HEADER TRANSFERASE 11-JUL-00 1FA0
TITLE STRUCTURE OF YEAST POLY(A) POLYMERASE BOUND TO MANGANATE AND 3'-DATP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(A)-POLYMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 1-530;
COMPND 5 EC: 2.7.7.19;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PJDELTA10PAP
KEYWDS POLYMERASE, NUCLEOTIDYL TRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.BARD,A.M.ZHELKOVSKY,S.HELMLING,C.L.MOORE,A.BOHM
REVDAT 4 07-FEB-24 1FA0 1 REMARK LINK
REVDAT 3 24-FEB-09 1FA0 1 VERSN
REVDAT 2 01-APR-03 1FA0 1 JRNL
REVDAT 1 30-AUG-00 1FA0 0
JRNL AUTH J.BARD,A.M.ZHELKOVSKY,S.HELMLING,T.N.EARNEST,C.L.MOORE,
JRNL AUTH 2 A.BOHM
JRNL TITL STRUCTURE OF YEAST POLY(A) POLYMERASE ALONE AND IN COMPLEX
JRNL TITL 2 WITH 3'-DATP.
JRNL REF SCIENCE V. 289 1346 2000
JRNL REFN ISSN 0036-8075
JRNL PMID 10958780
JRNL DOI 10.1126/SCIENCE.289.5483.1346
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1052123.240
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.0
REMARK 3 NUMBER OF REFLECTIONS : 50383
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) : 0.233
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.500
REMARK 3 FREE R VALUE TEST SET COUNT : 5098
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.69
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 52.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3075
REMARK 3 BIN R VALUE (WORKING SET) : 0.3112
REMARK 3 BIN FREE R VALUE : 0.3443
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 300
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8059
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 109
REMARK 3 SOLVENT ATOMS : 82
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 44.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -20.26000
REMARK 3 B22 (A**2) : 10.19000
REMARK 3 B33 (A**2) : 10.06000
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) : 0.69
REMARK 3 ESD FROM SIGMAA (A) : -0.1
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) : 0.73
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.500
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) : 0.940 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.670 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.300 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.170 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 40.70
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.PA
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARA
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : CORD_POP.PAR
REMARK 3 PARAMETER FILE 5 : DNA-RNA_REP_C2ENDORNA.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : CORD_POP.TOP
REMARK 3 TOPOLOGY FILE 5 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FA0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-00.
REMARK 100 THE DEPOSITION ID IS D_1000011427.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-FEB-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.24
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : OTHER
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58367
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 4.140
REMARK 200 R MERGE (I) : 0.04400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 32.3600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.30700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG,ETHYLENE GLYCOL, PH 7.24, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, 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 36.90000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 119.25000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.55000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 119.25000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.90000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.55000
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 MET A 1
REMARK 465 SER A 2
REMARK 465 TYR A 428
REMARK 465 GLY A 429
REMARK 465 SER A 430
REMARK 465 HIS A 431
REMARK 465 LYS A 432
REMARK 465 THR A 433
REMARK 465 GLU A 434
REMARK 465 THR A 435
REMARK 465 ALA A 436
REMARK 465 LEU A 437
REMARK 465 ASN A 438
REMARK 465 ALA A 439
REMARK 465 GLU A 524
REMARK 465 ASN A 525
REMARK 465 GLU A 526
REMARK 465 LYS A 527
REMARK 465 ARG A 528
REMARK 465 PRO A 529
REMARK 465 SER A 530
REMARK 465 LYS A 531
REMARK 465 LYS A 532
REMARK 465 SER A 533
REMARK 465 LYS A 534
REMARK 465 ARG A 535
REMARK 465 LYS A 536
REMARK 465 ASN A 537
REMARK 465 MET B 1
REMARK 465 ASP B 445
REMARK 465 GLU B 446
REMARK 465 ASN B 447
REMARK 465 LYS B 448
REMARK 465 GLU B 449
REMARK 465 GLU B 450
REMARK 465 GLU B 451
REMARK 465 SER B 452
REMARK 465 ILE B 453
REMARK 465 LYS B 454
REMARK 465 ASP B 455
REMARK 465 ALA B 456
REMARK 465 GLU B 473
REMARK 465 ASN B 474
REMARK 465 LYS B 475
REMARK 465 LYS B 476
REMARK 465 GLU B 477
REMARK 465 LYS B 478
REMARK 465 LYS B 531
REMARK 465 LYS B 532
REMARK 465 SER B 533
REMARK 465 LYS B 534
REMARK 465 ARG B 535
REMARK 465 LYS B 536
REMARK 465 ASN B 537
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 LYS A 24 CG CD CE NZ
REMARK 470 LYS A 34 CG CD CE NZ
REMARK 470 GLU A 114 CG CD OE1 OE2
REMARK 470 SER A 122 OG
REMARK 470 GLN A 283 CG CD OE1 NE2
REMARK 470 GLN A 294 CG CD OE1 NE2
REMARK 470 ARG A 369 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 373 CG CD OE1 OE2
REMARK 470 LYS A 377 CG CD CE NZ
REMARK 470 THR A 417 OG1 CG2
REMARK 470 ASP A 419 CG OD1 OD2
REMARK 470 LYS A 427 CG CD CE NZ
REMARK 470 LEU A 440 CG CD1 CD2
REMARK 470 LYS A 441 CG CD CE NZ
REMARK 470 LEU A 442 CG CD1 CD2
REMARK 470 LYS A 448 CG CD CE NZ
REMARK 470 GLU A 449 CG CD OE1 OE2
REMARK 470 ASP A 455 CG OD1 OD2
REMARK 470 ILE A 472 CG1 CG2 CD1
REMARK 470 SER A 494 OG
REMARK 470 ASP A 498 CG OD1 OD2
REMARK 470 LYS A 503 CG CD CE NZ
REMARK 470 ARG B 61 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 69 CG CD CE NZ
REMARK 470 ARG B 369 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 373 CG CD OE1 OE2
REMARK 470 LYS B 377 CG CD CE NZ
REMARK 470 LYS B 385 CG CD CE NZ
REMARK 470 LYS B 407 CG CD CE NZ
REMARK 470 THR B 417 OG1 CG2
REMARK 470 ASP B 419 CG OD1 OD2
REMARK 470 LYS B 432 CG CD CE NZ
REMARK 470 LYS B 441 CG CD CE NZ
REMARK 470 LYS B 458 CG CD CE NZ
REMARK 470 ILE B 472 CG1 CG2 CD1
REMARK 470 VAL B 479 CG1 CG2
REMARK 470 ASP B 480 CG OD1 OD2
REMARK 470 ILE B 483 CG1 CG2 CD1
REMARK 470 ASN B 490 CG OD1 ND2
REMARK 470 SER B 494 OG
REMARK 470 LYS B 503 CG CD CE NZ
REMARK 470 GLU B 524 CG CD OE1 OE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 296 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 351 CG CD CE NZ
REMARK 480 LYS A 392 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 A 137 C - N - CA ANGL. DEV. = 10.2 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 GLN A 4 -35.39 146.17
REMARK 500 THR A 118 -86.41 -89.19
REMARK 500 GLU A 126 30.03 -68.76
REMARK 500 GLU A 132 153.66 178.00
REMARK 500 SER A 149 28.15 45.07
REMARK 500 ASN A 179 9.13 54.00
REMARK 500 ALA A 225 100.28 -163.23
REMARK 500 PRO A 269 33.18 -88.14
REMARK 500 PRO A 281 -88.70 -54.22
REMARK 500 LEU A 282 141.05 -17.15
REMARK 500 ASN A 288 97.95 -161.16
REMARK 500 ALA A 397 -107.15 1.01
REMARK 500 SER A 411 140.10 -170.07
REMARK 500 GLU A 422 47.89 -68.84
REMARK 500 MET A 423 -43.72 -156.46
REMARK 500 LEU A 442 109.08 -52.92
REMARK 500 ASN A 447 60.25 -101.48
REMARK 500 GLU A 451 -63.24 -23.07
REMARK 500 LYS A 454 -19.56 -45.12
REMARK 500 ALA A 456 137.22 -33.56
REMARK 500 ILE A 472 49.72 -81.23
REMARK 500 GLU A 473 -83.66 -72.00
REMARK 500 ASN A 474 40.98 171.41
REMARK 500 PHE A 495 -33.12 -151.80
REMARK 500 ASP A 501 -77.06 -104.02
REMARK 500 HIS A 502 -21.95 108.69
REMARK 500 SER B 3 164.72 179.81
REMARK 500 ILE B 9 6.42 -66.41
REMARK 500 ASN B 71 41.42 72.54
REMARK 500 THR B 118 -63.24 -124.41
REMARK 500 GLU B 129 -8.82 -55.91
REMARK 500 PRO B 142 146.00 -38.40
REMARK 500 ASN B 179 11.34 55.50
REMARK 500 GLU B 182 -61.43 -29.11
REMARK 500 ALA B 225 115.16 170.33
REMARK 500 SER B 252 -56.23 131.83
REMARK 500 PRO B 269 33.80 -88.83
REMARK 500 ASN B 288 98.80 -166.69
REMARK 500 LYS B 385 -6.81 -55.71
REMARK 500 ALA B 397 -128.76 27.45
REMARK 500 ILE B 401 149.95 -177.45
REMARK 500 PRO B 416 -73.73 -48.07
REMARK 500 VAL B 443 99.79 -55.33
REMARK 500 SER B 494 -141.32 -65.77
REMARK 500 PHE B 495 -118.50 55.65
REMARK 500 TYR B 499 20.12 -67.43
REMARK 500 HIS B 502 -23.72 67.32
REMARK 500 VAL B 504 -44.52 -137.33
REMARK 500 ASN B 525 49.53 -87.72
REMARK 500 GLU B 526 -161.17 -65.33
REMARK 500
REMARK 500 THIS ENTRY HAS 52 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 MN A 600 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 100 OD2
REMARK 620 2 ASP A 102 OD1 97.9
REMARK 620 3 3AT A 604 O3G 90.1 146.7
REMARK 620 4 3AT A 604 O2B 156.5 83.9 76.6
REMARK 620 5 3AT A 604 O1A 113.5 98.6 107.7 89.2
REMARK 620 6 HOH A 871 O 81.0 82.6 66.8 76.0 164.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 601 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 100 OD1
REMARK 620 2 ASP A 102 OD2 105.8
REMARK 620 3 ASP A 154 OD1 83.4 94.7
REMARK 620 4 3AT A 604 O1A 100.3 85.6 176.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 602 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 100 OD2
REMARK 620 2 ASP B 102 OD1 105.0
REMARK 620 3 3AT B 605 O1B 164.8 86.2
REMARK 620 4 3AT B 605 O1A 93.7 82.1 98.0
REMARK 620 5 3AT B 605 O1G 89.8 158.2 76.8 113.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 603 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 100 OD1
REMARK 620 2 ASP B 102 OD2 91.3
REMARK 620 3 ASP B 154 OD2 68.0 91.6
REMARK 620 4 3AT B 605 O1A 88.6 80.1 155.1
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 MN A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3AT A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3AT B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3AD A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3AD B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE POP A 817
DBREF 1FA0 A 1 537 UNP P29468 PAP_YEAST 1 537
DBREF 1FA0 B 1 537 UNP P29468 PAP_YEAST 1 537
SEQRES 1 A 537 MET SER SER GLN LYS VAL PHE GLY ILE THR GLY PRO VAL
SEQRES 2 A 537 SER THR VAL GLY ALA THR ALA ALA GLU ASN LYS LEU ASN
SEQRES 3 A 537 ASP SER LEU ILE GLN GLU LEU LYS LYS GLU GLY SER PHE
SEQRES 4 A 537 GLU THR GLU GLN GLU THR ALA ASN ARG VAL GLN VAL LEU
SEQRES 5 A 537 LYS ILE LEU GLN GLU LEU ALA GLN ARG PHE VAL TYR GLU
SEQRES 6 A 537 VAL SER LYS LYS LYS ASN MET SER ASP GLY MET ALA ARG
SEQRES 7 A 537 ASP ALA GLY GLY LYS ILE PHE THR TYR GLY SER TYR ARG
SEQRES 8 A 537 LEU GLY VAL HIS GLY PRO GLY SER ASP ILE ASP THR LEU
SEQRES 9 A 537 VAL VAL VAL PRO LYS HIS VAL THR ARG GLU ASP PHE PHE
SEQRES 10 A 537 THR VAL PHE ASP SER LEU LEU ARG GLU ARG LYS GLU LEU
SEQRES 11 A 537 ASP GLU ILE ALA PRO VAL PRO ASP ALA PHE VAL PRO ILE
SEQRES 12 A 537 ILE LYS ILE LYS PHE SER GLY ILE SER ILE ASP LEU ILE
SEQRES 13 A 537 CYS ALA ARG LEU ASP GLN PRO GLN VAL PRO LEU SER LEU
SEQRES 14 A 537 THR LEU SER ASP LYS ASN LEU LEU ARG ASN LEU ASP GLU
SEQRES 15 A 537 LYS ASP LEU ARG ALA LEU ASN GLY THR ARG VAL THR ASP
SEQRES 16 A 537 GLU ILE LEU GLU LEU VAL PRO LYS PRO ASN VAL PHE ARG
SEQRES 17 A 537 ILE ALA LEU ARG ALA ILE LYS LEU TRP ALA GLN ARG ARG
SEQRES 18 A 537 ALA VAL TYR ALA ASN ILE PHE GLY PHE PRO GLY GLY VAL
SEQRES 19 A 537 ALA TRP ALA MET LEU VAL ALA ARG ILE CYS GLN LEU TYR
SEQRES 20 A 537 PRO ASN ALA CYS SER ALA VAL ILE LEU ASN ARG PHE PHE
SEQRES 21 A 537 ILE ILE LEU SER GLU TRP ASN TRP PRO GLN PRO VAL ILE
SEQRES 22 A 537 LEU LYS PRO ILE GLU ASP GLY PRO LEU GLN VAL ARG VAL
SEQRES 23 A 537 TRP ASN PRO LYS ILE TYR ALA GLN ASP ARG SER HIS ARG
SEQRES 24 A 537 MET PRO VAL ILE THR PRO ALA TYR PRO SER MET CYS ALA
SEQRES 25 A 537 THR HIS ASN ILE THR GLU SER THR LYS LYS VAL ILE LEU
SEQRES 26 A 537 GLN GLU PHE VAL ARG GLY VAL GLN ILE THR ASN ASP ILE
SEQRES 27 A 537 PHE SER ASN LYS LYS SER TRP ALA ASN LEU PHE GLU LYS
SEQRES 28 A 537 ASN ASP PHE PHE PHE ARG TYR LYS PHE TYR LEU GLU ILE
SEQRES 29 A 537 THR ALA TYR THR ARG GLY SER ASP GLU GLN HIS LEU LYS
SEQRES 30 A 537 TRP SER GLY LEU VAL GLU SER LYS VAL ARG LEU LEU VAL
SEQRES 31 A 537 MET LYS LEU GLU VAL LEU ALA GLY ILE LYS ILE ALA HIS
SEQRES 32 A 537 PRO PHE THR LYS PRO PHE GLU SER SER TYR CYS CYS PRO
SEQRES 33 A 537 THR GLU ASP ASP TYR GLU MET ILE GLN ASP LYS TYR GLY
SEQRES 34 A 537 SER HIS LYS THR GLU THR ALA LEU ASN ALA LEU LYS LEU
SEQRES 35 A 537 VAL THR ASP GLU ASN LYS GLU GLU GLU SER ILE LYS ASP
SEQRES 36 A 537 ALA PRO LYS ALA TYR LEU SER THR MET TYR ILE GLY LEU
SEQRES 37 A 537 ASP PHE ASN ILE GLU ASN LYS LYS GLU LYS VAL ASP ILE
SEQRES 38 A 537 HIS ILE PRO CYS THR GLU PHE VAL ASN LEU CYS ARG SER
SEQRES 39 A 537 PHE ASN GLU ASP TYR GLY ASP HIS LYS VAL PHE ASN LEU
SEQRES 40 A 537 ALA LEU ARG PHE VAL LYS GLY TYR ASP LEU PRO ASP GLU
SEQRES 41 A 537 VAL PHE ASP GLU ASN GLU LYS ARG PRO SER LYS LYS SER
SEQRES 42 A 537 LYS ARG LYS ASN
SEQRES 1 B 537 MET SER SER GLN LYS VAL PHE GLY ILE THR GLY PRO VAL
SEQRES 2 B 537 SER THR VAL GLY ALA THR ALA ALA GLU ASN LYS LEU ASN
SEQRES 3 B 537 ASP SER LEU ILE GLN GLU LEU LYS LYS GLU GLY SER PHE
SEQRES 4 B 537 GLU THR GLU GLN GLU THR ALA ASN ARG VAL GLN VAL LEU
SEQRES 5 B 537 LYS ILE LEU GLN GLU LEU ALA GLN ARG PHE VAL TYR GLU
SEQRES 6 B 537 VAL SER LYS LYS LYS ASN MET SER ASP GLY MET ALA ARG
SEQRES 7 B 537 ASP ALA GLY GLY LYS ILE PHE THR TYR GLY SER TYR ARG
SEQRES 8 B 537 LEU GLY VAL HIS GLY PRO GLY SER ASP ILE ASP THR LEU
SEQRES 9 B 537 VAL VAL VAL PRO LYS HIS VAL THR ARG GLU ASP PHE PHE
SEQRES 10 B 537 THR VAL PHE ASP SER LEU LEU ARG GLU ARG LYS GLU LEU
SEQRES 11 B 537 ASP GLU ILE ALA PRO VAL PRO ASP ALA PHE VAL PRO ILE
SEQRES 12 B 537 ILE LYS ILE LYS PHE SER GLY ILE SER ILE ASP LEU ILE
SEQRES 13 B 537 CYS ALA ARG LEU ASP GLN PRO GLN VAL PRO LEU SER LEU
SEQRES 14 B 537 THR LEU SER ASP LYS ASN LEU LEU ARG ASN LEU ASP GLU
SEQRES 15 B 537 LYS ASP LEU ARG ALA LEU ASN GLY THR ARG VAL THR ASP
SEQRES 16 B 537 GLU ILE LEU GLU LEU VAL PRO LYS PRO ASN VAL PHE ARG
SEQRES 17 B 537 ILE ALA LEU ARG ALA ILE LYS LEU TRP ALA GLN ARG ARG
SEQRES 18 B 537 ALA VAL TYR ALA ASN ILE PHE GLY PHE PRO GLY GLY VAL
SEQRES 19 B 537 ALA TRP ALA MET LEU VAL ALA ARG ILE CYS GLN LEU TYR
SEQRES 20 B 537 PRO ASN ALA CYS SER ALA VAL ILE LEU ASN ARG PHE PHE
SEQRES 21 B 537 ILE ILE LEU SER GLU TRP ASN TRP PRO GLN PRO VAL ILE
SEQRES 22 B 537 LEU LYS PRO ILE GLU ASP GLY PRO LEU GLN VAL ARG VAL
SEQRES 23 B 537 TRP ASN PRO LYS ILE TYR ALA GLN ASP ARG SER HIS ARG
SEQRES 24 B 537 MET PRO VAL ILE THR PRO ALA TYR PRO SER MET CYS ALA
SEQRES 25 B 537 THR HIS ASN ILE THR GLU SER THR LYS LYS VAL ILE LEU
SEQRES 26 B 537 GLN GLU PHE VAL ARG GLY VAL GLN ILE THR ASN ASP ILE
SEQRES 27 B 537 PHE SER ASN LYS LYS SER TRP ALA ASN LEU PHE GLU LYS
SEQRES 28 B 537 ASN ASP PHE PHE PHE ARG TYR LYS PHE TYR LEU GLU ILE
SEQRES 29 B 537 THR ALA TYR THR ARG GLY SER ASP GLU GLN HIS LEU LYS
SEQRES 30 B 537 TRP SER GLY LEU VAL GLU SER LYS VAL ARG LEU LEU VAL
SEQRES 31 B 537 MET LYS LEU GLU VAL LEU ALA GLY ILE LYS ILE ALA HIS
SEQRES 32 B 537 PRO PHE THR LYS PRO PHE GLU SER SER TYR CYS CYS PRO
SEQRES 33 B 537 THR GLU ASP ASP TYR GLU MET ILE GLN ASP LYS TYR GLY
SEQRES 34 B 537 SER HIS LYS THR GLU THR ALA LEU ASN ALA LEU LYS LEU
SEQRES 35 B 537 VAL THR ASP GLU ASN LYS GLU GLU GLU SER ILE LYS ASP
SEQRES 36 B 537 ALA PRO LYS ALA TYR LEU SER THR MET TYR ILE GLY LEU
SEQRES 37 B 537 ASP PHE ASN ILE GLU ASN LYS LYS GLU LYS VAL ASP ILE
SEQRES 38 B 537 HIS ILE PRO CYS THR GLU PHE VAL ASN LEU CYS ARG SER
SEQRES 39 B 537 PHE ASN GLU ASP TYR GLY ASP HIS LYS VAL PHE ASN LEU
SEQRES 40 B 537 ALA LEU ARG PHE VAL LYS GLY TYR ASP LEU PRO ASP GLU
SEQRES 41 B 537 VAL PHE ASP GLU ASN GLU LYS ARG PRO SER LYS LYS SER
SEQRES 42 B 537 LYS ARG LYS ASN
HET MN A 600 1
HET MN A 601 1
HET 3AT A 604 30
HET 3AD A 606 18
HET POP A 817 9
HET MN B 602 1
HET MN B 603 1
HET 3AT B 605 30
HET 3AD B 607 18
HETNAM MN MANGANESE (II) ION
HETNAM 3AT 3'-DEOXYADENOSINE-5'-TRIPHOSPHATE
HETNAM 3AD 3'-DEOXYADENOSINE
HETNAM POP PYROPHOSPHATE 2-
HETSYN 3AT CORDYCEPIN TRIPHOSPHATE
FORMUL 3 MN 4(MN 2+)
FORMUL 5 3AT 2(C10 H16 N5 O12 P3)
FORMUL 6 3AD 2(C10 H13 N5 O3)
FORMUL 7 POP H2 O7 P2 2-
FORMUL 12 HOH *82(H2 O)
HELIX 1 1 GLN A 4 GLY A 8 5 5
HELIX 2 2 THR A 19 GLU A 36 1 18
HELIX 3 3 THR A 41 LYS A 69 1 29
HELIX 4 4 SER A 73 ALA A 80 1 8
HELIX 5 5 GLY A 88 GLY A 93 1 6
HELIX 6 6 THR A 112 GLU A 126 1 15
HELIX 7 7 ASP A 173 ARG A 178 5 6
HELIX 8 8 ASP A 181 LEU A 200 1 20
HELIX 9 9 LYS A 203 ARG A 221 1 19
HELIX 10 10 ALA A 225 GLY A 229 5 5
HELIX 11 11 GLY A 232 TYR A 247 1 16
HELIX 12 12 CYS A 251 TRP A 266 1 16
HELIX 13 13 TYR A 292 SER A 297 1 6
HELIX 14 14 THR A 317 SER A 340 1 24
HELIX 15 15 SER A 344 PHE A 349 1 6
HELIX 16 16 ASP A 353 TYR A 358 1 6
HELIX 17 17 SER A 371 GLU A 394 1 24
HELIX 18 18 ASP A 420 GLN A 425 1 6
HELIX 19 19 GLU A 450 ALA A 456 1 7
HELIX 20 20 ILE A 481 SER A 494 1 14
HELIX 21 21 TYR A 515 LEU A 517 5 3
HELIX 22 22 PRO A 518 ASP A 523 5 6
HELIX 23 23 SER B 3 GLY B 8 5 6
HELIX 24 24 THR B 19 GLU B 36 1 18
HELIX 25 25 THR B 41 LYS B 70 1 30
HELIX 26 26 SER B 73 ALA B 80 1 8
HELIX 27 27 GLY B 88 GLY B 93 1 6
HELIX 28 28 THR B 112 PHE B 117 1 6
HELIX 29 29 THR B 118 GLU B 126 1 9
HELIX 30 30 ASP B 173 ARG B 178 5 6
HELIX 31 31 ASP B 181 LEU B 200 1 20
HELIX 32 32 LYS B 203 ARG B 221 1 19
HELIX 33 33 GLY B 232 TYR B 247 1 16
HELIX 34 34 SER B 252 TRP B 266 1 15
HELIX 35 35 LEU B 282 VAL B 286 5 5
HELIX 36 36 TYR B 292 HIS B 298 1 7
HELIX 37 37 THR B 317 SER B 340 1 24
HELIX 38 38 SER B 344 PHE B 349 1 6
HELIX 39 39 ASP B 353 TYR B 358 1 6
HELIX 40 40 SER B 371 LEU B 396 1 26
HELIX 41 41 THR B 417 TYR B 428 1 12
HELIX 42 42 SER B 430 THR B 435 1 6
HELIX 43 43 ALA B 436 LEU B 440 5 5
HELIX 44 44 ILE B 481 ARG B 493 1 13
HELIX 45 45 ASN B 496 ASP B 501 5 6
HELIX 46 46 TYR B 515 LEU B 517 5 3
HELIX 47 47 PRO B 518 PHE B 522 5 5
SHEET 1 A 5 LYS A 83 TYR A 87 0
SHEET 2 A 5 ILE A 101 VAL A 107 -1 O ASP A 102 N TYR A 87
SHEET 3 A 5 ILE A 151 ARG A 159 1 O SER A 152 N ILE A 101
SHEET 4 A 5 ILE A 143 PHE A 148 -1 N ILE A 144 O LEU A 155
SHEET 5 A 5 LEU A 130 VAL A 136 -1 N ASP A 131 O LYS A 147
SHEET 1 B 4 PHE A 505 LYS A 513 0
SHEET 2 B 4 PHE A 360 THR A 368 -1 O TYR A 361 N VAL A 512
SHEET 3 B 4 LYS A 458 PHE A 470 -1 N TYR A 460 O THR A 368
SHEET 4 B 4 ILE A 399 PRO A 404 -1 N LYS A 400 O ASP A 469
SHEET 1 C 5 PHE A 505 LYS A 513 0
SHEET 2 C 5 PHE A 360 THR A 368 -1 O TYR A 361 N VAL A 512
SHEET 3 C 5 LYS A 458 PHE A 470 -1 N TYR A 460 O THR A 368
SHEET 4 C 5 PHE A 409 CYS A 414 -1 N PHE A 409 O THR A 463
SHEET 5 C 5 LYS A 441 LEU A 442 -1 O LYS A 441 N CYS A 414
SHEET 1 D 5 LYS B 83 TYR B 87 0
SHEET 2 D 5 ILE B 101 VAL B 107 -1 O ASP B 102 N TYR B 87
SHEET 3 D 5 ILE B 151 ARG B 159 1 O SER B 152 N ILE B 101
SHEET 4 D 5 ILE B 143 PHE B 148 -1 N ILE B 144 O LEU B 155
SHEET 5 D 5 LEU B 130 VAL B 136 -1 N ASP B 131 O LYS B 147
SHEET 1 E 2 VAL B 272 ILE B 273 0
SHEET 2 E 2 VAL B 302 ILE B 303 1 N ILE B 303 O VAL B 272
SHEET 1 F 4 PHE B 505 LYS B 513 0
SHEET 2 F 4 PHE B 360 THR B 368 -1 O TYR B 361 N VAL B 512
SHEET 3 F 4 LYS B 458 PHE B 470 -1 N TYR B 460 O THR B 368
SHEET 4 F 4 ILE B 399 ILE B 401 -1 N LYS B 400 O ASP B 469
SHEET 1 G 4 PHE B 505 LYS B 513 0
SHEET 2 G 4 PHE B 360 THR B 368 -1 O TYR B 361 N VAL B 512
SHEET 3 G 4 LYS B 458 PHE B 470 -1 N TYR B 460 O THR B 368
SHEET 4 G 4 PHE B 409 CYS B 414 -1 N PHE B 409 O THR B 463
LINK OD2 ASP A 100 MN MN A 600 1555 1555 2.06
LINK OD1 ASP A 100 MN MN A 601 1555 1555 2.19
LINK OD1 ASP A 102 MN MN A 600 1555 1555 2.29
LINK OD2 ASP A 102 MN MN A 601 1555 1555 2.21
LINK OD1 ASP A 154 MN MN A 601 1555 1555 1.89
LINK MN MN A 600 O3G 3AT A 604 1555 1555 2.17
LINK MN MN A 600 O2B 3AT A 604 1555 1555 2.43
LINK MN MN A 600 O1A 3AT A 604 1555 1555 2.05
LINK MN MN A 600 O HOH A 871 1555 1555 2.22
LINK MN MN A 601 O1A 3AT A 604 1555 1555 2.23
LINK OD2 ASP B 100 MN MN B 602 1555 1555 2.19
LINK OD1 ASP B 100 MN MN B 603 1555 1555 2.73
LINK OD1 ASP B 102 MN MN B 602 1555 1555 2.29
LINK OD2 ASP B 102 MN MN B 603 1555 1555 1.92
LINK OD2 ASP B 154 MN MN B 603 1555 1555 1.93
LINK MN MN B 602 O1B 3AT B 605 1555 1555 2.13
LINK MN MN B 602 O1A 3AT B 605 1555 1555 2.03
LINK MN MN B 602 O1G 3AT B 605 1555 1555 2.21
LINK MN MN B 603 O1A 3AT B 605 1555 1555 2.22
CISPEP 1 TRP A 268 PRO A 269 0 0.55
CISPEP 2 TYR A 307 PRO A 308 0 -0.26
CISPEP 3 TRP B 268 PRO B 269 0 0.47
CISPEP 4 TYR B 307 PRO B 308 0 -0.76
SITE 1 AC1 5 ASP A 100 ASP A 102 MN A 601 3AT A 604
SITE 2 AC1 5 HOH A 871
SITE 1 AC2 6 ASP A 100 ASP A 102 ASP A 154 MN A 600
SITE 2 AC2 6 3AT A 604 3AD A 606
SITE 1 AC3 4 SER B 89 ASP B 100 ASP B 102 3AT B 605
SITE 1 AC4 5 ASP B 100 ASP B 102 ASP B 154 3AT B 605
SITE 2 AC4 5 3AD B 607
SITE 1 AC5 11 TYR A 87 GLY A 88 SER A 89 SER A 99
SITE 2 AC5 11 ASP A 100 ASP A 102 MN A 600 MN A 601
SITE 3 AC5 11 3AD A 606 POP A 817 HOH A 871
SITE 1 AC6 12 SER B 89 SER B 99 ASP B 100 ASP B 102
SITE 2 AC6 12 PHE B 140 LYS B 215 VAL B 234 MN B 602
SITE 3 AC6 12 MN B 603 3AD B 607 HOH B 619 HOH B 635
SITE 1 AC7 8 TYR A 87 ASP A 102 VAL A 141 ASP A 154
SITE 2 AC7 8 ILE A 156 ARG A 186 MN A 601 3AT A 604
SITE 1 AC8 8 TYR B 87 ASP B 102 PHE B 140 VAL B 141
SITE 2 AC8 8 ASP B 154 ARG B 186 MN B 603 3AT B 605
SITE 1 AC9 12 GLY A 88 SER A 89 LEU A 92 VAL A 94
SITE 2 AC9 12 THR A 194 LEU A 211 LYS A 215 TYR A 224
SITE 3 AC9 12 GLY A 233 VAL A 234 3AT A 604 HOH A 862
CRYST1 73.800 109.100 238.500 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 0.013550 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009166 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004193 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
