 3 B33 (A**2) : 1.47650
REMARK 3 B12 (A**2) : -1.07260
REMARK 3 B13 (A**2) : 0.16740
REMARK 3 B23 (A**2) : -0.48550
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.194
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.103
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.097
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.142
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.098
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 9004 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 16380 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2570 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 148 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1226 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 9004 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 602 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 9973 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.05
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.26
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.02
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|32 - 123 }
REMARK 3 ORIGIN FOR THE GROUP (A): 1.1117 -18.3272 36.7110
REMARK 3 T TENSOR
REMARK 3 T11: -0.0225 T22: -0.0695
REMARK 3 T33: -0.0563 T12: 0.0247
REMARK 3 T13: 0.0299 T23: -0.0246
REMARK 3 L TENSOR
REMARK 3 L11: 0.5050 L22: 2.2364
REMARK 3 L33: 0.7251 L12: -0.0636
REMARK 3 L13: -0.0866 L23: 0.4325
REMARK 3 S TENSOR
REMARK 3 S11: -0.0139 S12: 0.0074 S13: -0.0652
REMARK 3 S21: -0.0533 S22: -0.0240 S23: 0.0005
REMARK 3 S31: 0.0716 S32: -0.0009 S33: 0.0380
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|124 - 145 }
REMARK 3 ORIGIN FOR THE GROUP (A): -4.2923 -3.1507 47.4210
REMARK 3 T TENSOR
REMARK 3 T11: -0.0258 T22: -0.0529
REMARK 3 T33: -0.0461 T12: 0.0108
REMARK 3 T13: 0.0177 T23: -0.0277
REMARK 3 L TENSOR
REMARK 3 L11: 3.3971 L22: 1.5810
REMARK 3 L33: 3.4711 L12: -0.6402
REMARK 3 L13: -3.4272 L23: 0.1503
REMARK 3 S TENSOR
REMARK 3 S11: -0.1007 S12: 0.0780 S13: -0.1036
REMARK 3 S21: 0.2212 S22: 0.0501 S23: 0.0815
REMARK 3 S31: 0.1524 S32: -0.1749 S33: 0.0506
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { A|146 - 196 }
REMARK 3 ORIGIN FOR THE GROUP (A): 15.3198 -7.8880 45.0847
REMARK 3 T TENSOR
REMARK 3 T11: -0.0288 T22: 0.0330
REMARK 3 T33: 0.0738 T12: 0.0455
REMARK 3 T13: -0.0319 T23: -0.0420
REMARK 3 L TENSOR
REMARK 3 L11: 0.4953 L22: 2.4540
REMARK 3 L33: 0.5035 L12: -0.0698
REMARK 3 L13: -0.0715 L23: 0.1506
REMARK 3 S TENSOR
REMARK 3 S11: -0.0665 S12: -0.1280 S13: -0.0089
REMARK 3 S21: 0.1287 S22: 0.0767 S23: -0.4825
REMARK 3 S31: 0.0552 S32: 0.1280 S33: -0.0101
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { A|197 - 309 }
REMARK 3 ORIGIN FOR THE GROUP (A): -0.7245 8.8984 34.9286
REMARK 3 T TENSOR
REMARK 3 T11: -0.0342 T22: -0.0596
REMARK 3 T33: -0.0469 T12: 0.0035
REMARK 3 T13: 0.0148 T23: -0.0423
REMARK 3 L TENSOR
REMARK 3 L11: 0.7561 L22: 1.7698
REMARK 3 L33: 1.3660 L12: -0.2217
REMARK 3 L13: 0.5090 L23: -0.4084
REMARK 3 S TENSOR
REMARK 3 S11: -0.0927 S12: -0.0646 S13: 0.0504
REMARK 3 S21: -0.1198 S22: 0.0498 S23: -0.0226
REMARK 3 S31: -0.1612 S32: -0.0696 S33: 0.0429
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: { B|32 - 123 }
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7988 -5.2281 11.0108
REMARK 3 T TENSOR
REMARK 3 T11: -0.0446 T22: -0.0634
REMARK 3 T33: -0.0371 T12: -0.0110
REMARK 3 T13: -0.0226 T23: -0.0246
REMARK 3 L TENSOR
REMARK 3 L11: 0.5648 L22: 2.4524
REMARK 3 L33: 1.0659 L12: -0.1549
REMARK 3 L13: -0.3596 L23: 0.0570
REMARK 3 S TENSOR
REMARK 3 S11: 0.0288 S12: 0.0261 S13: 0.0426
REMARK 3 S21: 0.0946 S22: -0.0717 S23: -0.0713
REMARK 3 S31: -0.0908 S32: -0.0098 S33: 0.0429
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: { B|124 - 145 }
REMARK 3 ORIGIN FOR THE GROUP (A): -3.4783 -20.3834 0.1873
REMARK 3 T TENSOR
REMARK 3 T11: -0.0207 T22: -0.0306
REMARK 3 T33: 0.0029 T12: 0.0167
REMARK 3 T13: -0.0219 T23: -0.0411
REMARK 3 L TENSOR
REMARK 3 L11: 0.9575 L22: 0.8311
REMARK 3 L33: 3.6013 L12: 0.1418
REMARK 3 L13: 2.0435 L23: 0.6269
REMARK 3 S TENSOR
REMARK 3 S11: -0.0139 S12: -0.1715 S13: 0.0308
REMARK 3 S21: -0.1462 S22: -0.1414 S23: 0.0556
REMARK 3 S31: -0.0646 S32: -0.2689 S33: 0.1553
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: { B|146 - 196 }
REMARK 3 ORIGIN FOR THE GROUP (A): 15.8630 -14.5426 2.6527
REMARK 3 T TENSOR
REMARK 3 T11: -0.1070 T22: 0.0201
REMARK 3 T33: 0.1143 T12: -0.0001
REMARK 3 T13: 0.0539 T23: 0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 0.2572 L22: 4.1951
REMARK 3 L33: 0.8650 L12: -0.5760
REMARK 3 L13: -0.0035 L23: 0.3157
REMARK 3 S TENSOR
REMARK 3 S11: 0.0321 S12: 0.1203 S13: 0.1208
REMARK 3 S21: -0.2440 S22: -0.0254 S23: -0.7581
REMARK 3 S31: -0.0548 S32: 0.1330 S33: -0.0067
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: { B|197 - 309 }
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0056 -32.5192 12.3719
REMARK 3 T TENSOR
REMARK 3 T11: -0.0620 T22: -0.0567
REMARK 3 T33: -0.0363 T12: 0.0120
REMARK 3 T13: -0.0075 T23: -0.0303
REMARK 3 L TENSOR
REMARK 3 L11: 0.5454 L22: 2.8560
REMARK 3 L33: 0.7845 L12: -0.0898
REMARK 3 L13: 0.0427 L23: -0.1231
REMARK 3 S TENSOR
REMARK 3 S11: -0.0051 S12: 0.0102 S13: -0.0342
REMARK 3 S21: 0.1276 S22: -0.0157 S23: 0.0081
REMARK 3 S31: 0.0946 S32: -0.0033 S33: 0.0209
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3ZK7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JAN-13.
REMARK 100 THE DEPOSITION ID IS D_1290055509.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95369
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 (SI111)
REMARK 200 OPTICS : SILICON MIRRORS (ADAPTIVE AND U
REMARK 200 -BENT)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57796
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.690
REMARK 200 RESOLUTION RANGE LOW (A) : 17.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.74000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1PSZ
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12.5% W/V PEG 1,000 12.5% W/V PEG
REMARK 280 3,350, 12.5% V/V MPD; 0.1 M TRIZMA/BICINE PH 8.7 AFTER 7-10 DAYS
REMARK 280 AT 293 K, FOLLOWING STREAK-SEEDING OF PRE-EQUILIBRATED (24 HOURS)
REMARK 280 DROPS
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 ILE A 90 47.40 38.27
REMARK 500 LYS A 113 -59.20 -127.82
REMARK 500 HIS A 139 46.70 -84.38
REMARK 500 LYS B 113 -59.11 -128.81
REMARK 500 HIS B 139 40.14 -84.41
REMARK 500 THR B 279 -70.05 -120.18
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 A2013 DISTANCE = 6.93 ANGSTROMS
REMARK 525 HOH A2329 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH A2330 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH B2128 DISTANCE = 7.29 ANGSTROMS
REMARK 525 HOH B2338 DISTANCE = 6.16 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS B 1310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 1310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS B 1311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 1311
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ZK8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PNEUMOCOCCAL SURFACE ANTIGEN PSAA E205Q IN THE
REMARK 900 METAL-FREE, OPEN STATE
REMARK 900 RELATED ID: 3ZK9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PNEUMOCOCCAL SURFACE ANTIGEN PSAA D280N IN THE
REMARK 900 METAL-FREE, OPEN STATE
REMARK 900 RELATED ID: 3ZKA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PNEUMOCOCCAL SURFACE ANTIGEN PSAA D280N IN THE
REMARK 900 METAL-BOUND, OPEN STATE
REMARK 900 RELATED ID: 3ZTT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PNEUMOCOCCAL SURFACE ANTIGEN PSAA WITH
REMARK 900 MANGANESE
DBREF 3ZK7 A 32 309 UNP P0A4G2 MTSA_STRPN 32 309
DBREF 3ZK7 B 32 309 UNP P0A4G2 MTSA_STRPN 32 309
SEQRES 1 A 278 LYS LEU LYS VAL VAL ALA THR ASN SER ILE ILE ALA ASP
SEQRES 2 A 278 ILE THR LYS ASN ILE ALA GLY ASP LYS ILE ASP LEU HIS
SEQRES 3 A 278 SER ILE VAL PRO ILE GLY GLN ASP PRO HIS GLU TYR GLU
SEQRES 4 A 278 PRO LEU PRO GLU ASP VAL LYS LYS THR SER GLU ALA ASP
SEQRES 5 A 278 LEU ILE PHE TYR ASN GLY ILE ASN LEU GLU THR GLY GLY
SEQRES 6 A 278 ASN ALA TRP PHE THR LYS LEU VAL GLU ASN ALA LYS LYS
SEQRES 7 A 278 THR GLU ASN LYS ASP TYR PHE ALA VAL SER ASP GLY VAL
SEQRES 8 A 278 ASP VAL ILE TYR LEU GLU GLY GLN ASN GLU LYS GLY LYS
SEQRES 9 A 278 GLU ASP PRO HIS ALA TRP LEU ASN LEU GLU ASN GLY ILE
SEQRES 10 A 278 ILE PHE ALA LYS ASN ILE ALA LYS GLN LEU SER ALA LYS
SEQRES 11 A 278 ASP PRO ASN ASN LYS GLU PHE TYR GLU LYS ASN LEU LYS
SEQRES 12 A 278 GLU TYR THR ASP LYS LEU ASP LYS LEU ASP LYS GLU SER
SEQRES 13 A 278 LYS ASP LYS PHE ASN LYS ILE PRO ALA GLU LYS LYS LEU
SEQRES 14 A 278 ILE VAL THR SER GLU GLY ALA PHE LYS TYR PHE SER LYS
SEQRES 15 A 278 ALA TYR GLY VAL PRO SER ALA TYR ILE TRP GLU ILE ASN
SEQRES 16 A 278 THR GLU GLU GLU GLY THR PRO GLU GLN ILE LYS THR LEU
SEQRES 17 A 278 VAL GLU LYS LEU ARG GLN THR LYS VAL PRO SER LEU PHE
SEQRES 18 A 278 VAL GLU SER SER VAL ASP ASP ARG PRO MET LYS THR VAL
SEQRES 19 A 278 SER GLN ASP THR ASN ILE PRO ILE TYR ALA GLN ILE PHE
SEQRES 20 A 278 THR ASP SER ILE ALA GLU GLN GLY LYS GLU GLY ASP SER
SEQRES 21 A 278 TYR TYR SER MET MET LYS TYR ASN LEU ASP LYS ILE ALA
SEQRES 22 A 278 GLU GLY LEU ALA LYS
SEQRES 1 B 278 LYS LEU LYS VAL VAL ALA THR ASN SER ILE ILE ALA ASP
SEQRES 2 B 278 ILE THR LYS ASN ILE ALA GLY ASP LYS ILE ASP LEU HIS
SEQRES 3 B 278 SER ILE VAL PRO ILE GLY GLN ASP PRO HIS GLU TYR GLU
SEQRES 4 B 278 PRO LEU PRO GLU ASP VAL LYS LYS THR SER GLU ALA ASP
SEQRES 5 B 278 LEU ILE PHE TYR ASN GLY ILE ASN LEU GLU THR GLY GLY
SEQRES 6 B 278 ASN ALA TRP PHE THR LYS LEU VAL GLU ASN ALA LYS LYS
SEQRES 7 B 278 THR GLU ASN LYS ASP TYR PHE ALA VAL SER ASP GLY VAL
SEQRES 8 B 278 ASP VAL ILE TYR LEU GLU GLY GLN ASN GLU LYS GLY LYS
SEQRES 9 B 278 GLU ASP PRO HIS ALA TRP LEU ASN LEU GLU ASN GLY ILE
SEQRES 10 B 278 ILE PHE ALA LYS ASN ILE ALA LYS GLN LEU SER ALA LYS
SEQRES 11 B 278 ASP PRO ASN ASN LYS GLU PHE TYR GLU LYS ASN LEU LYS
SEQRES 12 B 278 GLU TYR THR ASP LYS LEU ASP LYS LEU ASP LYS GLU SER
SEQRES 13 B 278 LYS ASP LYS PHE ASN LYS ILE PRO ALA GLU LYS LYS LEU
SEQRES 14 B 278 ILE VAL THR SER GLU GLY ALA PHE LYS TYR PHE SER LYS
SEQRES 15 B 278 ALA TYR GLY VAL PRO SER ALA TYR ILE TRP GLU ILE ASN
SEQRES 16 B 278 THR GLU GLU GLU GLY THR PRO GLU GLN ILE LYS THR LEU
SEQRES 17 B 278 VAL GLU LYS LEU ARG GLN THR LYS VAL PRO SER LEU PHE
SEQRES 18 B 278 VAL GLU SER SER VAL ASP ASP ARG PRO MET LYS THR VAL
SEQRES 19 B 278 SER GLN ASP THR ASN ILE PRO ILE TYR ALA GLN ILE PHE
SEQRES 20 B 278 THR ASP SER ILE ALA GLU GLN GLY LYS GLU GLY ASP SER
SEQRES 21 B 278 TYR TYR SER MET MET LYS TYR ASN LEU ASP LYS ILE ALA
SEQRES 22 B 278 GLU GLY LEU ALA LYS
HET TRS A1310 20
HET TRS A1311 20
HET TRS B1310 20
HET TRS B1311 20
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN TRS TRIS BUFFER
FORMUL 3 TRS 4(C4 H12 N O3 1+)
FORMUL 7 HOH *667(H2 O)
HELIX 1 1 ASN A 39 GLY A 51 1 13
HELIX 2 2 LEU A 72 ALA A 82 1 11
HELIX 3 3 ALA A 98 ALA A 107 1 10
HELIX 4 4 LEU A 127 GLN A 130 5 4
HELIX 5 5 HIS A 139 LEU A 142 5 4
HELIX 6 6 ASN A 143 ASP A 162 1 20
HELIX 7 7 ASN A 165 ILE A 194 1 30
HELIX 8 8 PRO A 195 LYS A 199 5 5
HELIX 9 9 PHE A 208 GLY A 216 1 9
HELIX 10 10 THR A 232 ARG A 244 1 13
HELIX 11 11 ASP A 259 ASN A 270 1 12
HELIX 12 12 SER A 291 LYS A 309 1 19
HELIX 13 13 ASN B 39 GLY B 51 1 13
HELIX 14 14 LEU B 72 ALA B 82 1 11
HELIX 15 15 ASN B 91 GLU B 93 5 3
HELIX 16 16 THR B 94 ALA B 107 1 14
HELIX 17 17 LEU B 127 GLN B 130 5 4
HELIX 18 18 HIS B 139 LEU B 142 5 4
HELIX 19 19 ASN B 143 ASP B 162 1 20
HELIX 20 20 ASN B 165 ILE B 194 1 30
HELIX 21 21 PRO B 195 LYS B 199 5 5
HELIX 22 22 PHE B 208 GLY B 216 1 9
HELIX 23 23 THR B 232 ARG B 244 1 13
HELIX 24 24 ASP B 259 ASN B 270 1 12
HELIX 25 25 SER B 291 LYS B 309 1 19
SHEET 1 AA 4 ILE A 54 SER A 58 0
SHEET 2 AA 4 LEU A 33 ALA A 37 1 O LEU A 33 N ASP A 55
SHEET 3 AA 4 LEU A 84 TYR A 87 1 O LEU A 84 N VAL A 36
SHEET 4 AA 4 TYR A 115 ALA A 117 1 O PHE A 116 N TYR A 87
SHEET 1 AB 2 ILE A 201 GLU A 205 0
SHEET 2 AB 2 SER A 219 TRP A 223 1 O ALA A 220 N THR A 203
SHEET 1 AC 2 LEU A 251 GLU A 254 0
SHEET 2 AC 2 ILE A 273 ILE A 277 1 N TYR A 274 O LEU A 251
SHEET 1 BA 4 ILE B 54 SER B 58 0
SHEET 2 BA 4 LEU B 33 ALA B 37 1 O LEU B 33 N ASP B 55
SHEET 3 BA 4 LEU B 84 TYR B 87 1 O LEU B 84 N VAL B 36
SHEET 4 BA 4 TYR B 115 ALA B 117 1 O PHE B 116 N TYR B 87
SHEET 1 BB 2 ILE B 201 GLU B 205 0
SHEET 2 BB 2 SER B 219 TRP B 223 1 O ALA B 220 N THR B 203
SHEET 1 BC 2 LEU B 251 GLU B 254 0
SHEET 2 BC 2 ILE B 273 ILE B 277 1 N TYR B 274 O LEU B 251
SITE 1 AC1 9 ILE A 62 GLY A 63 GLN A 64 HIS B 57
SITE 2 AC1 9 SER B 58 ILE B 59 TYR B 69 GLU B 74
SITE 3 AC1 9 ASP B 75
SITE 1 AC2 10 HIS A 57 SER A 58 ILE A 59 TYR A 69
SITE 2 AC2 10 GLU A 74 ASP A 75 HOH A2032 ILE B 62
SITE 3 AC2 10 GLY B 63 GLN B 64
SITE 1 AC3 6 ASP B 65 HIS B 67 HIS B 139 GLU B 205
SITE 2 AC3 6 ASP B 280 HOH B2293
SITE 1 AC4 5 ASP A 65 HIS A 67 HIS A 139 GLU A 205
SITE 2 AC4 5 ASP A 280
CRYST1 40.940 59.910 62.630 107.02 103.90 96.96 P 1 2
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 0.024426 0.002982 0.007470 0.00000
SCALE2 0.000000 0.016816 0.005958 0.00000
SCALE3 0.000000 0.000000 0.017450 0.00000
(ATOM LINES ARE NOT SHOWN.)
END