HEADER ISOMERASE 30-AUG-10 3OO2
TITLE 2.37 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF AN ALANINE RACEMASE
TITLE 2 (ALR) FROM STAPHYLOCOCCUS AUREUS SUBSP. AUREUS COL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALANINE RACEMASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 5.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS;
SOURCE 3 ORGANISM_TAXID: 93062;
SOURCE 4 STRAIN: COL;
SOURCE 5 GENE: ALR, ALR1, SACOL2060;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)/MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS ALANINE RACEMASE, INFECTIOUS DISEASES, CENTER FOR STRUCTURAL GENOMICS
KEYWDS 2 OF INFECTIOUS DISEASES (CSGID), ALANINE AND ASPARTATE METABOLISM AND
KEYWDS 3 D-ALANINE METABOLISM, BIOSYNTHESIS AND DEGRADATION OF MUREIN
KEYWDS 4 SACCULUS AND PEPTIDOGLYCAN, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.S.HALAVATY,L.SHUVALOVA,G.MINASOV,J.WINSOR,I.DUBROVSKA,K.KWON,
AUTHOR 2 W.F.ANDERSON,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
AUTHOR 3 (CSGID)
REVDAT 1 06-OCT-10 3OO2 0
JRNL AUTH A.S.HALAVATY,L.SHUVALOVA,G.MINASOV,J.WINSOR,I.DUBROVSKA,
JRNL AUTH 2 K.KWON,W.F.ANDERSON,
JRNL AUTH 3 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
JRNL AUTH 4 (CSGID)
JRNL TITL 2.37 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF AN ALANINE
JRNL TITL 2 RACEMASE (ALR) FROM STAPHYLOCOCCUS AUREUS SUBSP. AUREUS COL
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.37 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.37
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.59
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 28741
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) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1533
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) : 2.37
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.43
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2042
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.08
REMARK 3 BIN R VALUE (WORKING SET) : 0.2580
REMARK 3 BIN FREE R VALUE SET COUNT : 103
REMARK 3 BIN FREE R VALUE : 0.3650
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5866
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 120
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.52000
REMARK 3 B22 (A**2) : -1.62000
REMARK 3 B33 (A**2) : 0.10000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.285
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.218
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.971
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.903
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6051 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 4049 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8196 ; 1.567 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9932 ; 0.835 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 750 ; 3.007 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 273 ;29.905 ;24.689
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1081 ;11.545 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;14.623 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 933 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6682 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1160 ; 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): 3731 ; 1.105 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1513 ; 0.299 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6058 ; 1.949 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2320 ; 3.317 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2138 ; 4.850 ; 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 2 A 174
REMARK 3 ORIGIN FOR THE GROUP (A): -12.6358 53.2467 -10.2212
REMARK 3 T TENSOR
REMARK 3 T11: 0.0651 T22: 0.1110
REMARK 3 T33: 0.1167 T12: -0.0417
REMARK 3 T13: -0.0502 T23: 0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 1.1587 L22: 2.1201
REMARK 3 L33: 1.4655 L12: 0.8539
REMARK 3 L13: -0.1829 L23: 0.2976
REMARK 3 S TENSOR
REMARK 3 S11: -0.2172 S12: 0.1787 S13: -0.0096
REMARK 3 S21: -0.2563 S22: 0.0246 S23: 0.2592
REMARK 3 S31: -0.0687 S32: -0.1987 S33: 0.1925
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 175 A 269
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8424 58.3328 -14.2222
REMARK 3 T TENSOR
REMARK 3 T11: 0.1352 T22: 0.1853
REMARK 3 T33: 0.0201 T12: -0.0963
REMARK 3 T13: 0.0291 T23: 0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 1.0595 L22: 2.5667
REMARK 3 L33: 1.7450 L12: 0.4976
REMARK 3 L13: -0.1101 L23: 1.3320
REMARK 3 S TENSOR
REMARK 3 S11: -0.2499 S12: 0.3557 S13: -0.0490
REMARK 3 S21: -0.5333 S22: 0.2619 S23: -0.0976
REMARK 3 S31: -0.2469 S32: 0.1609 S33: -0.0120
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 270 A 382
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0823 73.8442 0.4201
REMARK 3 T TENSOR
REMARK 3 T11: 0.1454 T22: 0.0816
REMARK 3 T33: 0.0924 T12: -0.0883
REMARK 3 T13: -0.0105 T23: 0.0512
REMARK 3 L TENSOR
REMARK 3 L11: 1.6508 L22: 1.7129
REMARK 3 L33: 1.6845 L12: 0.2955
REMARK 3 L13: 0.3235 L23: 0.6737
REMARK 3 S TENSOR
REMARK 3 S11: -0.0898 S12: 0.1323 S13: 0.2106
REMARK 3 S21: -0.2788 S22: 0.1037 S23: -0.1884
REMARK 3 S31: -0.4397 S32: 0.1999 S33: -0.0140
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 2 B 133
REMARK 3 ORIGIN FOR THE GROUP (A): -4.7112 75.8146 19.6582
REMARK 3 T TENSOR
REMARK 3 T11: 0.0545 T22: 0.1728
REMARK 3 T33: 0.1026 T12: 0.0132
REMARK 3 T13: -0.0147 T23: -0.0482
REMARK 3 L TENSOR
REMARK 3 L11: 1.2878 L22: 3.7578
REMARK 3 L33: 1.1237 L12: 0.7871
REMARK 3 L13: 0.5574 L23: 1.2069
REMARK 3 S TENSOR
REMARK 3 S11: 0.0073 S12: -0.2201 S13: 0.1975
REMARK 3 S21: 0.1084 S22: -0.2944 S23: 0.4285
REMARK 3 S31: -0.0934 S32: -0.3360 S33: 0.2871
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 134 B 200
REMARK 3 ORIGIN FOR THE GROUP (A): 10.5673 85.7827 28.0407
REMARK 3 T TENSOR
REMARK 3 T11: 0.2075 T22: 0.1557
REMARK 3 T33: 0.1744 T12: -0.0799
REMARK 3 T13: -0.1091 T23: 0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 4.6551 L22: 4.9371
REMARK 3 L33: 4.5033 L12: -2.4659
REMARK 3 L13: 0.1869 L23: -0.6157
REMARK 3 S TENSOR
REMARK 3 S11: -0.0913 S12: -0.1444 S13: 0.6552
REMARK 3 S21: 0.6680 S22: -0.1613 S23: -0.5345
REMARK 3 S31: 0.1054 S32: 0.2453 S33: 0.2526
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 201 B 382
REMARK 3 ORIGIN FOR THE GROUP (A): 2.1354 53.0417 13.8799
REMARK 3 T TENSOR
REMARK 3 T11: 0.0746 T22: 0.0711
REMARK 3 T33: 0.0749 T12: -0.0326
REMARK 3 T13: -0.0202 T23: 0.0694
REMARK 3 L TENSOR
REMARK 3 L11: 1.4348 L22: 2.5931
REMARK 3 L33: 1.8772 L12: 0.3096
REMARK 3 L13: 0.5670 L23: 1.2946
REMARK 3 S TENSOR
REMARK 3 S11: 0.0684 S12: -0.1267 S13: -0.1975
REMARK 3 S21: 0.4174 S22: -0.0668 S23: 0.0037
REMARK 3 S31: 0.2058 S32: -0.0013 S33: -0.0016
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 : 1.20
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 3OO2 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-SEP-10.
REMARK 100 THE RCSB ID CODE IS RCSB061358.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-AUG-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : DIAMOND[111]
REMARK 200 OPTICS : BE-LENSES/DIAMOND LAUE MONO
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30323
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.370
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.3600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.37
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.41
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.57200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.660
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: BALBES MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7.6 MG/ML PROTEIN IN 10 MM TRIS/HCL PH
REMARK 280 8.3, 0.5 M NACL, 5 MM BME. CRYSTALS GREW FROM 0.1 M MIB BUFFER PH
REMARK 280 5.0, 25 % (W/V) PEG1500 (THE PACT SUITE CONDITION #14), VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295K
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 23.86750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.50400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 59.15500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.50400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.86750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 59.15500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 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 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 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 ALA A 267
REMARK 465 THR A 268
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 MET B 1
REMARK 465 GLY B 120
REMARK 465 GLU B 121
REMARK 465 GLN B 122
REMARK 465 GLU B 123
REMARK 465 GLY B 260
REMARK 465 GLU B 261
REMARK 465 SER B 262
REMARK 465 VAL B 263
REMARK 465 SER B 264
REMARK 465 TYR B 265
REMARK 465 GLY B 266
REMARK 465 ALA B 267
REMARK 465 THR B 268
REMARK 465 TYR B 269
REMARK 465 THR B 270
REMARK 465 ALA B 271
REMARK 465 THR B 272
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 MET A 136 90.89 -56.29
REMARK 500 ARG A 138 -86.54 -118.04
REMARK 500 GLN A 253 149.95 -171.93
REMARK 500 ASN A 300 48.98 36.55
REMARK 500 ASN A 334 54.08 -90.64
REMARK 500 LEU A 360 105.83 -53.59
REMARK 500 ALA B 90 -55.04 -28.55
REMARK 500 LYS B 91 -59.73 -26.35
REMARK 500 ILE B 115 43.02 -73.55
REMARK 500 LYS B 116 -14.49 -145.19
REMARK 500 ARG B 138 100.68 -26.66
REMARK 500 LEU B 139 134.23 -23.13
REMARK 500 CYS B 212 72.34 49.15
REMARK 500 VAL B 239 127.95 -32.38
REMARK 500 ASN B 334 41.75 -84.14
REMARK 500 THR B 351 -157.78 -148.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 383 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 160 O
REMARK 620 2 TYR A 157 O 99.1
REMARK 620 3 ILE A 154 O 96.8 72.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 383 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE B 154 O
REMARK 620 2 LEU B 160 O 105.2
REMARK 620 3 HOH B 446 O 76.7 148.2
REMARK 620 4 TYR B 157 O 72.1 83.9 66.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 383
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 384
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 385
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 386
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 383
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME B 384
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 385
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: IDP00688 RELATED DB: TARGETDB
DBREF 3OO2 A 1 382 UNP Q5HED1 ALR1_STAAC 1 382
DBREF 3OO2 B 1 382 UNP Q5HED1 ALR1_STAAC 1 382
SEQADV 3OO2 SER A -2 UNP Q5HED1 EXPRESSION TAG
SEQADV 3OO2 ASN A -1 UNP Q5HED1 EXPRESSION TAG
SEQADV 3OO2 ALA A 0 UNP Q5HED1 EXPRESSION TAG
SEQADV 3OO2 SER B -2 UNP Q5HED1 EXPRESSION TAG
SEQADV 3OO2 ASN B -1 UNP Q5HED1 EXPRESSION TAG
SEQADV 3OO2 ALA B 0 UNP Q5HED1 EXPRESSION TAG
SEQRES 1 A 385 SER ASN ALA MET SER ASP LYS TYR TYR ARG SER ALA TYR
SEQRES 2 A 385 MET ASN VAL ASP LEU ASN ALA VAL ALA SER ASN PHE LYS
SEQRES 3 A 385 VAL PHE SER THR LEU HIS PRO ASN LYS THR VAL MET ALA
SEQRES 4 A 385 VAL VAL LYS ALA ASN ALA TYR GLY LEU GLY SER VAL LYS
SEQRES 5 A 385 VAL ALA ARG HIS LEU MET GLU ASN GLY ALA THR PHE PHE
SEQRES 6 A 385 ALA VAL ALA THR LEU ASP GLU ALA ILE GLU LEU ARG MET
SEQRES 7 A 385 HIS GLY ILE THR ALA LYS ILE LEU VAL LEU GLY VAL LEU
SEQRES 8 A 385 PRO ALA LYS ASP ILE ASP LYS ALA ILE GLN HIS ARG VAL
SEQRES 9 A 385 ALA LEU THR VAL PRO SER LYS GLN TRP LEU LYS GLU ALA
SEQRES 10 A 385 ILE LYS ASN ILE SER GLY GLU GLN GLU LYS LYS LEU TRP
SEQRES 11 A 385 LEU HIS ILE LYS LEU ASP THR GLY MET GLY ARG LEU GLY
SEQRES 12 A 385 ILE LYS ASP THR LYS THR TYR GLN GLU VAL ILE GLU ILE
SEQRES 13 A 385 ILE GLN GLN TYR GLU GLN LEU VAL PHE GLU GLY VAL PHE
SEQRES 14 A 385 THR HIS PHE ALA CYS ALA ASP GLU PRO GLY ASP MET THR
SEQRES 15 A 385 THR GLU GLN TYR GLN ARG PHE LYS ASP MET VAL ASN GLU
SEQRES 16 A 385 ALA ILE LYS PRO GLU TYR ILE HIS CYS GLN ASN SER ALA
SEQRES 17 A 385 GLY SER LEU LEU MET ASP CYS GLN PHE CYS ASN ALA ILE
SEQRES 18 A 385 ARG PRO GLY ILE SER LEU TYR GLY TYR TYR PRO SER GLU
SEQRES 19 A 385 TYR VAL GLN GLN LYS VAL LYS VAL HIS LEU LYS PRO SER
SEQRES 20 A 385 VAL GLN LEU ILE ALA ASN VAL VAL GLN THR LYS THR LEU
SEQRES 21 A 385 GLN ALA GLY GLU SER VAL SER TYR GLY ALA THR TYR THR
SEQRES 22 A 385 ALA THR ASP PRO THR THR ILE ALA LEU LEU PRO ILE GLY
SEQRES 23 A 385 TYR ALA ASP GLY TYR LEU ARG ILE MET GLN GLY SER PHE
SEQRES 24 A 385 VAL ASN VAL ASN GLY HIS GLN CYS GLU VAL ILE GLY ARG
SEQRES 25 A 385 VAL CYS MET ASP GLN THR ILE VAL LYS VAL PRO ASP GLN
SEQRES 26 A 385 VAL LYS ALA GLY ASP SER VAL ILE LEU ILE ASP ASN HIS
SEQRES 27 A 385 ARG GLU SER PRO GLN SER VAL GLU VAL VAL ALA GLU LYS
SEQRES 28 A 385 GLN HIS THR ILE ASN TYR GLU VAL LEU CYS ASN LEU SER
SEQRES 29 A 385 ARG ARG LEU PRO ARG ILE TYR HIS ASP GLY ASP GLN ARG
SEQRES 30 A 385 PHE VAL THR ASN GLU LEU LEU LYS
SEQRES 1 B 385 SER ASN ALA MET SER ASP LYS TYR TYR ARG SER ALA TYR
SEQRES 2 B 385 MET ASN VAL ASP LEU ASN ALA VAL ALA SER ASN PHE LYS
SEQRES 3 B 385 VAL PHE SER THR LEU HIS PRO ASN LYS THR VAL MET ALA
SEQRES 4 B 385 VAL VAL LYS ALA ASN ALA TYR GLY LEU GLY SER VAL LYS
SEQRES 5 B 385 VAL ALA ARG HIS LEU MET GLU ASN GLY ALA THR PHE PHE
SEQRES 6 B 385 ALA VAL ALA THR LEU ASP GLU ALA ILE GLU LEU ARG MET
SEQRES 7 B 385 HIS GLY ILE THR ALA LYS ILE LEU VAL LEU GLY VAL LEU
SEQRES 8 B 385 PRO ALA LYS ASP ILE ASP LYS ALA ILE GLN HIS ARG VAL
SEQRES 9 B 385 ALA LEU THR VAL PRO SER LYS GLN TRP LEU LYS GLU ALA
SEQRES 10 B 385 ILE LYS ASN ILE SER GLY GLU GLN GLU LYS LYS LEU TRP
SEQRES 11 B 385 LEU HIS ILE LYS LEU ASP THR GLY MET GLY ARG LEU GLY
SEQRES 12 B 385 ILE LYS ASP THR LYS THR TYR GLN GLU VAL ILE GLU ILE
SEQRES 13 B 385 ILE GLN GLN TYR GLU GLN LEU VAL PHE GLU GLY VAL PHE
SEQRES 14 B 385 THR HIS PHE ALA CYS ALA ASP GLU PRO GLY ASP MET THR
SEQRES 15 B 385 THR GLU GLN TYR GLN ARG PHE LYS ASP MET VAL ASN GLU
SEQRES 16 B 385 ALA ILE LYS PRO GLU TYR ILE HIS CYS GLN ASN SER ALA
SEQRES 17 B 385 GLY SER LEU LEU MET ASP CYS GLN PHE CYS ASN ALA ILE
SEQRES 18 B 385 ARG PRO GLY ILE SER LEU TYR GLY TYR TYR PRO SER GLU
SEQRES 19 B 385 TYR VAL GLN GLN LYS VAL LYS VAL HIS LEU LYS PRO SER
SEQRES 20 B 385 VAL GLN LEU ILE ALA ASN VAL VAL GLN THR LYS THR LEU
SEQRES 21 B 385 GLN ALA GLY GLU SER VAL SER TYR GLY ALA THR TYR THR
SEQRES 22 B 385 ALA THR ASP PRO THR THR ILE ALA LEU LEU PRO ILE GLY
SEQRES 23 B 385 TYR ALA ASP GLY TYR LEU ARG ILE MET GLN GLY SER PHE
SEQRES 24 B 385 VAL ASN VAL ASN GLY HIS GLN CYS GLU VAL ILE GLY ARG
SEQRES 25 B 385 VAL CYS MET ASP GLN THR ILE VAL LYS VAL PRO ASP GLN
SEQRES 26 B 385 VAL LYS ALA GLY ASP SER VAL ILE LEU ILE ASP ASN HIS
SEQRES 27 B 385 ARG GLU SER PRO GLN SER VAL GLU VAL VAL ALA GLU LYS
SEQRES 28 B 385 GLN HIS THR ILE ASN TYR GLU VAL LEU CYS ASN LEU SER
SEQRES 29 B 385 ARG ARG LEU PRO ARG ILE TYR HIS ASP GLY ASP GLN ARG
SEQRES 30 B 385 PHE VAL THR ASN GLU LEU LEU LYS
HET NA A 383 1
HET BME A 384 4
HET BME A 385 4
HET PO4 A 386 5
HET NA B 383 1
HET BME B 384 4
HET PO4 B 385 5
HETNAM NA SODIUM ION
HETNAM BME BETA-MERCAPTOETHANOL
HETNAM PO4 PHOSPHATE ION
FORMUL 3 NA 2(NA 1+)
FORMUL 4 BME 3(C2 H6 O S)
FORMUL 6 PO4 2(O4 P 3-)
FORMUL 10 HOH *120(H2 O)
HELIX 1 1 LEU A 15 HIS A 29 1 15
HELIX 2 2 VAL A 38 GLY A 44 1 7
HELIX 3 3 GLY A 46 ASN A 57 1 12
HELIX 4 4 THR A 66 MET A 75 1 10
HELIX 5 5 PRO A 89 LYS A 91 5 3
HELIX 6 6 ASP A 92 HIS A 99 1 8
HELIX 7 7 SER A 107 ASN A 117 1 11
HELIX 8 8 ASP A 143 GLN A 155 1 13
HELIX 9 9 ASP A 177 GLU A 192 1 16
HELIX 10 10 ASN A 203 MET A 210 1 8
HELIX 11 11 GLY A 221 GLY A 226 5 6
HELIX 12 12 SER A 230 VAL A 237 1 8
HELIX 13 13 GLY A 283 GLY A 287 5 5
HELIX 14 14 LEU A 289 GLN A 293 5 5
HELIX 15 15 SER A 341 GLN A 349 1 9
HELIX 16 16 ILE A 352 LEU A 360 1 9
HELIX 17 17 ASN A 378 LYS A 382 5 5
HELIX 18 18 LEU B 15 HIS B 29 1 15
HELIX 19 19 VAL B 38 GLY B 44 1 7
HELIX 20 20 GLY B 46 GLU B 56 1 11
HELIX 21 21 THR B 66 HIS B 76 1 11
HELIX 22 22 PRO B 89 LYS B 91 5 3
HELIX 23 23 ASP B 92 HIS B 99 1 8
HELIX 24 24 SER B 107 ILE B 115 1 9
HELIX 25 25 ASP B 143 TYR B 157 1 15
HELIX 26 26 ASP B 177 ASN B 191 1 15
HELIX 27 27 ASN B 203 MET B 210 1 8
HELIX 28 28 GLY B 221 GLY B 226 5 6
HELIX 29 29 SER B 230 GLN B 235 1 6
HELIX 30 30 GLY B 283 GLY B 287 5 5
HELIX 31 31 LEU B 289 GLN B 293 5 5
HELIX 32 32 SER B 341 GLN B 349 1 9
HELIX 33 33 ILE B 352 LEU B 360 1 9
HELIX 34 34 ASN B 378 LYS B 382 5 5
SHEET 1 A10 GLN A 253 LEU A 257 0
SHEET 2 A10 THR A 275 LEU A 280 -1 O LEU A 279 N GLN A 253
SHEET 3 A10 THR A 315 VAL A 319 -1 O THR A 315 N LEU A 280
SHEET 4 A10 HIS A 302 ILE A 307 -1 N GLU A 305 O LYS A 318
SHEET 5 A10 PHE A 296 VAL A 299 -1 N VAL A 299 O HIS A 302
SHEET 6 A10 SER A 328 ILE A 332 -1 O ILE A 330 N ASN A 298
SHEET 7 A10 VAL A 245 ASN A 250 -1 N LEU A 247 O LEU A 331
SHEET 8 A10 ALA A 9 ASP A 14 -1 N TYR A 10 O ILE A 248
SHEET 9 A10 ARG A 366 ASP A 370 1 O ILE A 367 N VAL A 13
SHEET 10 A10 GLN A 373 THR A 377 -1 O PHE A 375 N TYR A 368
SHEET 1 B 9 THR A 33 VAL A 37 0
SHEET 2 B 9 PHE A 61 VAL A 64 1 O ALA A 63 N ALA A 36
SHEET 3 B 9 LYS A 81 VAL A 84 1 O LEU A 83 N PHE A 62
SHEET 4 B 9 VAL A 101 VAL A 105 1 O ALA A 102 N ILE A 82
SHEET 5 B 9 LEU A 126 LYS A 131 1 O HIS A 129 N LEU A 103
SHEET 6 B 9 LEU A 160 PHE A 166 1 O GLY A 164 N ILE A 130
SHEET 7 B 9 TYR A 198 GLN A 202 1 O TYR A 198 N GLU A 163
SHEET 8 B 9 ALA A 217 ILE A 218 1 O ALA A 217 N ILE A 199
SHEET 9 B 9 THR A 33 VAL A 37 1 N MET A 35 O ILE A 218
SHEET 1 C10 GLN B 253 LEU B 257 0
SHEET 2 C10 THR B 275 LEU B 280 -1 O THR B 275 N LEU B 257
SHEET 3 C10 THR B 315 VAL B 319 -1 O VAL B 319 N THR B 276
SHEET 4 C10 HIS B 302 ILE B 307 -1 N GLU B 305 O LYS B 318
SHEET 5 C10 PHE B 296 VAL B 299 -1 N VAL B 299 O HIS B 302
SHEET 6 C10 SER B 328 ILE B 332 -1 O ILE B 330 N ASN B 298
SHEET 7 C10 VAL B 245 ASN B 250 -1 N ALA B 249 O VAL B 329
SHEET 8 C10 ALA B 9 ASP B 14 -1 N TYR B 10 O ILE B 248
SHEET 9 C10 ARG B 366 HIS B 369 1 O ILE B 367 N MET B 11
SHEET 10 C10 ARG B 374 THR B 377 -1 O PHE B 375 N TYR B 368
SHEET 1 D 6 THR B 33 VAL B 34 0
SHEET 2 D 6 ALA B 217 ILE B 218 1 O ILE B 218 N THR B 33
SHEET 3 D 6 TYR B 198 GLN B 202 1 N ILE B 199 O ALA B 217
SHEET 4 D 6 LEU B 160 PHE B 166 1 N GLU B 163 O TYR B 198
SHEET 5 D 6 LEU B 126 LYS B 131 1 N ILE B 130 O GLY B 164
SHEET 6 D 6 LEU B 103 VAL B 105 1 N LEU B 103 O TRP B 127
SHEET 1 E 3 ALA B 36 VAL B 37 0
SHEET 2 E 3 PHE B 61 VAL B 64 1 O ALA B 63 N ALA B 36
SHEET 3 E 3 LYS B 81 VAL B 84 1 O LYS B 81 N PHE B 62
SSBOND 1 CYS A 201 CYS A 215 1555 1555 2.08
SSBOND 2 CYS B 201 CYS B 215 1555 1555 2.10
LINK O LEU A 160 NA NA A 383 1555 1555 2.24
LINK O TYR A 157 NA NA A 383 1555 1555 2.32
LINK O ILE B 154 NA NA B 383 1555 1555 2.36
LINK O LEU B 160 NA NA B 383 1555 1555 2.44
LINK NA NA B 383 O HOH B 446 1555 1555 2.47
LINK O TYR B 157 NA NA B 383 1555 1555 2.52
LINK O ILE A 154 NA NA A 383 1555 1555 2.64
LINK SG BCYS B 311 S2 BBME B 384 1555 1555 2.13
LINK SG ACYS A 311 S2 ABME A 385 1555 1555 1.94
LINK SG BCYS A 171 S2 BBME A 384 1555 1555 2.31
SITE 1 AC1 3 ILE A 154 TYR A 157 LEU A 160
SITE 1 AC2 5 ALA A 170 CYS A 171 ASP A 173 GLU A 174
SITE 2 AC2 5 ARG B 309
SITE 1 AC3 2 CYS A 311 ARG B 138
SITE 1 AC4 6 TYR A 43 ASN A 203 SER A 204 GLY A 221
SITE 2 AC4 6 ILE A 222 TYR A 354
SITE 1 AC5 4 ILE B 154 TYR B 157 LEU B 160 HOH B 446
SITE 1 AC6 2 ARG B 309 CYS B 311
SITE 1 AC7 8 TYR B 43 ASN B 203 SER B 204 GLY B 221
SITE 2 AC7 8 ILE B 222 TYR B 354 HOH B 402 HOH B 409
CRYST1 47.735 118.310 129.008 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 0.020949 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008452 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007751 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
