HEADER TRANSFERASE 28-OCT-11 3UE3
TITLE CRYSTAL STRUCTURE OF ACINETOBACTER BAUMANNI PBP3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SEPTUM FORMATION, PENICILLIN BINDING PROTEIN 3,
COMPND 3 PEPTIDOGLYCAN SYNTHETASE;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: UNP RESIDUES 64-609;
COMPND 6 EC: 2.4.1.129;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACINETOBACTER;
SOURCE 3 ORGANISM_TAXID: 525244;
SOURCE 4 GENE: FTSI, HMPREF0023_2561;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSPEPTIDASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.HAN
REVDAT 3 28-FEB-24 3UE3 1 SEQADV
REVDAT 2 26-JUN-13 3UE3 1 JRNL
REVDAT 1 14-DEC-11 3UE3 0
JRNL AUTH S.HAN,N.CASPERS,R.P.ZANIEWSKI,B.M.LACEY,A.P.TOMARAS,X.FENG,
JRNL AUTH 2 K.F.GEOGHEGAN,V.SHANMUGASUNDARAM
JRNL TITL DISTINCTIVE ATTRIBUTES OF BETA-LACTAM TARGET PROTEINS IN
JRNL TITL 2 ACINETOBACTER BAUMANNII RELEVANT TO DEVELOPMENT OF NEW
JRNL TITL 3 ANTIBIOTICS
JRNL REF J.AM.CHEM.SOC. V. 133 20536 2011
JRNL REFN ISSN 0002-7863
JRNL PMID 22050378
JRNL DOI 10.1021/JA208835Z
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.9.6
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.32
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 33931
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) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1721
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 : 17
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.37
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.79
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2735
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2144
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2594
REMARK 3 BIN R VALUE (WORKING SET) : 0.2114
REMARK 3 BIN FREE R VALUE : 0.2676
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.16
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 141
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 : 3305
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 165
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.34
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.53450
REMARK 3 B22 (A**2) : 16.04200
REMARK 3 B33 (A**2) : -14.50750
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.306
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.209
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
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 : 0.851
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.824
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3363 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4552 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1173 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 78 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 490 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3363 ; 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 : 443 ; 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 : 3799 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.05
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 21.58
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -10.7217 15.5768 -42.8714
REMARK 3 T TENSOR
REMARK 3 T11: -0.1734 T22: -0.0047
REMARK 3 T33: -0.0843 T12: -0.0092
REMARK 3 T13: 0.0530 T23: -0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 0.6988 L22: 1.6356
REMARK 3 L33: 0.7284 L12: 0.1423
REMARK 3 L13: 0.0026 L23: -0.4937
REMARK 3 S TENSOR
REMARK 3 S11: 0.0983 S12: -0.1635 S13: 0.0075
REMARK 3 S21: 0.0815 S22: -0.0593 S23: 0.0215
REMARK 3 S31: 0.0094 S32: 0.0097 S33: -0.0390
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3UE3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-NOV-11.
REMARK 100 THE DEPOSITION ID IS D_1000068638.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-SEP-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33995
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 105.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 4000, 0.1M TRIS PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 19.82850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 105.96000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.85350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 105.96000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.82850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.85350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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 56
REMARK 465 SER A 57
REMARK 465 HIS A 58
REMARK 465 HIS A 59
REMARK 465 HIS A 60
REMARK 465 HIS A 61
REMARK 465 HIS A 62
REMARK 465 HIS A 63
REMARK 465 ALA A 64
REMARK 465 ASN A 65
REMARK 465 ILE A 66
REMARK 465 LEU A 67
REMARK 465 ARG A 68
REMARK 465 VAL A 97
REMARK 465 ILE A 98
REMARK 465 ASP A 99
REMARK 465 PRO A 100
REMARK 465 ARG A 101
REMARK 465 ASP A 102
REMARK 465 TYR A 103
REMARK 465 TRP A 104
REMARK 465 ASP A 105
REMARK 465 ALA A 106
REMARK 465 LYS A 107
REMARK 465 THR A 108
REMARK 465 GLN A 109
REMARK 465 PHE A 110
REMARK 465 ASP A 111
REMARK 465 GLU A 112
REMARK 465 ILE A 113
REMARK 465 THR A 114
REMARK 465 ALA A 115
REMARK 465 GLU A 116
REMARK 465 LEU A 117
REMARK 465 LYS A 118
REMARK 465 LYS A 119
REMARK 465 ASP A 120
REMARK 465 PRO A 121
REMARK 465 ASN A 122
REMARK 465 ASN A 123
REMARK 465 ARG A 124
REMARK 465 ARG A 125
REMARK 465 LEU A 126
REMARK 465 ARG A 127
REMARK 465 ARG A 128
REMARK 465 GLN A 129
REMARK 465 LEU A 130
REMARK 465 PRO A 131
REMARK 465 ASN A 132
REMARK 465 LYS A 133
REMARK 465 ASN A 134
REMARK 465 LEU A 135
REMARK 465 ASN A 136
REMARK 465 LEU A 137
REMARK 465 ASP A 138
REMARK 465 GLU A 139
REMARK 465 LEU A 140
REMARK 465 ALA A 141
REMARK 465 ASP A 142
REMARK 465 VAL A 143
REMARK 465 VAL A 144
REMARK 465 GLY A 145
REMARK 465 MET A 146
REMARK 465 ASP A 147
REMARK 465 ARG A 148
REMARK 465 LYS A 149
REMARK 465 THR A 150
REMARK 465 LEU A 151
REMARK 465 LYS A 152
REMARK 465 LYS A 153
REMARK 465 HIS A 154
REMARK 465 MET A 155
REMARK 465 THR A 156
REMARK 465 ASP A 157
REMARK 465 ARG A 158
REMARK 465 ALA A 159
REMARK 465 ARG A 160
REMARK 465 SER A 161
REMARK 465 ARG A 162
REMARK 465 TYR A 163
REMARK 465 LEU A 164
REMARK 465 VAL A 165
REMARK 465 LEU A 166
REMARK 465 GLN A 167
REMARK 465 ARG A 168
REMARK 465 GLU A 169
REMARK 465 VAL A 170
REMARK 465 PRO A 171
REMARK 465 PRO A 172
REMARK 465 GLN A 173
REMARK 465 GLN A 174
REMARK 465 ALA A 175
REMARK 465 ASP A 176
REMARK 465 LEU A 177
REMARK 465 ILE A 178
REMARK 465 LEU A 179
REMARK 465 GLN A 180
REMARK 465 HIS A 181
REMARK 465 ASN A 182
REMARK 465 PHE A 183
REMARK 465 GLN A 184
REMARK 465 GLY A 185
REMARK 465 ILE A 237
REMARK 465 ARG A 238
REMARK 465 ASP A 239
REMARK 465 LYS A 240
REMARK 465 LYS A 241
REMARK 465 GLY A 242
REMARK 465 ASN A 243
REMARK 465 ARG A 244
REMARK 465 LEU A 245
REMARK 465 THR A 603
REMARK 465 SER A 604
REMARK 465 ILE A 605
REMARK 465 LYS A 606
REMARK 465 THR A 607
REMARK 465 ASN A 608
REMARK 465 PRO A 609
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 324 C - N - CA ANGL. DEV. = 20.8 DEGREES
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 GLN A 198 73.25 -115.29
REMARK 500 PRO A 199 -76.27 -58.66
REMARK 500 LEU A 223 30.57 -95.38
REMARK 500 SER A 248 117.47 -161.63
REMARK 500 SER A 308 -159.02 -110.97
REMARK 500 LEU A 317 152.77 68.02
REMARK 500 LYS A 320 -25.84 -36.86
REMARK 500 ASP A 321 -49.35 -145.93
REMARK 500 ARG A 324 75.16 118.27
REMARK 500 LEU A 438 -170.64 43.57
REMARK 500 ASN A 439 118.82 76.15
REMARK 500 ARG A 533 131.91 81.67
REMARK 500 ARG A 536 16.16 52.79
REMARK 500 ASP A 556 80.69 -158.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3UDF RELATED DB: PDB
REMARK 900 RELATED ID: 3UDI RELATED DB: PDB
REMARK 900 RELATED ID: 3UDX RELATED DB: PDB
REMARK 900 RELATED ID: 3UE0 RELATED DB: PDB
REMARK 900 RELATED ID: 3UE1 RELATED DB: PDB
DBREF 3UE3 A 64 609 UNP C0VN42 C0VN42_9GAMM 64 609
SEQADV 3UE3 MET A 56 UNP C0VN42 EXPRESSION TAG
SEQADV 3UE3 SER A 57 UNP C0VN42 EXPRESSION TAG
SEQADV 3UE3 HIS A 58 UNP C0VN42 EXPRESSION TAG
SEQADV 3UE3 HIS A 59 UNP C0VN42 EXPRESSION TAG
SEQADV 3UE3 HIS A 60 UNP C0VN42 EXPRESSION TAG
SEQADV 3UE3 HIS A 61 UNP C0VN42 EXPRESSION TAG
SEQADV 3UE3 HIS A 62 UNP C0VN42 EXPRESSION TAG
SEQADV 3UE3 HIS A 63 UNP C0VN42 EXPRESSION TAG
SEQRES 1 A 554 MET SER HIS HIS HIS HIS HIS HIS ALA ASN ILE LEU ARG
SEQRES 2 A 554 THR GLU ARG LEU GLU ALA MET ARG GLY VAL ILE SER ASP
SEQRES 3 A 554 ARG HIS GLY VAL PRO LEU ALA ILE SER THR PRO ILE MET
SEQRES 4 A 554 LYS ILE VAL ILE ASP PRO ARG ASP TYR TRP ASP ALA LYS
SEQRES 5 A 554 THR GLN PHE ASP GLU ILE THR ALA GLU LEU LYS LYS ASP
SEQRES 6 A 554 PRO ASN ASN ARG ARG LEU ARG ARG GLN LEU PRO ASN LYS
SEQRES 7 A 554 ASN LEU ASN LEU ASP GLU LEU ALA ASP VAL VAL GLY MET
SEQRES 8 A 554 ASP ARG LYS THR LEU LYS LYS HIS MET THR ASP ARG ALA
SEQRES 9 A 554 ARG SER ARG TYR LEU VAL LEU GLN ARG GLU VAL PRO PRO
SEQRES 10 A 554 GLN GLN ALA ASP LEU ILE LEU GLN HIS ASN PHE GLN GLY
SEQRES 11 A 554 VAL TYR THR GLU LYS SER TYR LYS ARG TYR TYR PRO GLN
SEQRES 12 A 554 PRO GLN PRO ASN ALA GLN ILE ILE GLY LEU THR ASN SER
SEQRES 13 A 554 GLU GLY ARG GLY ILE GLU GLY LEU GLU MET GLN LEU ASN
SEQRES 14 A 554 THR ARG LEU ALA GLY VAL ASP GLY GLU GLN LYS ILE ILE
SEQRES 15 A 554 ARG ASP LYS LYS GLY ASN ARG LEU LYS VAL SER GLU VAL
SEQRES 16 A 554 ILE LYS GLU VAL GLU SER GLY GLU ASN ILE THR LEU SER
SEQRES 17 A 554 ILE ASP SER ARG LEU GLN TYR ILE MET TYR ARG GLU LEU
SEQRES 18 A 554 THR ALA ALA GLY VAL ALA ASN ASN ALA ARG SER ALA THR
SEQRES 19 A 554 ALA ILE ALA VAL ASP VAL LYS THR GLY GLU ILE LEU ALA
SEQRES 20 A 554 MET THR SER TRP PRO SER TYR ASN PRO ASN ASP LYS GLY
SEQRES 21 A 554 GLY LEU SER ASN LYS ASP ALA MET ARG ASN ARG GLY ALA
SEQRES 22 A 554 ILE ASP MET PHE GLU PRO GLY SER THR MET LYS PRO PHE
SEQRES 23 A 554 THR VAL ALA ALA ALA LEU GLU SER GLY GLN TYR THR PRO
SEQRES 24 A 554 ASN SER ILE VAL ASN THR ALA PRO GLY THR MET ARG LEU
SEQRES 25 A 554 GLY TRP HIS THR ILE ARG ASP THR HIS ASN TYR GLY ALA
SEQRES 26 A 554 LEU THR LEU THR GLY ILE ILE VAL LYS SER SER ASN VAL
SEQRES 27 A 554 GLY SER ALA LYS LEU ALA LEU SER LEU PRO LYS GLU ALA
SEQRES 28 A 554 LEU PRO SER PHE PHE ARG ARG ALA GLY PHE GLY GLN SER
SEQRES 29 A 554 SER ASP VAL LYS PHE PRO GLY GLU SER ALA GLY LEU LEU
SEQRES 30 A 554 TYR SER ALA ASP LYS LEU ASN SER SER GLN LEU GLY THR
SEQRES 31 A 554 MET ALA TYR GLY TYR GLY LEU ASN ALA THR ILE LEU GLN
SEQRES 32 A 554 LEU ALA GLN GLY TYR ALA MET LEU ALA ASN HIS GLY VAL
SEQRES 33 A 554 GLU MET PRO LEU SER LEU HIS LYS LEU ASP GLN VAL PRO
SEQRES 34 A 554 GLU GLY ARG GLN VAL LEU ASP PRO LYS ILE ALA ASP GLN
SEQRES 35 A 554 VAL LEU MET MET LEU GLU GLN VAL THR LEU PRO GLY GLY
SEQRES 36 A 554 THR ALA LYS GLN ALA VAL ILE PRO GLY TYR ARG VAL GLY
SEQRES 37 A 554 GLY LYS THR GLY THR ALA HIS LYS LEU ARG ALA ASP ARG
SEQRES 38 A 554 LYS GLY TYR SER ASN SER GLU TYR ARG ALA LEU PHE ALA
SEQRES 39 A 554 GLY VAL ALA PRO VAL SER ASP PRO ARG LEU ALA MET ILE
SEQRES 40 A 554 VAL VAL VAL GLU ASN PRO GLN GLY ARG TYR TYR GLY GLY
SEQRES 41 A 554 LEU VAL ALA ALA PRO VAL PHE ALA LYS ILE MET GLN GLU
SEQRES 42 A 554 SER LEU ARG LEU LEU ASN VAL PRO LEU ASP LYS PRO LEU
SEQRES 43 A 554 ASP THR SER ILE LYS THR ASN PRO
FORMUL 2 HOH *165(H2 O)
HELIX 1 1 GLN A 198 GLY A 207 1 10
HELIX 2 2 GLU A 217 LEU A 223 1 7
HELIX 3 3 LEU A 223 GLY A 229 1 7
HELIX 4 4 ASP A 265 ASN A 283 1 19
HELIX 5 5 SER A 318 MET A 323 1 6
HELIX 6 6 ASN A 325 ASP A 330 1 6
HELIX 7 7 PRO A 334 THR A 337 5 4
HELIX 8 8 MET A 338 SER A 349 1 12
HELIX 9 9 LEU A 383 SER A 390 1 8
HELIX 10 10 SER A 391 LEU A 402 1 12
HELIX 11 11 GLU A 405 ALA A 414 1 10
HELIX 12 12 SER A 434 LEU A 438 5 5
HELIX 13 13 ASN A 439 ALA A 447 1 9
HELIX 14 14 THR A 455 ALA A 467 1 13
HELIX 15 15 ASP A 491 THR A 506 1 16
HELIX 16 16 ALA A 512 VAL A 516 5 5
HELIX 17 17 GLY A 574 VAL A 577 5 4
HELIX 18 18 ALA A 578 LEU A 593 1 16
SHEET 1 A 3 GLU A 70 LEU A 72 0
SHEET 2 A 3 GLY A 232 LYS A 235 -1 O GLN A 234 N GLU A 70
SHEET 3 A 3 GLU A 249 LYS A 252 -1 O ILE A 251 N GLU A 233
SHEET 1 B 4 GLU A 189 TYR A 195 0
SHEET 2 B 4 PRO A 86 LYS A 95 -1 N ILE A 93 O SER A 191
SHEET 3 B 4 ILE A 79 SER A 80 -1 N ILE A 79 O LEU A 87
SHEET 4 B 4 ILE A 260 THR A 261 1 O ILE A 260 N SER A 80
SHEET 1 C 5 ILE A 300 TRP A 306 0
SHEET 2 C 5 SER A 287 ASP A 294 -1 N ALA A 288 O TRP A 306
SHEET 3 C 5 LEU A 559 GLU A 566 -1 O GLU A 566 N SER A 287
SHEET 4 C 5 TYR A 544 ALA A 552 -1 N ALA A 546 O VAL A 565
SHEET 5 C 5 GLY A 523 HIS A 530 -1 N LYS A 525 O ALA A 549
SHEET 1 D 2 ILE A 357 ASN A 359 0
SHEET 2 D 2 ALA A 380 THR A 382 -1 O LEU A 381 N VAL A 358
SHEET 1 E 2 THR A 364 LEU A 367 0
SHEET 2 E 2 HIS A 370 ARG A 373 -1 O HIS A 370 N LEU A 367
SHEET 1 F 2 VAL A 471 GLU A 472 0
SHEET 2 F 2 ARG A 487 GLN A 488 -1 O ARG A 487 N GLU A 472
CISPEP 1 VAL A 247 SER A 248 0 -4.34
CISPEP 2 TRP A 306 PRO A 307 0 0.36
CISPEP 3 MET A 323 ARG A 324 0 9.35
CISPEP 4 ALA A 361 PRO A 362 0 1.87
CISPEP 5 ALA A 552 PRO A 553 0 -10.02
CRYST1 39.657 89.707 211.920 90.00 90.00 90.00 P 21 21 21 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 0.025216 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011147 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004719 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
