HEADER TRANSPORT PROTEIN 23-JAN-08 3C1H
TITLE SUBSTRATE BINDING, DEPROTONATION AND SELECTIVITY AT THE PERIPLASMIC
TITLE 2 ENTRANCE OF THE E. COLI AMMONIA CHANNEL AMTB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMMONIA CHANNEL;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AMMONIA TRANSPORTER;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: AMTB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: C43 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET22B-AMTBF107A
KEYWDS TRANSPORT PROTEIN, MEMBRANE PROTEIN, AMMONIA TRANSPORT, PHE-GATE
KEYWDS 2 MUTANT, AMTB, INNER MEMBRANE, TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.LUPO,F.K.WINKLER
REVDAT 6 01-NOV-23 3C1H 1 REMARK
REVDAT 5 10-NOV-21 3C1H 1 REMARK SEQADV
REVDAT 4 25-OCT-17 3C1H 1 REMARK
REVDAT 3 24-FEB-09 3C1H 1 VERSN
REVDAT 2 15-APR-08 3C1H 1 JRNL
REVDAT 1 18-MAR-08 3C1H 0
JRNL AUTH A.JAVELLE,D.LUPO,P.RIPOCHE,T.FULFORD,M.MERRICK,F.K.WINKLER
JRNL TITL SUBSTRATE BINDING, DEPROTONATION, AND SELECTIVITY AT THE
JRNL TITL 2 PERIPLASMIC ENTRANCE OF THE ESCHERICHIA COLI AMMONIA CHANNEL
JRNL TITL 3 AMTB.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 105 5040 2008
JRNL REFN ISSN 0027-8424
JRNL PMID 18362341
JRNL DOI 10.1073/PNAS.0711742105
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 27078
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1447
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1993
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.95
REMARK 3 BIN R VALUE (WORKING SET) : 0.3560
REMARK 3 BIN FREE R VALUE SET COUNT : 110
REMARK 3 BIN FREE R VALUE : 0.3790
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2634
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.84000
REMARK 3 B22 (A**2) : 1.84000
REMARK 3 B33 (A**2) : -2.76000
REMARK 3 B12 (A**2) : 0.92000
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): 0.192
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.166
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.170
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.199
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2726 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3714 ; 1.279 ; 1.945
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 362 ; 5.627 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 82 ;28.969 ;23.049
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 387 ;14.764 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 5 ; 9.861 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 446 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1984 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1768 ; 0.231 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2007 ; 0.316 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 177 ; 0.317 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 96 ; 0.197 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.128 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1803 ; 1.977 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2814 ; 2.980 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1067 ; 5.040 ; 4.500
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 899 ; 6.123 ; 6.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 1.00
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3C1H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-JAN-08.
REMARK 100 THE DEPOSITION ID IS D_1000046222.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28604
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.4100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.57000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.520
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1XQF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG 400, 0.1M SODIUM ACETATE, 0.2M
REMARK 280 AMMONIUM SULFATE, PH 4.6, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 42.33150
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 42.33150
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 42.33150
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -122.6 KCAL/MOL
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 BIOMT1 2 -0.500000 -0.866025 0.000000 108.17500
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 54.08750
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 93.68230
REMARK 350 BIOMT3 3 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 ALA A 1
REMARK 465 PRO A 2
REMARK 465 ILE A 182
REMARK 465 GLY A 183
REMARK 465 LYS A 184
REMARK 465 ARG A 185
REMARK 465 VAL A 186
REMARK 465 GLY A 187
REMARK 465 PHE A 188
REMARK 465 GLY A 189
REMARK 465 LYS A 190
REMARK 465 GLU A 191
REMARK 465 ALA A 192
REMARK 465 PHE A 193
REMARK 465 LYS A 194
REMARK 465 LEU A 302
REMARK 465 LYS A 303
REMARK 465 ARG A 304
REMARK 465 LEU A 305
REMARK 465 LEU A 306
REMARK 465 ARG A 307
REMARK 465 VAL A 308
REMARK 465 ASP A 309
REMARK 465 GLU A 387
REMARK 465 GLU A 388
REMARK 465 GLN A 389
REMARK 465 GLU A 390
REMARK 465 ARG A 391
REMARK 465 GLU A 392
REMARK 465 GLY A 393
REMARK 465 LEU A 394
REMARK 465 ASP A 395
REMARK 465 VAL A 396
REMARK 465 ASN A 397
REMARK 465 SER A 398
REMARK 465 HIS A 399
REMARK 465 GLY A 400
REMARK 465 GLU A 401
REMARK 465 ASN A 402
REMARK 465 ALA A 403
REMARK 465 TYR A 404
REMARK 465 ASN A 405
REMARK 465 ALA A 406
REMARK 465 ASP A 407
REMARK 465 GLN A 408
REMARK 465 ALA A 409
REMARK 465 GLN A 410
REMARK 465 GLN A 411
REMARK 465 PRO A 412
REMARK 465 ALA A 413
REMARK 465 GLN A 414
REMARK 465 ALA A 415
REMARK 465 ASP A 416
REMARK 465 LEU A 417
REMARK 465 GLU A 418
REMARK 465 HIS A 419
REMARK 465 HIS A 420
REMARK 465 HIS A 421
REMARK 465 HIS A 422
REMARK 465 HIS A 423
REMARK 465 HIS A 424
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 TYR A 62 -15.02 -152.11
REMARK 500 ASN A 72 -159.79 -105.22
REMARK 500 TRP A 80 47.79 -105.01
REMARK 500 GLU A 121 -70.17 -50.80
REMARK 500 SER A 139 -60.29 -120.39
REMARK 500 ASP A 160 86.08 -161.05
REMARK 500 VAL A 167 -60.25 -97.24
REMARK 500 ASN A 197 81.17 -152.75
REMARK 500 ASN A 224 -169.31 -120.46
REMARK 500 CYS A 312 42.93 37.41
REMARK 500 ALA A 334 128.32 -39.36
REMARK 500 ARG A 384 -137.37 55.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 425
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDA A 426
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 427
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XQF RELATED DB: PDB
REMARK 900 SAME WILD-TYPE AMTB IN THE PRESENCE OF MAGNESIUM
REMARK 900 RELATED ID: 1U7G RELATED DB: PDB
REMARK 900 TRIPLE MUTANT OF AMTB
REMARK 900 RELATED ID: 2B2F RELATED DB: PDB
REMARK 900 WILD-TYPE AMMONIUM TRANSPORTER AMT1 FROM ARCHAEOGLOBUS FULGIDUS
REMARK 900 RELATED ID: 3B9W RELATED DB: PDB
REMARK 900 NITROSOMONAS EUROPAEA RH50 FROM THE RHESUS PROTEIN FAMILY
REMARK 900 RELATED ID: 3C1G RELATED DB: PDB
REMARK 900 AMTB WILD-TYPE IN THE PRESENCE OF THALLIUM
REMARK 900 RELATED ID: 3C1I RELATED DB: PDB
REMARK 900 AMTB PHE-GATE MUTANT F215A
REMARK 900 RELATED ID: 3C1J RELATED DB: PDB
REMARK 900 AMTB PHE-GATE DOUBLE MUTANT F107A/F215A
DBREF 3C1H A 1 406 UNP P69681 AMTB_ECOLI 23 428
SEQADV 3C1H ALA A 107 UNP P69681 PHE 129 ENGINEERED MUTATION
SEQADV 3C1H ASP A 407 UNP P69681 EXPRESSION TAG
SEQADV 3C1H GLN A 408 UNP P69681 EXPRESSION TAG
SEQADV 3C1H ALA A 409 UNP P69681 EXPRESSION TAG
SEQADV 3C1H GLN A 410 UNP P69681 EXPRESSION TAG
SEQADV 3C1H GLN A 411 UNP P69681 EXPRESSION TAG
SEQADV 3C1H PRO A 412 UNP P69681 EXPRESSION TAG
SEQADV 3C1H ALA A 413 UNP P69681 EXPRESSION TAG
SEQADV 3C1H GLN A 414 UNP P69681 EXPRESSION TAG
SEQADV 3C1H ALA A 415 UNP P69681 EXPRESSION TAG
SEQADV 3C1H ASP A 416 UNP P69681 EXPRESSION TAG
SEQADV 3C1H LEU A 417 UNP P69681 EXPRESSION TAG
SEQADV 3C1H GLU A 418 UNP P69681 EXPRESSION TAG
SEQADV 3C1H HIS A 419 UNP P69681 EXPRESSION TAG
SEQADV 3C1H HIS A 420 UNP P69681 EXPRESSION TAG
SEQADV 3C1H HIS A 421 UNP P69681 EXPRESSION TAG
SEQADV 3C1H HIS A 422 UNP P69681 EXPRESSION TAG
SEQADV 3C1H HIS A 423 UNP P69681 EXPRESSION TAG
SEQADV 3C1H HIS A 424 UNP P69681 EXPRESSION TAG
SEQRES 1 A 424 ALA PRO ALA VAL ALA ASP LYS ALA ASP ASN ALA PHE MET
SEQRES 2 A 424 MET ILE CYS THR ALA LEU VAL LEU PHE MET THR ILE PRO
SEQRES 3 A 424 GLY ILE ALA LEU PHE TYR GLY GLY LEU ILE ARG GLY LYS
SEQRES 4 A 424 ASN VAL LEU SER MET LEU THR GLN VAL THR VAL THR PHE
SEQRES 5 A 424 ALA LEU VAL CYS ILE LEU TRP VAL VAL TYR GLY TYR SER
SEQRES 6 A 424 LEU ALA PHE GLY GLU GLY ASN ASN PHE PHE GLY ASN ILE
SEQRES 7 A 424 ASN TRP LEU MET LEU LYS ASN ILE GLU LEU THR ALA VAL
SEQRES 8 A 424 MET GLY SER ILE TYR GLN TYR ILE HIS VAL ALA PHE GLN
SEQRES 9 A 424 GLY SER ALA ALA CYS ILE THR VAL GLY LEU ILE VAL GLY
SEQRES 10 A 424 ALA LEU ALA GLU ARG ILE ARG PHE SER ALA VAL LEU ILE
SEQRES 11 A 424 PHE VAL VAL VAL TRP LEU THR LEU SER TYR ILE PRO ILE
SEQRES 12 A 424 ALA HIS MET VAL TRP GLY GLY GLY LEU LEU ALA SER HIS
SEQRES 13 A 424 GLY ALA LEU ASP PHE ALA GLY GLY THR VAL VAL HIS ILE
SEQRES 14 A 424 ASN ALA ALA ILE ALA GLY LEU VAL GLY ALA TYR LEU ILE
SEQRES 15 A 424 GLY LYS ARG VAL GLY PHE GLY LYS GLU ALA PHE LYS PRO
SEQRES 16 A 424 HIS ASN LEU PRO MET VAL PHE THR GLY THR ALA ILE LEU
SEQRES 17 A 424 TYR ILE GLY TRP PHE GLY PHE ASN ALA GLY SER ALA GLY
SEQRES 18 A 424 THR ALA ASN GLU ILE ALA ALA LEU ALA PHE VAL ASN THR
SEQRES 19 A 424 VAL VAL ALA THR ALA ALA ALA ILE LEU GLY TRP ILE PHE
SEQRES 20 A 424 GLY GLU TRP ALA LEU ARG GLY LYS PRO SER LEU LEU GLY
SEQRES 21 A 424 ALA CYS SER GLY ALA ILE ALA GLY LEU VAL GLY VAL THR
SEQRES 22 A 424 PRO ALA CYS GLY TYR ILE GLY VAL GLY GLY ALA LEU ILE
SEQRES 23 A 424 ILE GLY VAL VAL ALA GLY LEU ALA GLY LEU TRP GLY VAL
SEQRES 24 A 424 THR MET LEU LYS ARG LEU LEU ARG VAL ASP ASP PRO CYS
SEQRES 25 A 424 ASP VAL PHE GLY VAL HIS GLY VAL CYS GLY ILE VAL GLY
SEQRES 26 A 424 CYS ILE MET THR GLY ILE PHE ALA ALA SER SER LEU GLY
SEQRES 27 A 424 GLY VAL GLY PHE ALA GLU GLY VAL THR MET GLY HIS GLN
SEQRES 28 A 424 LEU LEU VAL GLN LEU GLU SER ILE ALA ILE THR ILE VAL
SEQRES 29 A 424 TRP SER GLY VAL VAL ALA PHE ILE GLY TYR LYS LEU ALA
SEQRES 30 A 424 ASP LEU THR VAL GLY LEU ARG VAL PRO GLU GLU GLN GLU
SEQRES 31 A 424 ARG GLU GLY LEU ASP VAL ASN SER HIS GLY GLU ASN ALA
SEQRES 32 A 424 TYR ASN ALA ASP GLN ALA GLN GLN PRO ALA GLN ALA ASP
SEQRES 33 A 424 LEU GLU HIS HIS HIS HIS HIS HIS
HET ACT A 425 4
HET LDA A 426 16
HET IMD A 427 5
HETNAM ACT ACETATE ION
HETNAM LDA LAURYL DIMETHYLAMINE-N-OXIDE
HETNAM IMD IMIDAZOLE
FORMUL 2 ACT C2 H3 O2 1-
FORMUL 3 LDA C14 H31 N O
FORMUL 4 IMD C3 H5 N2 1+
FORMUL 5 HOH *130(H2 O)
HELIX 1 1 ASP A 6 ILE A 25 1 20
HELIX 2 2 PRO A 26 ILE A 36 1 11
HELIX 3 3 ARG A 37 LYS A 39 5 3
HELIX 4 4 ASN A 40 TYR A 62 1 23
HELIX 5 5 TYR A 62 GLY A 69 1 8
HELIX 6 6 TRP A 80 LYS A 84 5 5
HELIX 7 7 GLN A 97 ALA A 120 1 24
HELIX 8 8 ARG A 124 SER A 139 1 16
HELIX 9 9 SER A 139 GLY A 149 1 11
HELIX 10 10 LEU A 153 GLY A 157 5 5
HELIX 11 11 VAL A 167 LEU A 181 1 15
HELIX 12 12 ASN A 197 SER A 219 1 23
HELIX 13 13 ASN A 224 GLY A 254 1 31
HELIX 14 14 SER A 257 THR A 273 1 17
HELIX 15 15 GLY A 280 MET A 301 1 22
HELIX 16 16 ASP A 310 CYS A 312 5 3
HELIX 17 17 ASP A 313 ALA A 333 1 21
HELIX 18 18 ALA A 334 GLY A 338 5 5
HELIX 19 19 THR A 347 VAL A 381 1 35
SHEET 1 A 2 VAL A 91 MET A 92 0
SHEET 2 A 2 ILE A 95 TYR A 96 -1 O ILE A 95 N MET A 92
CISPEP 1 ILE A 25 PRO A 26 0 0.22
CISPEP 2 ARG A 384 VAL A 385 0 -1.28
SITE 1 AC1 5 ALA A 158 LEU A 159 ASP A 160 TYR A 278
SITE 2 AC1 5 HOH A 509
SITE 1 AC2 11 ILE A 28 PHE A 31 ILE A 110 ALA A 162
SITE 2 AC2 11 HIS A 168 TRP A 212 PHE A 215 CYS A 312
SITE 3 AC2 11 ASP A 313 HIS A 318 HOH A 520
SITE 1 AC3 5 HIS A 100 PHE A 103 GLY A 218 SER A 219
SITE 2 AC3 5 GLY A 221
CRYST1 108.175 108.175 84.663 90.00 90.00 120.00 P 63 6
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 0.009244 0.005337 0.000000 0.00000
SCALE2 0.000000 0.010674 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011812 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
