HEADER HYDROLASE/DNA 16-OCT-06 2IS4
TITLE CRYSTAL STRUCTURE OF UVRD-DNA-ADPNP TERNARY COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 25-MER;
COMPND 3 CHAIN: C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DNA HELICASE II;
COMPND 7 CHAIN: A, B;
COMPND 8 EC: 3.6.1.-;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 5 ORGANISM_TAXID: 562;
SOURCE 6 GENE: UVRD;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DNA HELICASE, HYDROLASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR W.YANG,J.Y.LEE
REVDAT 5 30-AUG-23 2IS4 1 REMARK
REVDAT 4 20-OCT-21 2IS4 1 REMARK SEQADV LINK
REVDAT 3 18-OCT-17 2IS4 1 REMARK
REVDAT 2 24-FEB-09 2IS4 1 VERSN
REVDAT 1 09-JAN-07 2IS4 0
JRNL AUTH J.Y.LEE,W.YANG
JRNL TITL UVRD HELICASE UNWINDS DNA ONE BASE PAIR AT A TIME BY A
JRNL TITL 2 TWO-PART POWER STROKE.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 127 1349 2006
JRNL REFN ISSN 0092-8674
JRNL PMID 17190599
JRNL DOI 10.1016/J.CELL.2006.10.049
REMARK 2
REMARK 2 RESOLUTION. 2.60 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 278489.330
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 85.3
REMARK 3 NUMBER OF REFLECTIONS : 57871
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) : 0.215
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.200
REMARK 3 FREE R VALUE TEST SET COUNT : 5887
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
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) : 2.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 48.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4898
REMARK 3 BIN R VALUE (WORKING SET) : 0.3480
REMARK 3 BIN FREE R VALUE : 0.3950
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 520
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 : 9951
REMARK 3 NUCLEIC ACID ATOMS : 1015
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 118
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 77.04
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 79.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 21.11000
REMARK 3 B22 (A**2) : 9.58000
REMARK 3 B33 (A**2) : -30.70000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 9.21000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.37
REMARK 3 ESD FROM SIGMAA (A) : 0.52
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) : 0.43
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.57
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.820
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) : 1.430 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.480 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.930 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.080 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.31
REMARK 3 BSOL : 42.98
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 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : ANP.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : ANP.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2IS4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-NOV-06.
REMARK 100 THE DEPOSITION ID IS D_1000039947.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-NOV-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61012
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.7
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.3000
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) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 51.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.20600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY: 2IS1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, SODIUM FLUORIDE, PH 7.0,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 48.38950
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). THE ASSYMETRIC UNIT CONTAINS
REMARK 300 TWO BIOLOGICAL UNITS. BIOLOGICAL UNIT ONE CONTAINS CHAINS
REMARK 300 A, C (RESIDUES 1-10) AND D (RESIDUES 11-26).
REMARK 300 BIOLOGICAL UNIT TWO CONTAINS CHAINS B, C (RESIDUES 11-20)
REMARK 300 AND D (RESIDUES 22-26).
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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 DT C 21
REMARK 465 DT D 1
REMARK 465 SER A 161
REMARK 465 TYR A 162
REMARK 465 GLY A 163
REMARK 465 SER A 520
REMARK 465 TYR A 521
REMARK 465 ASN A 522
REMARK 465 GLU A 523
REMARK 465 GLU A 524
REMARK 465 ASP A 525
REMARK 465 GLU A 526
REMARK 465 ASP A 527
REMARK 465 LEU A 528
REMARK 465 GLY A 545
REMARK 465 GLN A 546
REMARK 465 ALA A 547
REMARK 465 ASP A 548
REMARK 465 MET A 663
REMARK 465 VAL A 664
REMARK 465 GLU A 665
REMARK 465 ASN A 666
REMARK 465 ASP A 667
REMARK 465 SER A 668
REMARK 465 GLY A 669
REMARK 465 TYR A 670
REMARK 465 LYS A 671
REMARK 465 LEU A 672
REMARK 465 GLY A 673
REMARK 465 GLN A 674
REMARK 465 ARG A 675
REMARK 465 VAL A 676
REMARK 465 ARG A 677
REMARK 465 HIS A 678
REMARK 465 ALA A 679
REMARK 465 LYS A 680
REMARK 465 GLN B 160
REMARK 465 SER B 161
REMARK 465 TYR B 162
REMARK 465 GLU B 500
REMARK 465 LYS B 501
REMARK 465 GLY B 502
REMARK 465 TYR B 521
REMARK 465 ASN B 522
REMARK 465 GLU B 523
REMARK 465 GLU B 524
REMARK 465 ASP B 525
REMARK 465 GLU B 526
REMARK 465 ASP B 527
REMARK 465 ALA B 539
REMARK 465 LEU B 540
REMARK 465 GLU B 541
REMARK 465 ALA B 542
REMARK 465 GLY B 543
REMARK 465 GLU B 544
REMARK 465 GLY B 545
REMARK 465 GLN B 546
REMARK 465 ALA B 547
REMARK 465 ALA B 648
REMARK 465 THR B 649
REMARK 465 SER B 655
REMARK 465 HIS B 656
REMARK 465 MET B 659
REMARK 465 GLY B 660
REMARK 465 THR B 661
REMARK 465 PRO B 662
REMARK 465 MET B 663
REMARK 465 VAL B 664
REMARK 465 GLU B 665
REMARK 465 ASN B 666
REMARK 465 ASP B 667
REMARK 465 SER B 668
REMARK 465 GLY B 669
REMARK 465 TYR B 670
REMARK 465 LYS B 671
REMARK 465 LEU B 672
REMARK 465 GLY B 673
REMARK 465 GLN B 674
REMARK 465 ARG B 675
REMARK 465 VAL B 676
REMARK 465 ARG B 677
REMARK 465 HIS B 678
REMARK 465 ALA B 679
REMARK 465 LYS B 680
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 DG C 22 P OP1 OP2
REMARK 470 DC D 2 P OP1 OP2
REMARK 470 MET A 1 CG SD CE
REMARK 470 ASP A 2 CG OD1 OD2
REMARK 470 VAL A 3 CG1 CG2
REMARK 470 GLN A 82 CD OE1 NE2
REMARK 470 ARG A 99 CD NE CZ NH1 NH2
REMARK 470 LYS A 124 CD CE NZ
REMARK 470 ARG A 125 CD NE CZ NH1 NH2
REMARK 470 LYS A 128 CD CE NZ
REMARK 470 GLU A 134 CD OE1 OE2
REMARK 470 LYS A 135 CD CE NZ
REMARK 470 ARG A 140 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 158 CG ND1 CD2 CE1 NE2
REMARK 470 ILE A 159 CG1 CG2 CD1
REMARK 470 GLN A 160 CG CD OE1 NE2
REMARK 470 ASN A 164 CG OD1 ND2
REMARK 470 LYS A 172 CG CD CE NZ
REMARK 470 LEU A 304 CG CD1 CD2
REMARK 470 LYS A 306 CG CD CE NZ
REMARK 470 LYS A 307 CG CD CE NZ
REMARK 470 VAL A 399 CG1 CG2
REMARK 470 ARG A 427 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 442 CD NE CZ NH1 NH2
REMARK 470 LYS A 448 CD CE NZ
REMARK 470 LEU A 450 CG CD1 CD2
REMARK 470 ARG A 460 CD NE CZ NH1 NH2
REMARK 470 GLN A 470 CG CD OE1 NE2
REMARK 470 LYS A 486 CG CD CE NZ
REMARK 470 ARG A 491 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 496 CG CD OE1 NE2
REMARK 470 GLU A 497 CG CD OE1 OE2
REMARK 470 LYS A 498 CG CD CE NZ
REMARK 470 GLU A 500 CG CD OE1 OE2
REMARK 470 LYS A 501 CG CD CE NZ
REMARK 470 GLN A 503 CG CD OE1 NE2
REMARK 470 GLU A 511 CD OE1 OE2
REMARK 470 MET A 529 CG SD CE
REMARK 470 LEU A 531 CG CD1 CD2
REMARK 470 GLN A 532 CG CD OE1 NE2
REMARK 470 GLU A 544 CG CD OE1 OE2
REMARK 470 THR A 549 OG1 CG2
REMARK 470 GLN A 551 CD OE1 NE2
REMARK 470 GLU A 588 CG CD OE1 OE2
REMARK 470 ARG A 591 CD NE CZ NH1 NH2
REMARK 470 ARG A 619 CD NE CZ NH1 NH2
REMARK 470 LEU A 620 CG CD1 CD2
REMARK 470 LYS A 623 CG CD CE NZ
REMARK 470 THR A 649 OG1 CG2
REMARK 470 VAL A 650 CG1 CG2
REMARK 470 ARG A 652 CD NE CZ NH1 NH2
REMARK 470 PRO A 662 CG CD
REMARK 470 MET B 1 CG SD CE
REMARK 470 ASP B 2 CG OD1 OD2
REMARK 470 VAL B 3 CG1 CG2
REMARK 470 GLU B 134 CD OE1 OE2
REMARK 470 GLN B 136 CG CD OE1 NE2
REMARK 470 ASN B 164 CG OD1 ND2
REMARK 470 VAL B 166 CG1 CG2
REMARK 470 LYS B 172 CG CD CE NZ
REMARK 470 GLN B 175 CG CD OE1 NE2
REMARK 470 LYS B 307 CD CE NZ
REMARK 470 ARG B 375 CD NE CZ NH1 NH2
REMARK 470 VAL B 399 CG1 CG2
REMARK 470 GLN B 428 CD OE1 NE2
REMARK 470 GLN B 434 CD OE1 NE2
REMARK 470 GLN B 446 CG CD OE1 NE2
REMARK 470 LYS B 448 CD CE NZ
REMARK 470 LEU B 450 CG CD1 CD2
REMARK 470 ARG B 460 CD NE CZ NH1 NH2
REMARK 470 GLU B 463 CG CD OE1 OE2
REMARK 470 ILE B 465 CG1 CG2 CD1
REMARK 470 THR B 481 OG1 CG2
REMARK 470 ARG B 483 CD NE CZ NH1 NH2
REMARK 470 LYS B 486 CD CE NZ
REMARK 470 GLN B 496 CG CD OE1 NE2
REMARK 470 GLU B 497 CG CD OE1 OE2
REMARK 470 LYS B 498 CD CE NZ
REMARK 470 GLN B 503 CG CD OE1 NE2
REMARK 470 SER B 520 OG
REMARK 470 LEU B 528 CG CD1 CD2
REMARK 470 MET B 529 CG SD CE
REMARK 470 PRO B 530 CG CD
REMARK 470 LEU B 531 CG CD1 CD2
REMARK 470 LEU B 535 CG CD1 CD2
REMARK 470 HIS B 537 CG ND1 CD2 CE1 NE2
REMARK 470 ASP B 548 CG OD1 OD2
REMARK 470 LYS B 623 CG CD CE NZ
REMARK 470 ARG B 647 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 650 CG1 CG2
REMARK 470 SER B 651 OG
REMARK 470 ARG B 652 CG CD NE CZ NH1 NH2
REMARK 470 PRO B 653 CG CD
REMARK 470 VAL B 654 CG1 CG2
REMARK 470 GLN B 657 CG CD OE1 NE2
REMARK 470 ARG B 658 CG CD NE CZ NH1 NH2
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 GLN A 551 N - CA - C ANGL. DEV. = -17.5 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 ASP A 2 79.69 -56.32
REMARK 500 VAL A 3 -48.11 -23.48
REMARK 500 LEU A 10 153.18 -49.20
REMARK 500 ALA A 19 50.94 -93.30
REMARK 500 THR A 80 -53.44 -20.85
REMARK 500 SER A 81 85.82 -39.38
REMARK 500 HIS A 101 36.75 -153.07
REMARK 500 GLN A 109 9.83 -68.13
REMARK 500 PHE A 111 128.43 -31.73
REMARK 500 PRO A 156 -39.86 -35.46
REMARK 500 HIS A 158 122.97 -23.71
REMARK 500 ILE A 159 -149.87 -139.09
REMARK 500 THR A 169 -73.01 -62.22
REMARK 500 LYS A 203 59.31 -158.63
REMARK 500 PRO A 204 -36.87 -39.11
REMARK 500 GLN A 223 -4.80 -59.19
REMARK 500 ASN A 226 -159.05 -102.07
REMARK 500 LEU A 235 -75.86 -56.55
REMARK 500 ALA A 259 95.75 -55.92
REMARK 500 ALA A 274 126.56 -21.39
REMARK 500 GLU A 280 -20.00 -145.98
REMARK 500 LYS A 307 -103.83 -52.53
REMARK 500 LEU A 308 89.91 76.44
REMARK 500 MET A 380 40.21 -92.81
REMARK 500 GLN A 386 -70.23 -45.31
REMARK 500 ASN A 400 97.58 173.61
REMARK 500 ASP A 403 88.37 -67.89
REMARK 500 GLU A 408 -74.88 -49.84
REMARK 500 THR A 415 112.90 -38.20
REMARK 500 ILE A 418 81.50 -66.37
REMARK 500 ASP A 420 -78.63 -55.34
REMARK 500 GLN A 434 42.13 78.58
REMARK 500 LEU A 435 -159.27 -116.19
REMARK 500 LEU A 444 -1.86 -59.86
REMARK 500 LEU A 445 -60.66 -94.50
REMARK 500 GLN A 446 41.57 -78.37
REMARK 500 GLU A 447 2.09 -158.21
REMARK 500 LYS A 448 76.04 21.75
REMARK 500 ALA A 451 -172.35 -51.11
REMARK 500 ALA A 454 -79.79 -57.97
REMARK 500 LEU A 458 -19.04 -46.61
REMARK 500 ASP A 474 -75.77 -88.95
REMARK 500 MET A 475 156.96 -28.62
REMARK 500 GLN A 496 -107.21 -87.91
REMARK 500 GLU A 497 -64.63 45.94
REMARK 500 LYS A 498 -75.62 -113.19
REMARK 500 GLU A 500 -87.01 -148.51
REMARK 500 GLN A 518 36.08 -82.96
REMARK 500 TRP A 550 72.68 -54.47
REMARK 500 ASP A 552 111.78 -36.37
REMARK 500
REMARK 500 THIS ENTRY HAS 101 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 A1001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 36 OG1
REMARK 620 2 ANP A 700 O1B 85.9
REMARK 620 3 ANP A 700 O2G 175.1 98.5
REMARK 620 4 HOH A1002 O 73.2 91.8 104.5
REMARK 620 5 HOH A1003 O 94.5 101.9 86.6 161.0
REMARK 620 6 HOH A1004 O 87.9 173.6 87.7 87.9 77.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 36 OG1
REMARK 620 2 ANP B 701 O1B 83.2
REMARK 620 3 ANP B 701 O2G 168.0 107.0
REMARK 620 4 HOH B1003 O 89.4 91.7 96.5
REMARK 620 5 HOH B1004 O 71.7 92.7 100.9 159.9
REMARK 620 6 HOH B1005 O 73.0 155.1 97.5 80.9 87.0
REMARK 620 N 1 2 3 4 5
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 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP B 701
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2IS1 RELATED DB: PDB
REMARK 900 RELATED ID: 2IS2 RELATED DB: PDB
DBREF 2IS4 A 1 680 UNP P03018 UVRD_ECOLI 1 680
DBREF 2IS4 B 1 680 UNP P03018 UVRD_ECOLI 1 680
DBREF 2IS4 C 1 26 PDB 2IS4 2IS4 1 26
DBREF 2IS4 D 1 26 PDB 2IS4 2IS4 1 26
SEQADV 2IS4 VAL A 399 UNP P03018 ALA 399 ENGINEERED MUTATION
SEQADV 2IS4 VAL B 399 UNP P03018 ALA 399 ENGINEERED MUTATION
SEQRES 1 C 26 DT DC DG DA DG DC DA DC DT DG DC DA DG
SEQRES 2 C 26 DT DG DC DT DC DG DT DT DG DT DT DT DA
SEQRES 1 D 26 DT DC DG DA DG DC DA DC DT DG DC DA DG
SEQRES 2 D 26 DT DG DC DT DC DG DT DT DG DT DT DT DA
SEQRES 1 A 680 MET ASP VAL SER TYR LEU LEU ASP SER LEU ASN ASP LYS
SEQRES 2 A 680 GLN ARG GLU ALA VAL ALA ALA PRO ARG SER ASN LEU LEU
SEQRES 3 A 680 VAL LEU ALA GLY ALA GLY SER GLY LYS THR ARG VAL LEU
SEQRES 4 A 680 VAL HIS ARG ILE ALA TRP LEU MET SER VAL GLU ASN CYS
SEQRES 5 A 680 SER PRO TYR SER ILE MET ALA VAL THR PHE THR ASN LYS
SEQRES 6 A 680 ALA ALA ALA GLU MET ARG HIS ARG ILE GLY GLN LEU MET
SEQRES 7 A 680 GLY THR SER GLN GLY GLY MET TRP VAL GLY THR PHE HIS
SEQRES 8 A 680 GLY LEU ALA HIS ARG LEU LEU ARG ALA HIS HIS MET ASP
SEQRES 9 A 680 ALA ASN LEU PRO GLN ASP PHE GLN ILE LEU ASP SER GLU
SEQRES 10 A 680 ASP GLN LEU ARG LEU LEU LYS ARG LEU ILE LYS ALA MET
SEQRES 11 A 680 ASN LEU ASP GLU LYS GLN TRP PRO PRO ARG GLN ALA MET
SEQRES 12 A 680 TRP TYR ILE ASN SER GLN LYS ASP GLU GLY LEU ARG PRO
SEQRES 13 A 680 HIS HIS ILE GLN SER TYR GLY ASN PRO VAL GLU GLN THR
SEQRES 14 A 680 TRP GLN LYS VAL TYR GLN ALA TYR GLN GLU ALA CYS ASP
SEQRES 15 A 680 ARG ALA GLY LEU VAL ASP PHE ALA GLU LEU LEU LEU ARG
SEQRES 16 A 680 ALA HIS GLU LEU TRP LEU ASN LYS PRO HIS ILE LEU GLN
SEQRES 17 A 680 HIS TYR ARG GLU ARG PHE THR ASN ILE LEU VAL ASP GLU
SEQRES 18 A 680 PHE GLN ASP THR ASN ASN ILE GLN TYR ALA TRP ILE ARG
SEQRES 19 A 680 LEU LEU ALA GLY ASP THR GLY LYS VAL MET ILE VAL GLY
SEQRES 20 A 680 ASP ASP ASP GLN SER ILE TYR GLY TRP ARG GLY ALA GLN
SEQRES 21 A 680 VAL GLU ASN ILE GLN ARG PHE LEU ASN ASP PHE PRO GLY
SEQRES 22 A 680 ALA GLU THR ILE ARG LEU GLU GLN ASN TYR ARG SER THR
SEQRES 23 A 680 SER ASN ILE LEU SER ALA ALA ASN ALA LEU ILE GLU ASN
SEQRES 24 A 680 ASN ASN GLY ARG LEU GLY LYS LYS LEU TRP THR ASP GLY
SEQRES 25 A 680 ALA ASP GLY GLU PRO ILE SER LEU TYR CYS ALA PHE ASN
SEQRES 26 A 680 GLU LEU ASP GLU ALA ARG PHE VAL VAL ASN ARG ILE LYS
SEQRES 27 A 680 THR TRP GLN ASP ASN GLY GLY ALA LEU ALA GLU CYS ALA
SEQRES 28 A 680 ILE LEU TYR ARG SER ASN ALA GLN SER ARG VAL LEU GLU
SEQRES 29 A 680 GLU ALA LEU LEU GLN ALA SER MET PRO TYR ARG ILE TYR
SEQRES 30 A 680 GLY GLY MET ARG PHE PHE GLU ARG GLN GLU ILE LYS ASP
SEQRES 31 A 680 ALA LEU SER TYR LEU ARG LEU ILE VAL ASN ARG ASN ASP
SEQRES 32 A 680 ASP ALA ALA PHE GLU ARG VAL VAL ASN THR PRO THR ARG
SEQRES 33 A 680 GLY ILE GLY ASP ARG THR LEU ASP VAL VAL ARG GLN THR
SEQRES 34 A 680 SER ARG ASP ARG GLN LEU THR LEU TRP GLN ALA CYS ARG
SEQRES 35 A 680 GLU LEU LEU GLN GLU LYS ALA LEU ALA GLY ARG ALA ALA
SEQRES 36 A 680 SER ALA LEU GLN ARG PHE MET GLU LEU ILE ASP ALA LEU
SEQRES 37 A 680 ALA GLN GLU THR ALA ASP MET PRO LEU HIS VAL GLN THR
SEQRES 38 A 680 ASP ARG VAL ILE LYS ASP SER GLY LEU ARG THR MET TYR
SEQRES 39 A 680 GLU GLN GLU LYS GLY GLU LYS GLY GLN THR ARG ILE GLU
SEQRES 40 A 680 ASN LEU GLU GLU LEU VAL THR ALA THR ARG GLN PHE SER
SEQRES 41 A 680 TYR ASN GLU GLU ASP GLU ASP LEU MET PRO LEU GLN ALA
SEQRES 42 A 680 PHE LEU SER HIS ALA ALA LEU GLU ALA GLY GLU GLY GLN
SEQRES 43 A 680 ALA ASP THR TRP GLN ASP ALA VAL GLN LEU MET THR LEU
SEQRES 44 A 680 HIS SER ALA LYS GLY LEU GLU PHE PRO GLN VAL PHE ILE
SEQRES 45 A 680 VAL GLY MET GLU GLU GLY MET PHE PRO SER GLN MET SER
SEQRES 46 A 680 LEU ASP GLU GLY GLY ARG LEU GLU GLU GLU ARG ARG LEU
SEQRES 47 A 680 ALA TYR VAL GLY VAL THR ARG ALA MET GLN LYS LEU THR
SEQRES 48 A 680 LEU THR TYR ALA GLU THR ARG ARG LEU TYR GLY LYS GLU
SEQRES 49 A 680 VAL TYR HIS ARG PRO SER ARG PHE ILE GLY GLU LEU PRO
SEQRES 50 A 680 GLU GLU CYS VAL GLU GLU VAL ARG LEU ARG ALA THR VAL
SEQRES 51 A 680 SER ARG PRO VAL SER HIS GLN ARG MET GLY THR PRO MET
SEQRES 52 A 680 VAL GLU ASN ASP SER GLY TYR LYS LEU GLY GLN ARG VAL
SEQRES 53 A 680 ARG HIS ALA LYS
SEQRES 1 B 680 MET ASP VAL SER TYR LEU LEU ASP SER LEU ASN ASP LYS
SEQRES 2 B 680 GLN ARG GLU ALA VAL ALA ALA PRO ARG SER ASN LEU LEU
SEQRES 3 B 680 VAL LEU ALA GLY ALA GLY SER GLY LYS THR ARG VAL LEU
SEQRES 4 B 680 VAL HIS ARG ILE ALA TRP LEU MET SER VAL GLU ASN CYS
SEQRES 5 B 680 SER PRO TYR SER ILE MET ALA VAL THR PHE THR ASN LYS
SEQRES 6 B 680 ALA ALA ALA GLU MET ARG HIS ARG ILE GLY GLN LEU MET
SEQRES 7 B 680 GLY THR SER GLN GLY GLY MET TRP VAL GLY THR PHE HIS
SEQRES 8 B 680 GLY LEU ALA HIS ARG LEU LEU ARG ALA HIS HIS MET ASP
SEQRES 9 B 680 ALA ASN LEU PRO GLN ASP PHE GLN ILE LEU ASP SER GLU
SEQRES 10 B 680 ASP GLN LEU ARG LEU LEU LYS ARG LEU ILE LYS ALA MET
SEQRES 11 B 680 ASN LEU ASP GLU LYS GLN TRP PRO PRO ARG GLN ALA MET
SEQRES 12 B 680 TRP TYR ILE ASN SER GLN LYS ASP GLU GLY LEU ARG PRO
SEQRES 13 B 680 HIS HIS ILE GLN SER TYR GLY ASN PRO VAL GLU GLN THR
SEQRES 14 B 680 TRP GLN LYS VAL TYR GLN ALA TYR GLN GLU ALA CYS ASP
SEQRES 15 B 680 ARG ALA GLY LEU VAL ASP PHE ALA GLU LEU LEU LEU ARG
SEQRES 16 B 680 ALA HIS GLU LEU TRP LEU ASN LYS PRO HIS ILE LEU GLN
SEQRES 17 B 680 HIS TYR ARG GLU ARG PHE THR ASN ILE LEU VAL ASP GLU
SEQRES 18 B 680 PHE GLN ASP THR ASN ASN ILE GLN TYR ALA TRP ILE ARG
SEQRES 19 B 680 LEU LEU ALA GLY ASP THR GLY LYS VAL MET ILE VAL GLY
SEQRES 20 B 680 ASP ASP ASP GLN SER ILE TYR GLY TRP ARG GLY ALA GLN
SEQRES 21 B 680 VAL GLU ASN ILE GLN ARG PHE LEU ASN ASP PHE PRO GLY
SEQRES 22 B 680 ALA GLU THR ILE ARG LEU GLU GLN ASN TYR ARG SER THR
SEQRES 23 B 680 SER ASN ILE LEU SER ALA ALA ASN ALA LEU ILE GLU ASN
SEQRES 24 B 680 ASN ASN GLY ARG LEU GLY LYS LYS LEU TRP THR ASP GLY
SEQRES 25 B 680 ALA ASP GLY GLU PRO ILE SER LEU TYR CYS ALA PHE ASN
SEQRES 26 B 680 GLU LEU ASP GLU ALA ARG PHE VAL VAL ASN ARG ILE LYS
SEQRES 27 B 680 THR TRP GLN ASP ASN GLY GLY ALA LEU ALA GLU CYS ALA
SEQRES 28 B 680 ILE LEU TYR ARG SER ASN ALA GLN SER ARG VAL LEU GLU
SEQRES 29 B 680 GLU ALA LEU LEU GLN ALA SER MET PRO TYR ARG ILE TYR
SEQRES 30 B 680 GLY GLY MET ARG PHE PHE GLU ARG GLN GLU ILE LYS ASP
SEQRES 31 B 680 ALA LEU SER TYR LEU ARG LEU ILE VAL ASN ARG ASN ASP
SEQRES 32 B 680 ASP ALA ALA PHE GLU ARG VAL VAL ASN THR PRO THR ARG
SEQRES 33 B 680 GLY ILE GLY ASP ARG THR LEU ASP VAL VAL ARG GLN THR
SEQRES 34 B 680 SER ARG ASP ARG GLN LEU THR LEU TRP GLN ALA CYS ARG
SEQRES 35 B 680 GLU LEU LEU GLN GLU LYS ALA LEU ALA GLY ARG ALA ALA
SEQRES 36 B 680 SER ALA LEU GLN ARG PHE MET GLU LEU ILE ASP ALA LEU
SEQRES 37 B 680 ALA GLN GLU THR ALA ASP MET PRO LEU HIS VAL GLN THR
SEQRES 38 B 680 ASP ARG VAL ILE LYS ASP SER GLY LEU ARG THR MET TYR
SEQRES 39 B 680 GLU GLN GLU LYS GLY GLU LYS GLY GLN THR ARG ILE GLU
SEQRES 40 B 680 ASN LEU GLU GLU LEU VAL THR ALA THR ARG GLN PHE SER
SEQRES 41 B 680 TYR ASN GLU GLU ASP GLU ASP LEU MET PRO LEU GLN ALA
SEQRES 42 B 680 PHE LEU SER HIS ALA ALA LEU GLU ALA GLY GLU GLY GLN
SEQRES 43 B 680 ALA ASP THR TRP GLN ASP ALA VAL GLN LEU MET THR LEU
SEQRES 44 B 680 HIS SER ALA LYS GLY LEU GLU PHE PRO GLN VAL PHE ILE
SEQRES 45 B 680 VAL GLY MET GLU GLU GLY MET PHE PRO SER GLN MET SER
SEQRES 46 B 680 LEU ASP GLU GLY GLY ARG LEU GLU GLU GLU ARG ARG LEU
SEQRES 47 B 680 ALA TYR VAL GLY VAL THR ARG ALA MET GLN LYS LEU THR
SEQRES 48 B 680 LEU THR TYR ALA GLU THR ARG ARG LEU TYR GLY LYS GLU
SEQRES 49 B 680 VAL TYR HIS ARG PRO SER ARG PHE ILE GLY GLU LEU PRO
SEQRES 50 B 680 GLU GLU CYS VAL GLU GLU VAL ARG LEU ARG ALA THR VAL
SEQRES 51 B 680 SER ARG PRO VAL SER HIS GLN ARG MET GLY THR PRO MET
SEQRES 52 B 680 VAL GLU ASN ASP SER GLY TYR LYS LEU GLY GLN ARG VAL
SEQRES 53 B 680 ARG HIS ALA LYS
HET MG A1001 1
HET ANP A 700 31
HET MG B1002 1
HET ANP B 701 31
HETNAM MG MAGNESIUM ION
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
FORMUL 5 MG 2(MG 2+)
FORMUL 6 ANP 2(C10 H17 N6 O12 P3)
FORMUL 9 HOH *118(H2 O)
HELIX 1 1 ASP A 2 SER A 9 1 8
HELIX 2 2 ASN A 11 ALA A 19 1 9
HELIX 3 3 GLY A 34 VAL A 49 1 16
HELIX 4 4 SER A 53 TYR A 55 5 3
HELIX 5 5 THR A 63 MET A 78 1 16
HELIX 6 6 PHE A 90 HIS A 101 1 12
HELIX 7 7 HIS A 101 ASN A 106 1 6
HELIX 8 8 ASP A 115 MET A 130 1 16
HELIX 9 9 PRO A 138 GLU A 152 1 15
HELIX 10 10 ASN A 164 GLY A 185 1 22
HELIX 11 11 PHE A 189 ASN A 202 1 14
HELIX 12 12 LYS A 203 PHE A 214 1 12
HELIX 13 13 GLU A 221 THR A 225 5 5
HELIX 14 14 ASN A 226 GLY A 238 1 13
HELIX 15 15 ASP A 248 SER A 252 5 5
HELIX 16 16 TYR A 254 GLY A 258 5 5
HELIX 17 17 GLU A 262 PHE A 271 1 10
HELIX 18 18 THR A 286 GLU A 298 1 13
HELIX 19 19 ASN A 325 ASP A 342 1 18
HELIX 20 20 ALA A 346 ALA A 348 5 3
HELIX 21 21 SER A 356 ALA A 358 5 3
HELIX 22 22 GLN A 359 ALA A 370 1 12
HELIX 23 23 ARG A 385 VAL A 399 1 15
HELIX 24 24 ASP A 403 ASN A 412 1 10
HELIX 25 25 GLY A 419 ASP A 432 1 14
HELIX 26 26 TRP A 438 LEU A 444 1 7
HELIX 27 27 ALA A 451 ALA A 473 1 23
HELIX 28 28 PRO A 476 ASP A 487 1 12
HELIX 29 29 GLY A 489 TYR A 494 1 6
HELIX 30 30 LYS A 501 GLN A 518 1 18
HELIX 31 31 MET A 529 ALA A 542 1 14
HELIX 32 32 LEU A 559 LYS A 563 1 5
HELIX 33 33 SER A 582 GLU A 588 1 7
HELIX 34 34 GLY A 590 THR A 604 1 15
HELIX 35 35 SER A 630 LEU A 636 1 7
HELIX 36 36 PRO A 637 GLU A 639 5 3
HELIX 37 37 ASP B 2 ASP B 8 1 7
HELIX 38 38 ASN B 11 ALA B 19 1 9
HELIX 39 39 GLY B 34 VAL B 49 1 16
HELIX 40 40 SER B 53 TYR B 55 5 3
HELIX 41 41 THR B 63 GLY B 79 1 17
HELIX 42 42 PHE B 90 ALA B 100 1 11
HELIX 43 43 ASP B 115 MET B 130 1 16
HELIX 44 44 PRO B 138 GLU B 152 1 15
HELIX 45 45 THR B 169 GLY B 185 1 17
HELIX 46 46 PHE B 189 ASN B 202 1 14
HELIX 47 47 LYS B 203 PHE B 214 1 12
HELIX 48 48 GLU B 221 THR B 225 5 5
HELIX 49 49 ASN B 226 GLY B 238 1 13
HELIX 50 50 ASP B 248 SER B 252 5 5
HELIX 51 51 TYR B 254 GLY B 258 5 5
HELIX 52 52 GLU B 262 PHE B 271 1 10
HELIX 53 53 THR B 286 GLU B 298 1 13
HELIX 54 54 GLU B 326 ASN B 343 1 18
HELIX 55 55 ALA B 346 ALA B 348 5 3
HELIX 56 56 SER B 356 ALA B 358 5 3
HELIX 57 57 GLN B 359 GLN B 369 1 11
HELIX 58 58 ARG B 381 GLU B 384 5 4
HELIX 59 59 ARG B 385 ASN B 400 1 16
HELIX 60 60 ASP B 403 VAL B 411 1 9
HELIX 61 61 GLY B 419 GLN B 434 1 16
HELIX 62 62 THR B 436 GLN B 446 1 11
HELIX 63 63 ALA B 451 THR B 472 1 22
HELIX 64 64 PRO B 476 SER B 488 1 13
HELIX 65 65 GLY B 489 GLN B 496 1 8
HELIX 66 66 GLN B 503 GLN B 518 1 16
HELIX 67 67 MET B 529 SER B 536 1 8
HELIX 68 68 LEU B 559 LYS B 563 1 5
HELIX 69 69 SER B 582 GLU B 588 1 7
HELIX 70 70 ARG B 591 ARG B 605 1 15
HELIX 71 71 SER B 630 GLU B 635 1 6
HELIX 72 72 PRO B 637 GLU B 639 5 3
SHEET 1 A 6 TRP A 86 THR A 89 0
SHEET 2 A 6 ILE A 57 THR A 61 1 N ALA A 59 O TRP A 86
SHEET 3 A 6 ASN A 216 VAL A 219 1 O ASN A 216 N MET A 58
SHEET 4 A 6 LYS A 242 GLY A 247 1 O MET A 244 N ILE A 217
SHEET 5 A 6 LEU A 25 LEU A 28 1 N VAL A 27 O ILE A 245
SHEET 6 A 6 GLU A 275 ARG A 278 1 O GLU A 275 N LEU A 26
SHEET 1 B 2 GLN A 112 LEU A 114 0
SHEET 2 B 2 LEU A 186 ASP A 188 1 O VAL A 187 N LEU A 114
SHEET 1 C 7 TYR A 374 ILE A 376 0
SHEET 2 C 7 VAL A 554 THR A 558 1 O VAL A 554 N ARG A 375
SHEET 3 C 7 CYS A 350 TYR A 354 1 N ILE A 352 O GLN A 555
SHEET 4 C 7 PHE A 567 ILE A 572 1 O PHE A 571 N LEU A 353
SHEET 5 C 7 ALA A 606 ALA A 615 1 O THR A 611 N ILE A 572
SHEET 6 C 7 ILE A 318 ALA A 323 1 N SER A 319 O LEU A 612
SHEET 7 C 7 VAL A 641 GLU A 643 1 O GLU A 642 N ILE A 318
SHEET 1 D 2 ARG A 618 ARG A 619 0
SHEET 2 D 2 GLU A 624 VAL A 625 -1 O VAL A 625 N ARG A 618
SHEET 1 E 6 TRP B 86 THR B 89 0
SHEET 2 E 6 ILE B 57 THR B 61 1 N ALA B 59 O TRP B 86
SHEET 3 E 6 ASN B 216 VAL B 219 1 O LEU B 218 N MET B 58
SHEET 4 E 6 LYS B 242 GLY B 247 1 O MET B 244 N ILE B 217
SHEET 5 E 6 LEU B 25 LEU B 28 1 N VAL B 27 O ILE B 245
SHEET 6 E 6 GLU B 275 ARG B 278 1 O GLU B 275 N LEU B 26
SHEET 1 F 2 GLN B 112 LEU B 114 0
SHEET 2 F 2 LEU B 186 ASP B 188 1 O VAL B 187 N LEU B 114
SHEET 1 G 6 TYR B 374 ILE B 376 0
SHEET 2 G 6 VAL B 554 THR B 558 1 O LEU B 556 N ARG B 375
SHEET 3 G 6 CYS B 350 TYR B 354 1 N ILE B 352 O GLN B 555
SHEET 4 G 6 PHE B 567 ILE B 572 1 O PHE B 571 N LEU B 353
SHEET 5 G 6 ALA B 606 ARG B 619 1 O THR B 611 N ILE B 572
SHEET 6 G 6 GLU B 624 VAL B 625 -1 O VAL B 625 N ARG B 618
SHEET 1 H 7 TYR B 374 ILE B 376 0
SHEET 2 H 7 VAL B 554 THR B 558 1 O LEU B 556 N ARG B 375
SHEET 3 H 7 CYS B 350 TYR B 354 1 N ILE B 352 O GLN B 555
SHEET 4 H 7 PHE B 567 ILE B 572 1 O PHE B 571 N LEU B 353
SHEET 5 H 7 ALA B 606 ARG B 619 1 O THR B 611 N ILE B 572
SHEET 6 H 7 ILE B 318 ASN B 325 1 N SER B 319 O LEU B 612
SHEET 7 H 7 VAL B 641 GLU B 643 1 O GLU B 642 N ILE B 318
LINK OG1 THR A 36 MG MG A1001 1555 1555 2.12
LINK O1B ANP A 700 MG MG A1001 1555 1555 1.85
LINK O2G ANP A 700 MG MG A1001 1555 1555 2.12
LINK MG MG A1001 O HOH A1002 1555 1555 2.31
LINK MG MG A1001 O HOH A1003 1555 1555 2.12
LINK MG MG A1001 O HOH A1004 1555 1555 1.99
LINK OG1 THR B 36 MG MG B1002 1555 1555 2.48
LINK O1B ANP B 701 MG MG B1002 1555 1555 1.80
LINK O2G ANP B 701 MG MG B1002 1555 1555 2.19
LINK MG MG B1002 O HOH B1003 1555 1555 1.79
LINK MG MG B1002 O HOH B1004 1555 1555 2.09
LINK MG MG B1002 O HOH B1005 1555 1555 2.20
CISPEP 1 THR A 413 PRO A 414 0 -0.39
CISPEP 2 PHE A 580 PRO A 581 0 0.13
CISPEP 3 THR B 413 PRO B 414 0 0.13
CISPEP 4 PHE B 580 PRO B 581 0 0.31
SITE 1 AC1 6 THR A 36 GLU A 221 ANP A 700 HOH A1002
SITE 2 AC1 6 HOH A1003 HOH A1004
SITE 1 AC2 6 THR B 36 GLU B 221 ANP B 701 HOH B1003
SITE 2 AC2 6 HOH B1004 HOH B1005
SITE 1 AC3 22 SER A 9 GLN A 14 ALA A 31 GLY A 32
SITE 2 AC3 22 SER A 33 GLY A 34 LYS A 35 THR A 36
SITE 3 AC3 22 ARG A 37 ARG A 73 GLU A 221 GLN A 251
SITE 4 AC3 22 TYR A 283 ARG A 284 GLY A 564 GLU A 566
SITE 5 AC3 22 ARG A 605 MG A1001 HOH A1002 HOH A1003
SITE 6 AC3 22 HOH A1004 HOH A1063
SITE 1 AC4 21 SER B 9 GLN B 14 ALA B 31 GLY B 32
SITE 2 AC4 21 SER B 33 GLY B 34 LYS B 35 THR B 36
SITE 3 AC4 21 ARG B 37 ARG B 73 GLU B 221 GLN B 251
SITE 4 AC4 21 TYR B 283 ARG B 284 GLY B 564 GLU B 566
SITE 5 AC4 21 ARG B 605 MG B1002 HOH B1003 HOH B1004
SITE 6 AC4 21 HOH B1058
CRYST1 104.112 96.779 111.044 90.00 93.85 90.00 P 1 21 1 4
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 0.009605 0.000000 0.000646 0.00000
SCALE2 0.000000 0.010333 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009026 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
