HEADER ISOMERASE/ISOMERASE INHIBITOR 17-DEC-14 4XBJ
TITLE Y274F ALANINE RACEMASE FROM E. COLI INHIBITED BY L-ALA-P
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALANINE RACEMASE, BIOSYNTHETIC;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 5.1.1.1;
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: ALR;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ISOMERASE, ISOMERASE-ISOMERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.J.SQUIRE,Y.YOSAATMADJA,W.M.PATRICK
REVDAT 3 27-SEP-23 4XBJ 1 REMARK
REVDAT 2 22-SEP-21 4XBJ 1 JRNL REMARK
REVDAT 1 23-DEC-15 4XBJ 0
JRNL AUTH V.W.SOO,Y.YOSAATMADJA,C.J.SQUIRE,W.M.PATRICK
JRNL TITL MECHANISTIC AND EVOLUTIONARY INSIGHTS FROM THE RECIPROCAL
JRNL TITL 2 PROMISCUITY OF TWO PYRIDOXAL PHOSPHATE-DEPENDENT ENZYMES.
JRNL REF J.BIOL.CHEM. V. 291 19873 2016
JRNL REFN ESSN 1083-351X
JRNL PMID 27474741
JRNL DOI 10.1074/JBC.M116.739557
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 90731
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) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4924
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) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6619
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.36
REMARK 3 BIN R VALUE (WORKING SET) : 0.1190
REMARK 3 BIN FREE R VALUE SET COUNT : 328
REMARK 3 BIN FREE R VALUE : 0.1740
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10758
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 106
REMARK 3 SOLVENT ATOMS : 236
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.27000
REMARK 3 B22 (A**2) : -0.27000
REMARK 3 B33 (A**2) : 0.55000
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): 0.040
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.034
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.057
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.051
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.919
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11165 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 10736 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15189 ; 1.142 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): 24586 ; 0.645 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1424 ; 7.394 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 470 ;36.104 ;22.723
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1773 ;15.011 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 105 ;16.293 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1713 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12643 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2535 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 5699 ; 1.894 ; 2.124
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5698 ; 1.894 ; 2.124
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7116 ; 2.505 ; 3.174
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 7117 ; 2.504 ; 3.175
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5466 ; 2.089 ; 2.266
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 5432 ; 2.071 ; 2.258
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 8023 ; 2.803 ; 3.324
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 12408 ; 3.870 ;16.749
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 12353 ; 3.843 ;16.771
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 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.487
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : K, H, -L
REMARK 3 TWIN FRACTION : 0.513
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4XBJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-DEC-14.
REMARK 100 THE DEPOSITION ID IS D_1000205402.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-NOV-14
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 7.0
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 MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 95615
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 19.910
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 11.40
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: 4WR3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.0, 1.6 M AMMONIUM
REMARK 280 SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6
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
REMARK 290 5555 Y,-X+Y,Z
REMARK 290 6555 X-Y,X,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 -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 0.00000
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 0.00000
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 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: 5420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 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: 5220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 MET A 1
REMARK 465 GLN A 2
REMARK 465 MET B 1
REMARK 465 MET C 1
REMARK 465 GLN C 2
REMARK 465 SER C 112
REMARK 465 GLU C 262
REMARK 465 GLY C 292
REMARK 465 GLU C 327
REMARK 465 ALA C 335
REMARK 465 GLU C 336
REMARK 465 MET D 1
REMARK 465 GLN D 2
REMARK 465 ALA D 3
REMARK 465 ASP D 51
REMARK 465 LEU D 113
REMARK 465 LYS D 167
REMARK 465 GLU D 221
REMARK 465 ASP D 222
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 GLU A 61 CG CD OE1 OE2
REMARK 470 LYS A 148 CG CD CE NZ
REMARK 470 LYS A 356 CG CD CE NZ
REMARK 470 LYS C 167 CG CD CE NZ
REMARK 470 GLU C 221 CG CD OE1 OE2
REMARK 470 ARG C 223 CG CD NE CZ NH1 NH2
REMARK 470 THR C 338 OG1 CG2
REMARK 470 LYS D 28 CG CD CE NZ
REMARK 470 GLU D 61 CG CD OE1 OE2
REMARK 470 SER D 112 OG
REMARK 470 GLU D 115 CG CD OE1 OE2
REMARK 470 GLN D 136 CG CD OE1 NE2
REMARK 470 LYS D 148 CG CD CE NZ
REMARK 470 ARG D 151 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 189 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 199 CG CD1 CD2
REMARK 470 ASP D 206 CB CG OD1 OD2
REMARK 470 ARG D 223 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 248 CG CD CE NZ
REMARK 470 GLU D 262 CG CD OE1 OE2
REMARK 470 ARG D 293 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 333 CG CD NE CZ NH1 NH2
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 O PRO A 50 NZ LYS A 73 2.09
REMARK 500
REMARK 500 REMARK: NULL
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 10 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 21 NE - CZ - NH1 ANGL. DEV. = -3.6 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 ALA A 4 107.77 -48.40
REMARK 500 LEU A 49 66.21 -117.87
REMARK 500 ARG A 129 -76.95 -118.75
REMARK 500 ARG A 162 40.00 -144.41
REMARK 500 ALA A 193 -153.55 -103.30
REMARK 500 PHE A 205 -133.45 48.24
REMARK 500 GLU A 221 64.44 -117.20
REMARK 500 ASP A 222 19.59 -140.06
REMARK 500 SER A 239 -151.89 -163.69
REMARK 500 ALA A 318 131.87 -37.99
REMARK 500 LEU A 329 84.75 -151.86
REMARK 500 ARG A 348 55.84 -90.94
REMARK 500 ALA B 4 109.42 -44.36
REMARK 500 ARG B 129 -72.71 -110.05
REMARK 500 ARG B 162 41.44 -145.00
REMARK 500 PRO B 186 -165.99 -76.93
REMARK 500 ALA B 193 -153.85 -114.96
REMARK 500 TRP B 200 79.91 -111.55
REMARK 500 PHE B 205 -138.17 43.08
REMARK 500 GLU B 221 55.03 -112.81
REMARK 500 ARG B 223 -9.60 83.60
REMARK 500 SER B 239 -149.42 -159.48
REMARK 500 LEU B 329 79.03 -155.10
REMARK 500 ARG B 348 56.18 -93.17
REMARK 500 ARG C 129 -85.85 -106.88
REMARK 500 ARG C 162 47.77 -144.86
REMARK 500 ALA C 193 -151.15 -96.32
REMARK 500 PHE C 205 -136.84 51.82
REMARK 500 THR C 225 -169.80 -116.52
REMARK 500 SER C 239 -150.48 -152.82
REMARK 500 ARG C 348 55.59 -96.86
REMARK 500 ALA D 26 54.48 -101.28
REMARK 500 LYS D 73 162.44 -47.45
REMARK 500 ARG D 129 -74.36 -120.34
REMARK 500 PRO D 134 -36.73 -38.01
REMARK 500 ARG D 162 38.22 -144.64
REMARK 500 GLU D 183 113.61 -35.27
REMARK 500 ALA D 193 -158.65 -124.42
REMARK 500 ASP D 206 -47.29 85.44
REMARK 500 SER D 239 -147.71 -162.25
REMARK 500 LEU D 329 80.33 -152.16
REMARK 500 ARG D 348 56.63 -91.66
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 IN5 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IN5 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IN5 C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4WR3 RELATED DB: PDB
REMARK 900 SAME MUTANT ALANINE RACEMASE BUT NOT INHIBITED
DBREF 4XBJ A 1 359 UNP P0A6B4 ALR1_ECOLI 1 359
DBREF 4XBJ B 1 359 UNP P0A6B4 ALR1_ECOLI 1 359
DBREF 4XBJ C 1 359 UNP P0A6B4 ALR1_ECOLI 1 359
DBREF 4XBJ D 1 359 UNP P0A6B4 ALR1_ECOLI 1 359
SEQADV 4XBJ PHE A 274 UNP P0A6B4 TYR 274 ENGINEERED MUTATION
SEQADV 4XBJ PHE B 274 UNP P0A6B4 TYR 274 ENGINEERED MUTATION
SEQADV 4XBJ PHE C 274 UNP P0A6B4 TYR 274 ENGINEERED MUTATION
SEQADV 4XBJ PHE D 274 UNP P0A6B4 TYR 274 ENGINEERED MUTATION
SEQRES 1 A 359 MET GLN ALA ALA THR VAL VAL ILE ASN ARG ARG ALA LEU
SEQRES 2 A 359 ARG HIS ASN LEU GLN ARG LEU ARG GLU LEU ALA PRO ALA
SEQRES 3 A 359 SER LYS MET VAL ALA VAL VAL LYS ALA ASN ALA TYR GLY
SEQRES 4 A 359 HIS GLY LEU LEU GLU THR ALA ARG THR LEU PRO ASP ALA
SEQRES 5 A 359 ASP ALA PHE GLY VAL ALA ARG LEU GLU GLU ALA LEU ARG
SEQRES 6 A 359 LEU ARG ALA GLY GLY ILE THR LYS PRO VAL LEU LEU LEU
SEQRES 7 A 359 GLU GLY PHE PHE ASP ALA ARG ASP LEU PRO THR ILE SER
SEQRES 8 A 359 ALA GLN HIS PHE HIS THR ALA VAL HIS ASN GLU GLU GLN
SEQRES 9 A 359 LEU ALA ALA LEU GLU GLU ALA SER LEU ASP GLU PRO VAL
SEQRES 10 A 359 THR VAL TRP MET LYS LEU ASP THR GLY MET HIS ARG LEU
SEQRES 11 A 359 GLY VAL ARG PRO GLU GLN ALA GLU ALA PHE TYR HIS ARG
SEQRES 12 A 359 LEU THR GLN CYS LYS ASN VAL ARG GLN PRO VAL ASN ILE
SEQRES 13 A 359 VAL SER HIS PHE ALA ARG ALA ASP GLU PRO LYS CYS GLY
SEQRES 14 A 359 ALA THR GLU LYS GLN LEU ALA ILE PHE ASN THR PHE CYS
SEQRES 15 A 359 GLU GLY LYS PRO GLY GLN ARG SER ILE ALA ALA SER GLY
SEQRES 16 A 359 GLY ILE LEU LEU TRP PRO GLN SER HIS PHE ASP TRP VAL
SEQRES 17 A 359 ARG PRO GLY ILE ILE LEU TYR GLY VAL SER PRO LEU GLU
SEQRES 18 A 359 ASP ARG SER THR GLY ALA ASP PHE GLY CYS GLN PRO VAL
SEQRES 19 A 359 MET SER LEU THR SER SER LEU ILE ALA VAL ARG GLU HIS
SEQRES 20 A 359 LYS ALA GLY GLU PRO VAL GLY TYR GLY GLY THR TRP VAL
SEQRES 21 A 359 SER GLU ARG ASP THR ARG LEU GLY VAL VAL ALA MET GLY
SEQRES 22 A 359 PHE GLY ASP GLY TYR PRO ARG ALA ALA PRO SER GLY THR
SEQRES 23 A 359 PRO VAL LEU VAL ASN GLY ARG GLU VAL PRO ILE VAL GLY
SEQRES 24 A 359 ARG VAL ALA MET ASP MET ILE CYS VAL ASP LEU GLY PRO
SEQRES 25 A 359 GLN ALA GLN ASP LYS ALA GLY ASP PRO VAL ILE LEU TRP
SEQRES 26 A 359 GLY GLU GLY LEU PRO VAL GLU ARG ILE ALA GLU MET THR
SEQRES 27 A 359 LYS VAL SER ALA TYR GLU LEU ILE THR ARG LEU THR SER
SEQRES 28 A 359 ARG VAL ALA MET LYS TYR VAL ASP
SEQRES 1 B 359 MET GLN ALA ALA THR VAL VAL ILE ASN ARG ARG ALA LEU
SEQRES 2 B 359 ARG HIS ASN LEU GLN ARG LEU ARG GLU LEU ALA PRO ALA
SEQRES 3 B 359 SER LYS MET VAL ALA VAL VAL LYS ALA ASN ALA TYR GLY
SEQRES 4 B 359 HIS GLY LEU LEU GLU THR ALA ARG THR LEU PRO ASP ALA
SEQRES 5 B 359 ASP ALA PHE GLY VAL ALA ARG LEU GLU GLU ALA LEU ARG
SEQRES 6 B 359 LEU ARG ALA GLY GLY ILE THR LYS PRO VAL LEU LEU LEU
SEQRES 7 B 359 GLU GLY PHE PHE ASP ALA ARG ASP LEU PRO THR ILE SER
SEQRES 8 B 359 ALA GLN HIS PHE HIS THR ALA VAL HIS ASN GLU GLU GLN
SEQRES 9 B 359 LEU ALA ALA LEU GLU GLU ALA SER LEU ASP GLU PRO VAL
SEQRES 10 B 359 THR VAL TRP MET LYS LEU ASP THR GLY MET HIS ARG LEU
SEQRES 11 B 359 GLY VAL ARG PRO GLU GLN ALA GLU ALA PHE TYR HIS ARG
SEQRES 12 B 359 LEU THR GLN CYS LYS ASN VAL ARG GLN PRO VAL ASN ILE
SEQRES 13 B 359 VAL SER HIS PHE ALA ARG ALA ASP GLU PRO LYS CYS GLY
SEQRES 14 B 359 ALA THR GLU LYS GLN LEU ALA ILE PHE ASN THR PHE CYS
SEQRES 15 B 359 GLU GLY LYS PRO GLY GLN ARG SER ILE ALA ALA SER GLY
SEQRES 16 B 359 GLY ILE LEU LEU TRP PRO GLN SER HIS PHE ASP TRP VAL
SEQRES 17 B 359 ARG PRO GLY ILE ILE LEU TYR GLY VAL SER PRO LEU GLU
SEQRES 18 B 359 ASP ARG SER THR GLY ALA ASP PHE GLY CYS GLN PRO VAL
SEQRES 19 B 359 MET SER LEU THR SER SER LEU ILE ALA VAL ARG GLU HIS
SEQRES 20 B 359 LYS ALA GLY GLU PRO VAL GLY TYR GLY GLY THR TRP VAL
SEQRES 21 B 359 SER GLU ARG ASP THR ARG LEU GLY VAL VAL ALA MET GLY
SEQRES 22 B 359 PHE GLY ASP GLY TYR PRO ARG ALA ALA PRO SER GLY THR
SEQRES 23 B 359 PRO VAL LEU VAL ASN GLY ARG GLU VAL PRO ILE VAL GLY
SEQRES 24 B 359 ARG VAL ALA MET ASP MET ILE CYS VAL ASP LEU GLY PRO
SEQRES 25 B 359 GLN ALA GLN ASP LYS ALA GLY ASP PRO VAL ILE LEU TRP
SEQRES 26 B 359 GLY GLU GLY LEU PRO VAL GLU ARG ILE ALA GLU MET THR
SEQRES 27 B 359 LYS VAL SER ALA TYR GLU LEU ILE THR ARG LEU THR SER
SEQRES 28 B 359 ARG VAL ALA MET LYS TYR VAL ASP
SEQRES 1 C 359 MET GLN ALA ALA THR VAL VAL ILE ASN ARG ARG ALA LEU
SEQRES 2 C 359 ARG HIS ASN LEU GLN ARG LEU ARG GLU LEU ALA PRO ALA
SEQRES 3 C 359 SER LYS MET VAL ALA VAL VAL LYS ALA ASN ALA TYR GLY
SEQRES 4 C 359 HIS GLY LEU LEU GLU THR ALA ARG THR LEU PRO ASP ALA
SEQRES 5 C 359 ASP ALA PHE GLY VAL ALA ARG LEU GLU GLU ALA LEU ARG
SEQRES 6 C 359 LEU ARG ALA GLY GLY ILE THR LYS PRO VAL LEU LEU LEU
SEQRES 7 C 359 GLU GLY PHE PHE ASP ALA ARG ASP LEU PRO THR ILE SER
SEQRES 8 C 359 ALA GLN HIS PHE HIS THR ALA VAL HIS ASN GLU GLU GLN
SEQRES 9 C 359 LEU ALA ALA LEU GLU GLU ALA SER LEU ASP GLU PRO VAL
SEQRES 10 C 359 THR VAL TRP MET LYS LEU ASP THR GLY MET HIS ARG LEU
SEQRES 11 C 359 GLY VAL ARG PRO GLU GLN ALA GLU ALA PHE TYR HIS ARG
SEQRES 12 C 359 LEU THR GLN CYS LYS ASN VAL ARG GLN PRO VAL ASN ILE
SEQRES 13 C 359 VAL SER HIS PHE ALA ARG ALA ASP GLU PRO LYS CYS GLY
SEQRES 14 C 359 ALA THR GLU LYS GLN LEU ALA ILE PHE ASN THR PHE CYS
SEQRES 15 C 359 GLU GLY LYS PRO GLY GLN ARG SER ILE ALA ALA SER GLY
SEQRES 16 C 359 GLY ILE LEU LEU TRP PRO GLN SER HIS PHE ASP TRP VAL
SEQRES 17 C 359 ARG PRO GLY ILE ILE LEU TYR GLY VAL SER PRO LEU GLU
SEQRES 18 C 359 ASP ARG SER THR GLY ALA ASP PHE GLY CYS GLN PRO VAL
SEQRES 19 C 359 MET SER LEU THR SER SER LEU ILE ALA VAL ARG GLU HIS
SEQRES 20 C 359 LYS ALA GLY GLU PRO VAL GLY TYR GLY GLY THR TRP VAL
SEQRES 21 C 359 SER GLU ARG ASP THR ARG LEU GLY VAL VAL ALA MET GLY
SEQRES 22 C 359 PHE GLY ASP GLY TYR PRO ARG ALA ALA PRO SER GLY THR
SEQRES 23 C 359 PRO VAL LEU VAL ASN GLY ARG GLU VAL PRO ILE VAL GLY
SEQRES 24 C 359 ARG VAL ALA MET ASP MET ILE CYS VAL ASP LEU GLY PRO
SEQRES 25 C 359 GLN ALA GLN ASP LYS ALA GLY ASP PRO VAL ILE LEU TRP
SEQRES 26 C 359 GLY GLU GLY LEU PRO VAL GLU ARG ILE ALA GLU MET THR
SEQRES 27 C 359 LYS VAL SER ALA TYR GLU LEU ILE THR ARG LEU THR SER
SEQRES 28 C 359 ARG VAL ALA MET LYS TYR VAL ASP
SEQRES 1 D 359 MET GLN ALA ALA THR VAL VAL ILE ASN ARG ARG ALA LEU
SEQRES 2 D 359 ARG HIS ASN LEU GLN ARG LEU ARG GLU LEU ALA PRO ALA
SEQRES 3 D 359 SER LYS MET VAL ALA VAL VAL LYS ALA ASN ALA TYR GLY
SEQRES 4 D 359 HIS GLY LEU LEU GLU THR ALA ARG THR LEU PRO ASP ALA
SEQRES 5 D 359 ASP ALA PHE GLY VAL ALA ARG LEU GLU GLU ALA LEU ARG
SEQRES 6 D 359 LEU ARG ALA GLY GLY ILE THR LYS PRO VAL LEU LEU LEU
SEQRES 7 D 359 GLU GLY PHE PHE ASP ALA ARG ASP LEU PRO THR ILE SER
SEQRES 8 D 359 ALA GLN HIS PHE HIS THR ALA VAL HIS ASN GLU GLU GLN
SEQRES 9 D 359 LEU ALA ALA LEU GLU GLU ALA SER LEU ASP GLU PRO VAL
SEQRES 10 D 359 THR VAL TRP MET LYS LEU ASP THR GLY MET HIS ARG LEU
SEQRES 11 D 359 GLY VAL ARG PRO GLU GLN ALA GLU ALA PHE TYR HIS ARG
SEQRES 12 D 359 LEU THR GLN CYS LYS ASN VAL ARG GLN PRO VAL ASN ILE
SEQRES 13 D 359 VAL SER HIS PHE ALA ARG ALA ASP GLU PRO LYS CYS GLY
SEQRES 14 D 359 ALA THR GLU LYS GLN LEU ALA ILE PHE ASN THR PHE CYS
SEQRES 15 D 359 GLU GLY LYS PRO GLY GLN ARG SER ILE ALA ALA SER GLY
SEQRES 16 D 359 GLY ILE LEU LEU TRP PRO GLN SER HIS PHE ASP TRP VAL
SEQRES 17 D 359 ARG PRO GLY ILE ILE LEU TYR GLY VAL SER PRO LEU GLU
SEQRES 18 D 359 ASP ARG SER THR GLY ALA ASP PHE GLY CYS GLN PRO VAL
SEQRES 19 D 359 MET SER LEU THR SER SER LEU ILE ALA VAL ARG GLU HIS
SEQRES 20 D 359 LYS ALA GLY GLU PRO VAL GLY TYR GLY GLY THR TRP VAL
SEQRES 21 D 359 SER GLU ARG ASP THR ARG LEU GLY VAL VAL ALA MET GLY
SEQRES 22 D 359 PHE GLY ASP GLY TYR PRO ARG ALA ALA PRO SER GLY THR
SEQRES 23 D 359 PRO VAL LEU VAL ASN GLY ARG GLU VAL PRO ILE VAL GLY
SEQRES 24 D 359 ARG VAL ALA MET ASP MET ILE CYS VAL ASP LEU GLY PRO
SEQRES 25 D 359 GLN ALA GLN ASP LYS ALA GLY ASP PRO VAL ILE LEU TRP
SEQRES 26 D 359 GLY GLU GLY LEU PRO VAL GLU ARG ILE ALA GLU MET THR
SEQRES 27 D 359 LYS VAL SER ALA TYR GLU LEU ILE THR ARG LEU THR SER
SEQRES 28 D 359 ARG VAL ALA MET LYS TYR VAL ASP
HET IN5 A 401 22
HET SO4 A 402 5
HET SO4 A 403 5
HET SO4 A 404 5
HET IN5 B 401 22
HET SO4 B 402 5
HET IN5 C 401 22
HET SO4 C 402 5
HET SO4 C 403 5
HET SO4 C 404 5
HET SO4 D 401 5
HETNAM IN5 {1-[(3-HYDROXY-METHYL-5-PHOSPHONOOXY-METHYL-PYRIDIN-4-
HETNAM 2 IN5 YLMETHYL)-AMINO]-ETHYL}-PHOSPHONIC ACID
HETNAM SO4 SULFATE ION
FORMUL 5 IN5 3(C10 H18 N2 O8 P2)
FORMUL 6 SO4 8(O4 S 2-)
FORMUL 16 HOH *236(H2 O)
HELIX 1 AA1 ARG A 10 ALA A 24 1 15
HELIX 2 AA2 VAL A 33 GLY A 39 1 7
HELIX 3 AA3 GLY A 41 LEU A 49 1 9
HELIX 4 AA4 ARG A 59 GLY A 69 1 11
HELIX 5 AA5 ASP A 83 ARG A 85 5 3
HELIX 6 AA6 ASP A 86 GLN A 93 1 8
HELIX 7 AA7 ASN A 101 ALA A 111 1 11
HELIX 8 AA8 ARG A 133 GLU A 135 5 3
HELIX 9 AA9 GLN A 136 GLN A 146 1 11
HELIX 10 AB1 GLY A 169 GLU A 183 1 15
HELIX 11 AB2 ALA A 193 TRP A 200 1 8
HELIX 12 AB3 PRO A 201 HIS A 204 5 4
HELIX 13 AB4 GLY A 211 GLY A 216 5 6
HELIX 14 AB5 THR A 225 GLY A 230 5 6
HELIX 15 AB6 GLY A 254 THR A 258 5 5
HELIX 16 AB7 PRO A 330 LYS A 339 1 10
HELIX 17 AB8 SER A 341 ARG A 348 1 8
HELIX 18 AB9 ARG B 10 ALA B 24 1 15
HELIX 19 AC1 VAL B 33 GLY B 39 1 7
HELIX 20 AC2 GLY B 41 LEU B 49 1 9
HELIX 21 AC3 ARG B 59 GLY B 69 1 11
HELIX 22 AC4 ASP B 83 ARG B 85 5 3
HELIX 23 AC5 ASP B 86 GLN B 93 1 8
HELIX 24 AC6 ASN B 101 ALA B 111 1 11
HELIX 25 AC7 ARG B 133 GLN B 146 1 14
HELIX 26 AC8 GLY B 169 GLU B 183 1 15
HELIX 27 AC9 ALA B 193 TRP B 200 1 8
HELIX 28 AD1 PRO B 201 HIS B 204 5 4
HELIX 29 AD2 GLY B 211 GLY B 216 5 6
HELIX 30 AD3 THR B 225 GLY B 230 5 6
HELIX 31 AD4 GLY B 254 THR B 258 5 5
HELIX 32 AD5 PRO B 330 LYS B 339 1 10
HELIX 33 AD6 SER B 341 ARG B 348 1 8
HELIX 34 AD7 ARG C 10 ALA C 24 1 15
HELIX 35 AD8 VAL C 33 GLY C 39 1 7
HELIX 36 AD9 GLY C 41 THR C 48 1 8
HELIX 37 AE1 ARG C 59 GLY C 69 1 11
HELIX 38 AE2 ASP C 83 ARG C 85 5 3
HELIX 39 AE3 ASP C 86 GLN C 93 1 8
HELIX 40 AE4 ASN C 101 ALA C 111 1 11
HELIX 41 AE5 ARG C 133 GLN C 146 1 14
HELIX 42 AE6 GLY C 169 GLU C 183 1 15
HELIX 43 AE7 ALA C 193 TRP C 200 1 8
HELIX 44 AE8 PRO C 201 HIS C 204 5 4
HELIX 45 AE9 GLY C 211 GLY C 216 5 6
HELIX 46 AF1 GLY C 226 GLY C 230 5 5
HELIX 47 AF2 GLY C 254 THR C 258 5 5
HELIX 48 AF3 SER C 341 ARG C 348 1 8
HELIX 49 AF4 ARG D 10 ALA D 24 1 15
HELIX 50 AF5 VAL D 33 GLY D 39 1 7
HELIX 51 AF6 GLY D 41 THR D 48 1 8
HELIX 52 AF7 ARG D 59 GLY D 69 1 11
HELIX 53 AF8 ASP D 83 ARG D 85 5 3
HELIX 54 AF9 ASP D 86 GLN D 93 1 8
HELIX 55 AG1 ASN D 101 ALA D 111 1 11
HELIX 56 AG2 GLN D 136 THR D 145 1 10
HELIX 57 AG3 GLY D 169 GLU D 183 1 15
HELIX 58 AG4 ALA D 193 TRP D 200 1 8
HELIX 59 AG5 PRO D 201 HIS D 204 5 4
HELIX 60 AG6 GLY D 211 GLY D 216 5 6
HELIX 61 AG7 THR D 225 GLY D 230 5 6
HELIX 62 AG8 GLY D 254 THR D 258 5 5
HELIX 63 AG9 PRO D 330 LYS D 339 1 10
HELIX 64 AH1 SER D 341 ARG D 348 1 8
SHEET 1 AA1 6 ARG A 293 PRO A 296 0
SHEET 2 AA1 6 PRO A 287 VAL A 290 -1 N VAL A 288 O VAL A 295
SHEET 3 AA1 6 PRO A 321 TRP A 325 -1 O ILE A 323 N LEU A 289
SHEET 4 AA1 6 MET A 235 HIS A 247 -1 N SER A 239 O VAL A 322
SHEET 5 AA1 6 THR A 265 VAL A 270 -1 O VAL A 269 N ILE A 242
SHEET 6 AA1 6 ILE A 306 ASP A 309 -1 O VAL A 308 N GLY A 268
SHEET 1 AA2 6 ARG A 293 PRO A 296 0
SHEET 2 AA2 6 PRO A 287 VAL A 290 -1 N VAL A 288 O VAL A 295
SHEET 3 AA2 6 PRO A 321 TRP A 325 -1 O ILE A 323 N LEU A 289
SHEET 4 AA2 6 MET A 235 HIS A 247 -1 N SER A 239 O VAL A 322
SHEET 5 AA2 6 THR A 5 ASN A 9 -1 N VAL A 7 O SER A 236
SHEET 6 AA2 6 ALA A 354 VAL A 358 1 O LYS A 356 N ILE A 8
SHEET 1 AA3 8 ARG A 189 SER A 190 0
SHEET 2 AA3 8 ASN A 155 VAL A 157 1 N ILE A 156 O SER A 190
SHEET 3 AA3 8 VAL A 119 LYS A 122 1 N MET A 121 O ASN A 155
SHEET 4 AA3 8 PHE A 95 VAL A 99 1 N THR A 97 O TRP A 120
SHEET 5 AA3 8 VAL A 75 LEU A 77 1 N LEU A 77 O HIS A 96
SHEET 6 AA3 8 ALA A 54 VAL A 57 1 N PHE A 55 O LEU A 76
SHEET 7 AA3 8 LYS A 28 VAL A 32 1 N ALA A 31 O ALA A 54
SHEET 8 AA3 8 TRP A 207 VAL A 208 1 O VAL A 208 N LYS A 28
SHEET 1 AA4 2 PRO A 252 VAL A 253 0
SHEET 2 AA4 2 TRP A 259 VAL A 260 -1 O TRP A 259 N VAL A 253
SHEET 1 AA5 6 ARG B 293 PRO B 296 0
SHEET 2 AA5 6 PRO B 287 VAL B 290 -1 N VAL B 290 O ARG B 293
SHEET 3 AA5 6 PRO B 321 TRP B 325 -1 O ILE B 323 N LEU B 289
SHEET 4 AA5 6 MET B 235 HIS B 247 -1 N LEU B 237 O LEU B 324
SHEET 5 AA5 6 THR B 265 VAL B 270 -1 O LEU B 267 N ARG B 245
SHEET 6 AA5 6 ILE B 306 ASP B 309 -1 O ILE B 306 N VAL B 270
SHEET 1 AA6 6 ARG B 293 PRO B 296 0
SHEET 2 AA6 6 PRO B 287 VAL B 290 -1 N VAL B 290 O ARG B 293
SHEET 3 AA6 6 PRO B 321 TRP B 325 -1 O ILE B 323 N LEU B 289
SHEET 4 AA6 6 MET B 235 HIS B 247 -1 N LEU B 237 O LEU B 324
SHEET 5 AA6 6 THR B 5 ASN B 9 -1 N THR B 5 O THR B 238
SHEET 6 AA6 6 ALA B 354 VAL B 358 1 O LYS B 356 N ILE B 8
SHEET 1 AA7 9 LYS B 28 VAL B 32 0
SHEET 2 AA7 9 ALA B 54 VAL B 57 1 O GLY B 56 N ALA B 31
SHEET 3 AA7 9 VAL B 75 LEU B 77 1 O LEU B 76 N PHE B 55
SHEET 4 AA7 9 PHE B 95 VAL B 99 1 O HIS B 96 N LEU B 77
SHEET 5 AA7 9 VAL B 119 LYS B 122 1 O LYS B 122 N VAL B 99
SHEET 6 AA7 9 ASN B 155 VAL B 157 1 O ASN B 155 N MET B 121
SHEET 7 AA7 9 ARG B 189 ALA B 192 1 O SER B 190 N ILE B 156
SHEET 8 AA7 9 TRP B 207 VAL B 208 1 O TRP B 207 N ARG B 189
SHEET 9 AA7 9 LYS B 28 VAL B 32 1 N LYS B 28 O VAL B 208
SHEET 1 AA8 2 PRO B 252 VAL B 253 0
SHEET 2 AA8 2 TRP B 259 VAL B 260 -1 O TRP B 259 N VAL B 253
SHEET 1 AA9 6 GLU C 294 PRO C 296 0
SHEET 2 AA9 6 PRO C 287 VAL C 290 -1 N VAL C 288 O VAL C 295
SHEET 3 AA9 6 PRO C 321 TRP C 325 -1 O ILE C 323 N LEU C 289
SHEET 4 AA9 6 MET C 235 HIS C 247 -1 N LEU C 237 O TRP C 325
SHEET 5 AA9 6 THR C 265 VAL C 270 -1 O VAL C 269 N ILE C 242
SHEET 6 AA9 6 ILE C 306 GLY C 311 -1 O VAL C 308 N GLY C 268
SHEET 1 AB1 6 GLU C 294 PRO C 296 0
SHEET 2 AB1 6 PRO C 287 VAL C 290 -1 N VAL C 288 O VAL C 295
SHEET 3 AB1 6 PRO C 321 TRP C 325 -1 O ILE C 323 N LEU C 289
SHEET 4 AB1 6 MET C 235 HIS C 247 -1 N LEU C 237 O TRP C 325
SHEET 5 AB1 6 THR C 5 ASN C 9 -1 N THR C 5 O THR C 238
SHEET 6 AB1 6 ALA C 354 VAL C 358 1 O ALA C 354 N VAL C 6
SHEET 1 AB2 8 ARG C 189 SER C 190 0
SHEET 2 AB2 8 ASN C 155 VAL C 157 1 N ILE C 156 O SER C 190
SHEET 3 AB2 8 VAL C 119 LYS C 122 1 N MET C 121 O ASN C 155
SHEET 4 AB2 8 PHE C 95 VAL C 99 1 N THR C 97 O TRP C 120
SHEET 5 AB2 8 VAL C 75 LEU C 77 1 N VAL C 75 O HIS C 96
SHEET 6 AB2 8 ALA C 54 VAL C 57 1 N PHE C 55 O LEU C 76
SHEET 7 AB2 8 LYS C 28 VAL C 32 1 N ALA C 31 O ALA C 54
SHEET 8 AB2 8 TRP C 207 VAL C 208 1 O VAL C 208 N VAL C 30
SHEET 1 AB3 2 PRO C 252 VAL C 253 0
SHEET 2 AB3 2 TRP C 259 VAL C 260 -1 O TRP C 259 N VAL C 253
SHEET 1 AB4 6 ARG D 293 PRO D 296 0
SHEET 2 AB4 6 PRO D 287 VAL D 290 -1 N VAL D 290 O ARG D 293
SHEET 3 AB4 6 PRO D 321 TRP D 325 -1 O ILE D 323 N LEU D 289
SHEET 4 AB4 6 MET D 235 HIS D 247 -1 N LEU D 237 O LEU D 324
SHEET 5 AB4 6 THR D 265 ALA D 271 -1 O VAL D 269 N ILE D 242
SHEET 6 AB4 6 MET D 305 ASP D 309 -1 O ILE D 306 N VAL D 270
SHEET 1 AB5 6 ARG D 293 PRO D 296 0
SHEET 2 AB5 6 PRO D 287 VAL D 290 -1 N VAL D 290 O ARG D 293
SHEET 3 AB5 6 PRO D 321 TRP D 325 -1 O ILE D 323 N LEU D 289
SHEET 4 AB5 6 MET D 235 HIS D 247 -1 N LEU D 237 O LEU D 324
SHEET 5 AB5 6 THR D 5 ASN D 9 -1 N THR D 5 O THR D 238
SHEET 6 AB5 6 ALA D 354 VAL D 358 1 O LYS D 356 N ILE D 8
SHEET 1 AB6 9 SER D 27 VAL D 32 0
SHEET 2 AB6 9 ALA D 54 VAL D 57 1 O ALA D 54 N ALA D 31
SHEET 3 AB6 9 VAL D 75 LEU D 77 1 O LEU D 76 N PHE D 55
SHEET 4 AB6 9 PHE D 95 VAL D 99 1 O HIS D 96 N LEU D 77
SHEET 5 AB6 9 VAL D 119 LYS D 122 1 O TRP D 120 N THR D 97
SHEET 6 AB6 9 ASN D 155 VAL D 157 1 O ASN D 155 N MET D 121
SHEET 7 AB6 9 ARG D 189 SER D 190 1 O SER D 190 N ILE D 156
SHEET 8 AB6 9 ASP D 206 VAL D 208 1 O TRP D 207 N ARG D 189
SHEET 9 AB6 9 SER D 27 VAL D 32 1 N LYS D 28 O ASP D 206
SHEET 1 AB7 2 PRO D 252 VAL D 253 0
SHEET 2 AB7 2 TRP D 259 VAL D 260 -1 O TRP D 259 N VAL D 253
CISPEP 1 GLN A 152 PRO A 153 0 -0.34
CISPEP 2 GLN B 152 PRO B 153 0 -2.35
CISPEP 3 GLN C 152 PRO C 153 0 3.53
CISPEP 4 GLN D 152 PRO D 153 0 7.36
SITE 1 AC1 18 LYS A 34 TYR A 38 ARG A 129 HIS A 159
SITE 2 AC1 18 ALA A 193 SER A 194 ARG A 209 GLY A 211
SITE 3 AC1 18 ILE A 212 TYR A 343 HOH A 516 HOH A 530
SITE 4 AC1 18 HOH A 566 HOH A 577 TYR B 255 ALA B 302
SITE 5 AC1 18 MET B 303 ASP B 304
SITE 1 AC2 5 LYS A 122 ARG A 129 LEU A 130 HIS A 159
SITE 2 AC2 5 HOH A 595
SITE 1 AC3 2 ARG A 266 ARG B 19
SITE 1 AC4 2 ARG A 19 ARG B 266
SITE 1 AC5 17 TYR A 255 ALA A 302 MET A 303 LYS B 34
SITE 2 AC5 17 TYR B 38 ARG B 129 HIS B 159 ALA B 193
SITE 3 AC5 17 SER B 194 ARG B 209 GLY B 211 ILE B 212
SITE 4 AC5 17 TYR B 343 HOH B 530 HOH B 538 HOH B 567
SITE 5 AC5 17 HOH B 569
SITE 1 AC6 6 LYS B 122 MET B 127 ARG B 129 LEU B 130
SITE 2 AC6 6 HIS B 159 HOH B 553
SITE 1 AC7 15 LYS C 34 TYR C 38 ARG C 129 HIS C 159
SITE 2 AC7 15 ALA C 193 SER C 194 ARG C 209 GLY C 211
SITE 3 AC7 15 ILE C 212 TYR C 343 HOH C 503 TYR D 255
SITE 4 AC7 15 ALA D 302 MET D 303 ASP D 304
SITE 1 AC8 3 GLU C 246 ARG C 266 HOH C 510
SITE 1 AC9 5 LYS C 122 MET C 127 ARG C 129 LEU C 130
SITE 2 AC9 5 HIS C 159
SITE 1 AD1 3 ARG C 19 ARG D 266 LYS D 317
SITE 1 AD2 6 TYR D 38 ALA D 193 SER D 194 GLY D 211
SITE 2 AD2 6 ILE D 212 TYR D 343
CRYST1 147.978 147.978 163.578 90.00 90.00 120.00 P 6 24
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 0.006758 0.003902 0.000000 0.00000
SCALE2 0.000000 0.007803 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006113 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
