HEADER RIBOSOMAL PROTEIN 19-OCT-10 3PAF
TITLE M. JANNASCHII L7AE MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 50S RIBOSOMAL PROTEIN L7AE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOCALDOCOCCUS JANNASCHII;
SOURCE 3 ORGANISM_COMMON: METHANOCOCCUS JANNASCHII;
SOURCE 4 ORGANISM_TAXID: 2190;
SOURCE 5 GENE: RPL7AE, MJ1203;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 ROSETTA DE3;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET 28A
KEYWDS RNA BINDING PROTEIN, ALPHA BETA SANDWICH, METHYLATION CORE PROTEIN,
KEYWDS 2 K-TURN RNA BINDING, NUCLEOLUS, RIBOSOMAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.BISWAS,E.S.MAXWELL
REVDAT 3 06-SEP-23 3PAF 1 REMARK SEQADV
REVDAT 2 08-NOV-17 3PAF 1 REMARK
REVDAT 1 02-NOV-11 3PAF 0
JRNL AUTH S.BISWAS,K.T.GAGNON,C.MATTOS,B.A.BROWN,E.S.MAXWELL
JRNL TITL STRUCTURE AND STABILITY OF M.JANNASCHII L7AE EL9 KTOQ MUTANT
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.2_432)
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.25
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.8
REMARK 3 NUMBER OF REFLECTIONS : 24624
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) : 0.183
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 1260
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 24.2514 - 3.5407 1.00 3121 167 0.1634 0.1571
REMARK 3 2 3.5407 - 2.8117 1.00 3010 143 0.1760 0.2219
REMARK 3 3 2.8117 - 2.4567 1.00 2963 152 0.1937 0.2411
REMARK 3 4 2.4567 - 2.2323 0.99 2918 151 0.1870 0.2516
REMARK 3 5 2.2323 - 2.0723 0.96 2777 165 0.1947 0.2279
REMARK 3 6 2.0723 - 1.9502 0.88 2568 148 0.2013 0.2503
REMARK 3 7 1.9502 - 1.8526 0.80 2307 132 0.1974 0.2397
REMARK 3 8 1.8526 - 1.7720 0.69 2002 101 0.2231 0.2316
REMARK 3 9 1.7720 - 1.7000 0.58 1698 101 0.2523 0.2930
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 1.13
REMARK 3 K_SOL : 0.36
REMARK 3 B_SOL : 42.77
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 21.14350
REMARK 3 B22 (A**2) : -11.39630
REMARK 3 B33 (A**2) : -9.74720
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 : 0.009 1830
REMARK 3 ANGLE : 1.180 2476
REMARK 3 CHIRALITY : 0.095 294
REMARK 3 PLANARITY : 0.005 320
REMARK 3 DIHEDRAL : 14.575 698
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): -0.8711 20.3060 -20.2133
REMARK 3 T TENSOR
REMARK 3 T11: 0.3020 T22: 0.1061
REMARK 3 T33: 0.1148 T12: -0.0014
REMARK 3 T13: 0.0403 T23: -0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 0.9423 L22: 2.3136
REMARK 3 L33: 0.9273 L12: 0.4696
REMARK 3 L13: -0.5029 L23: -0.5870
REMARK 3 S TENSOR
REMARK 3 S11: 0.0425 S12: -0.0538 S13: 0.0510
REMARK 3 S21: 0.6991 S22: -0.0639 S23: 0.1314
REMARK 3 S31: -0.2196 S32: 0.0328 S33: -0.0159
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): 17.1011 23.0252 -43.3653
REMARK 3 T TENSOR
REMARK 3 T11: 0.2269 T22: 0.1785
REMARK 3 T33: 0.3473 T12: -0.0414
REMARK 3 T13: 0.1253 T23: 0.0417
REMARK 3 L TENSOR
REMARK 3 L11: 1.5786 L22: 1.4601
REMARK 3 L33: 1.9620 L12: -1.2218
REMARK 3 L13: -0.5564 L23: 0.2956
REMARK 3 S TENSOR
REMARK 3 S11: 0.1481 S12: 0.0401 S13: 0.3726
REMARK 3 S21: -0.1760 S22: -0.0942 S23: -0.5750
REMARK 3 S31: -0.3431 S32: 0.1165 S33: -0.0829
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 3PAF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-10.
REMARK 100 THE DEPOSITION ID IS D_1000062157.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-AUG-08
REMARK 200 TEMPERATURE (KELVIN) : 200
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24624
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.2
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : 0.07400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 59.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.51900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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: PDB ENTRY 1ZWZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 2000MME, 0.1M SODIUM ACETATE,
REMARK 280 0.2M AMMONIUM SULFATE, PH 4.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 21.72150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.51950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.81700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.51950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.72150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.81700
REMARK 290 SMTRY3 4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 MET A 1 CG SD CE
REMARK 470 LYS A 8 CG CD CE NZ
REMARK 470 LYS A 15 CG CD CE NZ
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 LYS B 116 47.80 -84.91
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 SO4 A 118
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 119
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 118
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 119
DBREF 3PAF A 1 117 UNP P54066 RL7A_METJA 1 117
DBREF 3PAF B 1 117 UNP P54066 RL7A_METJA 1 117
SEQADV 3PAF GLN A 26 UNP P54066 LYS 26 ENGINEERED MUTATION
SEQADV 3PAF VAL A 87 UNP P54066 LEU 87 ENGINEERED MUTATION
SEQADV 3PAF SER A 88 UNP P54066 GLU 88 ENGINEERED MUTATION
SEQADV 3PAF ARG A 89 UNP P54066 VAL 89 ENGINEERED MUTATION
SEQADV 3PAF PRO A 90 UNP P54066 ALA 90 ENGINEERED MUTATION
SEQADV 3PAF GLN B 26 UNP P54066 LYS 26 ENGINEERED MUTATION
SEQADV 3PAF VAL B 87 UNP P54066 LEU 87 ENGINEERED MUTATION
SEQADV 3PAF SER B 88 UNP P54066 GLU 88 ENGINEERED MUTATION
SEQADV 3PAF ARG B 89 UNP P54066 VAL 89 ENGINEERED MUTATION
SEQADV 3PAF PRO B 90 UNP P54066 ALA 90 ENGINEERED MUTATION
SEQRES 1 A 117 MET ALA VAL TYR VAL LYS PHE LYS VAL PRO GLU GLU ILE
SEQRES 2 A 117 GLN LYS GLU LEU LEU ASP ALA VAL ALA LYS ALA GLN GLN
SEQRES 3 A 117 ILE LYS LYS GLY ALA ASN GLU VAL THR LYS ALA VAL GLU
SEQRES 4 A 117 ARG GLY ILE ALA LYS LEU VAL ILE ILE ALA GLU ASP VAL
SEQRES 5 A 117 LYS PRO GLU GLU VAL VAL ALA HIS LEU PRO TYR LEU CYS
SEQRES 6 A 117 GLU GLU LYS GLY ILE PRO TYR ALA TYR VAL ALA SER LYS
SEQRES 7 A 117 GLN ASP LEU GLY LYS ALA ALA GLY VAL SER ARG PRO ALA
SEQRES 8 A 117 SER SER VAL ALA ILE ILE ASN GLU GLY ASP ALA GLU GLU
SEQRES 9 A 117 LEU LYS VAL LEU ILE GLU LYS VAL ASN VAL LEU LYS GLN
SEQRES 1 B 117 MET ALA VAL TYR VAL LYS PHE LYS VAL PRO GLU GLU ILE
SEQRES 2 B 117 GLN LYS GLU LEU LEU ASP ALA VAL ALA LYS ALA GLN GLN
SEQRES 3 B 117 ILE LYS LYS GLY ALA ASN GLU VAL THR LYS ALA VAL GLU
SEQRES 4 B 117 ARG GLY ILE ALA LYS LEU VAL ILE ILE ALA GLU ASP VAL
SEQRES 5 B 117 LYS PRO GLU GLU VAL VAL ALA HIS LEU PRO TYR LEU CYS
SEQRES 6 B 117 GLU GLU LYS GLY ILE PRO TYR ALA TYR VAL ALA SER LYS
SEQRES 7 B 117 GLN ASP LEU GLY LYS ALA ALA GLY VAL SER ARG PRO ALA
SEQRES 8 B 117 SER SER VAL ALA ILE ILE ASN GLU GLY ASP ALA GLU GLU
SEQRES 9 B 117 LEU LYS VAL LEU ILE GLU LYS VAL ASN VAL LEU LYS GLN
HET SO4 A 118 5
HET SO4 A 119 5
HET ACT B 118 7
HET ACT B 119 7
HETNAM SO4 SULFATE ION
HETNAM ACT ACETATE ION
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 ACT 2(C2 H3 O2 1-)
FORMUL 7 HOH *186(H2 O)
HELIX 1 1 PRO A 10 ALA A 24 1 15
HELIX 2 2 GLY A 30 ARG A 40 1 11
HELIX 3 3 PRO A 54 VAL A 58 5 5
HELIX 4 4 HIS A 60 GLY A 69 1 10
HELIX 5 5 SER A 77 ALA A 85 1 9
HELIX 6 6 ASP A 101 GLN A 117 1 17
HELIX 7 7 PRO B 10 LYS B 23 1 14
HELIX 8 8 GLY B 30 ARG B 40 1 11
HELIX 9 9 PRO B 54 VAL B 58 5 5
HELIX 10 10 HIS B 60 GLY B 69 1 10
HELIX 11 11 SER B 77 ALA B 85 1 9
HELIX 12 12 ASP B 101 VAL B 114 1 14
SHEET 1 A 4 GLN A 26 LYS A 29 0
SHEET 2 A 4 SER A 93 ASN A 98 -1 O ALA A 95 N LYS A 28
SHEET 3 A 4 LEU A 45 ALA A 49 -1 N ILE A 47 O VAL A 94
SHEET 4 A 4 TYR A 72 VAL A 75 1 O ALA A 73 N ILE A 48
SHEET 1 B 4 GLN B 26 LYS B 29 0
SHEET 2 B 4 SER B 93 ASN B 98 -1 O ALA B 95 N LYS B 28
SHEET 3 B 4 LEU B 45 ALA B 49 -1 N LEU B 45 O ILE B 96
SHEET 4 B 4 TYR B 72 VAL B 75 1 O ALA B 73 N ILE B 48
CISPEP 1 LYS A 53 PRO A 54 0 0.48
CISPEP 2 LYS B 53 PRO B 54 0 -4.34
SITE 1 AC1 7 TYR A 63 VAL A 87 SER A 88 ARG A 89
SITE 2 AC1 7 HOH A 159 GLU B 39 LYS B 68
SITE 1 AC2 2 PRO A 10 GLU A 11
SITE 1 AC3 6 GLU A 110 GLY B 30 ALA B 31 SER B 92
SITE 2 AC3 6 HOH B 133 HOH B 143
SITE 1 AC4 3 GLU B 33 LYS B 36 ARG B 40
CRYST1 43.443 55.634 103.039 90.00 90.00 90.00 P 21 21 21 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 0.023019 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017975 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009705 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
