HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 11-JUL-05 2A9F
TITLE CRYSTAL STRUCTURE OF A PUTATIVE MALIC ENZYME ((S)-MALATE:NAD+
TITLE 2 OXIDOREDUCTASE (DECARBOXYLATING))
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE MALIC ENZYME ((S)-MALATE:NAD+ OXIDOREDUCTASE
COMPND 3 (DECARBOXYLATING));
COMPND 4 CHAIN: A, B;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PYOGENES;
SOURCE 3 ORGANISM_TAXID: 1314;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYPOTHETICAL PROTEIN, PUTATIVE MALIC ENZYME ((S)-MALATE:NAD+
KEYWDS 2 OXIDOREDUCTASE (DECARBOXYLATING)), STRUCTURAL GENOMICS, PSI, PROTEIN
KEYWDS 3 STRUCTURE INITIATIVE, NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL
KEYWDS 4 GENOMICS, NYSGXRC, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SEETHARAMAN,S.SWAMINATHAN,S.K.BURLEY,NEW YORK SGX RESEARCH CENTER
AUTHOR 2 FOR STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 5 14-FEB-24 2A9F 1 REMARK
REVDAT 4 03-FEB-21 2A9F 1 AUTHOR REMARK SEQADV LINK
REVDAT 3 05-OCT-16 2A9F 1 REMARK VERSN
REVDAT 2 24-FEB-09 2A9F 1 VERSN
REVDAT 1 02-AUG-05 2A9F 0
JRNL AUTH J.SEETHARAMAN,S.SWAMINATHAN
JRNL TITL CRYSTAL STRUCTURE OF A PUTATIVE MALIC ENZYME
JRNL TITL 2 ((S)-MALATE:NAD+ OXIDOREDUCTASE (DECARBOXYLATING))
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.79
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 206885.570
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.2
REMARK 3 NUMBER OF REFLECTIONS : 26434
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 SET) : 0.260
REMARK 3 FREE R VALUE : 0.304
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1016
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3604
REMARK 3 BIN R VALUE (WORKING SET) : 0.4090
REMARK 3 BIN FREE R VALUE : 0.4660
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 128
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.045
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5563
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 49
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.86000
REMARK 3 B22 (A**2) : -1.20000
REMARK 3 B33 (A**2) : -9.66000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.45
REMARK 3 ESD FROM SIGMAA (A) : 0.47
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.53
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.58
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.180
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.320 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.180 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.770 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.330 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.27
REMARK 3 BSOL : 29.49
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : &_1_TOPOLOGY_INFILE_1
REMARK 3 TOPOLOGY FILE 2 : &_1_TOPOLOGY_INFILE_2
REMARK 3 TOPOLOGY FILE 3 : &_1_TOPOLOGY_INFILE_3
REMARK 3 TOPOLOGY FILE 4 : &_1_TOPOLOGY_INFILE_4
REMARK 3 TOPOLOGY FILE 5 : &_1_TOPOLOGY_INFILE_5
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2A9F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1000033651.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-DEC-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9790, 0.97939, 0.95
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CBASS
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28042
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 12.30
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.10
REMARK 200 R MERGE FOR SHELL (I) : 0.51300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE, SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NACL, BISTRIS, PEG3350, PH 5.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 34.12900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.79700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.62650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.79700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.12900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.62650
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: 8140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -82.0 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 MET A 1
REMARK 465 SER A 2
REMARK 465 HIS A 235
REMARK 465 HIS A 236
REMARK 465 LEU A 237
REMARK 465 LYS A 389
REMARK 465 SER A 390
REMARK 465 GLU A 391
REMARK 465 GLY A 392
REMARK 465 HIS A 393
REMARK 465 HIS A 394
REMARK 465 HIS A 395
REMARK 465 HIS A 396
REMARK 465 HIS A 397
REMARK 465 HIS A 398
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 HIS B 235
REMARK 465 HIS B 236
REMARK 465 LEU B 237
REMARK 465 VAL B 386
REMARK 465 VAL B 387
REMARK 465 LEU B 388
REMARK 465 LYS B 389
REMARK 465 SER B 390
REMARK 465 GLU B 391
REMARK 465 GLY B 392
REMARK 465 HIS B 393
REMARK 465 HIS B 394
REMARK 465 HIS B 395
REMARK 465 HIS B 396
REMARK 465 HIS B 397
REMARK 465 HIS B 398
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 LEU A 3 CG CD1 CD2
REMARK 470 LYS A 4 CG CD CE NZ
REMARK 470 GLN A 231 CG CD OE1 NE2
REMARK 470 LEU A 232 CG CD1 CD2
REMARK 470 PRO A 234 CG CD
REMARK 470 THR A 251 OG1 CG2
REMARK 470 ASP A 260 CG OD1 OD2
REMARK 470 PHE A 371 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 372 CG CD CE NZ
REMARK 470 ARG A 384 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 386 CG1 CG2
REMARK 470 LEU B 3 CG CD1 CD2
REMARK 470 LYS B 4 CG CD CE NZ
REMARK 470 LYS B 31 CG CD CE NZ
REMARK 470 GLN B 231 CG CD OE1 NE2
REMARK 470 PRO B 234 CG CD
REMARK 470 ASP B 260 CG OD1 OD2
REMARK 470 LYS B 278 CG CD CE NZ
REMARK 470 ARG B 282 CG CD NE CZ NH1 NH2
REMARK 470 PHE B 371 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 372 CG CD CE NZ
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 PRO B 129 C - N - CD ANGL. DEV. = -14.6 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 LYS A 4 65.61 163.23
REMARK 500 GLN A 6 -66.44 -139.89
REMARK 500 LEU A 7 -47.87 163.66
REMARK 500 GLN A 9 33.84 -64.97
REMARK 500 ILE A 30 24.06 -151.57
REMARK 500 TYR A 40 -151.85 -140.43
REMARK 500 THR A 41 -77.89 9.44
REMARK 500 PRO A 42 -75.89 -71.36
REMARK 500 LEU A 78 -123.14 44.24
REMARK 500 LEU A 80 -134.53 -93.29
REMARK 500 ASP A 82 94.48 -63.88
REMARK 500 ASP A 163 4.95 -61.46
REMARK 500 GLN A 164 -72.99 -123.24
REMARK 500 LEU A 181 24.04 -79.54
REMARK 500 LYS A 183 33.19 76.15
REMARK 500 ALA A 212 123.98 -21.82
REMARK 500 ASP A 219 -159.64 -116.53
REMARK 500 ALA A 229 58.53 -60.20
REMARK 500 LEU A 232 168.83 -41.62
REMARK 500 ALA A 233 27.60 -72.38
REMARK 500 LYS A 248 63.02 61.12
REMARK 500 THR A 251 -138.17 -139.31
REMARK 500 PHE A 262 152.60 166.33
REMARK 500 SER A 266 -0.22 -153.35
REMARK 500 ALA A 273 -56.77 -28.95
REMARK 500 ALA A 280 -171.33 -59.07
REMARK 500 ASN A 290 176.39 -47.60
REMARK 500 PRO A 291 -87.63 20.13
REMARK 500 ILE A 295 122.06 179.28
REMARK 500 ASN A 317 66.85 67.46
REMARK 500 LEU A 323 1.65 -68.41
REMARK 500 ALA A 324 -52.52 -123.18
REMARK 500 THR A 339 155.36 175.95
REMARK 500 PRO A 357 -71.62 -66.23
REMARK 500 ALA A 360 126.23 149.26
REMARK 500 LEU A 361 8.33 49.86
REMARK 500 ILE A 366 -155.84 -81.92
REMARK 500 ILE A 367 71.85 -109.53
REMARK 500 PRO A 368 -157.87 -78.94
REMARK 500 PHE A 371 -6.95 -21.50
REMARK 500 LYS A 381 -26.61 84.32
REMARK 500 ARG A 384 58.87 -62.69
REMARK 500 SER A 385 57.80 -157.28
REMARK 500 VAL A 387 0.41 -59.93
REMARK 500 ALA B 11 28.24 -60.71
REMARK 500 LEU B 12 -85.04 -121.53
REMARK 500 GLU B 13 52.93 22.12
REMARK 500 ILE B 30 -108.03 -130.12
REMARK 500 LYS B 31 -6.31 28.28
REMARK 500 TYR B 40 -153.30 -134.72
REMARK 500
REMARK 500 THIS ENTRY HAS 80 RAMACHANDRAN OUTLIERS.
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 MG A 801 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 137 OE2
REMARK 620 2 ASP A 138 OD1 98.2
REMARK 620 3 ASP A 163 OD1 97.8 99.8
REMARK 620 4 ASP A 163 OD2 68.0 64.8 51.3
REMARK 620 5 HOH A 818 O 164.7 88.9 67.6 103.6
REMARK 620 6 HOH A 819 O 96.0 80.3 166.1 137.7 98.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 800 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 137 OE2
REMARK 620 2 ASP B 138 OD1 82.6
REMARK 620 3 ASP B 163 OD2 68.1 66.6
REMARK 620 4 ASP B 163 OD1 88.2 114.3 50.0
REMARK 620 5 HOH B 807 O 170.2 107.1 116.5 88.9
REMARK 620 6 HOH B 818 O 78.9 157.5 117.0 77.9 91.3
REMARK 620 7 HOH B 819 O 83.0 70.9 130.7 169.1 98.8 94.1
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 801
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-T1727 RELATED DB: TARGETDB
DBREF 2A9F A 4 390 UNP Q99ZS1 Q99ZS1_STRP1 2 388
DBREF 2A9F B 4 390 UNP Q99ZS1 Q99ZS1_STRP1 2 388
SEQADV 2A9F MET A 1 UNP Q99ZS1 CLONING ARTIFACT
SEQADV 2A9F SER A 2 UNP Q99ZS1 CLONING ARTIFACT
SEQADV 2A9F LEU A 3 UNP Q99ZS1 CLONING ARTIFACT
SEQADV 2A9F GLU A 391 UNP Q99ZS1 CLONING ARTIFACT
SEQADV 2A9F GLY A 392 UNP Q99ZS1 CLONING ARTIFACT
SEQADV 2A9F HIS A 393 UNP Q99ZS1 EXPRESSION TAG
SEQADV 2A9F HIS A 394 UNP Q99ZS1 EXPRESSION TAG
SEQADV 2A9F HIS A 395 UNP Q99ZS1 EXPRESSION TAG
SEQADV 2A9F HIS A 396 UNP Q99ZS1 EXPRESSION TAG
SEQADV 2A9F HIS A 397 UNP Q99ZS1 EXPRESSION TAG
SEQADV 2A9F HIS A 398 UNP Q99ZS1 EXPRESSION TAG
SEQADV 2A9F MET B 1 UNP Q99ZS1 CLONING ARTIFACT
SEQADV 2A9F SER B 2 UNP Q99ZS1 CLONING ARTIFACT
SEQADV 2A9F LEU B 3 UNP Q99ZS1 CLONING ARTIFACT
SEQADV 2A9F GLU B 391 UNP Q99ZS1 CLONING ARTIFACT
SEQADV 2A9F GLY B 392 UNP Q99ZS1 CLONING ARTIFACT
SEQADV 2A9F HIS B 393 UNP Q99ZS1 EXPRESSION TAG
SEQADV 2A9F HIS B 394 UNP Q99ZS1 EXPRESSION TAG
SEQADV 2A9F HIS B 395 UNP Q99ZS1 EXPRESSION TAG
SEQADV 2A9F HIS B 396 UNP Q99ZS1 EXPRESSION TAG
SEQADV 2A9F HIS B 397 UNP Q99ZS1 EXPRESSION TAG
SEQADV 2A9F HIS B 398 UNP Q99ZS1 EXPRESSION TAG
SEQRES 1 A 398 MET SER LEU LYS ASN GLN LEU GLY GLN LEU ALA LEU GLU
SEQRES 2 A 398 GLN ALA LYS THR PHE GLY GLY LYS LEU GLU VAL GLN PRO
SEQRES 3 A 398 LYS VAL ASP ILE LYS THR LYS HIS ASP LEU SER ILE ALA
SEQRES 4 A 398 TYR THR PRO GLY VAL ALA SER VAL SER SER ALA ILE ALA
SEQRES 5 A 398 LYS ASP LYS THR LEU ALA TYR ASP LEU THR THR LYS LYS
SEQRES 6 A 398 ASN THR VAL ALA VAL ILE SER ASP GLY THR ALA VAL LEU
SEQRES 7 A 398 GLY LEU GLY ASP ILE GLY PRO GLU ALA ALA MET PRO VAL
SEQRES 8 A 398 MET GLU GLY LYS ALA ALA LEU PHE LYS ALA PHE ALA GLY
SEQRES 9 A 398 VAL ASP ALA ILE PRO ILE VAL LEU ASP THR LYS ASP THR
SEQRES 10 A 398 GLU GLU ILE ILE SER ILE VAL LYS ALA LEU ALA PRO THR
SEQRES 11 A 398 PHE GLY GLY ILE ASN LEU GLU ASP ILE SER ALA PRO ARG
SEQRES 12 A 398 CYS PHE GLU ILE GLU GLN ARG LEU ILE LYS GLU CYS HIS
SEQRES 13 A 398 ILE PRO VAL PHE HIS ASP ASP GLN HIS GLY THR ALA ILE
SEQRES 14 A 398 VAL VAL LEU ALA ALA ILE PHE ASN SER LEU LYS LEU LEU
SEQRES 15 A 398 LYS LYS SER LEU ASP GLU VAL SER ILE VAL VAL ASN GLY
SEQRES 16 A 398 GLY GLY SER ALA GLY LEU SER ILE THR ARG LYS LEU LEU
SEQRES 17 A 398 ALA ALA GLY ALA THR LYS VAL THR VAL VAL ASP LYS PHE
SEQRES 18 A 398 GLY ILE ILE ASN GLU GLN GLU ALA ALA GLN LEU ALA PRO
SEQRES 19 A 398 HIS HIS LEU ASP ILE ALA LYS VAL THR ASN ARG GLU PHE
SEQRES 20 A 398 LYS SER GLY THR LEU GLU ASP ALA LEU GLU GLY ALA ASP
SEQRES 21 A 398 ILE PHE ILE GLY VAL SER ALA PRO GLY VAL LEU LYS ALA
SEQRES 22 A 398 GLU TRP ILE SER LYS MET ALA ALA ARG PRO VAL ILE PHE
SEQRES 23 A 398 ALA MET ALA ASN PRO ILE PRO GLU ILE TYR PRO ASP GLU
SEQRES 24 A 398 ALA LEU GLU ALA GLY ALA TYR ILE VAL GLY THR GLY ARG
SEQRES 25 A 398 SER ASP PHE PRO ASN GLN ILE ASN ASN VAL LEU ALA PHE
SEQRES 26 A 398 PRO GLY ILE PHE ARG GLY ALA LEU ASP ALA ARG ALA LYS
SEQRES 27 A 398 THR ILE THR VAL GLU MET GLN ILE ALA ALA ALA LYS GLY
SEQRES 28 A 398 ILE ALA SER LEU VAL PRO ASP ASP ALA LEU SER THR THR
SEQRES 29 A 398 ASN ILE ILE PRO ASP ALA PHE LYS GLU GLY VAL ALA GLU
SEQRES 30 A 398 ILE VAL ALA LYS SER VAL ARG SER VAL VAL LEU LYS SER
SEQRES 31 A 398 GLU GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 B 398 MET SER LEU LYS ASN GLN LEU GLY GLN LEU ALA LEU GLU
SEQRES 2 B 398 GLN ALA LYS THR PHE GLY GLY LYS LEU GLU VAL GLN PRO
SEQRES 3 B 398 LYS VAL ASP ILE LYS THR LYS HIS ASP LEU SER ILE ALA
SEQRES 4 B 398 TYR THR PRO GLY VAL ALA SER VAL SER SER ALA ILE ALA
SEQRES 5 B 398 LYS ASP LYS THR LEU ALA TYR ASP LEU THR THR LYS LYS
SEQRES 6 B 398 ASN THR VAL ALA VAL ILE SER ASP GLY THR ALA VAL LEU
SEQRES 7 B 398 GLY LEU GLY ASP ILE GLY PRO GLU ALA ALA MET PRO VAL
SEQRES 8 B 398 MET GLU GLY LYS ALA ALA LEU PHE LYS ALA PHE ALA GLY
SEQRES 9 B 398 VAL ASP ALA ILE PRO ILE VAL LEU ASP THR LYS ASP THR
SEQRES 10 B 398 GLU GLU ILE ILE SER ILE VAL LYS ALA LEU ALA PRO THR
SEQRES 11 B 398 PHE GLY GLY ILE ASN LEU GLU ASP ILE SER ALA PRO ARG
SEQRES 12 B 398 CYS PHE GLU ILE GLU GLN ARG LEU ILE LYS GLU CYS HIS
SEQRES 13 B 398 ILE PRO VAL PHE HIS ASP ASP GLN HIS GLY THR ALA ILE
SEQRES 14 B 398 VAL VAL LEU ALA ALA ILE PHE ASN SER LEU LYS LEU LEU
SEQRES 15 B 398 LYS LYS SER LEU ASP GLU VAL SER ILE VAL VAL ASN GLY
SEQRES 16 B 398 GLY GLY SER ALA GLY LEU SER ILE THR ARG LYS LEU LEU
SEQRES 17 B 398 ALA ALA GLY ALA THR LYS VAL THR VAL VAL ASP LYS PHE
SEQRES 18 B 398 GLY ILE ILE ASN GLU GLN GLU ALA ALA GLN LEU ALA PRO
SEQRES 19 B 398 HIS HIS LEU ASP ILE ALA LYS VAL THR ASN ARG GLU PHE
SEQRES 20 B 398 LYS SER GLY THR LEU GLU ASP ALA LEU GLU GLY ALA ASP
SEQRES 21 B 398 ILE PHE ILE GLY VAL SER ALA PRO GLY VAL LEU LYS ALA
SEQRES 22 B 398 GLU TRP ILE SER LYS MET ALA ALA ARG PRO VAL ILE PHE
SEQRES 23 B 398 ALA MET ALA ASN PRO ILE PRO GLU ILE TYR PRO ASP GLU
SEQRES 24 B 398 ALA LEU GLU ALA GLY ALA TYR ILE VAL GLY THR GLY ARG
SEQRES 25 B 398 SER ASP PHE PRO ASN GLN ILE ASN ASN VAL LEU ALA PHE
SEQRES 26 B 398 PRO GLY ILE PHE ARG GLY ALA LEU ASP ALA ARG ALA LYS
SEQRES 27 B 398 THR ILE THR VAL GLU MET GLN ILE ALA ALA ALA LYS GLY
SEQRES 28 B 398 ILE ALA SER LEU VAL PRO ASP ASP ALA LEU SER THR THR
SEQRES 29 B 398 ASN ILE ILE PRO ASP ALA PHE LYS GLU GLY VAL ALA GLU
SEQRES 30 B 398 ILE VAL ALA LYS SER VAL ARG SER VAL VAL LEU LYS SER
SEQRES 31 B 398 GLU GLY HIS HIS HIS HIS HIS HIS
HET MG A 801 1
HET MG B 800 1
HETNAM MG MAGNESIUM ION
FORMUL 3 MG 2(MG 2+)
FORMUL 5 HOH *49(H2 O)
HELIX 1 1 LEU A 12 GLY A 19 1 8
HELIX 2 2 THR A 32 TYR A 40 1 9
HELIX 3 3 VAL A 44 ASP A 54 1 11
HELIX 4 4 LEU A 57 THR A 62 1 6
HELIX 5 5 THR A 63 LYS A 65 5 3
HELIX 6 6 GLY A 84 ALA A 103 1 20
HELIX 7 7 ASP A 116 ALA A 128 1 13
HELIX 8 8 PRO A 129 PHE A 131 5 3
HELIX 9 9 PRO A 142 CYS A 155 1 14
HELIX 10 10 ASP A 162 LEU A 181 1 20
HELIX 11 11 GLY A 197 GLY A 211 1 15
HELIX 12 12 ASP A 238 ASN A 244 1 7
HELIX 13 13 GLU A 253 GLY A 258 1 6
HELIX 14 14 LYS A 272 LYS A 278 1 7
HELIX 15 15 TYR A 296 GLU A 302 1 7
HELIX 16 16 ASN A 320 LEU A 323 5 4
HELIX 17 17 ALA A 324 ARG A 336 1 13
HELIX 18 18 THR A 341 LEU A 355 1 15
HELIX 19 19 LYS A 372 ALA A 380 1 9
HELIX 20 20 GLU B 13 GLY B 19 1 7
HELIX 21 21 THR B 32 TYR B 40 1 9
HELIX 22 22 GLY B 43 ASP B 54 1 12
HELIX 23 23 LEU B 57 THR B 62 1 6
HELIX 24 24 THR B 63 LYS B 65 5 3
HELIX 25 25 GLY B 84 ALA B 103 1 20
HELIX 26 26 ASP B 116 ALA B 128 1 13
HELIX 27 27 PRO B 129 PHE B 131 5 3
HELIX 28 28 PRO B 142 LYS B 153 1 12
HELIX 29 29 ASP B 162 LYS B 183 1 22
HELIX 30 30 GLY B 197 GLY B 211 1 15
HELIX 31 31 ILE B 239 ASN B 244 5 6
HELIX 32 32 TRP B 275 MET B 279 5 5
HELIX 33 33 TYR B 296 ALA B 303 1 8
HELIX 34 34 ASN B 320 LEU B 323 5 4
HELIX 35 35 ALA B 324 ALA B 335 1 12
HELIX 36 36 THR B 341 LEU B 355 1 15
HELIX 37 37 ALA B 370 ALA B 380 1 11
SHEET 1 A 2 LEU A 22 PRO A 26 0
SHEET 2 A 2 LEU B 22 PRO B 26 -1 O GLN B 25 N GLU A 23
SHEET 1 B 4 ASP A 106 VAL A 111 0
SHEET 2 B 4 THR A 67 SER A 72 1 N VAL A 68 O ASP A 106
SHEET 3 B 4 GLY A 133 LEU A 136 1 O ASN A 135 N ALA A 69
SHEET 4 B 4 VAL A 159 HIS A 161 1 O PHE A 160 N ILE A 134
SHEET 1 C 6 GLY A 222 ILE A 223 0
SHEET 2 C 6 LYS A 214 ASP A 219 -1 N ASP A 219 O GLY A 222
SHEET 3 C 6 SER A 190 ASN A 194 1 N VAL A 193 O VAL A 218
SHEET 4 C 6 PHE A 262 GLY A 264 1 O GLY A 264 N ASN A 194
SHEET 5 C 6 VAL A 284 ALA A 287 1 O PHE A 286 N ILE A 263
SHEET 6 C 6 ILE A 307 THR A 310 1 O GLY A 309 N ILE A 285
SHEET 1 D 4 ASP B 106 VAL B 111 0
SHEET 2 D 4 THR B 67 SER B 72 1 N VAL B 68 O ASP B 106
SHEET 3 D 4 GLY B 133 LEU B 136 1 O ASN B 135 N ALA B 69
SHEET 4 D 4 VAL B 159 HIS B 161 1 O PHE B 160 N LEU B 136
SHEET 1 E 6 GLY B 222 ILE B 223 0
SHEET 2 E 6 VAL B 215 ASP B 219 -1 N ASP B 219 O GLY B 222
SHEET 3 E 6 ILE B 191 ASN B 194 1 N VAL B 193 O THR B 216
SHEET 4 E 6 PHE B 262 VAL B 265 1 O PHE B 262 N VAL B 192
SHEET 5 E 6 VAL B 284 ALA B 287 1 O PHE B 286 N ILE B 263
SHEET 6 E 6 ILE B 307 THR B 310 1 O ILE B 307 N ILE B 285
LINK OE2 GLU A 137 MG MG A 801 1555 1555 1.96
LINK OD1 ASP A 138 MG MG A 801 1555 1555 2.02
LINK OD1 ASP A 163 MG MG A 801 1555 1555 2.02
LINK OD2 ASP A 163 MG MG A 801 1555 1555 2.79
LINK MG MG A 801 O HOH A 818 1555 1555 2.17
LINK MG MG A 801 O HOH A 819 1555 1555 1.99
LINK OE2 GLU B 137 MG MG B 800 1555 1555 1.97
LINK OD1 ASP B 138 MG MG B 800 1555 1555 2.09
LINK OD2 ASP B 163 MG MG B 800 1555 1555 2.75
LINK OD1 ASP B 163 MG MG B 800 1555 1555 2.33
LINK MG MG B 800 O HOH B 807 1555 1555 2.67
LINK MG MG B 800 O HOH B 818 1555 1555 2.04
LINK MG MG B 800 O HOH B 819 1555 1555 2.02
CISPEP 1 ALA A 141 PRO A 142 0 0.16
CISPEP 2 THR B 41 PRO B 42 0 0.31
CISPEP 3 ALA B 141 PRO B 142 0 0.14
CISPEP 4 ASN B 290 PRO B 291 0 0.30
SITE 1 AC1 6 GLU B 137 ASP B 138 ASP B 163 HOH B 807
SITE 2 AC1 6 HOH B 818 HOH B 819
SITE 1 AC2 5 GLU A 137 ASP A 138 ASP A 163 HOH A 818
SITE 2 AC2 5 HOH A 819
CRYST1 68.258 79.253 145.594 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 0.014650 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012618 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006868 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
