HEADER CHAPERONE, LIGAND BINDING 07-JAN-03 1NLQ
TITLE THE CRYSTAL STRUCTURE OF DROSOPHILA NLP-CORE PROVIDES INSIGHT INTO
TITLE 2 PENTAMER FORMATION AND HISTONE BINDING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEOPLASMIN-LIKE PROTEIN;
COMPND 3 CHAIN: A, B, C, D, E;
COMPND 4 FRAGMENT: N-TERMINAL CORE;
COMPND 5 SYNONYM: DNLP, CHROMATIN DECONDENSATION PROTEIN 1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 GENE: NLP OR CRP1 OR CG7917;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS DNLP, NUCLEOPLASMIN, CHAPERONE, HISTONE BINDING, LIGAND BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR V.M.H.NAMBOODIRI,S.DUTTA,I.V.AKEY,J.F.HEAD,C.W.AKEY
REVDAT 3 14-FEB-24 1NLQ 1 REMARK LINK
REVDAT 2 24-FEB-09 1NLQ 1 VERSN
REVDAT 1 01-MAR-03 1NLQ 0
JRNL AUTH V.M.H.NAMBOODIRI,S.DUTTA,I.V.AKEY,J.F.HEAD,C.W.AKEY
JRNL TITL THE CRYSTAL STRUCTURE OF DROSOPHILA NLP-CORE PROVIDES
JRNL TITL 2 INSIGHT INTO PENTAMER FORMATION AND HISTONE BINDING
JRNL REF STRUCTURE V. 11 175 2003
JRNL REFN ISSN 0969-2126
JRNL PMID 12575937
JRNL DOI 10.1016/S0969-2126(03)00007-8
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.15
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.4
REMARK 3 NUMBER OF REFLECTIONS : 76420
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) : 0.234
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 6207
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3140
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3787
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 358
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) : 1.25000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : -1.36000
REMARK 3 B13 (A**2) : 0.12000
REMARK 3 B23 (A**2) : -0.09000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.17
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) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NLQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-03.
REMARK 100 THE DEPOSITION ID IS D_1000017984.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-APR-01; NULL
REMARK 200 TEMPERATURE (KELVIN) : 100; NULL
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : NSLS; NSLS
REMARK 200 BEAMLINE : X8C; X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97950; 0.919997, 0.916998,
REMARK 200 0.919781
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111);
REMARK 200 SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : MIRRORS; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; NULL
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 80828
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
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 (%) : 97.3
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.03700
REMARK 200 R SYM (I) : 0.02900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 39.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.5
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.26500
REMARK 200 R SYM FOR SHELL (I) : 0.25300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, SODIUM CHLORIDE, MAGNESIUM
REMARK 280 CHLORIDE, TRIS, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 296.0K
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 30.04450
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 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A PENTAMER
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: 8650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
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 ALA A 2
REMARK 465 VAL A 108
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLU B 3
REMARK 465 ASP B 23
REMARK 465 GLU B 24
REMARK 465 ASP B 25
REMARK 465 TYR B 26
REMARK 465 ALA B 27
REMARK 465 ASP B 106
REMARK 465 ASP B 107
REMARK 465 VAL B 108
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 GLU C 3
REMARK 465 ASP C 23
REMARK 465 GLU C 24
REMARK 465 ASP C 25
REMARK 465 TYR C 26
REMARK 465 ALA C 27
REMARK 465 ARG C 28
REMARK 465 ASP C 106
REMARK 465 ASP C 107
REMARK 465 VAL C 108
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 GLU D 3
REMARK 465 VAL D 22
REMARK 465 ASP D 23
REMARK 465 GLU D 24
REMARK 465 ASP D 25
REMARK 465 TYR D 26
REMARK 465 ALA D 27
REMARK 465 ARG D 28
REMARK 465 LYS D 105
REMARK 465 ASP D 106
REMARK 465 ASP D 107
REMARK 465 VAL D 108
REMARK 465 MET E 1
REMARK 465 ALA E 2
REMARK 465 GLU E 3
REMARK 465 ASP E 23
REMARK 465 GLU E 24
REMARK 465 ASP E 25
REMARK 465 TYR E 26
REMARK 465 ASP E 106
REMARK 465 ASP E 107
REMARK 465 VAL E 108
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 3 CB CG CD OE1 OE2
REMARK 470 GLU A 24 CG CD OE1 OE2
REMARK 470 VAL B 22 CB CG1 CG2
REMARK 470 ARG B 28 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 105 CG CD CE NZ
REMARK 470 LYS E 105 CB CG 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 OE2 GLU A 52 O HOH A 408 2.10
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 21 54.23 -157.97
REMARK 500 VAL A 22 99.50 -46.55
REMARK 500 GLU A 24 -103.30 5.47
REMARK 500 TYR A 26 119.61 -176.76
REMARK 500 LYS A 57 -30.82 -39.14
REMARK 500 GLU A 71 -56.56 -127.39
REMARK 500 GLU A 83 62.49 32.65
REMARK 500 GLN B 61 104.29 -161.36
REMARK 500 GLU B 71 -58.47 -128.76
REMARK 500 GLU B 83 72.02 31.67
REMARK 500 SER B 84 146.63 179.69
REMARK 500 ASP C 21 -155.89 -128.57
REMARK 500 LYS C 68 119.82 -163.89
REMARK 500 GLU C 71 -56.83 -131.85
REMARK 500 GLU C 83 169.36 -45.47
REMARK 500 SER C 84 -113.16 -65.53
REMARK 500 LYS D 68 118.47 -165.89
REMARK 500 GLU D 71 -60.04 -132.68
REMARK 500 GLU D 83 74.99 27.15
REMARK 500 GLU E 71 -55.86 -129.27
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 E 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 16 OD2
REMARK 620 2 HOH A 403 O 86.4
REMARK 620 3 HOH A 404 O 86.3 89.3
REMARK 620 4 HOH A 405 O 93.7 178.5 92.3
REMARK 620 5 HOH A 406 O 92.7 90.4 179.0 88.1
REMARK 620 6 HOH A 407 O 168.3 81.9 93.8 98.0 87.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 16 OD2
REMARK 620 2 LEU E 90 O 83.4
REMARK 620 3 HOH E 426 O 96.4 93.6
REMARK 620 4 HOH E 440 O 150.5 84.6 57.6
REMARK 620 5 HOH E 463 O 69.5 152.5 85.0 116.8
REMARK 620 6 HOH E 464 O 104.3 90.3 159.3 102.6 100.7
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 E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1K5J RELATED DB: PDB
REMARK 900 A RELATED HISTONE CHAPERONE FROM XENOPUS LAEVIS
DBREF 1NLQ A 1 108 UNP Q27415 NLP_DROME 1 108
DBREF 1NLQ B 1 108 UNP Q27415 NLP_DROME 1 108
DBREF 1NLQ C 1 108 UNP Q27415 NLP_DROME 1 108
DBREF 1NLQ D 1 108 UNP Q27415 NLP_DROME 1 108
DBREF 1NLQ E 1 108 UNP Q27415 NLP_DROME 1 108
SEQRES 1 A 108 MET ALA GLU GLU SER PHE TYR GLY VAL THR LEU THR ALA
SEQRES 2 A 108 GLU SER ASP SER VAL THR TRP ASP VAL ASP GLU ASP TYR
SEQRES 3 A 108 ALA ARG GLY GLN LYS LEU VAL ILE LYS GLN ILE LEU LEU
SEQRES 4 A 108 GLY ALA GLU ALA LYS GLU ASN GLU PHE ASN VAL VAL GLU
SEQRES 5 A 108 VAL ASN THR PRO LYS ASP SER VAL GLN ILE PRO ILE ALA
SEQRES 6 A 108 VAL LEU LYS ALA GLY GLU THR ARG ALA VAL ASN PRO ASP
SEQRES 7 A 108 VAL GLU PHE TYR GLU SER LYS VAL THR PHE LYS LEU ILE
SEQRES 8 A 108 LYS GLY SER GLY PRO VAL TYR ILE HIS GLY HIS ASN ILE
SEQRES 9 A 108 LYS ASP ASP VAL
SEQRES 1 B 108 MET ALA GLU GLU SER PHE TYR GLY VAL THR LEU THR ALA
SEQRES 2 B 108 GLU SER ASP SER VAL THR TRP ASP VAL ASP GLU ASP TYR
SEQRES 3 B 108 ALA ARG GLY GLN LYS LEU VAL ILE LYS GLN ILE LEU LEU
SEQRES 4 B 108 GLY ALA GLU ALA LYS GLU ASN GLU PHE ASN VAL VAL GLU
SEQRES 5 B 108 VAL ASN THR PRO LYS ASP SER VAL GLN ILE PRO ILE ALA
SEQRES 6 B 108 VAL LEU LYS ALA GLY GLU THR ARG ALA VAL ASN PRO ASP
SEQRES 7 B 108 VAL GLU PHE TYR GLU SER LYS VAL THR PHE LYS LEU ILE
SEQRES 8 B 108 LYS GLY SER GLY PRO VAL TYR ILE HIS GLY HIS ASN ILE
SEQRES 9 B 108 LYS ASP ASP VAL
SEQRES 1 C 108 MET ALA GLU GLU SER PHE TYR GLY VAL THR LEU THR ALA
SEQRES 2 C 108 GLU SER ASP SER VAL THR TRP ASP VAL ASP GLU ASP TYR
SEQRES 3 C 108 ALA ARG GLY GLN LYS LEU VAL ILE LYS GLN ILE LEU LEU
SEQRES 4 C 108 GLY ALA GLU ALA LYS GLU ASN GLU PHE ASN VAL VAL GLU
SEQRES 5 C 108 VAL ASN THR PRO LYS ASP SER VAL GLN ILE PRO ILE ALA
SEQRES 6 C 108 VAL LEU LYS ALA GLY GLU THR ARG ALA VAL ASN PRO ASP
SEQRES 7 C 108 VAL GLU PHE TYR GLU SER LYS VAL THR PHE LYS LEU ILE
SEQRES 8 C 108 LYS GLY SER GLY PRO VAL TYR ILE HIS GLY HIS ASN ILE
SEQRES 9 C 108 LYS ASP ASP VAL
SEQRES 1 D 108 MET ALA GLU GLU SER PHE TYR GLY VAL THR LEU THR ALA
SEQRES 2 D 108 GLU SER ASP SER VAL THR TRP ASP VAL ASP GLU ASP TYR
SEQRES 3 D 108 ALA ARG GLY GLN LYS LEU VAL ILE LYS GLN ILE LEU LEU
SEQRES 4 D 108 GLY ALA GLU ALA LYS GLU ASN GLU PHE ASN VAL VAL GLU
SEQRES 5 D 108 VAL ASN THR PRO LYS ASP SER VAL GLN ILE PRO ILE ALA
SEQRES 6 D 108 VAL LEU LYS ALA GLY GLU THR ARG ALA VAL ASN PRO ASP
SEQRES 7 D 108 VAL GLU PHE TYR GLU SER LYS VAL THR PHE LYS LEU ILE
SEQRES 8 D 108 LYS GLY SER GLY PRO VAL TYR ILE HIS GLY HIS ASN ILE
SEQRES 9 D 108 LYS ASP ASP VAL
SEQRES 1 E 108 MET ALA GLU GLU SER PHE TYR GLY VAL THR LEU THR ALA
SEQRES 2 E 108 GLU SER ASP SER VAL THR TRP ASP VAL ASP GLU ASP TYR
SEQRES 3 E 108 ALA ARG GLY GLN LYS LEU VAL ILE LYS GLN ILE LEU LEU
SEQRES 4 E 108 GLY ALA GLU ALA LYS GLU ASN GLU PHE ASN VAL VAL GLU
SEQRES 5 E 108 VAL ASN THR PRO LYS ASP SER VAL GLN ILE PRO ILE ALA
SEQRES 6 E 108 VAL LEU LYS ALA GLY GLU THR ARG ALA VAL ASN PRO ASP
SEQRES 7 E 108 VAL GLU PHE TYR GLU SER LYS VAL THR PHE LYS LEU ILE
SEQRES 8 E 108 LYS GLY SER GLY PRO VAL TYR ILE HIS GLY HIS ASN ILE
SEQRES 9 E 108 LYS ASP ASP VAL
HET MG A 402 1
HET MG E 401 1
HETNAM MG MAGNESIUM ION
FORMUL 6 MG 2(MG 2+)
FORMUL 8 HOH *358(H2 O)
HELIX 1 1 PRO A 56 SER A 59 5 4
HELIX 2 2 PRO B 56 SER B 59 5 4
HELIX 3 3 PRO C 56 SER C 59 5 4
HELIX 4 4 PRO E 56 SER E 59 5 4
SHEET 1 A 4 GLU A 4 LEU A 11 0
SHEET 2 A 4 VAL A 97 ILE A 104 -1 O ASN A 103 N SER A 5
SHEET 3 A 4 LYS A 31 LEU A 39 -1 N GLN A 36 O HIS A 100
SHEET 4 A 4 ALA A 74 VAL A 75 -1 O VAL A 75 N ILE A 37
SHEET 1 B 4 GLU A 4 LEU A 11 0
SHEET 2 B 4 VAL A 97 ILE A 104 -1 O ASN A 103 N SER A 5
SHEET 3 B 4 LYS A 31 LEU A 39 -1 N GLN A 36 O HIS A 100
SHEET 4 B 4 VAL A 79 TYR A 82 -1 O VAL A 79 N ILE A 34
SHEET 1 C 4 SER A 17 TRP A 20 0
SHEET 2 C 4 VAL A 86 LYS A 92 -1 O VAL A 86 N TRP A 20
SHEET 3 C 4 PHE A 48 THR A 55 -1 N GLU A 52 O LYS A 89
SHEET 4 C 4 VAL A 60 LYS A 68 -1 O LEU A 67 N ASN A 49
SHEET 1 D 4 SER B 5 LEU B 11 0
SHEET 2 D 4 VAL B 97 ILE B 104 -1 O GLY B 101 N TYR B 7
SHEET 3 D 4 LYS B 31 LEU B 39 -1 N GLN B 36 O HIS B 100
SHEET 4 D 4 ALA B 74 VAL B 75 -1 O VAL B 75 N ILE B 37
SHEET 1 E 4 SER B 5 LEU B 11 0
SHEET 2 E 4 VAL B 97 ILE B 104 -1 O GLY B 101 N TYR B 7
SHEET 3 E 4 LYS B 31 LEU B 39 -1 N GLN B 36 O HIS B 100
SHEET 4 E 4 VAL B 79 TYR B 82 -1 O VAL B 79 N ILE B 34
SHEET 1 F 4 SER B 17 TRP B 20 0
SHEET 2 F 4 VAL B 86 LYS B 92 -1 O VAL B 86 N TRP B 20
SHEET 3 F 4 PHE B 48 THR B 55 -1 N ASN B 54 O THR B 87
SHEET 4 F 4 VAL B 60 LYS B 68 -1 O LEU B 67 N ASN B 49
SHEET 1 G 4 SER C 5 LEU C 11 0
SHEET 2 G 4 VAL C 97 ILE C 104 -1 O GLY C 101 N TYR C 7
SHEET 3 G 4 LYS C 31 LEU C 39 -1 N GLN C 36 O HIS C 100
SHEET 4 G 4 ALA C 74 VAL C 75 -1 O VAL C 75 N ILE C 37
SHEET 1 H 4 SER C 5 LEU C 11 0
SHEET 2 H 4 VAL C 97 ILE C 104 -1 O GLY C 101 N TYR C 7
SHEET 3 H 4 LYS C 31 LEU C 39 -1 N GLN C 36 O HIS C 100
SHEET 4 H 4 VAL C 79 PHE C 81 -1 O VAL C 79 N ILE C 34
SHEET 1 I 4 SER C 17 TRP C 20 0
SHEET 2 I 4 VAL C 86 LYS C 92 -1 O VAL C 86 N TRP C 20
SHEET 3 I 4 PHE C 48 THR C 55 -1 N GLU C 52 O LYS C 89
SHEET 4 I 4 VAL C 60 LYS C 68 -1 O ILE C 64 N VAL C 51
SHEET 1 J 4 SER D 5 LEU D 11 0
SHEET 2 J 4 VAL D 97 ILE D 104 -1 O ILE D 99 N VAL D 9
SHEET 3 J 4 LYS D 31 LEU D 39 -1 N GLN D 36 O HIS D 100
SHEET 4 J 4 ALA D 74 VAL D 75 -1 O VAL D 75 N ILE D 37
SHEET 1 K 4 SER D 5 LEU D 11 0
SHEET 2 K 4 VAL D 97 ILE D 104 -1 O ILE D 99 N VAL D 9
SHEET 3 K 4 LYS D 31 LEU D 39 -1 N GLN D 36 O HIS D 100
SHEET 4 K 4 VAL D 79 TYR D 82 -1 O VAL D 79 N ILE D 34
SHEET 1 L 4 SER D 17 TRP D 20 0
SHEET 2 L 4 VAL D 86 LYS D 92 -1 O VAL D 86 N TRP D 20
SHEET 3 L 4 PHE D 48 THR D 55 -1 N GLU D 52 O LYS D 89
SHEET 4 L 4 VAL D 60 LYS D 68 -1 O ILE D 64 N VAL D 51
SHEET 1 M 4 SER E 5 LEU E 11 0
SHEET 2 M 4 VAL E 97 ILE E 104 -1 O GLY E 101 N TYR E 7
SHEET 3 M 4 LYS E 31 LEU E 39 -1 N GLN E 36 O HIS E 100
SHEET 4 M 4 ALA E 74 VAL E 75 -1 O VAL E 75 N ILE E 37
SHEET 1 N 4 SER E 5 LEU E 11 0
SHEET 2 N 4 VAL E 97 ILE E 104 -1 O GLY E 101 N TYR E 7
SHEET 3 N 4 LYS E 31 LEU E 39 -1 N GLN E 36 O HIS E 100
SHEET 4 N 4 VAL E 79 TYR E 82 -1 O VAL E 79 N ILE E 34
SHEET 1 O 4 SER E 17 TRP E 20 0
SHEET 2 O 4 VAL E 86 LYS E 92 -1 O VAL E 86 N TRP E 20
SHEET 3 O 4 PHE E 48 THR E 55 -1 N GLU E 52 O LYS E 89
SHEET 4 O 4 VAL E 60 LYS E 68 -1 O LEU E 67 N ASN E 49
LINK OD2 ASP A 16 MG MG E 401 1555 1555 2.14
LINK MG MG A 402 OD2 ASP E 16 1555 1555 3.12
LINK MG MG A 402 O LEU E 90 1555 1555 2.84
LINK MG MG A 402 O HOH E 426 1555 1555 2.75
LINK MG MG A 402 O HOH E 440 1555 1555 2.71
LINK MG MG A 402 O HOH E 463 1555 1555 2.29
LINK MG MG A 402 O HOH E 464 1555 1555 3.05
LINK O HOH A 403 MG MG E 401 1555 1555 2.15
LINK O HOH A 404 MG MG E 401 1555 1555 2.09
LINK O HOH A 405 MG MG E 401 1555 1555 2.13
LINK O HOH A 406 MG MG E 401 1555 1555 2.16
LINK O HOH A 407 MG MG E 401 1555 1555 1.85
CISPEP 1 GLY A 95 PRO A 96 0 0.04
CISPEP 2 GLY B 95 PRO B 96 0 0.19
CISPEP 3 GLY C 95 PRO C 96 0 0.16
CISPEP 4 GLY D 95 PRO D 96 0 0.29
CISPEP 5 GLY E 95 PRO E 96 0 -0.03
SITE 1 AC1 6 ASP A 16 HOH A 403 HOH A 404 HOH A 405
SITE 2 AC1 6 HOH A 406 HOH A 407
SITE 1 AC2 6 ASP E 16 LEU E 90 HOH E 426 HOH E 440
SITE 2 AC2 6 HOH E 463 HOH E 464
CRYST1 57.608 60.089 73.426 90.00 90.79 90.00 P 1 21 1 10
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 0.017359 0.000000 0.000239 0.00000
SCALE2 0.000000 0.016642 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013620 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
