HEADER LIGASE 16-APR-03 1P31
TITLE CRYSTAL STRUCTURE OF UDP-N-ACETYLMURAMIC ACID:L-ALANINE LIGASE (MURC)
TITLE 2 FROM HAEMOPHILUS INFLUENZAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UDP-N-ACETYLMURAMATE--ALANINE LIGASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: UDP-N-ACETYLMURAMOYL-L-ALANINE SYNTHETASE;
COMPND 5 EC: 6.3.2.8;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE;
SOURCE 3 ORGANISM_TAXID: 727;
SOURCE 4 GENE: MURC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DL41;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSX29
KEYWDS ALPHA/BETA PROTEIN, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.MOL,A.BROOUN,D.R.DOUGAN,M.T.HILGERS,L.W.TARI,R.A.WIJNANDS,
AUTHOR 2 M.W.KNUTH,D.E.MCREE,R.V.SWANSON
REVDAT 3 13-JUL-11 1P31 1 VERSN
REVDAT 2 24-FEB-09 1P31 1 VERSN
REVDAT 1 15-JUL-03 1P31 0
JRNL AUTH C.D.MOL,A.BROOUN,D.R.DOUGAN,M.T.HILGERS,L.W.TARI,
JRNL AUTH 2 R.A.WIJNANDS,M.W.KNUTH,D.E.MCREE,R.V.SWANSON
JRNL TITL CRYSTAL STRUCTURES OF ACTIVE FULLY ASSEMBLED SUBSTRATE- AND
JRNL TITL 2 PRODUCT-BOUND COMPLEXES OF UDP-N-ACETYLMURAMIC
JRNL TITL 3 ACID:L-ALANINE LIGASE (MURC) FROM HAEMOPHILUS INFLUENZAE.
JRNL REF J.BACTERIOL. V. 185 4152 2003
JRNL REFN ISSN 0021-9193
JRNL PMID 12837790
JRNL DOI 10.1128/JB.185.14.4152-4162.2003
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.19
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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.8
REMARK 3 NUMBER OF REFLECTIONS : 73241
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) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3868
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5507
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1980
REMARK 3 BIN FREE R VALUE SET COUNT : 269
REMARK 3 BIN FREE R VALUE : 0.2490
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7115
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 92
REMARK 3 SOLVENT ATOMS : 700
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 13.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.08000
REMARK 3 B22 (A**2) : -1.65000
REMARK 3 B33 (A**2) : -0.43000
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): 0.144
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.134
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.080
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.590
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7357 ; 0.008 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9973 ; 1.112 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 927 ; 5.523 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1137 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5530 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3669 ; 0.194 ; 0.200
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): 657 ; 0.119 ; 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): 83 ; 0.177 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 47 ; 0.164 ; 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): 4593 ; 0.443 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7384 ; 0.885 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2764 ; 1.879 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2587 ; 2.960 ; 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 : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 12 A 118
REMARK 3 ORIGIN FOR THE GROUP (A): 59.1950 52.9870 -12.9310
REMARK 3 T TENSOR
REMARK 3 T11: 0.1005 T22: 0.1441
REMARK 3 T33: 0.0768 T12: -0.0348
REMARK 3 T13: -0.0027 T23: 0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 2.0053 L22: 4.8587
REMARK 3 L33: 2.1914 L12: 0.0342
REMARK 3 L13: -0.1149 L23: -0.5648
REMARK 3 S TENSOR
REMARK 3 S11: -0.1041 S12: 0.3078 S13: 0.1276
REMARK 3 S21: -0.4966 S22: 0.0208 S23: 0.0498
REMARK 3 S31: 0.0947 S32: -0.0817 S33: 0.0833
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 119 A 324
REMARK 3 ORIGIN FOR THE GROUP (A): 52.8830 49.2010 13.9200
REMARK 3 T TENSOR
REMARK 3 T11: 0.0120 T22: 0.0749
REMARK 3 T33: 0.0714 T12: -0.0054
REMARK 3 T13: 0.0245 T23: -0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 0.7107 L22: 2.0815
REMARK 3 L33: 2.3653 L12: 0.0138
REMARK 3 L13: -0.1401 L23: 0.5063
REMARK 3 S TENSOR
REMARK 3 S11: -0.0634 S12: 0.0024 S13: -0.0615
REMARK 3 S21: 0.1591 S22: -0.0450 S23: 0.2166
REMARK 3 S31: 0.1826 S32: -0.1814 S33: 0.1085
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 325 A 473
REMARK 3 ORIGIN FOR THE GROUP (A): 45.5680 76.0930 9.6040
REMARK 3 T TENSOR
REMARK 3 T11: 0.0089 T22: 0.0782
REMARK 3 T33: 0.1048 T12: 0.0029
REMARK 3 T13: 0.0118 T23: 0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 1.3473 L22: 2.1784
REMARK 3 L33: 1.2051 L12: -0.1875
REMARK 3 L13: 0.4376 L23: -0.0802
REMARK 3 S TENSOR
REMARK 3 S11: -0.0269 S12: 0.0186 S13: -0.0505
REMARK 3 S21: 0.0576 S22: 0.0344 S23: 0.1621
REMARK 3 S31: -0.0642 S32: -0.0363 S33: -0.0075
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 12 B 118
REMARK 3 ORIGIN FOR THE GROUP (A): 9.2980 29.2070 -9.2850
REMARK 3 T TENSOR
REMARK 3 T11: 0.1127 T22: 0.0817
REMARK 3 T33: 0.0720 T12: 0.0133
REMARK 3 T13: -0.0239 T23: 0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 1.3951 L22: 3.6552
REMARK 3 L33: 1.8738 L12: -0.7964
REMARK 3 L13: 0.4196 L23: -1.1018
REMARK 3 S TENSOR
REMARK 3 S11: 0.0806 S12: 0.0890 S13: 0.0574
REMARK 3 S21: -0.3875 S22: -0.0340 S23: 0.0096
REMARK 3 S31: 0.1686 S32: -0.0157 S33: -0.0465
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 119 B 324
REMARK 3 ORIGIN FOR THE GROUP (A): 14.5790 25.1600 17.6670
REMARK 3 T TENSOR
REMARK 3 T11: 0.0207 T22: 0.0632
REMARK 3 T33: 0.0581 T12: 0.0213
REMARK 3 T13: -0.0281 T23: -0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 0.8037 L22: 1.4113
REMARK 3 L33: 1.5481 L12: 0.0004
REMARK 3 L13: 0.4505 L23: -0.3642
REMARK 3 S TENSOR
REMARK 3 S11: -0.0082 S12: -0.0320 S13: 0.0121
REMARK 3 S21: 0.0668 S22: -0.0052 S23: -0.0107
REMARK 3 S31: 0.0702 S32: -0.0196 S33: 0.0135
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 325 B 473
REMARK 3 ORIGIN FOR THE GROUP (A): 5.8440 50.9400 16.8500
REMARK 3 T TENSOR
REMARK 3 T11: 0.0593 T22: 0.1013
REMARK 3 T33: 0.0786 T12: 0.0289
REMARK 3 T13: -0.0160 T23: -0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 1.3420 L22: 2.7388
REMARK 3 L33: 1.5094 L12: -0.0947
REMARK 3 L13: 0.3060 L23: -0.0695
REMARK 3 S TENSOR
REMARK 3 S11: -0.0598 S12: -0.0488 S13: 0.0626
REMARK 3 S21: 0.2333 S22: 0.0775 S23: -0.1448
REMARK 3 S31: -0.1012 S32: -0.0858 S33: -0.0177
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1P31 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-APR-03.
REMARK 100 THE RCSB ID CODE IS RCSB018948.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-JUL-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.3
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 : SI CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77944
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.0
REMARK 200 DATA REDUNDANCY : 4.450
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.45000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, GLYCEROL, MAGNESIUM
REMARK 280 CHLORIDE, TRIS, PH 8.1, NANOVOLUME, 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 45.76150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.08700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.13700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.08700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.76150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.13700
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 MSE A 1
REMARK 465 LYS A 2
REMARK 465 HIS A 3
REMARK 465 SER A 4
REMARK 465 HIS A 5
REMARK 465 GLU A 6
REMARK 465 GLU A 7
REMARK 465 ILE A 8
REMARK 465 ARG A 9
REMARK 465 LYS A 10
REMARK 465 ILE A 11
REMARK 465 ASN A 475
REMARK 465 MSE B 1
REMARK 465 LYS B 2
REMARK 465 HIS B 3
REMARK 465 SER B 4
REMARK 465 HIS B 5
REMARK 465 GLU B 6
REMARK 465 GLU B 7
REMARK 465 ILE B 8
REMARK 465 LYS B 474
REMARK 465 ASN B 475
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 SER A 435 O HOH A 965 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O SER B 435 O HOH A 965 4465 2.19
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 ASP B 386 CB - CG - OD2 ANGL. DEV. = 5.6 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 179 17.49 58.42
REMARK 500 ARG A 377 136.88 74.82
REMARK 500 ASN B 193 168.09 177.23
REMARK 500 ARG B 377 137.50 77.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1008 DISTANCE = 5.33 ANGSTROMS
REMARK 525 HOH A1057 DISTANCE = 7.21 ANGSTROMS
REMARK 525 HOH A1098 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH B 906 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH B1094 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH B1198 DISTANCE = 5.09 ANGSTROMS
REMARK 525 HOH B1211 DISTANCE = 5.45 ANGSTROMS
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 MG A 611 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 962 O
REMARK 620 2 HOH A1058 O 94.1
REMARK 620 3 HOH A1060 O 94.4 92.3
REMARK 620 4 HOH A1061 O 172.2 87.0 93.3
REMARK 620 5 HOH A1059 O 96.0 168.7 91.8 82.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 776 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 198 NE2
REMARK 620 2 HOH A1014 O 90.0
REMARK 620 3 HOH A1089 O 97.2 80.4
REMARK 620 4 EPU A 598 O1E 78.4 74.5 154.5
REMARK 620 5 HOH A1090 O 165.3 89.6 97.1 87.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 732 O
REMARK 620 2 EPU B 602 O1E 104.1
REMARK 620 3 HIS B 198 NE2 84.0 91.0
REMARK 620 4 HOH B 737 O 171.8 78.0 104.0
REMARK 620 5 HOH B 736 O 90.6 164.9 94.1 87.0
REMARK 620 6 HOH B 735 O 87.8 86.0 170.3 84.4 91.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 710 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B1151 O
REMARK 620 2 HOH B1148 O 79.7
REMARK 620 3 HOH B1152 O 90.3 170.0
REMARK 620 4 HOH B1150 O 79.0 92.8 85.9
REMARK 620 5 HOH B1149 O 164.8 85.2 104.8 100.2
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 776
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 710
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPU A 598
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPU B 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1P3D RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF UDP-N-ACETYLMURAMIC ACID:L-ALANINE
REMARK 900 LIGASE (MURC) IN COMPLEX WITH UMA AND ANP
DBREF 1P31 A 1 475 UNP P45066 MURC_HAEIN 1 475
DBREF 1P31 B 1 475 UNP P45066 MURC_HAEIN 1 475
SEQADV 1P31 MSE A 1 UNP P45066 MET 1 MODIFIED RESIDUE
SEQADV 1P31 MSE A 15 UNP P45066 MET 15 MODIFIED RESIDUE
SEQADV 1P31 MSE A 31 UNP P45066 MET 31 MODIFIED RESIDUE
SEQADV 1P31 MSE A 110 UNP P45066 MET 110 MODIFIED RESIDUE
SEQADV 1P31 MSE A 115 UNP P45066 MET 115 MODIFIED RESIDUE
SEQADV 1P31 MSE A 135 UNP P45066 MET 135 MODIFIED RESIDUE
SEQADV 1P31 MSE A 138 UNP P45066 MET 138 MODIFIED RESIDUE
SEQADV 1P31 MSE A 187 UNP P45066 MET 187 MODIFIED RESIDUE
SEQADV 1P31 MSE A 194 UNP P45066 MET 194 MODIFIED RESIDUE
SEQADV 1P31 MSE A 199 UNP P45066 MET 199 MODIFIED RESIDUE
SEQADV 1P31 MSE A 209 UNP P45066 MET 209 MODIFIED RESIDUE
SEQADV 1P31 MSE A 228 UNP P45066 MET 228 MODIFIED RESIDUE
SEQADV 1P31 MSE A 236 UNP P45066 MET 236 MODIFIED RESIDUE
SEQADV 1P31 MSE A 371 UNP P45066 MET 371 MODIFIED RESIDUE
SEQADV 1P31 MSE A 400 UNP P45066 MET 400 MODIFIED RESIDUE
SEQADV 1P31 MSE B 1 UNP P45066 MET 1 MODIFIED RESIDUE
SEQADV 1P31 MSE B 15 UNP P45066 MET 15 MODIFIED RESIDUE
SEQADV 1P31 MSE B 31 UNP P45066 MET 31 MODIFIED RESIDUE
SEQADV 1P31 MSE B 110 UNP P45066 MET 110 MODIFIED RESIDUE
SEQADV 1P31 MSE B 115 UNP P45066 MET 115 MODIFIED RESIDUE
SEQADV 1P31 MSE B 135 UNP P45066 MET 135 MODIFIED RESIDUE
SEQADV 1P31 MSE B 138 UNP P45066 MET 138 MODIFIED RESIDUE
SEQADV 1P31 MSE B 187 UNP P45066 MET 187 MODIFIED RESIDUE
SEQADV 1P31 MSE B 194 UNP P45066 MET 194 MODIFIED RESIDUE
SEQADV 1P31 MSE B 199 UNP P45066 MET 199 MODIFIED RESIDUE
SEQADV 1P31 MSE B 209 UNP P45066 MET 209 MODIFIED RESIDUE
SEQADV 1P31 MSE B 228 UNP P45066 MET 228 MODIFIED RESIDUE
SEQADV 1P31 MSE B 236 UNP P45066 MET 236 MODIFIED RESIDUE
SEQADV 1P31 MSE B 371 UNP P45066 MET 371 MODIFIED RESIDUE
SEQADV 1P31 MSE B 400 UNP P45066 MET 400 MODIFIED RESIDUE
SEQRES 1 A 475 MSE LYS HIS SER HIS GLU GLU ILE ARG LYS ILE ILE PRO
SEQRES 2 A 475 GLU MSE ARG ARG VAL GLN GLN ILE HIS PHE ILE GLY ILE
SEQRES 3 A 475 GLY GLY ALA GLY MSE SER GLY ILE ALA GLU ILE LEU LEU
SEQRES 4 A 475 ASN GLU GLY TYR GLN ILE SER GLY SER ASP ILE ALA ASP
SEQRES 5 A 475 GLY VAL VAL THR GLN ARG LEU ALA GLN ALA GLY ALA LYS
SEQRES 6 A 475 ILE TYR ILE GLY HIS ALA GLU GLU HIS ILE GLU GLY ALA
SEQRES 7 A 475 SER VAL VAL VAL VAL SER SER ALA ILE LYS ASP ASP ASN
SEQRES 8 A 475 PRO GLU LEU VAL THR SER LYS GLN LYS ARG ILE PRO VAL
SEQRES 9 A 475 ILE GLN ARG ALA GLN MSE LEU ALA GLU ILE MSE ARG PHE
SEQRES 10 A 475 ARG HIS GLY ILE ALA VAL ALA GLY THR HIS GLY LYS THR
SEQRES 11 A 475 THR THR THR ALA MSE ILE SER MSE ILE TYR THR GLN ALA
SEQRES 12 A 475 LYS LEU ASP PRO THR PHE VAL ASN GLY GLY LEU VAL LYS
SEQRES 13 A 475 SER ALA GLY LYS ASN ALA HIS LEU GLY ALA SER ARG TYR
SEQRES 14 A 475 LEU ILE ALA GLU ALA ASP GLU SER ASP ALA SER PHE LEU
SEQRES 15 A 475 HIS LEU GLN PRO MSE VAL SER VAL VAL THR ASN MSE GLU
SEQRES 16 A 475 PRO ASP HIS MSE ASP THR TYR GLU GLY ASP PHE GLU LYS
SEQRES 17 A 475 MSE LYS ALA THR TYR VAL LYS PHE LEU HIS ASN LEU PRO
SEQRES 18 A 475 PHE TYR GLY LEU ALA VAL MSE CYS ALA ASP ASP PRO VAL
SEQRES 19 A 475 LEU MSE GLU LEU VAL PRO LYS VAL GLY ARG GLN VAL ILE
SEQRES 20 A 475 THR TYR GLY PHE SER GLU GLN ALA ASP TYR ARG ILE GLU
SEQRES 21 A 475 ASP TYR GLU GLN THR GLY PHE GLN GLY HIS TYR THR VAL
SEQRES 22 A 475 ILE CYS PRO ASN ASN GLU ARG ILE ASN VAL LEU LEU ASN
SEQRES 23 A 475 VAL PRO GLY LYS HIS ASN ALA LEU ASN ALA THR ALA ALA
SEQRES 24 A 475 LEU ALA VAL ALA LYS GLU GLU GLY ILE ALA ASN GLU ALA
SEQRES 25 A 475 ILE LEU GLU ALA LEU ALA ASP PHE GLN GLY ALA GLY ARG
SEQRES 26 A 475 ARG PHE ASP GLN LEU GLY GLU PHE ILE ARG PRO ASN GLY
SEQRES 27 A 475 LYS VAL ARG LEU VAL ASP ASP TYR GLY HIS HIS PRO THR
SEQRES 28 A 475 GLU VAL GLY VAL THR ILE LYS ALA ALA ARG GLU GLY TRP
SEQRES 29 A 475 GLY ASP LYS ARG ILE VAL MSE ILE PHE GLN PRO HIS ARG
SEQRES 30 A 475 TYR SER ARG THR ARG ASP LEU PHE ASP ASP PHE VAL GLN
SEQRES 31 A 475 VAL LEU SER GLN VAL ASP ALA LEU ILE MSE LEU ASP VAL
SEQRES 32 A 475 TYR ALA ALA GLY GLU ALA PRO ILE VAL GLY ALA ASP SER
SEQRES 33 A 475 LYS SER LEU CYS ARG SER ILE ARG ASN LEU GLY LYS VAL
SEQRES 34 A 475 ASP PRO ILE LEU VAL SER ASP THR SER GLN LEU GLY ASP
SEQRES 35 A 475 VAL LEU ASP GLN ILE ILE GLN ASP GLY ASP LEU ILE LEU
SEQRES 36 A 475 ALA GLN GLY ALA GLY SER VAL SER LYS ILE SER ARG GLY
SEQRES 37 A 475 LEU ALA GLU SER TRP LYS ASN
SEQRES 1 B 475 MSE LYS HIS SER HIS GLU GLU ILE ARG LYS ILE ILE PRO
SEQRES 2 B 475 GLU MSE ARG ARG VAL GLN GLN ILE HIS PHE ILE GLY ILE
SEQRES 3 B 475 GLY GLY ALA GLY MSE SER GLY ILE ALA GLU ILE LEU LEU
SEQRES 4 B 475 ASN GLU GLY TYR GLN ILE SER GLY SER ASP ILE ALA ASP
SEQRES 5 B 475 GLY VAL VAL THR GLN ARG LEU ALA GLN ALA GLY ALA LYS
SEQRES 6 B 475 ILE TYR ILE GLY HIS ALA GLU GLU HIS ILE GLU GLY ALA
SEQRES 7 B 475 SER VAL VAL VAL VAL SER SER ALA ILE LYS ASP ASP ASN
SEQRES 8 B 475 PRO GLU LEU VAL THR SER LYS GLN LYS ARG ILE PRO VAL
SEQRES 9 B 475 ILE GLN ARG ALA GLN MSE LEU ALA GLU ILE MSE ARG PHE
SEQRES 10 B 475 ARG HIS GLY ILE ALA VAL ALA GLY THR HIS GLY LYS THR
SEQRES 11 B 475 THR THR THR ALA MSE ILE SER MSE ILE TYR THR GLN ALA
SEQRES 12 B 475 LYS LEU ASP PRO THR PHE VAL ASN GLY GLY LEU VAL LYS
SEQRES 13 B 475 SER ALA GLY LYS ASN ALA HIS LEU GLY ALA SER ARG TYR
SEQRES 14 B 475 LEU ILE ALA GLU ALA ASP GLU SER ASP ALA SER PHE LEU
SEQRES 15 B 475 HIS LEU GLN PRO MSE VAL SER VAL VAL THR ASN MSE GLU
SEQRES 16 B 475 PRO ASP HIS MSE ASP THR TYR GLU GLY ASP PHE GLU LYS
SEQRES 17 B 475 MSE LYS ALA THR TYR VAL LYS PHE LEU HIS ASN LEU PRO
SEQRES 18 B 475 PHE TYR GLY LEU ALA VAL MSE CYS ALA ASP ASP PRO VAL
SEQRES 19 B 475 LEU MSE GLU LEU VAL PRO LYS VAL GLY ARG GLN VAL ILE
SEQRES 20 B 475 THR TYR GLY PHE SER GLU GLN ALA ASP TYR ARG ILE GLU
SEQRES 21 B 475 ASP TYR GLU GLN THR GLY PHE GLN GLY HIS TYR THR VAL
SEQRES 22 B 475 ILE CYS PRO ASN ASN GLU ARG ILE ASN VAL LEU LEU ASN
SEQRES 23 B 475 VAL PRO GLY LYS HIS ASN ALA LEU ASN ALA THR ALA ALA
SEQRES 24 B 475 LEU ALA VAL ALA LYS GLU GLU GLY ILE ALA ASN GLU ALA
SEQRES 25 B 475 ILE LEU GLU ALA LEU ALA ASP PHE GLN GLY ALA GLY ARG
SEQRES 26 B 475 ARG PHE ASP GLN LEU GLY GLU PHE ILE ARG PRO ASN GLY
SEQRES 27 B 475 LYS VAL ARG LEU VAL ASP ASP TYR GLY HIS HIS PRO THR
SEQRES 28 B 475 GLU VAL GLY VAL THR ILE LYS ALA ALA ARG GLU GLY TRP
SEQRES 29 B 475 GLY ASP LYS ARG ILE VAL MSE ILE PHE GLN PRO HIS ARG
SEQRES 30 B 475 TYR SER ARG THR ARG ASP LEU PHE ASP ASP PHE VAL GLN
SEQRES 31 B 475 VAL LEU SER GLN VAL ASP ALA LEU ILE MSE LEU ASP VAL
SEQRES 32 B 475 TYR ALA ALA GLY GLU ALA PRO ILE VAL GLY ALA ASP SER
SEQRES 33 B 475 LYS SER LEU CYS ARG SER ILE ARG ASN LEU GLY LYS VAL
SEQRES 34 B 475 ASP PRO ILE LEU VAL SER ASP THR SER GLN LEU GLY ASP
SEQRES 35 B 475 VAL LEU ASP GLN ILE ILE GLN ASP GLY ASP LEU ILE LEU
SEQRES 36 B 475 ALA GLN GLY ALA GLY SER VAL SER LYS ILE SER ARG GLY
SEQRES 37 B 475 LEU ALA GLU SER TRP LYS ASN
MODRES 1P31 MSE A 15 MET SELENOMETHIONINE
MODRES 1P31 MSE A 31 MET SELENOMETHIONINE
MODRES 1P31 MSE A 110 MET SELENOMETHIONINE
MODRES 1P31 MSE A 115 MET SELENOMETHIONINE
MODRES 1P31 MSE A 135 MET SELENOMETHIONINE
MODRES 1P31 MSE A 138 MET SELENOMETHIONINE
MODRES 1P31 MSE A 187 MET SELENOMETHIONINE
MODRES 1P31 MSE A 194 MET SELENOMETHIONINE
MODRES 1P31 MSE A 199 MET SELENOMETHIONINE
MODRES 1P31 MSE A 209 MET SELENOMETHIONINE
MODRES 1P31 MSE A 228 MET SELENOMETHIONINE
MODRES 1P31 MSE A 236 MET SELENOMETHIONINE
MODRES 1P31 MSE A 371 MET SELENOMETHIONINE
MODRES 1P31 MSE A 400 MET SELENOMETHIONINE
MODRES 1P31 MSE B 15 MET SELENOMETHIONINE
MODRES 1P31 MSE B 31 MET SELENOMETHIONINE
MODRES 1P31 MSE B 110 MET SELENOMETHIONINE
MODRES 1P31 MSE B 115 MET SELENOMETHIONINE
MODRES 1P31 MSE B 135 MET SELENOMETHIONINE
MODRES 1P31 MSE B 138 MET SELENOMETHIONINE
MODRES 1P31 MSE B 187 MET SELENOMETHIONINE
MODRES 1P31 MSE B 194 MET SELENOMETHIONINE
MODRES 1P31 MSE B 199 MET SELENOMETHIONINE
MODRES 1P31 MSE B 209 MET SELENOMETHIONINE
MODRES 1P31 MSE B 228 MET SELENOMETHIONINE
MODRES 1P31 MSE B 236 MET SELENOMETHIONINE
MODRES 1P31 MSE B 371 MET SELENOMETHIONINE
MODRES 1P31 MSE B 400 MET SELENOMETHIONINE
HET MSE A 15 8
HET MSE A 31 8
HET MSE A 110 8
HET MSE A 115 8
HET MSE A 135 8
HET MSE A 138 8
HET MSE A 187 8
HET MSE A 194 8
HET MSE A 199 8
HET MSE A 209 8
HET MSE A 228 8
HET MSE A 236 8
HET MSE A 371 8
HET MSE A 400 8
HET MSE B 15 8
HET MSE B 31 8
HET MSE B 110 8
HET MSE B 115 8
HET MSE B 135 8
HET MSE B 138 8
HET MSE B 187 8
HET MSE B 194 8
HET MSE B 199 8
HET MSE B 209 8
HET MSE B 228 8
HET MSE B 236 8
HET MSE B 371 8
HET MSE B 400 8
HET MG A 776 1
HET MG B 710 1
HET MG B 601 1
HET MG A 611 1
HET EPU A 598 44
HET EPU B 602 44
HETNAM MSE SELENOMETHIONINE
HETNAM MG MAGNESIUM ION
HETNAM EPU URIDINE-DIPHOSPHATE-2(N-ACETYLGLUCOSAMINYL) BUTYRIC
HETNAM 2 EPU ACID
HETSYN EPU ENOLPYRUVYL-URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE
FORMUL 1 MSE 28(C5 H11 N O2 SE)
FORMUL 3 MG 4(MG 2+)
FORMUL 7 EPU 2(C20 H29 N3 O19 P2)
FORMUL 9 HOH *700(H2 O)
HELIX 1 1 GLY A 28 GLY A 42 1 15
HELIX 2 2 GLY A 53 GLY A 63 1 11
HELIX 3 3 ALA A 71 GLU A 76 5 6
HELIX 4 4 ASN A 91 LYS A 100 1 10
HELIX 5 5 ARG A 107 PHE A 117 1 11
HELIX 6 6 GLY A 128 ALA A 143 1 16
HELIX 7 7 ALA A 179 LEU A 184 5 6
HELIX 8 8 HIS A 198 GLU A 203 1 6
HELIX 9 9 ASP A 205 HIS A 218 1 14
HELIX 10 10 ASP A 232 GLY A 243 1 12
HELIX 11 11 GLY A 289 GLY A 307 1 19
HELIX 12 12 ALA A 309 PHE A 320 1 12
HELIX 13 13 HIS A 349 TRP A 364 1 16
HELIX 14 14 ARG A 377 LEU A 384 1 8
HELIX 15 15 LEU A 384 SER A 393 1 10
HELIX 16 16 ASP A 415 GLY A 427 1 13
HELIX 17 17 ASP A 436 SER A 438 5 3
HELIX 18 18 GLN A 439 ILE A 448 1 10
HELIX 19 19 SER A 461 TRP A 473 1 13
HELIX 20 20 GLY B 28 GLY B 42 1 15
HELIX 21 21 GLY B 53 ALA B 62 1 10
HELIX 22 22 ALA B 71 GLU B 76 5 6
HELIX 23 23 ASN B 91 LYS B 100 1 10
HELIX 24 24 ARG B 107 PHE B 117 1 11
HELIX 25 25 GLY B 128 ALA B 143 1 16
HELIX 26 26 ALA B 179 LEU B 184 5 6
HELIX 27 27 ASP B 205 HIS B 218 1 14
HELIX 28 28 ASP B 232 GLY B 243 1 12
HELIX 29 29 GLY B 289 GLY B 307 1 19
HELIX 30 30 ALA B 309 ASP B 319 1 11
HELIX 31 31 HIS B 349 TRP B 364 1 16
HELIX 32 32 ARG B 377 LEU B 384 1 8
HELIX 33 33 LEU B 384 SER B 393 1 10
HELIX 34 34 ASP B 415 GLY B 427 1 13
HELIX 35 35 ASP B 436 SER B 438 5 3
HELIX 36 36 GLN B 439 ILE B 448 1 10
HELIX 37 37 SER B 461 TRP B 473 1 13
SHEET 1 A 5 LYS A 65 ILE A 68 0
SHEET 2 A 5 GLN A 44 ASP A 49 1 N GLY A 47 O TYR A 67
SHEET 3 A 5 GLN A 20 ILE A 24 1 N ILE A 21 O GLN A 44
SHEET 4 A 5 VAL A 80 VAL A 83 1 O VAL A 82 N HIS A 22
SHEET 5 A 5 VAL A 104 GLN A 106 1 O ILE A 105 N VAL A 83
SHEET 1 B10 ALA A 162 HIS A 163 0
SHEET 2 B10 THR A 148 VAL A 150 -1 N PHE A 149 O HIS A 163
SHEET 3 B10 TYR A 169 GLU A 173 1 O TYR A 169 N THR A 148
SHEET 4 B10 HIS A 119 ALA A 124 1 N ILE A 121 O LEU A 170
SHEET 5 B10 VAL A 188 VAL A 191 1 O VAL A 190 N ALA A 124
SHEET 6 B10 LEU A 225 CYS A 229 1 O VAL A 227 N SER A 189
SHEET 7 B10 GLN A 245 GLY A 250 1 O ILE A 247 N ALA A 226
SHEET 8 B10 TYR A 257 THR A 265 1 O ILE A 259 N GLY A 250
SHEET 9 B10 GLN A 268 ILE A 274 -1 O THR A 272 N GLU A 260
SHEET 10 B10 ARG A 280 LEU A 285 -1 O VAL A 283 N TYR A 271
SHEET 1 C 6 ASP A 328 ARG A 335 0
SHEET 2 C 6 GLY A 338 ASP A 345 -1 O ASP A 344 N ASP A 328
SHEET 3 C 6 LEU A 453 GLN A 457 1 O ILE A 454 N ARG A 341
SHEET 4 C 6 ILE A 369 PHE A 373 1 N ILE A 372 O GLN A 457
SHEET 5 C 6 ALA A 397 LEU A 401 1 O ILE A 399 N MSE A 371
SHEET 6 C 6 ILE A 432 VAL A 434 1 O VAL A 434 N MSE A 400
SHEET 1 D 5 LYS B 65 ILE B 68 0
SHEET 2 D 5 GLN B 44 ASP B 49 1 N GLY B 47 O TYR B 67
SHEET 3 D 5 GLN B 20 ILE B 24 1 N ILE B 21 O GLN B 44
SHEET 4 D 5 VAL B 80 VAL B 83 1 O VAL B 82 N HIS B 22
SHEET 5 D 5 VAL B 104 GLN B 106 1 O ILE B 105 N VAL B 81
SHEET 1 E10 LYS B 160 HIS B 163 0
SHEET 2 E10 THR B 148 VAL B 155 -1 N VAL B 155 O LYS B 160
SHEET 3 E10 TYR B 169 GLU B 173 1 O TYR B 169 N THR B 148
SHEET 4 E10 HIS B 119 ALA B 124 1 N ILE B 121 O LEU B 170
SHEET 5 E10 VAL B 188 VAL B 191 1 O VAL B 190 N ALA B 122
SHEET 6 E10 LEU B 225 CYS B 229 1 O VAL B 227 N VAL B 191
SHEET 7 E10 GLN B 245 GLY B 250 1 O ILE B 247 N ALA B 226
SHEET 8 E10 TYR B 257 THR B 265 1 O ILE B 259 N GLY B 250
SHEET 9 E10 GLN B 268 ILE B 274 -1 O THR B 272 N GLU B 260
SHEET 10 E10 ARG B 280 LEU B 285 -1 O VAL B 283 N TYR B 271
SHEET 1 F 6 ASP B 328 ARG B 335 0
SHEET 2 F 6 GLY B 338 ASP B 345 -1 O VAL B 340 N PHE B 333
SHEET 3 F 6 LEU B 453 GLN B 457 1 O ILE B 454 N ARG B 341
SHEET 4 F 6 ILE B 369 PHE B 373 1 N VAL B 370 O LEU B 453
SHEET 5 F 6 ALA B 397 LEU B 401 1 O ILE B 399 N MSE B 371
SHEET 6 F 6 ILE B 432 VAL B 434 1 O VAL B 434 N MSE B 400
LINK C GLU A 14 N MSE A 15 1555 1555 1.33
LINK C MSE A 15 N ARG A 16 1555 1555 1.33
LINK C GLY A 30 N MSE A 31 1555 1555 1.33
LINK C MSE A 31 N SER A 32 1555 1555 1.33
LINK C GLN A 109 N MSE A 110 1555 1555 1.34
LINK C MSE A 110 N LEU A 111 1555 1555 1.33
LINK C ILE A 114 N MSE A 115 1555 1555 1.33
LINK C MSE A 115 N ARG A 116 1555 1555 1.33
LINK C ALA A 134 N MSE A 135 1555 1555 1.34
LINK C MSE A 135 N ILE A 136 1555 1555 1.33
LINK C SER A 137 N MSE A 138 1555 1555 1.33
LINK C MSE A 138 N ILE A 139 1555 1555 1.34
LINK C PRO A 186 N MSE A 187 1555 1555 1.33
LINK C MSE A 187 N VAL A 188 1555 1555 1.33
LINK C ASN A 193 N MSE A 194 1555 1555 1.33
LINK C MSE A 194 N GLU A 195 1555 1555 1.33
LINK C HIS A 198 N MSE A 199 1555 1555 1.33
LINK C MSE A 199 N ASP A 200 1555 1555 1.33
LINK C LYS A 208 N MSE A 209 1555 1555 1.33
LINK C MSE A 209 N LYS A 210 1555 1555 1.33
LINK C VAL A 227 N MSE A 228 1555 1555 1.33
LINK C MSE A 228 N CYS A 229 1555 1555 1.33
LINK C LEU A 235 N MSE A 236 1555 1555 1.33
LINK C MSE A 236 N GLU A 237 1555 1555 1.33
LINK C VAL A 370 N MSE A 371 1555 1555 1.33
LINK C MSE A 371 N ILE A 372 1555 1555 1.33
LINK C ILE A 399 N MSE A 400 1555 1555 1.33
LINK C MSE A 400 N LEU A 401 1555 1555 1.33
LINK MG MG A 611 O HOH A 962 1555 1555 2.10
LINK MG MG A 611 O HOH A1058 1555 1555 2.27
LINK MG MG A 611 O HOH A1060 1555 1555 1.98
LINK MG MG A 611 O HOH A1061 1555 1555 2.19
LINK MG MG A 611 O HOH A1059 1555 1555 2.06
LINK MG MG A 776 NE2 HIS A 198 1555 1555 2.36
LINK MG MG A 776 O HOH A1014 1555 1555 2.39
LINK MG MG A 776 O HOH A1089 1555 1555 2.01
LINK MG MG A 776 O1E EPU A 598 1555 1555 2.21
LINK MG MG A 776 O HOH A1090 1555 1555 2.04
LINK C GLU B 14 N MSE B 15 1555 1555 1.33
LINK C MSE B 15 N ARG B 16 1555 1555 1.33
LINK C GLY B 30 N MSE B 31 1555 1555 1.33
LINK C MSE B 31 N SER B 32 1555 1555 1.33
LINK C GLN B 109 N MSE B 110 1555 1555 1.33
LINK C MSE B 110 N LEU B 111 1555 1555 1.33
LINK C ILE B 114 N MSE B 115 1555 1555 1.33
LINK C MSE B 115 N ARG B 116 1555 1555 1.33
LINK C ALA B 134 N MSE B 135 1555 1555 1.33
LINK C MSE B 135 N ILE B 136 1555 1555 1.33
LINK C SER B 137 N MSE B 138 1555 1555 1.33
LINK C MSE B 138 N ILE B 139 1555 1555 1.33
LINK C PRO B 186 N MSE B 187 1555 1555 1.33
LINK C MSE B 187 N VAL B 188 1555 1555 1.33
LINK C ASN B 193 N MSE B 194 1555 1555 1.32
LINK C MSE B 194 N GLU B 195 1555 1555 1.33
LINK C HIS B 198 N MSE B 199 1555 1555 1.33
LINK C MSE B 199 N ASP B 200 1555 1555 1.33
LINK C LYS B 208 N MSE B 209 1555 1555 1.33
LINK C MSE B 209 N LYS B 210 1555 1555 1.33
LINK C VAL B 227 N MSE B 228 1555 1555 1.33
LINK C MSE B 228 N CYS B 229 1555 1555 1.33
LINK C LEU B 235 N MSE B 236 1555 1555 1.33
LINK C MSE B 236 N GLU B 237 1555 1555 1.33
LINK C VAL B 370 N MSE B 371 1555 1555 1.32
LINK C MSE B 371 N ILE B 372 1555 1555 1.33
LINK C ILE B 399 N MSE B 400 1555 1555 1.32
LINK C MSE B 400 N LEU B 401 1555 1555 1.33
LINK MG MG B 601 O HOH B 732 1555 1555 1.95
LINK MG MG B 601 O1E EPU B 602 1555 1555 2.12
LINK MG MG B 601 NE2 HIS B 198 1555 1555 2.17
LINK MG MG B 601 O HOH B 737 1555 1555 2.09
LINK MG MG B 601 O HOH B 736 1555 1555 2.06
LINK MG MG B 601 O HOH B 735 1555 1555 2.21
LINK MG MG B 710 O HOH B1151 1555 1555 2.56
LINK MG MG B 710 O HOH B1148 1555 1555 2.43
LINK MG MG B 710 O HOH B1152 1555 1555 2.03
LINK MG MG B 710 O HOH B1150 1555 1555 2.04
LINK MG MG B 710 O HOH B1149 1555 1555 1.93
SITE 1 AC1 5 HIS A 198 EPU A 598 HOH A1014 HOH A1089
SITE 2 AC1 5 HOH A1090
SITE 1 AC2 5 HOH B1148 HOH B1149 HOH B1150 HOH B1151
SITE 2 AC2 5 HOH B1152
SITE 1 AC3 6 HIS B 198 EPU B 602 HOH B 732 HOH B 735
SITE 2 AC3 6 HOH B 736 HOH B 737
SITE 1 AC4 5 HOH A 962 HOH A1058 HOH A1059 HOH A1060
SITE 2 AC4 5 HOH A1061
SITE 1 AC5 29 GLY A 25 GLY A 27 GLY A 28 ALA A 29
SITE 2 AC5 29 GLY A 30 MSE A 31 ASP A 49 ILE A 50
SITE 3 AC5 29 HIS A 70 SER A 84 SER A 85 ILE A 87
SITE 4 AC5 29 ARG A 107 GLU A 173 ASP A 175 SER A 177
SITE 5 AC5 29 HIS A 198 MG A 776 HOH A 812 HOH A 905
SITE 6 AC5 29 HOH A 914 HOH A 935 HOH A 986 HOH A 987
SITE 7 AC5 29 HOH A 988 HOH A 992 HOH A 999 HOH A1014
SITE 8 AC5 29 HOH A1090
SITE 1 AC6 34 GLY B 25 GLY B 27 GLY B 28 ALA B 29
SITE 2 AC6 34 GLY B 30 MSE B 31 ASP B 49 ILE B 50
SITE 3 AC6 34 HIS B 70 SER B 84 SER B 85 ALA B 86
SITE 4 AC6 34 ILE B 87 ARG B 107 GLU B 173 ASP B 175
SITE 5 AC6 34 SER B 177 HIS B 198 MG B 601 HOH B 614
SITE 6 AC6 34 HOH B 619 HOH B 626 HOH B 653 HOH B 654
SITE 7 AC6 34 HOH B 735 HOH B 737 HOH B 746 HOH B 863
SITE 8 AC6 34 HOH B 915 HOH B 955 HOH B 956 HOH B1071
SITE 9 AC6 34 HOH B1158 HOH B1160
CRYST1 91.523 92.274 118.174 90.00 90.00 90.00 P 21 21 21 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 0.010926 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010837 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008462 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
