HEADER HYDROLASE/DNA 31-MAY-16 5K97
TITLE FLAP ENDONUCLEASE 1 (FEN1) D233N WITH CLEAVED PRODUCT FRAGMENT AND
TITLE 2 SM3+
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLAP ENDONUCLEASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FEN-1,DNASE IV,FLAP STRUCTURE-SPECIFIC ENDONUCLEASE 1,
COMPND 5 MATURATION FACTOR 1,HFEN-1;
COMPND 6 EC: 3.1.-.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: DNA (5'-
COMPND 11 D(*AP*CP*TP*CP*TP*GP*CP*CP*TP*CP*AP*AP*GP*AP*CP*GP*GP*T)-3');
COMPND 12 CHAIN: D;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: DNA (5'-D(P*TP*GP*AP*GP*GP*CP*AP*GP*AP*GP*T)-3');
COMPND 16 CHAIN: E;
COMPND 17 ENGINEERED: YES;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: DNA (5'-D(*AP*CP*CP*GP*TP*CP*C)-3');
COMPND 20 CHAIN: F;
COMPND 21 ENGINEERED: YES;
COMPND 22 MOL_ID: 5;
COMPND 23 MOLECULE: DNA (5'-D(P*TP*T)-3');
COMPND 24 CHAIN: G;
COMPND 25 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: FEN1, RAD2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 11 ORGANISM_TAXID: 32630;
SOURCE 12 OTHER_DETAILS: DNA OLIGONUCLEOTIDE SYNTHESIS;
SOURCE 13 MOL_ID: 3;
SOURCE 14 SYNTHETIC: YES;
SOURCE 15 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 16 ORGANISM_TAXID: 32630;
SOURCE 17 OTHER_DETAILS: DNA OLIGONUCLEOTIDE SYNTHESIS;
SOURCE 18 MOL_ID: 4;
SOURCE 19 SYNTHETIC: YES;
SOURCE 20 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 21 ORGANISM_TAXID: 32630;
SOURCE 22 OTHER_DETAILS: DNA OLIGONUCLEOTIDE SYNTHESIS;
SOURCE 23 MOL_ID: 5;
SOURCE 24 SYNTHETIC: YES;
SOURCE 25 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 26 ORGANISM_TAXID: 32630;
SOURCE 27 OTHER_DETAILS: DNA OLIGONUCLEOTIDE SYNTHESIS
KEYWDS METALLOPROTEIN, REPLICATION, DNA DAMAGE, DNA REPAIR, BASE EXCISION
KEYWDS 2 REPAIR, PROTEIN-DNA, 5' NUCLEASE, FEN, PRODUCT, HYDROLASE-DNA
KEYWDS 3 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.E.TSUTAKAWA,A.S.ARVAI,J.A.TAINER
REVDAT 5 28-FEB-24 5K97 1 LINK
REVDAT 4 04-DEC-19 5K97 1 REMARK
REVDAT 3 27-SEP-17 5K97 1 REMARK
REVDAT 2 19-JUL-17 5K97 1 JRNL
REVDAT 1 28-JUN-17 5K97 0
JRNL AUTH S.E.TSUTAKAWA,M.J.THOMPSON,A.S.ARVAI,A.J.NEIL,S.J.SHAW,
JRNL AUTH 2 S.I.ALGASAIER,J.C.KIM,L.D.FINGER,E.JARDINE,V.J.B.GOTHAM,
JRNL AUTH 3 A.H.SARKER,M.Z.HER,F.RASHID,S.M.HAMDAN,S.M.MIRKIN,
JRNL AUTH 4 J.A.GRASBY,J.A.TAINER
JRNL TITL PHOSPHATE STEERING BY FLAP ENDONUCLEASE 1 PROMOTES 5'-FLAP
JRNL TITL 2 SPECIFICITY AND INCISION TO PREVENT GENOME INSTABILITY.
JRNL REF NAT COMMUN V. 8 15855 2017
JRNL REFN ESSN 2041-1723
JRNL PMID 28653660
JRNL DOI 10.1038/NCOMMS15855
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_2383: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 74847
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 3830
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 34.8541 - 6.2941 0.94 2512 138 0.1924 0.2224
REMARK 3 2 6.2941 - 5.0006 1.00 2643 140 0.1603 0.2164
REMARK 3 3 5.0006 - 4.3698 1.00 2621 146 0.1312 0.1531
REMARK 3 4 4.3698 - 3.9709 1.00 2674 144 0.1371 0.1709
REMARK 3 5 3.9709 - 3.6866 1.00 2671 144 0.1515 0.1710
REMARK 3 6 3.6866 - 3.4695 1.00 2625 152 0.1602 0.2166
REMARK 3 7 3.4695 - 3.2959 1.00 2617 136 0.1725 0.1881
REMARK 3 8 3.2959 - 3.1525 1.00 2661 145 0.1875 0.2442
REMARK 3 9 3.1525 - 3.0312 1.00 2658 142 0.2121 0.2746
REMARK 3 10 3.0312 - 2.9267 1.00 2659 142 0.2019 0.2026
REMARK 3 11 2.9267 - 2.8352 1.00 2608 146 0.2127 0.2924
REMARK 3 12 2.8352 - 2.7542 1.00 2663 140 0.2048 0.2737
REMARK 3 13 2.7542 - 2.6817 1.00 2682 140 0.2037 0.2180
REMARK 3 14 2.6817 - 2.6163 1.00 2652 137 0.2115 0.2820
REMARK 3 15 2.6163 - 2.5568 1.00 2613 144 0.2081 0.2899
REMARK 3 16 2.5568 - 2.5024 1.00 2626 140 0.2089 0.2209
REMARK 3 17 2.5024 - 2.4524 1.00 2704 136 0.2061 0.2019
REMARK 3 18 2.4524 - 2.4061 1.00 2684 142 0.2096 0.2563
REMARK 3 19 2.4061 - 2.3632 1.00 2625 148 0.2141 0.2583
REMARK 3 20 2.3632 - 2.3231 1.00 2656 136 0.2129 0.2368
REMARK 3 21 2.3231 - 2.2856 1.00 2607 142 0.2222 0.2513
REMARK 3 22 2.2856 - 2.2505 1.00 2649 148 0.2421 0.2500
REMARK 3 23 2.2505 - 2.2174 1.00 2663 146 0.2416 0.2660
REMARK 3 24 2.2174 - 2.1862 1.00 2598 150 0.2591 0.2971
REMARK 3 25 2.1862 - 2.1566 1.00 2701 142 0.2806 0.2811
REMARK 3 26 2.1566 - 2.1286 0.98 2595 139 0.3179 0.3374
REMARK 3 27 2.1286 - 2.1020 0.89 2350 125 0.3350 0.3691
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.730
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.47
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 3718
REMARK 3 ANGLE : 0.531 5134
REMARK 3 CHIRALITY : 0.040 565
REMARK 3 PLANARITY : 0.003 540
REMARK 3 DIHEDRAL : 15.952 2153
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5K97 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1000221899.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-SEP-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : ?76.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 12.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1158
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39124
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 13.80
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5
REMARK 200 DATA REDUNDANCY IN SHELL : 10.40
REMARK 200 R MERGE FOR SHELL (I) : 0.65100
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.6
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% MPEG 2K, 20% KCL, 5% ETHYLENE
REMARK 280 GLYCOL, 100 MM HEPES PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 283K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 34.84933
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 69.69867
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 69.69867
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 34.84933
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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, E, F, G
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 518 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 604 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 930 LIES ON A SPECIAL POSITION.
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 DA G 2
REMARK 465 DA G 3
REMARK 465 DC G 4
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 512 O HOH A 822 2.05
REMARK 500 O HOH D 134 O HOH D 184 2.07
REMARK 500 O HOH A 763 O HOH A 927 2.08
REMARK 500 O HOH D 123 O HOH E 116 2.09
REMARK 500 O HOH D 158 O HOH D 166 2.12
REMARK 500 O HOH A 578 O HOH A 642 2.12
REMARK 500 O HOH A 536 O HOH A 677 2.14
REMARK 500 O HOH A 562 O HOH A 775 2.17
REMARK 500 O HOH A 771 O HOH A 916 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 DT E 7 P DT E 7 OP3 -0.128
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 GLU A 120 -74.90 -89.28
REMARK 500 SER A 157 -117.43 -145.09
REMARK 500 LYS A 200 75.70 51.83
REMARK 500 LYS A 254 -52.75 75.36
REMARK 500 LEU A 275 32.78 -99.21
REMARK 500 GLN A 315 31.23 70.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 938 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A 939 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH E 151 DISTANCE = 5.83 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SM A 401 SM
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 2 N
REMARK 620 2 GLU A 160 OE2 133.4
REMARK 620 3 ASP A 181 OD1 48.6 101.0
REMARK 620 4 ASP A 181 OD2 60.0 138.4 55.5
REMARK 620 5 HOH A 689 O 120.3 97.6 159.9 105.0
REMARK 620 6 DT E 7 OP3 99.0 50.9 106.9 158.1 90.8
REMARK 620 7 DT E 7 OP1 51.6 91.2 75.4 111.3 111.9 47.5
REMARK 620 8 DT E 7 OP2 84.5 88.5 122.6 132.6 65.1 41.8 47.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SM A 408 SM
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 49 O
REMARK 620 2 ASP A 51 OD1 86.1
REMARK 620 3 ASP A 51 OD2 86.0 42.2
REMARK 620 4 HOH A 724 O 60.4 119.5 83.7
REMARK 620 5 HOH A 803 O 113.4 75.1 113.8 161.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SM A 406 SM
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 57 OE1
REMARK 620 2 GLU A 57 OE2 55.1
REMARK 620 3 GLU A 285 OE1 58.9 103.1
REMARK 620 4 GLU A 285 OE2 58.5 103.9 2.0
REMARK 620 5 GLU A 313 OE1 90.8 143.5 41.5 40.4
REMARK 620 6 GLN A 342 O 106.2 150.9 50.0 49.7 18.8
REMARK 620 7 HOH A 537 O 141.9 140.3 115.6 114.5 74.1 68.7
REMARK 620 8 HOH A 588 O 70.5 99.9 91.2 89.3 77.0 92.6 72.0
REMARK 620 9 HOH A 598 O 109.4 75.3 163.4 161.6 134.9 133.8 65.1 73.0
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SM A 407 SM
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 57 OE1
REMARK 620 2 GLU A 59 OE1 78.5
REMARK 620 3 GLU A 59 OE2 105.5 52.8
REMARK 620 4 GLU A 313 OE2 66.8 71.3 123.5
REMARK 620 5 GLN A 342 O 124.2 94.1 113.1 58.7
REMARK 620 6 GLN A 342 OXT 125.6 94.3 112.1 60.0 1.4
REMARK 620 7 HOH A 589 O 147.5 123.4 77.3 139.1 81.2 80.0
REMARK 620 8 HOH A 639 O 148.6 78.1 75.9 86.0 38.1 37.0 63.9
REMARK 620 9 HOH A 668 O 75.3 115.3 79.6 139.4 148.5 147.9 73.5 134.3
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SM A 402 SM
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 86 OD1
REMARK 620 2 ASP A 86 OD2 41.7
REMARK 620 3 GLU A 158 OE1 93.2 129.6
REMARK 620 4 GLU A 160 OE1 97.3 124.8 70.1
REMARK 620 5 HOH A 525 O 59.8 51.1 135.4 78.5
REMARK 620 6 HOH E 113 O 136.3 94.6 126.4 112.0 94.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SM A 409 SM
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 102 OE2
REMARK 620 2 HOH A 545 O 74.9
REMARK 620 3 HOH A 848 O 67.2 139.5
REMARK 620 4 HOH A 891 O 113.2 111.2 73.3
REMARK 620 5 HOH A 901 O 97.7 95.2 103.1 143.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SM A 404 SM
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 158 OE1
REMARK 620 2 GLU A 160 OE1 63.0
REMARK 620 3 GLU A 160 OE2 115.4 57.2
REMARK 620 4 HOH A 525 O 94.4 89.1 106.4
REMARK 620 5 HOH A 689 O 54.8 72.0 84.7 148.5
REMARK 620 6 DT E 7 OP3 142.7 123.6 68.3 121.1 90.4
REMARK 620 7 DT E 7 OP2 98.5 128.9 100.4 141.6 59.8 46.7
REMARK 620 8 HOH E 103 O 152.5 118.2 81.3 58.9 152.5 62.4 99.6
REMARK 620 9 HOH E 113 O 89.9 152.6 148.0 89.8 95.8 79.7 54.3 84.1
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SM A 403 SM
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 160 OE2
REMARK 620 2 ASP A 179 OD1 148.9
REMARK 620 3 ASP A 179 OD2 106.2 42.9
REMARK 620 4 ASP A 181 OD1 116.7 94.2 137.1
REMARK 620 5 DT E 7 OP3 60.9 104.0 75.7 126.7
REMARK 620 6 DT E 7 OP1 102.6 86.8 96.5 76.7 55.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 405 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 237 OG
REMARK 620 2 ILE A 238 O 98.8
REMARK 620 3 ILE A 241 O 119.2 71.8
REMARK 620 4 HOH A 640 O 79.2 121.7 60.2
REMARK 620 5 DT D 5 OP1 144.8 92.1 96.0 122.4
REMARK 620 6 HOH D 131 O 90.7 167.8 110.0 67.3 75.8
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 SM A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SM A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SM A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SM A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SM A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SM A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SM A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SM A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 410
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5K96 RELATED DB: PDB
DBREF 5K97 A 2 336 UNP P39748 FEN1_HUMAN 2 336
DBREF 5K97 D 1 18 PDB 5K97 5K97 1 18
DBREF 5K97 E 7 17 PDB 5K97 5K97 7 17
DBREF 5K97 F 1 7 PDB 5K97 5K97 1 7
DBREF 5K97 G 2 6 PDB 5K97 5K97 2 6
SEQADV 5K97 ASN A 233 UNP P39748 ASP 233 ENGINEERED MUTATION
SEQADV 5K97 LEU A 337 UNP P39748 EXPRESSION TAG
SEQADV 5K97 GLU A 338 UNP P39748 EXPRESSION TAG
SEQADV 5K97 VAL A 339 UNP P39748 EXPRESSION TAG
SEQADV 5K97 LEU A 340 UNP P39748 EXPRESSION TAG
SEQADV 5K97 PHE A 341 UNP P39748 EXPRESSION TAG
SEQADV 5K97 GLN A 342 UNP P39748 EXPRESSION TAG
SEQRES 1 A 341 GLY ILE GLN GLY LEU ALA LYS LEU ILE ALA ASP VAL ALA
SEQRES 2 A 341 PRO SER ALA ILE ARG GLU ASN ASP ILE LYS SER TYR PHE
SEQRES 3 A 341 GLY ARG LYS VAL ALA ILE ASP ALA SER MET SER ILE TYR
SEQRES 4 A 341 GLN PHE LEU ILE ALA VAL ARG GLN GLY GLY ASP VAL LEU
SEQRES 5 A 341 GLN ASN GLU GLU GLY GLU THR THR SER HIS LEU MET GLY
SEQRES 6 A 341 MET PHE TYR ARG THR ILE ARG MET MET GLU ASN GLY ILE
SEQRES 7 A 341 LYS PRO VAL TYR VAL PHE ASP GLY LYS PRO PRO GLN LEU
SEQRES 8 A 341 LYS SER GLY GLU LEU ALA LYS ARG SER GLU ARG ARG ALA
SEQRES 9 A 341 GLU ALA GLU LYS GLN LEU GLN GLN ALA GLN ALA ALA GLY
SEQRES 10 A 341 ALA GLU GLN GLU VAL GLU LYS PHE THR LYS ARG LEU VAL
SEQRES 11 A 341 LYS VAL THR LYS GLN HIS ASN ASP GLU CYS LYS HIS LEU
SEQRES 12 A 341 LEU SER LEU MET GLY ILE PRO TYR LEU ASP ALA PRO SER
SEQRES 13 A 341 GLU ALA GLU ALA SER CYS ALA ALA LEU VAL LYS ALA GLY
SEQRES 14 A 341 LYS VAL TYR ALA ALA ALA THR GLU ASP MET ASP CYS LEU
SEQRES 15 A 341 THR PHE GLY SER PRO VAL LEU MET ARG HIS LEU THR ALA
SEQRES 16 A 341 SER GLU ALA LYS LYS LEU PRO ILE GLN GLU PHE HIS LEU
SEQRES 17 A 341 SER ARG ILE LEU GLN GLU LEU GLY LEU ASN GLN GLU GLN
SEQRES 18 A 341 PHE VAL ASP LEU CYS ILE LEU LEU GLY SER ASN TYR CYS
SEQRES 19 A 341 GLU SER ILE ARG GLY ILE GLY PRO LYS ARG ALA VAL ASP
SEQRES 20 A 341 LEU ILE GLN LYS HIS LYS SER ILE GLU GLU ILE VAL ARG
SEQRES 21 A 341 ARG LEU ASP PRO ASN LYS TYR PRO VAL PRO GLU ASN TRP
SEQRES 22 A 341 LEU HIS LYS GLU ALA HIS GLN LEU PHE LEU GLU PRO GLU
SEQRES 23 A 341 VAL LEU ASP PRO GLU SER VAL GLU LEU LYS TRP SER GLU
SEQRES 24 A 341 PRO ASN GLU GLU GLU LEU ILE LYS PHE MET CYS GLY GLU
SEQRES 25 A 341 LYS GLN PHE SER GLU GLU ARG ILE ARG SER GLY VAL LYS
SEQRES 26 A 341 ARG LEU SER LYS SER ARG GLN GLY SER THR LEU GLU VAL
SEQRES 27 A 341 LEU PHE GLN
SEQRES 1 D 18 DA DC DT DC DT DG DC DC DT DC DA DA DG
SEQRES 2 D 18 DA DC DG DG DT
SEQRES 1 E 11 DT DG DA DG DG DC DA DG DA DG DT
SEQRES 1 F 7 DA DC DC DG DT DC DC
SEQRES 1 G 5 DA DA DC DT DT
HET SM A 401 1
HET SM A 402 1
HET SM A 403 1
HET SM A 404 1
HET K A 405 1
HET SM A 406 1
HET SM A 407 1
HET SM A 408 1
HET SM A 409 1
HET EDO A 410 10
HETNAM SM SAMARIUM (III) ION
HETNAM K POTASSIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 6 SM 8(SM 3+)
FORMUL 10 K K 1+
FORMUL 15 EDO C2 H6 O2
FORMUL 16 HOH *623(H2 O)
HELIX 1 AA1 GLY A 5 ALA A 14 1 10
HELIX 2 AA2 ASP A 22 PHE A 27 5 6
HELIX 3 AA3 ALA A 35 VAL A 46 1 12
HELIX 4 AA4 THR A 61 ASN A 77 1 17
HELIX 5 AA5 PRO A 90 LEU A 92 5 3
HELIX 6 AA6 LYS A 93 ALA A 117 1 25
HELIX 7 AA7 GLU A 122 LEU A 130 1 9
HELIX 8 AA8 THR A 134 GLY A 149 1 16
HELIX 9 AA9 GLU A 158 ALA A 169 1 12
HELIX 10 AB1 MET A 180 PHE A 185 1 6
HELIX 11 AB2 LEU A 209 GLY A 217 1 9
HELIX 12 AB3 ASN A 219 GLY A 231 1 13
HELIX 13 AB4 GLY A 242 LYS A 254 1 13
HELIX 14 AB5 SER A 255 LEU A 263 1 9
HELIX 15 AB6 LEU A 275 GLU A 285 1 11
HELIX 16 AB7 ASN A 302 CYS A 311 1 10
HELIX 17 AB8 SER A 317 THR A 336 1 20
SHEET 1 AA1 7 ILE A 18 GLU A 20 0
SHEET 2 AA1 7 GLN A 205 HIS A 208 -1 O GLU A 206 N ARG A 19
SHEET 3 AA1 7 VAL A 189 ARG A 192 -1 N LEU A 190 O PHE A 207
SHEET 4 AA1 7 ALA A 174 ALA A 176 1 N ALA A 175 O MET A 191
SHEET 5 AA1 7 LYS A 30 ASP A 34 1 N ALA A 32 O ALA A 176
SHEET 6 AA1 7 LYS A 80 PHE A 85 1 O VAL A 84 N ILE A 33
SHEET 7 AA1 7 TYR A 152 ASP A 154 1 O LEU A 153 N PHE A 85
SHEET 1 AA2 2 ARG A 47 GLN A 48 0
SHEET 2 AA2 2 ASP A 51 VAL A 52 -1 O ASP A 51 N GLN A 48
LINK N GLY A 2 SM SM A 401 1555 1555 3.38
LINK O GLY A 49 SM SM A 408 1555 1555 2.99
LINK OD1 ASP A 51 SM SM A 408 1555 1555 3.15
LINK OD2 ASP A 51 SM SM A 408 1555 1555 2.93
LINK OE1 GLU A 57 SM SM A 406 1555 1555 2.40
LINK OE2 GLU A 57 SM SM A 406 1555 1555 2.30
LINK OE1 GLU A 57 SM SM A 407 1555 1555 2.92
LINK OE1 GLU A 59 SM SM A 407 1555 1555 2.61
LINK OE2 GLU A 59 SM SM A 407 1555 1555 2.28
LINK OD1 ASP A 86 SM SM A 402 1555 1555 3.05
LINK OD2 ASP A 86 SM SM A 402 1555 1555 3.11
LINK OE2 GLU A 102 SM SM A 409 1555 1555 3.42
LINK OE1 GLU A 158 SM SM A 402 1555 1555 2.30
LINK OE1 GLU A 158 SM SM A 404 1555 1555 3.42
LINK OE2 GLU A 160 SM SM A 401 1555 1555 2.74
LINK OE1 GLU A 160 SM SM A 402 1555 1555 3.05
LINK OE2 GLU A 160 SM SM A 403 1555 1555 2.33
LINK OE1 GLU A 160 SM SM A 404 1555 1555 2.29
LINK OE2 GLU A 160 SM SM A 404 1555 1555 2.32
LINK OD1 ASP A 179 SM SM A 403 1555 1555 3.22
LINK OD2 ASP A 179 SM SM A 403 1555 1555 2.29
LINK OD1 ASP A 181 SM SM A 401 1555 1555 2.36
LINK OD2 ASP A 181 SM SM A 401 1555 1555 2.34
LINK OD1 ASP A 181 SM SM A 403 1555 1555 2.30
LINK OG SER A 237 K K A 405 1555 1555 2.95
LINK O ILE A 238 K K A 405 1555 1555 2.67
LINK O ILE A 241 K K A 405 1555 1555 3.02
LINK OE1 GLU A 285 SM SM A 406 1555 3434 2.73
LINK OE2 GLU A 285 SM SM A 406 1555 3434 2.40
LINK OE1 GLU A 313 SM SM A 406 1555 1555 2.36
LINK OE2 GLU A 313 SM SM A 407 1555 1555 2.31
LINK O GLN A 342 SM SM A 406 1555 4557 2.48
LINK O GLN A 342 SM SM A 407 1555 4557 2.47
LINK OXT GLN A 342 SM SM A 407 1555 4557 2.37
LINK SM SM A 401 O HOH A 689 1555 1555 2.28
LINK SM SM A 401 OP3 DT E 7 1555 1555 3.21
LINK SM SM A 401 OP1 DT E 7 1555 1555 2.31
LINK SM SM A 401 OP2 DT E 7 1555 1555 3.44
LINK SM SM A 402 O HOH A 525 1555 1555 2.71
LINK SM SM A 402 O HOH E 113 1555 1555 2.31
LINK SM SM A 403 OP3 DT E 7 1555 1555 2.74
LINK SM SM A 403 OP1 DT E 7 1555 1555 2.31
LINK SM SM A 404 O HOH A 525 1555 1555 2.88
LINK SM SM A 404 O HOH A 689 1555 1555 3.21
LINK SM SM A 404 OP3 DT E 7 1555 1555 2.30
LINK SM SM A 404 OP2 DT E 7 1555 1555 3.28
LINK SM SM A 404 O HOH E 103 1555 1555 2.32
LINK SM SM A 404 O HOH E 113 1555 1555 2.31
LINK K K A 405 O HOH A 640 1555 1555 2.73
LINK K K A 405 OP1 DT D 5 1555 1555 2.84
LINK K K A 405 O HOH D 131 1555 1555 2.85
LINK SM SM A 406 O HOH A 537 1555 2345 2.29
LINK SM SM A 406 O HOH A 588 1555 1555 2.37
LINK SM SM A 406 O HOH A 598 1555 2345 2.34
LINK SM SM A 407 O HOH A 589 1555 4557 2.34
LINK SM SM A 407 O HOH A 639 1555 4557 2.35
LINK SM SM A 407 O HOH A 668 1555 4557 2.36
LINK SM SM A 408 O HOH A 724 1555 1555 3.10
LINK SM SM A 408 O HOH A 803 1555 1555 2.31
LINK SM SM A 409 O HOH A 545 1555 1555 2.30
LINK SM SM A 409 O HOH A 848 1555 1555 3.31
LINK SM SM A 409 O HOH A 891 1555 6347 3.04
LINK SM SM A 409 O HOH A 901 1555 1555 2.86
SITE 1 AC1 7 GLY A 2 GLU A 160 ASP A 181 SM A 403
SITE 2 AC1 7 SM A 404 HOH A 689 DT E 7
SITE 1 AC2 6 ASP A 86 GLU A 158 GLU A 160 SM A 404
SITE 2 AC2 6 HOH A 525 HOH E 113
SITE 1 AC3 5 GLU A 160 ASP A 179 ASP A 181 SM A 401
SITE 2 AC3 5 DT E 7
SITE 1 AC4 8 GLU A 158 GLU A 160 SM A 401 SM A 402
SITE 2 AC4 8 HOH A 525 DT E 7 HOH E 103 HOH E 113
SITE 1 AC5 6 SER A 237 ILE A 238 ILE A 241 HOH A 640
SITE 2 AC5 6 DT D 5 HOH D 131
SITE 1 AC6 7 GLU A 57 GLU A 285 GLU A 313 GLN A 342
SITE 2 AC6 7 HOH A 537 HOH A 588 HOH A 598
SITE 1 AC7 7 GLU A 57 GLU A 59 GLU A 313 GLN A 342
SITE 2 AC7 7 HOH A 589 HOH A 639 HOH A 668
SITE 1 AC8 4 GLY A 49 ASP A 51 HOH A 724 HOH A 803
SITE 1 AC9 4 GLU A 102 HOH A 545 HOH A 891 HOH A 901
SITE 1 AD1 6 GLY A 2 ILE A 3 ASP A 179 MET A 180
SITE 2 AD1 6 HOH A 596 DG E 8
CRYST1 105.236 105.236 104.548 90.00 90.00 120.00 P 31 2 1 6
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 0.009502 0.005486 0.000000 0.00000
SCALE2 0.000000 0.010972 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009565 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
