HEADER CHAPERONE 09-JAN-11 3Q9Q
TITLE HSPB1 FRAGMENT SECOND CRYSTAL FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEAT SHOCK PROTEIN BETA-1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 90-171;
COMPND 5 SYNONYM: HSPB1, 28 KDA HEAT SHOCK PROTEIN, ESTROGEN-REGULATED 24 KDA
COMPND 6 PROTEIN, HEAT SHOCK 27 KDA PROTEIN, HSP 27, STRESS-RESPONSIVE PROTEIN
COMPND 7 27, SRP27;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HSPB1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPEP-TEV
KEYWDS ALPHA-CRYSTALLIN DOMAIN, CHAPERONE, CHARCOT-MARIE-TOOTH DISEASE,
KEYWDS 2 NEURONOPATHY, IG-LIKE FOLD, STRESS RESPONSE, INTRA-CELLULAR
KEYWDS 3 CHAPERONES, NUCLEUS
EXPDTA X-RAY DIFFRACTION
AUTHOR E.V.BARANOVA,S.BEELEN,N.B.GUSEV,S.V.STRELKOV
REVDAT 1 06-JUL-11 3Q9Q 0
JRNL AUTH E.V.BARANOVA,S.D.WEEKS,S.BEELEN,O.V.BUKACH,N.B.GUSEV,
JRNL AUTH 2 S.V.STRELKOV
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF ALPHA-CRYSTALLIN DOMAIN
JRNL TITL 2 DIMERS OF HUMAN SMALL HEAT SHOCK PROTEINS HSPB1 AND HSPB6
JRNL REF J.MOL.BIOL. 2011
JRNL REFN ESSN 1089-8638
JRNL PMID 21641913
JRNL DOI 10.1016/J.JMB.2011.05.024
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.99
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 10572
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.283
REMARK 3 R VALUE (WORKING SET) : 0.281
REMARK 3 FREE R VALUE : 0.312
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.480
REMARK 3 FREE R VALUE TEST SET COUNT : 791
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 39.9969 - 3.9968 1.00 1781 145 0.2735 0.3150
REMARK 3 2 3.9968 - 3.1728 1.00 1656 123 0.2658 0.2561
REMARK 3 3 3.1728 - 2.7718 1.00 1603 129 0.2863 0.3364
REMARK 3 4 2.7718 - 2.5184 1.00 1597 130 0.2959 0.3744
REMARK 3 5 2.5184 - 2.3379 1.00 1587 130 0.2939 0.3096
REMARK 3 6 2.3379 - 2.2001 1.00 1557 134 0.3101 0.3469
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 : 0.38
REMARK 3 B_SOL : 71.60
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.020
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.710
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 66.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.55610
REMARK 3 B22 (A**2) : -0.55610
REMARK 3 B33 (A**2) : 1.11220
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : -0.00000
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 : 0.005 1184
REMARK 3 ANGLE : 1.018 1618
REMARK 3 CHIRALITY : 0.081 189
REMARK 3 PLANARITY : 0.006 207
REMARK 3 DIHEDRAL : 17.612 437
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain A
REMARK 3 ORIGIN FOR THE GROUP (A): 22.5701 6.6768 14.7839
REMARK 3 T TENSOR
REMARK 3 T11: 0.1980 T22: 0.2220
REMARK 3 T33: 0.2284 T12: -0.0589
REMARK 3 T13: -0.0184 T23: 0.0379
REMARK 3 L TENSOR
REMARK 3 L11: 1.8172 L22: 1.4929
REMARK 3 L33: 1.4639 L12: -1.0723
REMARK 3 L13: 0.0844 L23: 0.0940
REMARK 3 S TENSOR
REMARK 3 S11: -0.0513 S12: 0.0700 S13: -0.0145
REMARK 3 S21: -0.0255 S22: -0.0499 S23: 0.0585
REMARK 3 S31: -0.0713 S32: -0.0139 S33: 0.0921
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain B
REMARK 3 ORIGIN FOR THE GROUP (A): 11.5577 19.9057 44.7233
REMARK 3 T TENSOR
REMARK 3 T11: 1.1362 T22: 0.4138
REMARK 3 T33: 0.3904 T12: -0.3424
REMARK 3 T13: -0.0314 T23: -0.0677
REMARK 3 L TENSOR
REMARK 3 L11: 1.7200 L22: -0.3140
REMARK 3 L33: 3.4008 L12: -2.3865
REMARK 3 L13: 1.0370 L23: -0.8235
REMARK 3 S TENSOR
REMARK 3 S11: 0.4724 S12: 0.1459 S13: -0.4618
REMARK 3 S21: -0.4661 S22: -0.3891 S23: -0.0265
REMARK 3 S31: -1.2831 S32: 0.7991 S33: -0.1256
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: chain A and (resseq 94:114 or resseq 116:
REMARK 3 126 or resseq 133:170 )
REMARK 3 SELECTION : chain B and (resseq 94:114 or resseq 116:
REMARK 3 126 or resseq 133:170 )
REMARK 3 ATOM PAIRS NUMBER : 529
REMARK 3 RMSD : 0.049
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3Q9Q COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JAN-11.
REMARK 100 THE RCSB ID CODE IS RCSB063371.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-FEB-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9999
REMARK 200 MONOCHROMATOR : SI(111) MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10572
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 43.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 9.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.76000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.000
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: 3Q9P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.2M AMMONIUM SULFATE, 0.2M DI-
REMARK 280 AMMONIUM TARTRATE, PH 5.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z
REMARK 290 6555 X-Y,X,Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 X,X-Y,-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 -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 0.00000
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 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 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 0.00000
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: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLY A 87
REMARK 465 GLY A 88
REMARK 465 GLN A 128
REMARK 465 ASP A 129
REMARK 465 GLU A 130
REMARK 465 HIS A 131
REMARK 465 GLY A 132
REMARK 465 LYS A 171
REMARK 465 GLY B 87
REMARK 465 GLY B 88
REMARK 465 SER B 89
REMARK 465 HIS B 90
REMARK 465 THR B 91
REMARK 465 ALA B 92
REMARK 465 ASP B 93
REMARK 465 ARG B 127
REMARK 465 GLN B 128
REMARK 465 ASP B 129
REMARK 465 GLU B 130
REMARK 465 HIS B 131
REMARK 465 GLY B 132
REMARK 465 LYS B 171
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 90 49.45 -107.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3Q9P RELATED DB: PDB
DBREF 3Q9Q A 90 171 UNP P04792 HSPB1_HUMAN 90 171
DBREF 3Q9Q B 90 171 UNP P04792 HSPB1_HUMAN 90 171
SEQADV 3Q9Q GLY A 87 UNP P04792 EXPRESSION TAG
SEQADV 3Q9Q GLY A 88 UNP P04792 EXPRESSION TAG
SEQADV 3Q9Q SER A 89 UNP P04792 EXPRESSION TAG
SEQADV 3Q9Q ALA A 125 UNP P04792 GLU 125 ENGINEERED MUTATION
SEQADV 3Q9Q ALA A 126 UNP P04792 GLU 126 ENGINEERED MUTATION
SEQADV 3Q9Q GLY B 87 UNP P04792 EXPRESSION TAG
SEQADV 3Q9Q GLY B 88 UNP P04792 EXPRESSION TAG
SEQADV 3Q9Q SER B 89 UNP P04792 EXPRESSION TAG
SEQADV 3Q9Q ALA B 125 UNP P04792 GLU 125 ENGINEERED MUTATION
SEQADV 3Q9Q ALA B 126 UNP P04792 GLU 126 ENGINEERED MUTATION
SEQRES 1 A 85 GLY GLY SER HIS THR ALA ASP ARG TRP ARG VAL SER LEU
SEQRES 2 A 85 ASP VAL ASN HIS PHE ALA PRO ASP GLU LEU THR VAL LYS
SEQRES 3 A 85 THR LYS ASP GLY VAL VAL GLU ILE THR GLY LYS HIS ALA
SEQRES 4 A 85 ALA ARG GLN ASP GLU HIS GLY TYR ILE SER ARG CYS PHE
SEQRES 5 A 85 THR ARG LYS TYR THR LEU PRO PRO GLY VAL ASP PRO THR
SEQRES 6 A 85 GLN VAL SER SER SER LEU SER PRO GLU GLY THR LEU THR
SEQRES 7 A 85 VAL GLU ALA PRO MET PRO LYS
SEQRES 1 B 85 GLY GLY SER HIS THR ALA ASP ARG TRP ARG VAL SER LEU
SEQRES 2 B 85 ASP VAL ASN HIS PHE ALA PRO ASP GLU LEU THR VAL LYS
SEQRES 3 B 85 THR LYS ASP GLY VAL VAL GLU ILE THR GLY LYS HIS ALA
SEQRES 4 B 85 ALA ARG GLN ASP GLU HIS GLY TYR ILE SER ARG CYS PHE
SEQRES 5 B 85 THR ARG LYS TYR THR LEU PRO PRO GLY VAL ASP PRO THR
SEQRES 6 B 85 GLN VAL SER SER SER LEU SER PRO GLU GLY THR LEU THR
SEQRES 7 B 85 VAL GLU ALA PRO MET PRO LYS
FORMUL 3 HOH *58(H2 O)
HELIX 1 1 ASP A 149 VAL A 153 5 5
HELIX 2 2 ASP B 149 VAL B 153 5 5
SHEET 1 A 3 ARG A 94 ASP A 100 0
SHEET 2 A 3 THR A 162 PRO A 168 -1 O ALA A 167 N TRP A 95
SHEET 3 A 3 SER A 154 LEU A 157 -1 N SER A 156 O THR A 164
SHEET 1 B 3 GLU A 108 LYS A 114 0
SHEET 2 B 3 VAL A 117 HIS A 124 -1 O GLU A 119 N LYS A 112
SHEET 3 B 3 ARG A 136 THR A 143 -1 O ARG A 140 N ILE A 120
SHEET 1 C 3 TRP B 95 ASP B 100 0
SHEET 2 C 3 THR B 162 ALA B 167 -1 O ALA B 167 N TRP B 95
SHEET 3 C 3 SER B 154 LEU B 157 -1 N SER B 156 O THR B 164
SHEET 1 D 3 GLU B 108 LYS B 114 0
SHEET 2 D 3 VAL B 117 HIS B 124 -1 O GLU B 119 N LYS B 112
SHEET 3 D 3 ARG B 136 THR B 143 -1 O ARG B 140 N ILE B 120
CISPEP 1 ASP B 115 GLY B 116 0 -3.86
CRYST1 74.455 74.455 119.971 90.00 90.00 120.00 P 6 2 2 24
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 0.013431 0.007754 0.000000 0.00000
SCALE2 0.000000 0.015509 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008335 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
