HEADER CHAPERONE 08-AUG-13 4M5S
TITLE HUMAN ALPHAB CRYSTALLIN CORE DOMAIN IN COMPLEX WITH C-TERMINAL PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-CRYSTALLIN B CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CORE DOMAIN (UNP RESIDUES 68-153);
COMPND 5 SYNONYM: ALPHA(B)-CRYSTALLIN, HEAT SHOCK PROTEIN BETA-5, HSPB5, RENAL
COMPND 6 CARCINOMA ANTIGEN NY-REN-27, ROSENTHAL FIBER COMPONENT;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: ALPHA-CRYSTALLIN B CHAIN;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: C-TERMINAL PEPTIDE (UNP RESIDUES 156-164);
COMPND 12 SYNONYM: ALPHA(B)-CRYSTALLIN, HEAT SHOCK PROTEIN BETA-5, HSPB5, RENAL
COMPND 13 CARCINOMA ANTIGEN NY-REN-27, ROSENTHAL FIBER COMPONENT;
COMPND 14 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: CRYA2, CRYAB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) ROSETTA 2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: CRYA2, CRYAB;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET15-MBP
KEYWDS SMALL HEAT SHOCK PROTEIN, AMYLOID, CHAPERONE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.LAGANOWSKY,D.CASCIO,M.R.SAWAYA,D.EISENBERG
REVDAT 3 28-FEB-24 4M5S 1 REMARK SEQADV
REVDAT 2 14-MAY-14 4M5S 1 JRNL
REVDAT 1 09-APR-14 4M5S 0
JRNL AUTH G.K.HOCHBERG,H.ECROYD,C.LIU,D.COX,D.CASCIO,M.R.SAWAYA,
JRNL AUTH 2 M.P.COLLIER,J.STROUD,J.A.CARVER,A.J.BALDWIN,C.V.ROBINSON,
JRNL AUTH 3 D.S.EISENBERG,J.L.BENESCH,A.LAGANOWSKY
JRNL TITL THE STRUCTURED CORE DOMAIN OF ALPHA B-CRYSTALLIN CAN PREVENT
JRNL TITL 2 AMYLOID FIBRILLATION AND ASSOCIATED TOXICITY.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 111 E1562 2014
JRNL REFN ISSN 0027-8424
JRNL PMID 24711386
JRNL DOI 10.1073/PNAS.1322673111
REMARK 2
REMARK 2 RESOLUTION. 1.37 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.1_1168
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) : 1.37
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.57
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 21882
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.158
REMARK 3 R VALUE (WORKING SET) : 0.156
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1095
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 19.5706 - 2.7378 0.95 2669 141 0.1816 0.1992
REMARK 3 2 2.7378 - 2.1740 0.99 2681 141 0.1643 0.1912
REMARK 3 3 2.1740 - 1.8995 0.99 2620 138 0.1295 0.1644
REMARK 3 4 1.8995 - 1.7259 0.98 2607 137 0.1215 0.1648
REMARK 3 5 1.7259 - 1.6023 0.98 2588 136 0.1188 0.1764
REMARK 3 6 1.6023 - 1.5078 0.98 2565 135 0.1183 0.1519
REMARK 3 7 1.5078 - 1.4323 0.97 2538 134 0.1399 0.2060
REMARK 3 8 1.4323 - 1.3700 0.96 2519 133 0.1743 0.2392
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) : 0.120
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.920
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.64
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.19
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 : 0.016 850
REMARK 3 ANGLE : 1.640 1148
REMARK 3 CHIRALITY : 0.135 126
REMARK 3 PLANARITY : 0.008 152
REMARK 3 DIHEDRAL : 15.965 341
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 4M5S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-AUG-13.
REMARK 100 THE DEPOSITION ID IS D_1000081501.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : CRYO-COOLED DOUBLE CRYSTAL
REMARK 200 SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21884
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.370
REMARK 200 RESOLUTION RANGE LOW (A) : 19.569
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.1300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.37
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.41
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.48600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.330
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SPG, PH 6.0, 25% PEG1500, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 17.69000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 23.93000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 61.42000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 17.69000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 23.93000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 61.42000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 17.69000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 23.93000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 61.42000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 17.69000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 23.93000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 61.42000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 110 CG CD OE1 OE2
REMARK 470 GLU B 164 CD OE1 OE2
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 ND2 ASN A 78 O HOH A 354 2.13
REMARK 500 NE2 HIS A 83 O1 SIN A 201 2.13
REMARK 500 O HOH A 352 O HOH B 211 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NE2 HIS A 83 O4 SIN A 201 3555 2.14
REMARK 500
REMARK 500 REMARK: NULL
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 ARG B 157 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIN A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF ALPHA-CRYSTALLIN B
REMARK 800 CHAIN
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4M5T RELATED DB: PDB
DBREF 4M5S A 68 153 UNP P02511 CRYAB_HUMAN 68 153
DBREF 4M5S B 156 164 UNP P02511 CRYAB_HUMAN 156 164
SEQADV 4M5S GLY A 67 UNP P02511 EXPRESSION TAG
SEQADV 4M5S GLY B 155 UNP P02511 EXPRESSION TAG
SEQRES 1 A 87 GLY MET ARG LEU GLU LYS ASP ARG PHE SER VAL ASN LEU
SEQRES 2 A 87 ASP VAL LYS HIS PHE SER PRO GLU GLU LEU LYS VAL LYS
SEQRES 3 A 87 VAL LEU GLY ASP VAL ILE GLU VAL HIS GLY LYS HIS GLU
SEQRES 4 A 87 GLU ARG GLN ASP GLU HIS GLY PHE ILE SER ARG GLU PHE
SEQRES 5 A 87 HIS ARG LYS TYR ARG ILE PRO ALA ASP VAL ASP PRO LEU
SEQRES 6 A 87 THR ILE THR SER SER LEU SER SER ASP GLY VAL LEU THR
SEQRES 7 A 87 VAL ASN GLY PRO ARG LYS GLN VAL SER
SEQRES 1 B 10 GLY GLU ARG THR ILE PRO ILE THR ARG GLU
HET SIN A 201 8
HETNAM SIN SUCCINIC ACID
FORMUL 3 SIN C4 H6 O4
FORMUL 4 HOH *70(H2 O)
HELIX 1 1 SER A 85 GLU A 87 5 3
HELIX 2 2 ASP A 129 ILE A 133 5 5
SHEET 1 A 5 MET A 68 LEU A 70 0
SHEET 2 A 5 ARG A 74 ASP A 80 -1 O SER A 76 N ARG A 69
SHEET 3 A 5 VAL A 142 PRO A 148 -1 O LEU A 143 N LEU A 79
SHEET 4 A 5 THR A 134 LEU A 137 -1 N SER A 136 O THR A 144
SHEET 5 A 5 ARG B 157 THR B 158 -1 O ARG B 157 N LEU A 137
SHEET 1 B 4 GLY A 112 ARG A 123 0
SHEET 2 B 4 VAL A 97 ASP A 109 -1 N HIS A 104 O ARG A 116
SHEET 3 B 4 LEU A 89 LEU A 94 -1 N LYS A 92 O GLU A 99
SHEET 4 B 4 ILE B 161 THR B 162 1 O THR B 162 N VAL A 91
SITE 1 AC1 2 HIS A 83 ARG A 116
SITE 1 AC2 34 ARG A 69 PRO A 86 VAL A 91 LYS A 92
SITE 2 AC2 34 VAL A 93 LEU A 94 LYS A 121 PRO A 130
SITE 3 AC2 34 LEU A 131 ILE A 133 SER A 135 SER A 136
SITE 4 AC2 34 LEU A 137 SER A 138 ARG A 149 LYS A 150
SITE 5 AC2 34 GLN A 151 VAL A 152 HOH A 305 HOH A 307
SITE 6 AC2 34 HOH A 332 HOH A 342 GLY B 155 HOH B 201
SITE 7 AC2 34 HOH B 202 HOH B 203 HOH B 204 HOH B 205
SITE 8 AC2 34 HOH B 206 HOH B 207 HOH B 208 HOH B 209
SITE 9 AC2 34 HOH B 210 HOH B 212
CRYST1 35.380 47.860 122.840 90.00 90.00 90.00 I 2 2 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.028265 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020894 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008141 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
