HEADER DNA BINDING PROTEIN 15-MAY-17 5NZY
TITLE CRYSTAL STRUCTURE OF DNA CROSS-LINK REPAIR PROTEIN 1A IN COMPLEX WITH
TITLE 2 CEFOTAXIME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA CROSS-LINK REPAIR 1A PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SNM1 HOMOLOG A,HSNM1A;
COMPND 5 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: DCLRE1A, KIAA0086, SNM1, SNM1A;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS EXONULCEASE, CEPHALOSPORIN, CROSS-LINK REPAIR, DCLRE1A, DNA BINDING
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.NEWMAN,H.AITKENHEAD,K.KUPINSKA,N.A.BURGESS-BROWN,R.TALON,
AUTHOR 2 T.KROJER,F.VON DELFT,C.H.ARROWSMITH,A.EDWARDS,C.BOUNTRA,O.GILEADI
REVDAT 3 17-JAN-24 5NZY 1 COMPND JRNL HETNAM
REVDAT 2 30-AUG-17 5NZY 1 REMARK
REVDAT 1 14-JUN-17 5NZY 0
JRNL AUTH J.A.NEWMAN,H.AITKENHEAD,K.KUPINSKA,N.A.BURGESS-BROWN,
JRNL AUTH 2 R.TALON,T.KROJER,F.VON DELFT,C.H.ARROWSMITH,A.EDWARDS,
JRNL AUTH 3 C.BOUNTRA,O.GILEADI
JRNL TITL CRYSTAL STRUCTURE OF DNA CROSS-LINK REPAIR PROTEIN 1A IN
JRNL TITL 2 COMPLEX WITH CEFOTAXIME
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.03
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 45975
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.890
REMARK 3 FREE R VALUE TEST SET COUNT : 2246
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 50.0573 - 3.9066 1.00 3024 165 0.1650 0.1937
REMARK 3 2 3.9066 - 3.1010 0.99 2849 162 0.1725 0.2121
REMARK 3 3 3.1010 - 2.7090 0.98 2800 145 0.2076 0.2302
REMARK 3 4 2.7090 - 2.4613 0.97 2767 136 0.2112 0.2454
REMARK 3 5 2.4613 - 2.2849 0.97 2746 143 0.2079 0.2946
REMARK 3 6 2.2849 - 2.1502 0.97 2725 160 0.2088 0.2871
REMARK 3 7 2.1502 - 2.0425 0.98 2770 125 0.2107 0.2699
REMARK 3 8 2.0425 - 1.9536 0.98 2767 152 0.2249 0.2558
REMARK 3 9 1.9536 - 1.8784 0.98 2726 161 0.2539 0.3140
REMARK 3 10 1.8784 - 1.8136 0.98 2753 139 0.2690 0.3763
REMARK 3 11 1.8136 - 1.7569 0.98 2743 143 0.2919 0.3035
REMARK 3 12 1.7569 - 1.7066 0.97 2727 144 0.2995 0.3391
REMARK 3 13 1.7066 - 1.6617 0.98 2747 124 0.3132 0.3497
REMARK 3 14 1.6617 - 1.6212 0.97 2696 136 0.3292 0.3137
REMARK 3 15 1.6212 - 1.5843 0.93 2603 114 0.3417 0.3956
REMARK 3 16 1.5843 - 1.5506 0.82 2286 97 0.4031 0.3873
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 30.660
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 2848
REMARK 3 ANGLE : 0.751 3879
REMARK 3 CHIRALITY : 0.052 428
REMARK 3 PLANARITY : 0.005 494
REMARK 3 DIHEDRAL : 13.473 1687
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 5NZY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1200004974.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-APR-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.975
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47632
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 112.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 1.35000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 5AGO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30 % PEG 1000, 0.1 M MIB BUFFER PH
REMARK 280 6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 278K
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 25.56100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.37150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.91500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.37150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.56100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.91500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
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 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 LYS A 698
REMARK 465 LYS A 699
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 GLU A 723 CG CD OE1 OE2
REMARK 470 ARG A 856 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 903 CG CD OE1 OE2
REMARK 470 LYS A 940 CG CD CE NZ
REMARK 470 LYS A 947 CD CE NZ
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 1232 O HOH A 1396 2.08
REMARK 500 O HOH A 1321 O HOH A 1380 2.14
REMARK 500 NE2 HIS A 737 O HOH A 1201 2.16
REMARK 500 OD2 ASP A 815 O HOH A 1201 2.19
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 HIS A 793 -105.68 -116.65
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 NI A1101 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 732 NE2
REMARK 620 2 HIS A 734 ND1 90.5
REMARK 620 3 HIS A 793 NE2 98.1 94.1
REMARK 620 4 ASP A 815 OD2 88.0 169.0 96.9
REMARK 620 5 HOH A1254 O 100.1 93.0 160.4 76.6
REMARK 620 6 HOH A1396 O 171.4 95.4 87.7 85.0 73.4
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 NI A 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CE3 A 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CE3 A 1103
DBREF 5NZY A 698 1040 UNP Q6PJP8 DCR1A_HUMAN 698 1040
SEQRES 1 A 343 LYS LYS THR CYS PRO PHE TYR LYS LYS ILE PRO GLY THR
SEQRES 2 A 343 GLY PHE THR VAL ASP ALA PHE GLN TYR GLY VAL VAL GLU
SEQRES 3 A 343 GLY CYS THR ALA TYR PHE LEU THR HIS PHE HIS SER ASP
SEQRES 4 A 343 HIS TYR ALA GLY LEU SER LYS HIS PHE THR PHE PRO VAL
SEQRES 5 A 343 TYR CYS SER GLU ILE THR GLY ASN LEU LEU LYS ASN LYS
SEQRES 6 A 343 LEU HIS VAL GLN GLU GLN TYR ILE HIS PRO LEU PRO LEU
SEQRES 7 A 343 ASP THR GLU CYS ILE VAL ASN GLY VAL LYS VAL VAL LEU
SEQRES 8 A 343 LEU ASP ALA ASN HIS CYS PRO GLY ALA VAL MET ILE LEU
SEQRES 9 A 343 PHE TYR LEU PRO ASN GLY THR VAL ILE LEU HIS THR GLY
SEQRES 10 A 343 ASP PHE ARG ALA ASP PRO SER MET GLU ARG SER LEU LEU
SEQRES 11 A 343 ALA ASP GLN LYS VAL HIS MET LEU TYR LEU ASP THR THR
SEQRES 12 A 343 TYR CYS SER PRO GLU TYR THR PHE PRO SER GLN GLN GLU
SEQRES 13 A 343 VAL ILE ARG PHE ALA ILE ASN THR ALA PHE GLU ALA VAL
SEQRES 14 A 343 THR LEU ASN PRO HIS ALA LEU VAL VAL CYS GLY THR TYR
SEQRES 15 A 343 SER ILE GLY LYS GLU LYS VAL PHE LEU ALA ILE ALA ASP
SEQRES 16 A 343 VAL LEU GLY SER LYS VAL GLY MET SER GLN GLU LYS TYR
SEQRES 17 A 343 LYS THR LEU GLN CYS LEU ASN ILE PRO GLU ILE ASN SER
SEQRES 18 A 343 LEU ILE THR THR ASP MET CYS SER SER LEU VAL HIS LEU
SEQRES 19 A 343 LEU PRO MET MET GLN ILE ASN PHE LYS GLY LEU GLN SER
SEQRES 20 A 343 HIS LEU LYS LYS CYS GLY GLY LYS TYR ASN GLN ILE LEU
SEQRES 21 A 343 ALA PHE ARG PRO THR GLY TRP THR HIS SER ASN LYS PHE
SEQRES 22 A 343 THR ARG ILE ALA ASP VAL ILE PRO GLN THR LYS GLY ASN
SEQRES 23 A 343 ILE SER ILE TYR GLY ILE PRO TYR SER GLU HIS SER SER
SEQRES 24 A 343 TYR LEU GLU MET LYS ARG PHE VAL GLN TRP LEU LYS PRO
SEQRES 25 A 343 GLN LYS ILE ILE PRO THR VAL ASN VAL GLY THR TRP LYS
SEQRES 26 A 343 SER ARG SER THR MET GLU LYS TYR PHE ARG GLU TRP LYS
SEQRES 27 A 343 LEU GLU ALA GLY TYR
HET NI A1101 1
HET CE3 A1102 30
HET CE3 A1103 30
HETNAM NI NICKEL (II) ION
HETNAM CE3 (6R,7R)-3-(ACETYLOXYMETHYL)-7-[[(2Z)-2-(2-AMINO-1,3-
HETNAM 2 CE3 THIAZOL-4-YL)-2-METHOXYIMINO-ETHANOYL]AMINO]-8-OXO-5-
HETNAM 3 CE3 THIA-1-AZABICY CLO[4.2.0]OCT-2-ENE-2-CARBOXYLIC ACID
HETSYN CE3 CEFOTAXIME
FORMUL 2 NI NI 2+
FORMUL 3 CE3 2(C16 H17 N5 O7 S2)
FORMUL 5 HOH *290(H2 O)
HELIX 1 AA1 PRO A 702 TYR A 704 5 3
HELIX 2 AA2 HIS A 734 ALA A 739 1 6
HELIX 3 AA3 GLU A 753 LEU A 763 1 11
HELIX 4 AA4 GLN A 766 GLN A 768 5 3
HELIX 5 AA5 ASP A 819 GLN A 830 5 12
HELIX 6 AA6 SER A 850 ASN A 869 1 20
HELIX 7 AA7 LYS A 883 LEU A 894 1 12
HELIX 8 AA8 SER A 901 CYS A 910 1 10
HELIX 9 AA9 GLU A 915 SER A 918 5 4
HELIX 10 AB1 ASP A 923 SER A 927 5 5
HELIX 11 AB2 MET A 935 ILE A 937 5 3
HELIX 12 AB3 ASN A 938 LYS A 947 1 10
HELIX 13 AB4 LYS A 948 LYS A 952 5 5
HELIX 14 AB5 SER A 996 LYS A 1008 1 13
HELIX 15 AB6 THR A 1020 GLY A 1039 1 20
SHEET 1 AA1 5 LYS A 706 ILE A 707 0
SHEET 2 AA1 5 PHE A 712 VAL A 714 -1 O PHE A 712 N ILE A 707
SHEET 3 AA1 5 ALA A 727 PHE A 729 1 O PHE A 729 N THR A 713
SHEET 4 AA1 5 VAL A 749 SER A 752 1 O TYR A 750 N TYR A 728
SHEET 5 AA1 5 ILE A 770 LEU A 773 1 O HIS A 771 N VAL A 749
SHEET 1 AA2 6 CYS A 779 VAL A 781 0
SHEET 2 AA2 6 VAL A 784 ASP A 790 -1 O VAL A 786 N CYS A 779
SHEET 3 AA2 6 VAL A 798 TYR A 803 -1 O LEU A 801 N VAL A 787
SHEET 4 AA2 6 VAL A 809 HIS A 812 -1 O ILE A 810 N PHE A 802
SHEET 5 AA2 6 MET A 834 LEU A 837 1 O TYR A 836 N LEU A 811
SHEET 6 AA2 6 LYS A1011 PRO A1014 1 O ILE A1013 N LEU A 835
SHEET 1 AA3 7 ILE A 920 THR A 921 0
SHEET 2 AA3 7 VAL A 898 GLY A 899 1 N VAL A 898 O THR A 921
SHEET 3 AA3 7 VAL A 929 PRO A 933 1 O VAL A 929 N GLY A 899
SHEET 4 AA3 7 ALA A 872 THR A 878 1 N VAL A 874 O HIS A 930
SHEET 5 AA3 7 GLN A 955 PRO A 961 1 O LEU A 957 N VAL A 875
SHEET 6 AA3 7 ILE A 984 ILE A 989 1 O TYR A 987 N ALA A 958
SHEET 7 AA3 7 GLN A 979 LYS A 981 -1 N GLN A 979 O ILE A 986
SSBOND 1 CYS A 925 CYS A 949 1555 1555 2.03
LINK NE2 HIS A 732 NI NI A1101 1555 1555 2.15
LINK ND1 HIS A 734 NI NI A1101 1555 1555 2.13
LINK NE2 HIS A 793 NI NI A1101 1555 1555 2.20
LINK OD2 ASP A 815 NI NI A1101 1555 1555 2.28
LINK NI NI A1101 O HOH A1254 1555 1555 2.02
LINK NI NI A1101 O HOH A1396 1555 1555 2.17
SITE 1 AC1 6 HIS A 732 HIS A 734 HIS A 793 ASP A 815
SITE 2 AC1 6 HOH A1254 HOH A1396
SITE 1 AC2 17 ALA A 828 GLN A 830 LYS A 831 HIS A 833
SITE 2 AC2 17 ILE A 937 ASN A 938 PHE A 939 ARG A 960
SITE 3 AC2 17 THR A 962 GLN A 979 ILE A 986 GLY A 988
SITE 4 AC2 17 HOH A1230 HOH A1260 HOH A1314 HOH A1331
SITE 5 AC2 17 HOH A1363
SITE 1 AC3 20 THR A 700 PRO A 702 PHE A 703 TYR A 704
SITE 2 AC3 20 GLN A 718 ASP A 736 PRO A 820 ARG A 824
SITE 3 AC3 20 SER A 850 GLN A 852 GLU A 853 ARG A1002
SITE 4 AC3 20 ASN A1017 VAL A1018 GLY A1019 HOH A1205
SITE 5 AC3 20 HOH A1236 HOH A1252 HOH A1275 HOH A1306
CRYST1 51.122 55.830 112.743 90.00 90.00 90.00 P 21 21 21 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 0.019561 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017912 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008870 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
