HEADER SIGNALING PROTEIN 13-AUG-10 3OEO
TITLE THE CRYSTAL STRUCTURE E. COLI SPY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SPHEROPLAST PROTEIN Y;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: MATURE FORM OF ECSPY, UNP RESIDUES 24-161;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: SPY, B1743, JW1732;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A+
KEYWDS LTXXQ, EXTRACYTOPLASMIC STRESS RESPONSE-RELATED, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR E.KWON,D.Y.KIM,C.A.GROSS,J.D.GROSS,K.K.KIM
REVDAT 3 21-FEB-24 3OEO 1 REMARK LINK
REVDAT 2 10-NOV-10 3OEO 1 JRNL
REVDAT 1 22-SEP-10 3OEO 0
JRNL AUTH E.KWON,D.Y.KIM,C.A.GROSS,J.D.GROSS,K.K.KIM
JRNL TITL THE CRYSTAL STRUCTURE ESCHERICHIA COLI SPY.
JRNL REF PROTEIN SCI. V. 19 2252 2010
JRNL REFN ISSN 0961-8368
JRNL PMID 20799348
JRNL DOI 10.1002/PRO.489
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 17348
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 + TEST SET) : 0.255
REMARK 3 R VALUE (WORKING SET) : 0.252
REMARK 3 FREE R VALUE : 0.300
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 915
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1252
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.3180
REMARK 3 BIN FREE R VALUE SET COUNT : 76
REMARK 3 BIN FREE R VALUE : 0.3540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3016
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 88
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 84.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -30.89000
REMARK 3 B22 (A**2) : -30.89000
REMARK 3 B33 (A**2) : 61.78000
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.119
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.074
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.226
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.139
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.922
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.894
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3048 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4060 ; 1.116 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 360 ; 6.004 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 172 ;37.661 ;25.814
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 668 ;19.766 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;16.226 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 432 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2268 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1824 ; 0.392 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2944 ; 0.726 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1224 ; 0.746 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1116 ; 1.261 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 4
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.263
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : -H, H+K, -L
REMARK 3 TWIN FRACTION : 0.250
REMARK 3 TWIN DOMAIN : 3
REMARK 3 TWIN OPERATOR : -H,-K,L
REMARK 3 TWIN FRACTION : 0.237
REMARK 3 TWIN DOMAIN : 4
REMARK 3 TWIN OPERATOR : -H-K, K, -L
REMARK 3 TWIN FRACTION : 0.250
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -10 A 9999
REMARK 3 ORIGIN FOR THE GROUP (A): -5.8830 -16.6220 6.0440
REMARK 3 T TENSOR
REMARK 3 T11: 0.2501 T22: 0.2194
REMARK 3 T33: 0.2095 T12: -0.0352
REMARK 3 T13: -0.1308 T23: -0.1308
REMARK 3 L TENSOR
REMARK 3 L11: 1.9775 L22: 0.6319
REMARK 3 L33: 9.9880 L12: 0.4863
REMARK 3 L13: -2.5245 L23: -1.9571
REMARK 3 S TENSOR
REMARK 3 S11: 0.1416 S12: 0.2000 S13: -0.2690
REMARK 3 S21: -0.1256 S22: -0.0840 S23: 0.1926
REMARK 3 S31: 0.2507 S32: -0.5468 S33: -0.0576
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B -10 B 9999
REMARK 3 ORIGIN FOR THE GROUP (A): -5.8050 16.3520 -5.7260
REMARK 3 T TENSOR
REMARK 3 T11: 0.4274 T22: 0.1529
REMARK 3 T33: 0.1666 T12: 0.1424
REMARK 3 T13: 0.0810 T23: -0.0887
REMARK 3 L TENSOR
REMARK 3 L11: 2.1259 L22: 1.4166
REMARK 3 L33: 9.8138 L12: -0.3920
REMARK 3 L13: 2.5731 L23: -2.6168
REMARK 3 S TENSOR
REMARK 3 S11: 0.1981 S12: -0.0085 S13: 0.0966
REMARK 3 S21: 0.1007 S22: -0.2594 S23: 0.2569
REMARK 3 S31: -0.6627 S32: -0.1365 S33: 0.0613
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C -10 C 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 5.9210 -16.5040 -6.0840
REMARK 3 T TENSOR
REMARK 3 T11: 0.1738 T22: 0.1378
REMARK 3 T33: 0.1506 T12: 0.0654
REMARK 3 T13: -0.0912 T23: 0.0412
REMARK 3 L TENSOR
REMARK 3 L11: 1.1029 L22: 2.7001
REMARK 3 L33: 10.0665 L12: -0.5496
REMARK 3 L13: -3.0795 L23: 3.2015
REMARK 3 S TENSOR
REMARK 3 S11: -0.0364 S12: -0.1715 S13: -0.2331
REMARK 3 S21: 0.1937 S22: -0.2972 S23: -0.2086
REMARK 3 S31: 0.4482 S32: 0.3348 S33: 0.3335
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D -10 D 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 5.7800 16.5760 6.1460
REMARK 3 T TENSOR
REMARK 3 T11: 0.3694 T22: 0.2298
REMARK 3 T33: 0.1888 T12: -0.1065
REMARK 3 T13: 0.1133 T23: 0.0355
REMARK 3 L TENSOR
REMARK 3 L11: 1.7682 L22: 2.0756
REMARK 3 L33: 9.8206 L12: 0.5750
REMARK 3 L13: 3.7215 L23: 2.6678
REMARK 3 S TENSOR
REMARK 3 S11: 0.1751 S12: 0.3638 S13: 0.0705
REMARK 3 S21: -0.0821 S22: -0.1278 S23: -0.1691
REMARK 3 S31: -0.1928 S32: 0.7168 S33: -0.0473
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3OEO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-AUG-10.
REMARK 100 THE DEPOSITION ID IS D_1000061020.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-AUG-09
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.11587, 0.97944, 0.97976,
REMARK 200 0.98771, 0.97220
REMARK 200 MONOCHROMATOR : DOUBLE FLAT CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18354
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.38500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: 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 (%): 55.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M ACETATE PH 4.6, 26-32% (W/V)
REMARK 280 PEG400, 0.2 M CDCL2, AND 2 MM TCEP, EVAPORATION, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
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 84.23133
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 42.11567
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 ALA A 24
REMARK 465 ASP A 25
REMARK 465 THR A 26
REMARK 465 THR A 27
REMARK 465 THR A 28
REMARK 465 ALA A 29
REMARK 465 ALA A 30
REMARK 465 PRO A 31
REMARK 465 ALA A 32
REMARK 465 ASP A 33
REMARK 465 ALA A 34
REMARK 465 LYS A 35
REMARK 465 PRO A 36
REMARK 465 MET A 37
REMARK 465 MET A 38
REMARK 465 HIS A 39
REMARK 465 HIS A 40
REMARK 465 LYS A 41
REMARK 465 GLY A 42
REMARK 465 LYS A 43
REMARK 465 PHE A 44
REMARK 465 GLY A 45
REMARK 465 PRO A 46
REMARK 465 HIS A 47
REMARK 465 GLN A 48
REMARK 465 ASP A 49
REMARK 465 MET A 50
REMARK 465 MET A 51
REMARK 465 PHE A 52
REMARK 465 LYS A 144
REMARK 465 ARG A 145
REMARK 465 LEU A 146
REMARK 465 THR A 147
REMARK 465 GLU A 148
REMARK 465 ARG A 149
REMARK 465 PRO A 150
REMARK 465 ALA A 151
REMARK 465 ALA A 152
REMARK 465 LYS A 153
REMARK 465 GLY A 154
REMARK 465 LYS A 155
REMARK 465 MET A 156
REMARK 465 PRO A 157
REMARK 465 ALA A 158
REMARK 465 THR A 159
REMARK 465 ALA A 160
REMARK 465 GLU A 161
REMARK 465 ALA B 24
REMARK 465 ASP B 25
REMARK 465 THR B 26
REMARK 465 THR B 27
REMARK 465 THR B 28
REMARK 465 ALA B 29
REMARK 465 ALA B 30
REMARK 465 PRO B 31
REMARK 465 ALA B 32
REMARK 465 ASP B 33
REMARK 465 ALA B 34
REMARK 465 LYS B 35
REMARK 465 PRO B 36
REMARK 465 MET B 37
REMARK 465 MET B 38
REMARK 465 HIS B 39
REMARK 465 HIS B 40
REMARK 465 LYS B 41
REMARK 465 GLY B 42
REMARK 465 LYS B 43
REMARK 465 PHE B 44
REMARK 465 GLY B 45
REMARK 465 PRO B 46
REMARK 465 HIS B 47
REMARK 465 GLN B 48
REMARK 465 ASP B 49
REMARK 465 MET B 50
REMARK 465 MET B 51
REMARK 465 PHE B 52
REMARK 465 LYS B 144
REMARK 465 ARG B 145
REMARK 465 LEU B 146
REMARK 465 THR B 147
REMARK 465 GLU B 148
REMARK 465 ARG B 149
REMARK 465 PRO B 150
REMARK 465 ALA B 151
REMARK 465 ALA B 152
REMARK 465 LYS B 153
REMARK 465 GLY B 154
REMARK 465 LYS B 155
REMARK 465 MET B 156
REMARK 465 PRO B 157
REMARK 465 ALA B 158
REMARK 465 THR B 159
REMARK 465 ALA B 160
REMARK 465 GLU B 161
REMARK 465 ALA C 24
REMARK 465 ASP C 25
REMARK 465 THR C 26
REMARK 465 THR C 27
REMARK 465 THR C 28
REMARK 465 ALA C 29
REMARK 465 ALA C 30
REMARK 465 PRO C 31
REMARK 465 ALA C 32
REMARK 465 ASP C 33
REMARK 465 ALA C 34
REMARK 465 LYS C 35
REMARK 465 PRO C 36
REMARK 465 MET C 37
REMARK 465 MET C 38
REMARK 465 HIS C 39
REMARK 465 HIS C 40
REMARK 465 LYS C 41
REMARK 465 GLY C 42
REMARK 465 LYS C 43
REMARK 465 PHE C 44
REMARK 465 GLY C 45
REMARK 465 PRO C 46
REMARK 465 HIS C 47
REMARK 465 GLN C 48
REMARK 465 ASP C 49
REMARK 465 MET C 50
REMARK 465 MET C 51
REMARK 465 PHE C 52
REMARK 465 LYS C 144
REMARK 465 ARG C 145
REMARK 465 LEU C 146
REMARK 465 THR C 147
REMARK 465 GLU C 148
REMARK 465 ARG C 149
REMARK 465 PRO C 150
REMARK 465 ALA C 151
REMARK 465 ALA C 152
REMARK 465 LYS C 153
REMARK 465 GLY C 154
REMARK 465 LYS C 155
REMARK 465 MET C 156
REMARK 465 PRO C 157
REMARK 465 ALA C 158
REMARK 465 THR C 159
REMARK 465 ALA C 160
REMARK 465 GLU C 161
REMARK 465 ALA D 24
REMARK 465 ASP D 25
REMARK 465 THR D 26
REMARK 465 THR D 27
REMARK 465 THR D 28
REMARK 465 ALA D 29
REMARK 465 ALA D 30
REMARK 465 PRO D 31
REMARK 465 ALA D 32
REMARK 465 ASP D 33
REMARK 465 ALA D 34
REMARK 465 LYS D 35
REMARK 465 PRO D 36
REMARK 465 MET D 37
REMARK 465 MET D 38
REMARK 465 HIS D 39
REMARK 465 HIS D 40
REMARK 465 LYS D 41
REMARK 465 GLY D 42
REMARK 465 LYS D 43
REMARK 465 PHE D 44
REMARK 465 GLY D 45
REMARK 465 PRO D 46
REMARK 465 HIS D 47
REMARK 465 GLN D 48
REMARK 465 ASP D 49
REMARK 465 MET D 50
REMARK 465 MET D 51
REMARK 465 PHE D 52
REMARK 465 LYS D 144
REMARK 465 ARG D 145
REMARK 465 LEU D 146
REMARK 465 THR D 147
REMARK 465 GLU D 148
REMARK 465 ARG D 149
REMARK 465 PRO D 150
REMARK 465 ALA D 151
REMARK 465 ALA D 152
REMARK 465 LYS D 153
REMARK 465 GLY D 154
REMARK 465 LYS D 155
REMARK 465 MET D 156
REMARK 465 PRO D 157
REMARK 465 ALA D 158
REMARK 465 THR D 159
REMARK 465 ALA D 160
REMARK 465 GLU D 161
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 ALA D 106 O HOH D 178 1.97
REMARK 500 ND2 ASN A 124 O ILE C 91 2.16
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 OD1 ASP D 97 CD CD B 8 2554 1.98
REMARK 500 CD CD B 7 O HOH C 168 1565 2.07
REMARK 500 CD CD B 7 O HOH C 170 1565 2.07
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 ARG A 73 -71.34 -99.79
REMARK 500 ASP A 74 -86.87 -60.91
REMARK 500 MET A 108 51.94 -92.44
REMARK 500 ASN A 115 -72.69 -74.26
REMARK 500 LEU A 117 -78.02 -53.16
REMARK 500 ASP B 54 -156.41 -107.20
REMARK 500 LEU B 55 -157.12 77.67
REMARK 500 THR B 58 -144.67 20.17
REMARK 500 VAL B 99 2.13 -69.03
REMARK 500 LYS B 107 -19.82 -46.62
REMARK 500 MET B 108 31.56 -97.52
REMARK 500 GLU B 121 -30.22 -31.63
REMARK 500 ASN B 128 32.42 -74.67
REMARK 500 LEU C 55 -8.54 -53.88
REMARK 500 ASP C 74 35.02 -94.35
REMARK 500 PHE C 96 94.13 -63.10
REMARK 500 ASP C 97 97.27 -68.51
REMARK 500 LYS C 107 -17.96 -46.59
REMARK 500 PRO C 132 -56.77 -28.65
REMARK 500 LEU D 81 16.67 44.20
REMARK 500 THR D 92 61.81 -109.51
REMARK 500 LYS D 98 -70.19 -69.24
REMARK 500 VAL D 99 -35.56 -25.19
REMARK 500 GLU D 102 -15.69 -44.24
REMARK 500 HIS D 119 -65.21 -92.68
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 CD A 5 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 59 OD1
REMARK 620 2 HOH A 167 O 68.1
REMARK 620 3 HOH A 180 O 176.1 112.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 14 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 181 O
REMARK 620 2 HOH C 179 O 71.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 18 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 89 OD1
REMARK 620 2 HOH C 183 O 116.3
REMARK 620 3 HOH C 185 O 154.9 63.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 162 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 82 OE1
REMARK 620 2 GLU A 82 OE2 50.1
REMARK 620 3 HOH A 182 O 176.3 126.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B 162 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 109 OE1
REMARK 620 2 GLU B 109 OE2 81.5
REMARK 620 3 GLU C 109 OE1 106.3 167.0
REMARK 620 4 GLU D 109 OE1 116.4 68.2 115.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B 8 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 97 OD2
REMARK 620 2 HOH B 179 O 74.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD C 9 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 59 OD1
REMARK 620 2 ASP C 59 OD2 55.1
REMARK 620 3 HOH C 175 O 116.9 91.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD C 19 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 143 OE2
REMARK 620 2 HOH C 183 O 142.0
REMARK 620 3 HOH C 184 O 78.4 72.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD C 21 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 89 OD1
REMARK 620 2 HOH C 186 O 111.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD C 162 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 97 OD2
REMARK 620 2 HOH C 163 O 54.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD D 10 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH D 20 O
REMARK 620 2 ASP D 59 OD2 76.5
REMARK 620 3 HOH D 184 O 131.2 102.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD D 13 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 119 NE2
REMARK 620 2 HOH D 180 O 79.8
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 14
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 18
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 22
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 23
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 15
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 162
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD C 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD C 11
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD C 17
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD C 19
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD C 20
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD C 21
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD C 162
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD D 10
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD D 13
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD D 16
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD D 162
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3OEJ RELATED DB: PDB
DBREF 3OEO A 24 161 UNP C5W4R8 C5W4R8_ECOBB 24 161
DBREF 3OEO B 24 161 UNP C5W4R8 C5W4R8_ECOBB 24 161
DBREF 3OEO C 24 161 UNP C5W4R8 C5W4R8_ECOBB 24 161
DBREF 3OEO D 24 161 UNP C5W4R8 C5W4R8_ECOBB 24 161
SEQRES 1 A 138 ALA ASP THR THR THR ALA ALA PRO ALA ASP ALA LYS PRO
SEQRES 2 A 138 MET MET HIS HIS LYS GLY LYS PHE GLY PRO HIS GLN ASP
SEQRES 3 A 138 MET MET PHE LYS ASP LEU ASN LEU THR ASP ALA GLN LYS
SEQRES 4 A 138 GLN GLN ILE ARG GLU ILE MET LYS GLY GLN ARG ASP GLN
SEQRES 5 A 138 MET LYS ARG PRO PRO LEU GLU GLU ARG ARG ALA MET HIS
SEQRES 6 A 138 ASP ILE ILE THR SER ASP THR PHE ASP LYS VAL LYS ALA
SEQRES 7 A 138 GLU ALA GLN ILE ALA LYS MET GLU GLU GLN ARG LYS ALA
SEQRES 8 A 138 ASN MET LEU ALA HIS MET GLU THR GLN ASN LYS ILE TYR
SEQRES 9 A 138 ASN ILE LEU THR PRO GLU GLN LYS LYS GLN PHE ASN ALA
SEQRES 10 A 138 ASN PHE GLU LYS ARG LEU THR GLU ARG PRO ALA ALA LYS
SEQRES 11 A 138 GLY LYS MET PRO ALA THR ALA GLU
SEQRES 1 B 138 ALA ASP THR THR THR ALA ALA PRO ALA ASP ALA LYS PRO
SEQRES 2 B 138 MET MET HIS HIS LYS GLY LYS PHE GLY PRO HIS GLN ASP
SEQRES 3 B 138 MET MET PHE LYS ASP LEU ASN LEU THR ASP ALA GLN LYS
SEQRES 4 B 138 GLN GLN ILE ARG GLU ILE MET LYS GLY GLN ARG ASP GLN
SEQRES 5 B 138 MET LYS ARG PRO PRO LEU GLU GLU ARG ARG ALA MET HIS
SEQRES 6 B 138 ASP ILE ILE THR SER ASP THR PHE ASP LYS VAL LYS ALA
SEQRES 7 B 138 GLU ALA GLN ILE ALA LYS MET GLU GLU GLN ARG LYS ALA
SEQRES 8 B 138 ASN MET LEU ALA HIS MET GLU THR GLN ASN LYS ILE TYR
SEQRES 9 B 138 ASN ILE LEU THR PRO GLU GLN LYS LYS GLN PHE ASN ALA
SEQRES 10 B 138 ASN PHE GLU LYS ARG LEU THR GLU ARG PRO ALA ALA LYS
SEQRES 11 B 138 GLY LYS MET PRO ALA THR ALA GLU
SEQRES 1 C 138 ALA ASP THR THR THR ALA ALA PRO ALA ASP ALA LYS PRO
SEQRES 2 C 138 MET MET HIS HIS LYS GLY LYS PHE GLY PRO HIS GLN ASP
SEQRES 3 C 138 MET MET PHE LYS ASP LEU ASN LEU THR ASP ALA GLN LYS
SEQRES 4 C 138 GLN GLN ILE ARG GLU ILE MET LYS GLY GLN ARG ASP GLN
SEQRES 5 C 138 MET LYS ARG PRO PRO LEU GLU GLU ARG ARG ALA MET HIS
SEQRES 6 C 138 ASP ILE ILE THR SER ASP THR PHE ASP LYS VAL LYS ALA
SEQRES 7 C 138 GLU ALA GLN ILE ALA LYS MET GLU GLU GLN ARG LYS ALA
SEQRES 8 C 138 ASN MET LEU ALA HIS MET GLU THR GLN ASN LYS ILE TYR
SEQRES 9 C 138 ASN ILE LEU THR PRO GLU GLN LYS LYS GLN PHE ASN ALA
SEQRES 10 C 138 ASN PHE GLU LYS ARG LEU THR GLU ARG PRO ALA ALA LYS
SEQRES 11 C 138 GLY LYS MET PRO ALA THR ALA GLU
SEQRES 1 D 138 ALA ASP THR THR THR ALA ALA PRO ALA ASP ALA LYS PRO
SEQRES 2 D 138 MET MET HIS HIS LYS GLY LYS PHE GLY PRO HIS GLN ASP
SEQRES 3 D 138 MET MET PHE LYS ASP LEU ASN LEU THR ASP ALA GLN LYS
SEQRES 4 D 138 GLN GLN ILE ARG GLU ILE MET LYS GLY GLN ARG ASP GLN
SEQRES 5 D 138 MET LYS ARG PRO PRO LEU GLU GLU ARG ARG ALA MET HIS
SEQRES 6 D 138 ASP ILE ILE THR SER ASP THR PHE ASP LYS VAL LYS ALA
SEQRES 7 D 138 GLU ALA GLN ILE ALA LYS MET GLU GLU GLN ARG LYS ALA
SEQRES 8 D 138 ASN MET LEU ALA HIS MET GLU THR GLN ASN LYS ILE TYR
SEQRES 9 D 138 ASN ILE LEU THR PRO GLU GLN LYS LYS GLN PHE ASN ALA
SEQRES 10 D 138 ASN PHE GLU LYS ARG LEU THR GLU ARG PRO ALA ALA LYS
SEQRES 11 D 138 GLY LYS MET PRO ALA THR ALA GLU
HET CD A 5 1
HET CD A 14 1
HET CD A 18 1
HET CD A 22 1
HET CD A 23 1
HET CD A 162 1
HET CD B 7 1
HET CD B 8 1
HET CD B 12 1
HET CD B 15 1
HET CD B 162 1
HET CD C 9 1
HET CD C 11 1
HET CD C 17 1
HET CD C 19 1
HET CD C 20 1
HET CD C 21 1
HET CD C 162 1
HET CD D 10 1
HET CD D 13 1
HET CD D 16 1
HET CD D 162 1
HETNAM CD CADMIUM ION
FORMUL 5 CD 22(CD 2+)
FORMUL 27 HOH *88(H2 O)
HELIX 1 1 ALA A 60 ARG A 73 1 14
HELIX 2 2 GLU A 82 THR A 92 1 11
HELIX 3 3 ASP A 97 ALA A 106 1 10
HELIX 4 4 GLU A 109 ASN A 128 1 20
HELIX 5 5 THR A 131 PHE A 142 1 12
HELIX 6 6 ASP B 59 LYS B 70 1 12
HELIX 7 7 PRO B 80 THR B 92 1 13
HELIX 8 8 ASP B 97 MET B 108 1 12
HELIX 9 9 MET B 108 ASN B 128 1 21
HELIX 10 10 THR B 131 GLU B 143 1 13
HELIX 11 11 THR C 58 ARG C 73 1 16
HELIX 12 12 PRO C 80 ILE C 90 1 11
HELIX 13 13 ASP C 97 MET C 108 1 12
HELIX 14 14 MET C 108 ASN C 128 1 21
HELIX 15 15 THR C 131 GLU C 143 1 13
HELIX 16 16 THR D 58 GLN D 75 1 18
HELIX 17 17 GLU D 83 THR D 92 1 10
HELIX 18 18 ASP D 97 LEU D 130 1 34
HELIX 19 19 THR D 131 PHE D 142 1 12
LINK CD CD A 5 OD1 ASP A 59 1555 1555 2.65
LINK CD CD A 5 O HOH A 167 1555 1555 2.12
LINK CD CD A 5 O HOH A 180 1555 1555 2.14
LINK CD CD A 14 O HOH A 181 1555 1555 2.56
LINK CD CD A 14 O HOH C 179 1555 1555 2.14
LINK CD CD A 18 OD1 ASP A 89 1555 1555 2.49
LINK CD CD A 18 O HOH C 183 1555 1555 2.65
LINK CD CD A 18 O HOH C 185 1555 1555 2.44
LINK CD CD A 22 O HOH C 187 1555 1555 2.66
LINK CD CD A 23 O HOH A 188 1555 1555 2.19
LINK OE1 GLU A 82 CD CD A 162 1555 1555 2.56
LINK OE2 GLU A 82 CD CD A 162 1555 1555 2.63
LINK OE1 GLU A 109 CD CD B 162 1555 1555 2.28
LINK CD CD A 162 O HOH A 182 1555 1555 2.68
LINK CD CD B 7 O HOH B 178 1555 1555 2.05
LINK CD CD B 8 OD2 ASP B 97 1555 1555 2.02
LINK CD CD B 8 O HOH B 179 1555 1555 2.50
LINK CD CD B 15 OE1 GLU B 82 1555 1555 2.56
LINK OE2 GLU B 109 CD CD B 162 1555 1555 2.02
LINK CD CD B 162 OE1 GLU C 109 1555 1555 2.00
LINK CD CD B 162 OE1 GLU D 109 1555 1555 2.38
LINK CD CD C 9 OD1 ASP C 59 1555 1555 2.11
LINK CD CD C 9 OD2 ASP C 59 1555 1555 2.55
LINK CD CD C 9 O HOH C 175 1555 1555 1.93
LINK CD CD C 11 NE2 HIS C 119 1555 1555 2.16
LINK CD CD C 17 O HOH C 182 1555 1555 1.96
LINK CD CD C 19 OE2 GLU C 143 1555 1555 2.35
LINK CD CD C 19 O HOH C 183 1555 1555 2.22
LINK CD CD C 19 O HOH C 184 1555 1555 2.42
LINK CD CD C 20 O HOH C 185 1555 1555 2.39
LINK CD CD C 21 OD1 ASP C 89 1555 1555 2.21
LINK CD CD C 21 O HOH C 186 1555 1555 2.41
LINK OD2 ASP C 97 CD CD C 162 1555 1555 2.16
LINK CD CD C 162 O HOH C 163 1555 1555 2.60
LINK CD CD D 10 O HOH D 20 1555 1555 2.25
LINK CD CD D 10 OD2 ASP D 59 1555 1555 2.08
LINK CD CD D 10 O HOH D 184 1555 1555 2.17
LINK CD CD D 13 NE2 HIS D 119 1555 1555 2.17
LINK CD CD D 13 O HOH D 180 1555 1555 2.54
LINK OE1 GLU D 110 CD CD D 162 1555 1555 2.01
SITE 1 AC1 4 ASP A 59 HOH A 167 HOH A 180 GLU D 67
SITE 1 AC2 2 HOH A 181 HOH C 179
SITE 1 AC3 6 ASP A 89 ASP B 89 HOH B 169 CD C 19
SITE 2 AC3 6 HOH C 183 HOH C 185
SITE 1 AC4 4 CD A 23 GLU A 143 CD C 21 HOH C 187
SITE 1 AC5 7 CD A 22 HOH A 188 GLU B 143 HOH B 168
SITE 2 AC5 7 CD C 21 HOH C 186 HIS D 88
SITE 1 AC6 3 GLU A 82 HOH A 182 ASP B 94
SITE 1 AC7 6 ASP B 59 HOH B 178 GLU C 67 HOH C 168
SITE 2 AC7 6 HOH C 170 HOH C 173
SITE 1 AC8 4 ASP B 97 VAL B 99 HOH B 179 ASP D 97
SITE 1 AC9 3 ASP A 94 GLU B 82 HOH B 181
SITE 1 BC1 6 GLU A 109 GLU B 109 HOH B 182 GLU C 109
SITE 2 BC1 6 HOH C 167 GLU D 109
SITE 1 BC2 5 GLU B 67 ASP C 59 HOH C 172 HOH C 175
SITE 2 BC2 5 HOH C 180
SITE 1 BC3 2 HIS C 119 HOH C 181
SITE 1 BC4 3 GLU C 82 HOH C 182 ASP D 94
SITE 1 BC5 6 CD A 18 ARG A 85 CD C 20 GLU C 143
SITE 2 BC5 6 HOH C 183 HOH C 184
SITE 1 BC6 5 CD C 19 GLU C 143 HOH C 183 HOH C 185
SITE 2 BC6 5 GLU D 143
SITE 1 BC7 6 CD A 22 CD A 23 ASP C 89 HOH C 186
SITE 2 BC7 6 HOH C 187 ASP D 89
SITE 1 BC8 4 ASP A 97 ASP C 97 HOH C 163 HOH C 189
SITE 1 BC9 4 GLU A 67 HOH D 20 ASP D 59 HOH D 184
SITE 1 CC1 2 HIS D 119 HOH D 180
SITE 1 CC2 2 ASP C 94 GLU D 82
SITE 1 CC3 3 GLU C 110 GLU D 110 HOH D 182
CRYST1 69.195 69.195 126.347 90.00 90.00 120.00 P 32 12
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 0.014452 0.008344 0.000000 0.00000
SCALE2 0.000000 0.016688 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007915 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
