HEADER BIOSYNTHETIC PROTEIN 02-NOV-07 2ZC6
TITLE PENICILLIN-BINDING PROTEIN 1A (PBP 1A) ACYL-ENZYME COMPLEX
TITLE 2 (TEBIPENEM) FROM STREPTOCOCCUS PNEUMONIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PENICILLIN-BINDING PROTEIN 1A;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: UNP RESIDUES 47-70;
COMPND 5 SYNONYM: PBP-1A, EXPORTED PROTEIN 2;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: TRANSGLYCOSYLASE DOMAIN;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PENICILLIN-BINDING PROTEIN 1A;
COMPND 10 CHAIN: B, D;
COMPND 11 FRAGMENT: UNP RESIDUES 264-653;
COMPND 12 ENGINEERED: YES;
COMPND 13 MUTATION: YES;
COMPND 14 OTHER_DETAILS: TRANSPEPTIDASE DOMAIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE 3 GENE: PBPA, EXP2;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE 9 GENE: PBP1A;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1
KEYWDS PEPTIDOGLYCAN SYNTHESIS, CELL WALL, PENICILLIN-BINDING,
KEYWDS 2 ANTIBIOTICS, TEBIPENEM, ANTIBIOTIC RESISTANCE, CELL SHAPE,
KEYWDS 3 CELL WALL BIOGENESIS/DEGRADATION, MULTIFUNCTIONAL ENZYME,
KEYWDS 4 SECRETED, BIOSYNTHETIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.YAMADA,T.WATANABE,Y.TAKEUCHI
REVDAT 3 24-FEB-09 2ZC6 1 VERSN
REVDAT 2 03-JUN-08 2ZC6 1 JRNL
REVDAT 1 08-APR-08 2ZC6 0
JRNL AUTH M.YAMADA,T.WATANABE,N.BABA,Y.TAKEUCHI,F.OHSAWA,
JRNL AUTH 2 S.GOMI
JRNL TITL CRYSTAL STRUCTURES OF BIAPENEM AND TEBIPENEM
JRNL TITL 2 COMPLEXED WITH PENICILLIN-BINDING PROTEINS 2X AND
JRNL TITL 3 1A FROM STREPTOCOCCUS PNEUMONIAE
JRNL REF ANTIMICROB.AGENTS CHEMOTHER. V. 52 2053 2008
JRNL REFN ISSN 0066-4804
JRNL PMID 18391040
JRNL DOI 10.1128/AAC.01456-07
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 27562
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) : 0.230
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1473
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2001
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.48
REMARK 3 BIN R VALUE (WORKING SET) : 0.3250
REMARK 3 BIN FREE R VALUE SET COUNT : 100
REMARK 3 BIN FREE R VALUE : 0.3890
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6300
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 40
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 56.87
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.98
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.46000
REMARK 3 B22 (A**2) : 0.13000
REMARK 3 B33 (A**2) : 0.33000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.129
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.359
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.918
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.873
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6506 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8863 ; 1.024 ; 1.949
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 796 ; 5.519 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 315 ;37.243 ;25.175
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1016 ;16.327 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;18.400 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 956 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5054 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2846 ; 0.194 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4465 ; 0.302 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 214 ; 0.136 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 4 ; 0.105 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 55 ; 0.220 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.146 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): 6 ; 0.081 ; 0.200
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3968 ; 0.394 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6391 ; 0.720 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2538 ; 0.602 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2468 ; 1.043 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2ZC6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-NOV-07.
REMARK 100 THE RCSB ID CODE IS RCSB027786.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUL-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : ROTATED-INCLINED DOUBLE-
REMARK 200 CRYSTAL
REMARK 200 OPTICS : ROTATED-INCLINED DOUBLE-
REMARK 200 CRYSTAL MONOCHROMATOR, RHODIUM
REMARK 200 -COATED HORIZONTAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR
REMARK 200 DATA SCALING SOFTWARE : CRYSTALCLEAR
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29074
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 29.880
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.12300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.36400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MORLEP
REMARK 200 STARTING MODEL: PDB ENTRY 2C6W
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.004-0.006M ZINC SULFATE, 0.05M
REMARK 280 MES, PH6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 92.87750
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.13850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 92.87750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 25.13850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -102.2 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 LEU A 47
REMARK 465 VAL A 48
REMARK 465 ALA A 49
REMARK 465 THR A 50
REMARK 465 GLY A 67
REMARK 465 SER A 68
REMARK 465 GLU A 69
REMARK 465 ARG A 70
REMARK 465 SER B 264
REMARK 465 ALA B 265
REMARK 465 SER B 266
REMARK 465 GLY B 651
REMARK 465 ALA B 652
REMARK 465 ARG B 653
REMARK 465 LEU C 47
REMARK 465 VAL C 48
REMARK 465 ALA C 49
REMARK 465 THR C 50
REMARK 465 GLY C 67
REMARK 465 SER C 68
REMARK 465 GLU C 69
REMARK 465 ARG C 70
REMARK 465 SER D 264
REMARK 465 ALA D 265
REMARK 465 SER D 266
REMARK 465 GLY D 651
REMARK 465 ALA D 652
REMARK 465 ARG D 653
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 THR A 51 OG1 CG2
REMARK 470 LYS A 59 NZ
REMARK 470 ASP B 317 CG OD1 OD2
REMARK 470 THR C 51 OG1 CG2
REMARK 470 LYS C 59 NZ
REMARK 470 ASP D 317 CG OD1 OD2
REMARK 470 GLU D 638 CG CD OE1 OE2
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 ASN B 338 -12.61 -141.32
REMARK 500 HIS B 349 76.64 56.04
REMARK 500 SER B 351 47.90 -80.94
REMARK 500 SER B 352 77.65 -152.17
REMARK 500 ASP B 396 74.17 -109.85
REMARK 500 ARG B 413 5.49 58.96
REMARK 500 GLU B 471 -77.87 -90.89
REMARK 500 SER B 472 14.91 56.80
REMARK 500 LYS B 474 -104.56 -127.90
REMARK 500 THR B 574 154.21 176.81
REMARK 500 THR B 588 -163.58 -103.14
REMARK 500 ASN B 643 110.45 -161.75
REMARK 500 ASN D 338 -2.46 -152.38
REMARK 500 GLN D 350 61.99 -105.80
REMARK 500 PRO D 402 125.16 -32.46
REMARK 500 ARG D 413 18.68 54.88
REMARK 500 GLU D 471 -53.37 -145.04
REMARK 500 SER D 472 -12.09 63.63
REMARK 500 LYS D 474 -118.61 -126.33
REMARK 500 HIS D 503 -11.01 -140.25
REMARK 500 THR D 588 -168.49 -108.97
REMARK 500 ASN D 643 84.91 -168.90
REMARK 500
REMARK 500 REMARK: NULL
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 ZN B 801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 309 ND1
REMARK 620 2 TYR B 319 OH 101.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 802 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 395 ND1
REMARK 620 2 GLU B 435 OE1 117.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 808 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 318 OE2
REMARK 620 2 TYR D 319 OH 106.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 806 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 395 ND1
REMARK 620 2 GLU D 435 OE1 97.9
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 801
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 802
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 803
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 804
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 805
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 806
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 807
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 808
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TEB B 701
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TEB D 701
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ZC3 RELATED DB: PDB
REMARK 900 RELATED ID: 2ZC4 RELATED DB: PDB
REMARK 900 RELATED ID: 2ZC5 RELATED DB: PDB
DBREF 2ZC6 A 47 70 UNP Q8DR59 PBPA_STRR6 47 70
DBREF 2ZC6 B 264 653 UNP Q549Y6 Q549Y6_STRPN 264 653
DBREF 2ZC6 C 47 70 UNP Q8DR59 PBPA_STRR6 47 70
DBREF 2ZC6 D 264 653 UNP Q549Y6 Q549Y6_STRPN 264 653
SEQADV 2ZC6 GLN B 545 UNP Q549Y6 ARG 545 ENGINEERED
SEQADV 2ZC6 GLN D 545 UNP Q549Y6 ARG 545 ENGINEERED
SEQRES 1 A 24 LEU VAL ALA THR THR SER SER LYS ILE TYR ASP ASN LYS
SEQRES 2 A 24 ASN GLN LEU ILE ALA ASP LEU GLY SER GLU ARG
SEQRES 1 B 390 SER ALA SER ASN TYR PRO ALA TYR MET ASP ASN TYR LEU
SEQRES 2 B 390 LYS GLU VAL ILE ASN GLN VAL GLU GLU GLU THR GLY TYR
SEQRES 3 B 390 ASN LEU LEU THR THR GLY MET ASP VAL TYR THR ASN VAL
SEQRES 4 B 390 ASP GLN GLU ALA GLN LYS HIS LEU TRP ASP ILE TYR ASN
SEQRES 5 B 390 THR ASP GLU TYR VAL ALA TYR PRO ASP ASP GLU LEU GLN
SEQRES 6 B 390 VAL ALA SER THR ILE VAL ASP VAL SER ASN GLY LYS VAL
SEQRES 7 B 390 ILE ALA GLN LEU GLY ALA ARG HIS GLN SER SER ASN VAL
SEQRES 8 B 390 SER PHE GLY ILE ASN GLN ALA VAL GLU THR ASN ARG ASP
SEQRES 9 B 390 TRP GLY SER THR MET LYS PRO ILE THR ASP TYR ALA PRO
SEQRES 10 B 390 ALA LEU GLU TYR GLY VAL TYR ASP SER THR ALA THR ILE
SEQRES 11 B 390 VAL HIS ASP GLU PRO TYR ASN TYR PRO GLY THR ASN THR
SEQRES 12 B 390 PRO VAL TYR ASN TRP ASP ARG GLY TYR PHE GLY ASN ILE
SEQRES 13 B 390 THR LEU GLN TYR ALA LEU GLN GLN SER ARG ASN VAL PRO
SEQRES 14 B 390 ALA VAL GLU THR LEU ASN LYS VAL GLY LEU ASN ARG ALA
SEQRES 15 B 390 LYS THR PHE LEU ASN GLY LEU GLY ILE ASP TYR PRO SER
SEQRES 16 B 390 ILE HIS TYR SER ASN ALA ILE SER SER ASN THR THR GLU
SEQRES 17 B 390 SER ASP LYS LYS TYR GLY ALA SER SER GLU LYS MET ALA
SEQRES 18 B 390 ALA ALA TYR ALA ALA PHE ALA ASN GLY GLY THR TYR TYR
SEQRES 19 B 390 LYS PRO MET TYR ILE HIS LYS VAL VAL PHE SER ASP GLY
SEQRES 20 B 390 SER GLU LYS GLU PHE SER ASN VAL GLY THR ARG ALA MET
SEQRES 21 B 390 LYS GLU THR THR ALA TYR MET MET THR ASP MET MET LYS
SEQRES 22 B 390 THR VAL LEU SER TYR GLY THR GLY GLN ASN ALA TYR LEU
SEQRES 23 B 390 ALA TRP LEU PRO GLN ALA GLY LYS THR GLY THR SER ASN
SEQRES 24 B 390 TYR THR ASP GLU GLU ILE GLU ASN HIS ILE LYS THR SER
SEQRES 25 B 390 GLN PHE VAL ALA PRO ASP GLU LEU PHE ALA GLY TYR THR
SEQRES 26 B 390 ARG LYS TYR SER MET ALA VAL TRP THR GLY TYR SER ASN
SEQRES 27 B 390 ARG LEU THR PRO LEU VAL GLY ASN GLY LEU THR VAL ALA
SEQRES 28 B 390 ALA LYS VAL TYR ARG SER MET MET THR TYR LEU SER GLU
SEQRES 29 B 390 GLY SER ASN PRO GLU ASP TRP ASN ILE PRO GLU GLY LEU
SEQRES 30 B 390 TYR ARG ASN GLY GLU PHE VAL PHE LYS ASN GLY ALA ARG
SEQRES 1 C 24 LEU VAL ALA THR THR SER SER LYS ILE TYR ASP ASN LYS
SEQRES 2 C 24 ASN GLN LEU ILE ALA ASP LEU GLY SER GLU ARG
SEQRES 1 D 390 SER ALA SER ASN TYR PRO ALA TYR MET ASP ASN TYR LEU
SEQRES 2 D 390 LYS GLU VAL ILE ASN GLN VAL GLU GLU GLU THR GLY TYR
SEQRES 3 D 390 ASN LEU LEU THR THR GLY MET ASP VAL TYR THR ASN VAL
SEQRES 4 D 390 ASP GLN GLU ALA GLN LYS HIS LEU TRP ASP ILE TYR ASN
SEQRES 5 D 390 THR ASP GLU TYR VAL ALA TYR PRO ASP ASP GLU LEU GLN
SEQRES 6 D 390 VAL ALA SER THR ILE VAL ASP VAL SER ASN GLY LYS VAL
SEQRES 7 D 390 ILE ALA GLN LEU GLY ALA ARG HIS GLN SER SER ASN VAL
SEQRES 8 D 390 SER PHE GLY ILE ASN GLN ALA VAL GLU THR ASN ARG ASP
SEQRES 9 D 390 TRP GLY SER THR MET LYS PRO ILE THR ASP TYR ALA PRO
SEQRES 10 D 390 ALA LEU GLU TYR GLY VAL TYR ASP SER THR ALA THR ILE
SEQRES 11 D 390 VAL HIS ASP GLU PRO TYR ASN TYR PRO GLY THR ASN THR
SEQRES 12 D 390 PRO VAL TYR ASN TRP ASP ARG GLY TYR PHE GLY ASN ILE
SEQRES 13 D 390 THR LEU GLN TYR ALA LEU GLN GLN SER ARG ASN VAL PRO
SEQRES 14 D 390 ALA VAL GLU THR LEU ASN LYS VAL GLY LEU ASN ARG ALA
SEQRES 15 D 390 LYS THR PHE LEU ASN GLY LEU GLY ILE ASP TYR PRO SER
SEQRES 16 D 390 ILE HIS TYR SER ASN ALA ILE SER SER ASN THR THR GLU
SEQRES 17 D 390 SER ASP LYS LYS TYR GLY ALA SER SER GLU LYS MET ALA
SEQRES 18 D 390 ALA ALA TYR ALA ALA PHE ALA ASN GLY GLY THR TYR TYR
SEQRES 19 D 390 LYS PRO MET TYR ILE HIS LYS VAL VAL PHE SER ASP GLY
SEQRES 20 D 390 SER GLU LYS GLU PHE SER ASN VAL GLY THR ARG ALA MET
SEQRES 21 D 390 LYS GLU THR THR ALA TYR MET MET THR ASP MET MET LYS
SEQRES 22 D 390 THR VAL LEU SER TYR GLY THR GLY GLN ASN ALA TYR LEU
SEQRES 23 D 390 ALA TRP LEU PRO GLN ALA GLY LYS THR GLY THR SER ASN
SEQRES 24 D 390 TYR THR ASP GLU GLU ILE GLU ASN HIS ILE LYS THR SER
SEQRES 25 D 390 GLN PHE VAL ALA PRO ASP GLU LEU PHE ALA GLY TYR THR
SEQRES 26 D 390 ARG LYS TYR SER MET ALA VAL TRP THR GLY TYR SER ASN
SEQRES 27 D 390 ARG LEU THR PRO LEU VAL GLY ASN GLY LEU THR VAL ALA
SEQRES 28 D 390 ALA LYS VAL TYR ARG SER MET MET THR TYR LEU SER GLU
SEQRES 29 D 390 GLY SER ASN PRO GLU ASP TRP ASN ILE PRO GLU GLY LEU
SEQRES 30 D 390 TYR ARG ASN GLY GLU PHE VAL PHE LYS ASN GLY ALA ARG
HET ZN B 801 1
HET ZN B 802 1
HET ZN B 803 1
HET ZN B 804 1
HET ZN D 805 1
HET ZN D 806 1
HET ZN D 807 1
HET ZN D 808 1
HET TEB B 701 25
HET TEB D 701 25
HETNAM ZN ZINC ION
HETNAM TEB (4R,5S)-3-(1-(4,5-DIHYDROTHIAZOL-2-YL)AZETIDIN-3-
HETNAM 2 TEB YLTHIO)-5-((2S,3R)-3-HYDROXY-1-OXOBUTAN-2-YL)-4-
HETNAM 3 TEB METHYL-4,5- DIHYDRO-1H-PYRROLE-2-CARBOXYLIC ACID
FORMUL 5 ZN 8(ZN 2+)
FORMUL 13 TEB 2(C16 H23 N3 O4 S2)
FORMUL 15 HOH *40(H2 O)
HELIX 1 1 PRO B 269 TYR B 271 5 3
HELIX 2 2 MET B 272 GLY B 288 1 17
HELIX 3 3 ASP B 303 THR B 316 1 14
HELIX 4 4 TRP B 368 SER B 370 5 3
HELIX 5 5 THR B 371 ASP B 377 1 7
HELIX 6 6 ASP B 377 TYR B 384 1 8
HELIX 7 7 LEU B 421 SER B 428 1 8
HELIX 8 8 ASN B 430 GLY B 441 1 12
HELIX 9 9 GLY B 441 GLY B 451 1 11
HELIX 10 10 HIS B 460 ILE B 465 5 6
HELIX 11 11 SER B 479 ASN B 492 1 14
HELIX 12 12 LYS B 524 TYR B 541 1 18
HELIX 13 13 THR B 564 HIS B 571 1 8
HELIX 14 14 ASN B 609 LEU B 611 5 3
HELIX 15 15 THR B 612 GLU B 627 1 16
HELIX 16 16 PRO D 269 TYR D 271 5 3
HELIX 17 17 MET D 272 GLY D 288 1 17
HELIX 18 18 ASP D 303 THR D 316 1 14
HELIX 19 19 ASN D 359 GLU D 363 5 5
HELIX 20 20 TRP D 368 THR D 371 5 4
HELIX 21 21 MET D 372 ASP D 377 1 6
HELIX 22 22 ASP D 377 TYR D 384 1 8
HELIX 23 23 LEU D 421 GLN D 427 1 7
HELIX 24 24 ARG D 429 GLY D 441 1 13
HELIX 25 25 GLY D 441 LEU D 452 1 12
HELIX 26 26 HIS D 460 ILE D 465 5 6
HELIX 27 27 SER D 479 ASN D 492 1 14
HELIX 28 28 LYS D 524 TYR D 541 1 18
HELIX 29 29 GLY D 544 TYR D 548 5 5
HELIX 30 30 THR D 564 HIS D 571 1 8
HELIX 31 31 ASN D 609 LEU D 611 5 3
HELIX 32 32 THR D 612 GLU D 627 1 16
SHEET 1 A 5 LEU A 62 ASP A 65 0
SHEET 2 A 5 LYS A 54 TYR A 56 -1 N ILE A 55 O ILE A 63
SHEET 3 A 5 MET B 296 THR B 300 1 O VAL B 298 N LYS A 54
SHEET 4 A 5 ILE B 502 PHE B 507 -1 O HIS B 503 N TYR B 299
SHEET 5 A 5 GLU B 512 GLU B 514 -1 O LYS B 513 N VAL B 505
SHEET 1 B 5 VAL B 341 LEU B 345 0
SHEET 2 B 5 GLN B 328 ASP B 335 -1 N ILE B 333 O ALA B 343
SHEET 3 B 5 TYR B 591 GLY B 598 -1 O GLY B 598 N GLN B 328
SHEET 4 B 5 ASP B 581 TYR B 587 -1 N PHE B 584 O VAL B 595
SHEET 5 B 5 ALA B 555 THR B 560 -1 N GLY B 559 O LEU B 583
SHEET 1 C 2 ILE B 393 ASP B 396 0
SHEET 2 C 2 GLY B 417 THR B 420 -1 O ILE B 419 N VAL B 394
SHEET 1 D 2 THR B 495 TYR B 496 0
SHEET 2 D 2 THR B 520 ARG B 521 -1 O THR B 520 N TYR B 496
SHEET 1 E 2 VAL B 578 ALA B 579 0
SHEET 2 E 2 LEU B 606 VAL B 607 -1 O LEU B 606 N ALA B 579
SHEET 1 F 2 LEU B 640 ASN B 643 0
SHEET 2 F 2 PHE B 646 LYS B 649 -1 O PHE B 646 N ASN B 643
SHEET 1 G 5 LEU C 62 ASP C 65 0
SHEET 2 G 5 LYS C 54 TYR C 56 -1 N ILE C 55 O ILE C 63
SHEET 3 G 5 MET D 296 THR D 300 1 O THR D 300 N TYR C 56
SHEET 4 G 5 ILE D 502 PHE D 507 -1 O VAL D 506 N ASP D 297
SHEET 5 G 5 GLU D 512 GLU D 514 -1 O LYS D 513 N VAL D 505
SHEET 1 H 5 VAL D 341 LEU D 345 0
SHEET 2 H 5 GLN D 328 ASP D 335 -1 N ILE D 333 O ALA D 343
SHEET 3 H 5 TYR D 591 GLY D 598 -1 O SER D 592 N VAL D 334
SHEET 4 H 5 GLU D 582 THR D 588 -1 N PHE D 584 O VAL D 595
SHEET 5 H 5 GLN D 554 THR D 560 -1 N GLY D 559 O LEU D 583
SHEET 1 I 2 ILE D 393 ASP D 396 0
SHEET 2 I 2 GLY D 417 THR D 420 -1 O ILE D 419 N VAL D 394
SHEET 1 J 2 THR D 495 TYR D 496 0
SHEET 2 J 2 THR D 520 ARG D 521 -1 O THR D 520 N TYR D 496
SHEET 1 K 2 LEU D 640 ASN D 643 0
SHEET 2 K 2 PHE D 646 LYS D 649 -1 O PHE D 648 N TYR D 641
LINK ND1 HIS B 309 ZN ZN B 801 1555 1555 2.20
LINK OH TYR B 319 ZN ZN B 801 1555 1555 2.31
LINK OH TYR B 319 ZN ZN B 804 1555 1555 2.27
LINK ND1 HIS B 395 ZN ZN B 802 1555 1555 2.32
LINK OE1 GLU B 435 ZN ZN B 802 1555 1555 1.90
LINK ND1 HIS B 460 ZN ZN B 803 1555 1555 2.10
LINK ND1 HIS D 309 ZN ZN D 805 1555 1555 2.00
LINK OE2 GLU D 318 ZN ZN D 808 1555 1555 2.00
LINK OH TYR D 319 ZN ZN D 808 1555 1555 2.06
LINK ND1 HIS D 395 ZN ZN D 806 1555 1555 2.21
LINK OE1 GLU D 435 ZN ZN D 806 1555 1555 2.08
LINK ND1 HIS D 460 ZN ZN D 807 1555 1555 1.90
LINK C7 TEB B 701 OG SER B 370 1555 1555 1.36
LINK C7 TEB D 701 OG SER D 370 1555 1555 1.36
SITE 1 AC1 4 HIS B 309 ASP B 312 TYR B 319 GLU B 514
SITE 1 AC2 3 HIS B 395 GLU B 397 GLU B 435
SITE 1 AC3 3 HIS B 460 GLU D 566 HIS D 571
SITE 1 AC4 4 ASP B 312 GLU B 318 TYR B 319 HIS B 503
SITE 1 AC5 4 HIS D 309 ASP D 312 TYR D 319 GLU D 514
SITE 1 AC6 3 HIS D 395 GLU D 397 GLU D 435
SITE 1 AC7 3 GLU B 566 HIS B 571 HIS D 460
SITE 1 AC8 4 GLU D 318 TYR D 319 LYS D 504 GLU D 512
SITE 1 AC9 10 SER B 370 TRP B 411 SER B 428 ASN B 430
SITE 2 AC9 10 ILE B 465 THR B 543 LYS B 557 THR B 558
SITE 3 AC9 10 GLY B 559 THR B 560
SITE 1 BC1 8 SER D 370 TRP D 411 SER D 428 ASN D 430
SITE 2 BC1 8 LYS D 557 THR D 558 GLY D 559 THR D 560
CRYST1 185.755 50.277 109.535 90.00 90.00 90.00 P 21 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.005383 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019890 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009130 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
