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HEADER HYDROLASE 22-APR-24 9BI7
TITLE YQIA, KLEBSIELLA PNEUMONIAE SERINE HYDROLASE, UNBOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: KLEBSIELLA PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 573;
SOURCE 4 GENE: YQIA, B5L96_16095, B6I68_11455, BANRA_00684, BB784_03840,
SOURCE 5 BL124_00019630, CK244_014295, DL426_23790, DW281_23375, EAO17_10155,
SOURCE 6 FXN67_07320, G4V31_19105, G7Z27_03770, GJJ08_003500, GJJ13_003365,
SOURCE 7 GJJ18_06885, GNF00_15605, GS419_03475, HJX03_03495, NCTC11679_00755,
SOURCE 8 NCTC13443_06427, NCTC13635_02885, NCTC5047_02742, NCTC5052_03996,
SOURCE 9 NCTC8849_05396, NCTC9601_00008, NCTC9637_01258, NCTC9645_02747,
SOURCE 10 NCTC9661_01486, QIG75_16940, SAMEA3499874_00665, SAMEA3499901_04234,
SOURCE 11 SAMEA3512100_04022, SAMEA3515122_03433, SAMEA3538658_02075,
SOURCE 12 SAMEA3538828_03988, SAMEA3720909_03528, SAMEA4364603_00807,
SOURCE 13 SAMEA4370542_02038, SAMEA4873597_05118, SAMEA4873632_04098,
SOURCE 14 VKR_00711;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS SERINE HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.T.RANDALL,M.FELLNER
REVDAT 1 07-MAY-25 9BI7 0
JRNL AUTH G.T.RANDALL,M.FELLNER
JRNL TITL YQIA, KLEBSIELLA PNEUMONIAE SERINE HYDROLASE, UNBOUND
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.87
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 29546
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.170
REMARK 3 FREE R VALUE TEST SET COUNT : 1528
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 44.8700 - 3.3400 1.00 2667 184 0.1540 0.2029
REMARK 3 2 3.3400 - 2.6500 1.00 2621 119 0.1741 0.2152
REMARK 3 3 2.6500 - 2.3100 1.00 2547 143 0.1817 0.1922
REMARK 3 4 2.3100 - 2.1000 1.00 2562 131 0.1681 0.2003
REMARK 3 5 2.1000 - 1.9500 1.00 2535 136 0.1736 0.2098
REMARK 3 6 1.9500 - 1.8400 1.00 2528 129 0.1821 0.2284
REMARK 3 7 1.8400 - 1.7400 1.00 2533 138 0.1922 0.2364
REMARK 3 8 1.7400 - 1.6700 1.00 2513 136 0.2034 0.2375
REMARK 3 9 1.6700 - 1.6000 1.00 2548 109 0.2232 0.2937
REMARK 3 10 1.6000 - 1.5500 1.00 2476 166 0.2567 0.3011
REMARK 3 11 1.5500 - 1.5000 0.99 2488 137 0.2804 0.2803
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.420
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) : 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 : 0.009 1603
REMARK 3 ANGLE : 1.004 2198
REMARK 3 CHIRALITY : 0.056 239
REMARK 3 PLANARITY : 0.008 290
REMARK 3 DIHEDRAL : 6.984 217
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 3:97 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.551 -7.085 -1.576
REMARK 3 T TENSOR
REMARK 3 T11: 0.1259 T22: 0.1324
REMARK 3 T33: 0.1427 T12: -0.0264
REMARK 3 T13: -0.0213 T23: 0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 2.6027 L22: 2.2130
REMARK 3 L33: 1.5525 L12: -0.1888
REMARK 3 L13: 0.7619 L23: -0.5120
REMARK 3 S TENSOR
REMARK 3 S11: 0.0267 S12: 0.0099 S13: 0.0400
REMARK 3 S21: 0.0119 S22: 0.0222 S23: -0.0091
REMARK 3 S31: 0.0219 S32: -0.0608 S33: -0.0616
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND RESID 98:131 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.209 -2.809 -18.628
REMARK 3 T TENSOR
REMARK 3 T11: 0.2060 T22: 0.2167
REMARK 3 T33: 0.2247 T12: 0.0081
REMARK 3 T13: 0.0013 T23: 0.0688
REMARK 3 L TENSOR
REMARK 3 L11: 5.1780 L22: 2.5670
REMARK 3 L33: 5.3947 L12: -0.6440
REMARK 3 L13: -0.2026 L23: 0.4787
REMARK 3 S TENSOR
REMARK 3 S11: -0.0693 S12: 0.0242 S13: 0.0056
REMARK 3 S21: -0.0811 S22: -0.2037 S23: -0.2278
REMARK 3 S31: 0.2019 S32: 0.5114 S33: 0.1645
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND RESID 132:191 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.093 2.360 -3.691
REMARK 3 T TENSOR
REMARK 3 T11: 0.1596 T22: 0.1833
REMARK 3 T33: 0.2504 T12: -0.0433
REMARK 3 T13: -0.0321 T23: 0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 2.1997 L22: 3.3227
REMARK 3 L33: 2.7640 L12: 0.8956
REMARK 3 L13: -0.4862 L23: -0.0474
REMARK 3 S TENSOR
REMARK 3 S11: -0.0372 S12: 0.0279 S13: 0.0134
REMARK 3 S21: 0.0354 S22: -0.0400 S23: -0.0975
REMARK 3 S31: -0.0849 S32: 0.0640 S33: 0.0691
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 9BI7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-APR-24.
REMARK 100 THE DEPOSITION ID IS D_1000283427.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-MAR-24
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.954
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29609
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 44.870
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 17.10
REMARK 200 R MERGE (I) : 0.12200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.8000
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) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 16.60
REMARK 200 R MERGE FOR SHELL (I) : 5.99800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.8.3
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.3 M CACL2 6H2O, 10 % W/V PEG6K, 0.1
REMARK 280 M TRIS PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
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 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 53.57400
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 26.78700
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 26.78700
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 53.57400
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 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 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 -2
REMARK 465 PRO A -1
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 OE1 GLU A 46 O HOH A 301 2.14
REMARK 500 O GLY A 59 O HOH A 302 2.14
REMARK 500 OE1 GLN A 129 O HOH A 303 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 O HOH A 355 O HOH A 355 6554 2.09
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 SER A 12 -157.54 -107.15
REMARK 500 SER A 69 -121.99 55.76
REMARK 500 SER A 69 -121.99 54.44
REMARK 500 ARG A 94 61.40 -117.80
REMARK 500 PHE A 174 101.84 78.58
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 CA A 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET A 1 O
REMARK 620 2 THR A 3 OG1 89.2
REMARK 620 3 GLU A 61 OE1 91.1 161.5
REMARK 620 4 GLU A 168 OE1 82.1 28.3 133.6
REMARK 620 5 GLU A 168 OE2 81.1 31.2 130.8 2.9
REMARK 620 6 HOH A 336 O 86.2 85.0 76.6 57.3 54.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 100 OD1
REMARK 620 2 ASN A 101 O 85.5
REMARK 620 3 ASN A 101 OD1 89.5 31.9
REMARK 620 4 HOH A 332 O 92.0 17.2 47.7
REMARK 620 5 HOH A 342 O 94.1 28.1 58.5 11.0
REMARK 620 6 HOH A 345 O 97.5 13.5 26.6 22.8 33.0
REMARK 620 7 HOH A 353 O 110.2 24.8 38.8 22.9 29.1 15.0
REMARK 620 N 1 2 3 4 5 6
DBREF1 9BI7 A 1 191 UNP A0A0W8AWE3_KLEPN
DBREF2 9BI7 A A0A0W8AWE3 1 191
SEQADV 9BI7 GLY A -2 UNP A0A0W8AWE EXPRESSION TAG
SEQADV 9BI7 PRO A -1 UNP A0A0W8AWE EXPRESSION TAG
SEQADV 9BI7 GLY A 0 UNP A0A0W8AWE EXPRESSION TAG
SEQRES 1 A 194 GLY PRO GLY MET ALA THR LEU LEU TYR LEU HIS GLY PHE
SEQRES 2 A 194 ASN SER SER PRO ARG SER ALA LYS ALA THR ALA LEU LYS
SEQRES 3 A 194 THR TRP LEU ALA GLN HIS TYR PRO GLU ILE THR MET VAL
SEQRES 4 A 194 VAL PRO GLU LEU PRO PRO TYR PRO ALA GLU THR ALA GLU
SEQRES 5 A 194 LEU LEU GLU SER ILE VAL LEU GLU HIS GLY GLY GLU PRO
SEQRES 6 A 194 LEU GLY VAL VAL GLY SER SER LEU GLY GLY TYR TYR ALA
SEQRES 7 A 194 THR TRP LEU SER GLN CYS PHE MET LEU PRO ALA VAL VAL
SEQRES 8 A 194 VAL ASN PRO ALA VAL ARG PRO PHE GLU LEU LEU ASN ASN
SEQRES 9 A 194 PHE LEU GLY HIS ASN GLU ASN PRO TYR THR GLY GLN GLN
SEQRES 10 A 194 TYR VAL LEU GLU SER ARG HIS ILE TYR ASP LEU LYS VAL
SEQRES 11 A 194 MET GLN ILE ASP PRO LEU GLU ALA PRO ASP LEU LEU TRP
SEQRES 12 A 194 LEU LEU GLN GLN THR GLY ASP GLU VAL LEU ASP TYR ARG
SEQRES 13 A 194 GLN ALA VAL HIS TYR TYR ALA SER CYS ARG GLN THR VAL
SEQRES 14 A 194 GLU GLU GLY GLY ASN HIS ALA PHE VAL GLY PHE ASP ASP
SEQRES 15 A 194 HIS PHE THR GLN ILE ILE GLU PHE LEU GLY LEU ARG
HET CA A 201 1
HET CA A 202 1
HET CL A 203 1
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
FORMUL 2 CA 2(CA 2+)
FORMUL 4 CL CL 1-
FORMUL 5 HOH *94(H2 O)
HELIX 1 AA1 SER A 16 TYR A 30 1 15
HELIX 2 AA2 TYR A 43 GLY A 59 1 17
HELIX 3 AA3 LEU A 70 MET A 83 1 14
HELIX 4 AA4 ARG A 94 ASN A 101 1 8
HELIX 5 AA5 GLU A 118 VAL A 127 1 10
HELIX 6 AA6 ALA A 135 ASP A 137 5 3
HELIX 7 AA7 ASP A 151 TYR A 159 1 9
HELIX 8 AA8 GLY A 176 ASP A 179 5 4
HELIX 9 AA9 HIS A 180 LEU A 188 1 9
SHEET 1 AA1 6 THR A 34 VAL A 36 0
SHEET 2 AA1 6 THR A 3 LEU A 7 1 N LEU A 4 O THR A 34
SHEET 3 AA1 6 LEU A 63 SER A 68 1 O GLY A 64 N LEU A 5
SHEET 4 AA1 6 ALA A 86 VAL A 89 1 O VAL A 89 N GLY A 67
SHEET 5 AA1 6 LEU A 139 GLN A 144 1 O LEU A 142 N VAL A 88
SHEET 6 AA1 6 ARG A 163 GLU A 167 1 O THR A 165 N LEU A 141
SHEET 1 AA2 2 GLY A 104 GLU A 107 0
SHEET 2 AA2 2 GLN A 114 LEU A 117 -1 O LEU A 117 N GLY A 104
LINK O MET A 1 CA CA A 201 1555 1555 2.44
LINK OG1 THR A 3 CA CA A 201 1555 1555 2.40
LINK OE1 GLU A 61 CA CA A 201 1555 1555 2.43
LINK OD1 ASN A 100 CA CA A 202 1555 5554 2.24
LINK O ASN A 101 CA CA A 202 1555 1555 2.37
LINK OD1 ASN A 101 CA CA A 202 1555 5554 2.29
LINK OE1 GLU A 168 CA CA A 201 1555 4655 2.46
LINK OE2 GLU A 168 CA CA A 201 1555 4655 2.44
LINK CA CA A 201 O HOH A 336 1555 1555 2.31
LINK CA CA A 202 O HOH A 332 1555 1555 2.41
LINK CA CA A 202 O HOH A 342 1555 1555 2.54
LINK CA CA A 202 O HOH A 345 1555 1555 2.52
LINK CA CA A 202 O HOH A 353 1555 5554 2.28
CISPEP 1 ASP A 131 PRO A 132 0 1.40
CRYST1 62.459 62.459 80.361 90.00 90.00 120.00 P 32 2 1 6
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 0.016011 0.009244 0.000000 0.00000
SCALE2 0.000000 0.018487 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012444 0.00000
TER 3051 ARG A 191
MASTER 339 0 3 9 8 0 0 6 1620 1 10 15
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