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HEADER HYDROLASE 31-JUL-19 6KMO
TITLE CRYSTAL STRUCTURE OF A NOVEL ESTERASE CINB FROM ENTEROBACTER ASBURIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTER ASBURIAE;
SOURCE 3 ORGANISM_TAXID: 61645;
SOURCE 4 ATCC: 35953;
SOURCE 5 GENE: AN689_0218030;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS ENTEROBACTER ASBURIAE, ESTERASE, CINB, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.SHANG,Y.XU
REVDAT 1 04-SEP-19 6KMO 0
JRNL AUTH F.SHANG,Y.XU
JRNL TITL CRYSTAL STRUCTURE OF A NOVEL ESTERASE CINB FROM ENTEROBACTER
JRNL TITL 2 ASBURIAE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.15.2_3472
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.69
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 129082
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.128
REMARK 3 R VALUE (WORKING SET) : 0.127
REMARK 3 FREE R VALUE : 0.151
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.540
REMARK 3 FREE R VALUE TEST SET COUNT : 1984
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 3.4900 - 2.7700 1.00 9165 148 0.1308 0.1363
REMARK 3 2 2.7700 - 2.4200 1.00 9168 138 0.1237 0.1465
REMARK 3 3 2.4200 - 2.2000 1.00 9149 151 0.1190 0.1447
REMARK 3 4 2.2000 - 2.0400 1.00 9092 136 0.1206 0.1559
REMARK 3 5 2.0400 - 1.9200 1.00 9132 154 0.1235 0.1529
REMARK 3 6 1.9200 - 1.8300 1.00 9122 127 0.1216 0.1404
REMARK 3 7 1.8300 - 1.7500 1.00 9089 154 0.1171 0.1553
REMARK 3 8 1.7500 - 1.6800 0.99 9060 134 0.1182 0.1542
REMARK 3 9 1.6800 - 1.6200 0.99 9080 140 0.1196 0.1304
REMARK 3 10 1.6200 - 1.5700 0.99 9039 144 0.1213 0.1385
REMARK 3 11 1.5700 - 1.5300 0.99 8995 137 0.1241 0.1463
REMARK 3 12 1.5300 - 1.4900 0.99 8971 131 0.1339 0.1569
REMARK 3 13 1.4900 - 1.4500 0.95 8650 143 0.1503 0.1756
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.088
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 12.793
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 8.79
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.11
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 : 0.008 5260
REMARK 3 ANGLE : 0.978 7181
REMARK 3 CHIRALITY : 0.075 801
REMARK 3 PLANARITY : 0.007 951
REMARK 3 DIHEDRAL : 2.426 4135
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 6KMO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-AUG-19.
REMARK 100 THE DEPOSITION ID IS D_1300013237.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-APR-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 5C (4A)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979617
REMARK 200 MONOCHROMATOR : NULL
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 : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 129477
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07200
REMARK 200 FOR THE DATA SET : 20.1250
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.48
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.22400
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.16 M AMMONIUM ACETATE, 0.1 M SODIUM
REMARK 280 CITRATE TRIBASIC DEHYDRATE PH 5.6, 22% (W/V) POLYETHYLENE GLYCOL
REMARK 280 4000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 287.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 44.69800
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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 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 MET A 1
REMARK 465 LYS A 2
REMARK 465 ALA A 18
REMARK 465 SER A 19
REMARK 465 ALA A 20
REMARK 465 GLN A 21
REMARK 465 THR A 22
REMARK 465 MET B 1
REMARK 465 LYS B 2
REMARK 465 ALA B 17
REMARK 465 ALA B 18
REMARK 465 SER B 19
REMARK 465 ALA B 20
REMARK 465 GLN B 21
REMARK 465 THR B 22
REMARK 465 LYS B 43
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 H GLY A 97 O HOH A 506 1.54
REMARK 500 HE21 GLN B 195 O HOH B 407 1.60
REMARK 500 OG SER A 96 O HOH A 501 1.80
REMARK 500 O HOH A 560 O HOH A 782 1.80
REMARK 500 O HOH B 529 O HOH B 730 1.83
REMARK 500 O HOH A 726 O HOH A 928 1.84
REMARK 500 O HOH A 840 O HOH A 904 1.84
REMARK 500 O HOH A 533 O HOH A 851 1.86
REMARK 500 O HOH A 828 O HOH A 908 1.91
REMARK 500 O HOH A 694 O HOH A 728 1.92
REMARK 500 O HOH A 889 O HOH B 797 1.93
REMARK 500 NZ LYS B 67 O HOH B 401 1.94
REMARK 500 O HOH B 571 O HOH B 660 1.96
REMARK 500 O HOH A 744 O HOH A 753 1.97
REMARK 500 O HOH B 428 O HOH B 542 1.97
REMARK 500 O HOH A 753 O HOH A 941 1.98
REMARK 500 O HOH A 659 O HOH A 825 2.01
REMARK 500 O HOH A 852 O HOH A 896 2.02
REMARK 500 O HOH A 912 O HOH A 917 2.05
REMARK 500 O HOH A 828 O HOH A 947 2.05
REMARK 500 O HOH B 650 O HOH B 730 2.05
REMARK 500 O HOH B 690 O HOH B 718 2.06
REMARK 500 O HOH A 934 O HOH B 791 2.06
REMARK 500 O HOH A 501 O HOH A 848 2.06
REMARK 500 O HOH B 526 O HOH B 722 2.07
REMARK 500 O HOH A 729 O HOH A 805 2.07
REMARK 500 O HOH B 467 O HOH B 667 2.07
REMARK 500 O HOH A 712 O HOH A 942 2.08
REMARK 500 O HOH B 616 O HOH B 662 2.08
REMARK 500 O HOH B 634 O HOH B 807 2.09
REMARK 500 O HOH A 648 O HOH A 775 2.10
REMARK 500 O HOH B 553 O HOH B 721 2.10
REMARK 500 O HOH A 849 O HOH A 908 2.11
REMARK 500 O HOH B 653 O HOH B 826 2.11
REMARK 500 O HOH B 513 O HOH B 706 2.14
REMARK 500 O HOH B 562 O HOH B 682 2.14
REMARK 500 O HOH A 513 O HOH A 672 2.14
REMARK 500 O HOH A 819 O HOH A 833 2.14
REMARK 500 O HOH B 700 O HOH B 739 2.15
REMARK 500 O HOH A 846 O HOH A 890 2.15
REMARK 500 O HOH B 650 O HOH B 703 2.16
REMARK 500 O HOH A 926 O HOH A 958 2.17
REMARK 500 O HOH B 649 O HOH B 824 2.17
REMARK 500 O HOH B 728 O HOH B 817 2.17
REMARK 500 O HOH B 767 O HOH B 828 2.17
REMARK 500 O HOH A 732 O HOH A 827 2.18
REMARK 500 O HOH B 690 O HOH B 737 2.19
REMARK 500 O HOH A 920 O HOH A 958 2.19
REMARK 500 O HOH B 537 O HOH B 622 2.19
REMARK 500 O HOH A 510 O HOH A 530 2.19
REMARK 500
REMARK 500 THIS ENTRY HAS 52 CLOSE CONTACTS
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 OG1 THR B 3 HD22 ASN B 197 1454 1.29
REMARK 500 O HOH A 858 O HOH B 611 2745 2.06
REMARK 500 OG1 THR B 3 ND2 ASN B 197 1454 2.10
REMARK 500 O HOH A 820 O HOH B 727 1455 2.17
REMARK 500 O HOH A 524 O HOH B 427 2746 2.17
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 TRP A 110 -31.50 71.28
REMARK 500 ASP A 114 -173.77 178.30
REMARK 500 SER A 180 -120.95 69.64
REMARK 500 SER A 180 -122.67 63.56
REMARK 500 TRP A 208 61.42 39.14
REMARK 500 PHE A 228 -84.68 64.23
REMARK 500 PHE A 228 -61.36 83.57
REMARK 500 SER A 254 75.28 -118.94
REMARK 500 LEU A 276 64.53 -111.29
REMARK 500 TRP B 110 -26.11 72.11
REMARK 500 ASP B 114 -172.32 -177.91
REMARK 500 SER B 180 -119.70 68.35
REMARK 500 SER B 180 -121.57 65.27
REMARK 500 PHE B 228 -59.86 78.18
REMARK 500 SER B 254 76.36 -118.87
REMARK 500 LEU B 276 65.53 -113.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 960 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH B 850 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH B 851 DISTANCE = 6.10 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NH4 A 401
DBREF1 6KMO A 1 337 UNP A0A1D3AXI2_ENTAS
DBREF2 6KMO A A0A1D3AXI2 1 337
DBREF1 6KMO B 1 337 UNP A0A1D3AXI2_ENTAS
DBREF2 6KMO B A0A1D3AXI2 1 337
SEQADV 6KMO ILE A 9 UNP A0A1D3AXI VAL 9 ENGINEERED MUTATION
SEQADV 6KMO ALA A 23 UNP A0A1D3AXI THR 23 ENGINEERED MUTATION
SEQADV 6KMO ILE B 9 UNP A0A1D3AXI VAL 9 ENGINEERED MUTATION
SEQADV 6KMO ALA B 23 UNP A0A1D3AXI THR 23 ENGINEERED MUTATION
SEQRES 1 A 337 MET LYS THR LEU THR ALA ILE LEU ILE SER SER VAL PHE
SEQRES 2 A 337 ALA SER ALA ALA ALA SER ALA GLN THR ALA ASN THR PRO
SEQRES 3 A 337 THR PRO THR ALA GLY VAL GLN ALA PHE LEU ASN VAL LEU
SEQRES 4 A 337 ASN SER GLY LYS GLY LYS PRO MET GLU GLN MET THR PRO
SEQRES 5 A 337 GLN GLU ALA ARG GLN VAL LEU ILE GLY ALA GLN GLN GLY
SEQRES 6 A 337 ALA LYS LEU PRO PRO ALA GLN VAL SER GLU LYS THR ILE
SEQRES 7 A 337 GLN VAL ASN GLY GLN ALA ILE LYS LEU LYS ILE VAL LYS
SEQRES 8 A 337 PRO GLU ASN ALA SER GLY THR LEU PRO ALA PHE MET PHE
SEQRES 9 A 337 PHE HIS GLY GLY GLY TRP VAL LEU GLY ASP PHE PRO THR
SEQRES 10 A 337 HIS GLU ARG LEU ILE ARG ASP LEU VAL ARG ALA SER GLY
SEQRES 11 A 337 ALA ALA ALA VAL TYR VAL ASP TYR THR PRO SER PRO GLU
SEQRES 12 A 337 ALA HIS PHE PRO VAL ALA ILE ASN GLN ALA TYR GLU ALA
SEQRES 13 A 337 THR LYS TRP VAL ALA GLU HIS GLY GLN GLU ILE GLY VAL
SEQRES 14 A 337 ASP GLY SER ARG LEU GLY LEU VAL GLY ASN SER VAL GLY
SEQRES 15 A 337 GLY ASN MET VAL ALA SER VAL ALA LEU GLN ALA LYS GLN
SEQRES 16 A 337 PHE ASN GLY PRO LYS ILE ARG TYR ASN VAL MET LEU TRP
SEQRES 17 A 337 PRO VAL THR ASP ALA ASN PHE ASP THR ALA SER TYR ASN
SEQRES 18 A 337 GLN PHE GLU ASN GLY TYR PHE LEU SER LYS ASN MET MET
SEQRES 19 A 337 LYS TRP PHE TRP ASP ASN TYR THR THR SER ALA ALA ASP
SEQRES 20 A 337 ARG ASN ASN ILE LEU ALA SER PRO LEU ARG ALA SER THR
SEQRES 21 A 337 ALA GLN LEU LYS GLY PHE PRO GLU THR LEU ILE GLN THR
SEQRES 22 A 337 ALA GLU LEU ASP VAL LEU ARG ASP GLU GLY GLU ALA PHE
SEQRES 23 A 337 GLY ARG LYS LEU ASP ALA ALA GLY VAL PRO VAL THR VAL
SEQRES 24 A 337 THR ARG TYR ASN GLY MET ILE HIS ASP TYR GLY LEU LEU
SEQRES 25 A 337 ASN PRO LEU SER GLN GLU PRO THR VAL LYS VAL ALA LEU
SEQRES 26 A 337 GLU GLN ALA GLY ALA ALA LEU HIS GLU HIS LEU LYS
SEQRES 1 B 337 MET LYS THR LEU THR ALA ILE LEU ILE SER SER VAL PHE
SEQRES 2 B 337 ALA SER ALA ALA ALA SER ALA GLN THR ALA ASN THR PRO
SEQRES 3 B 337 THR PRO THR ALA GLY VAL GLN ALA PHE LEU ASN VAL LEU
SEQRES 4 B 337 ASN SER GLY LYS GLY LYS PRO MET GLU GLN MET THR PRO
SEQRES 5 B 337 GLN GLU ALA ARG GLN VAL LEU ILE GLY ALA GLN GLN GLY
SEQRES 6 B 337 ALA LYS LEU PRO PRO ALA GLN VAL SER GLU LYS THR ILE
SEQRES 7 B 337 GLN VAL ASN GLY GLN ALA ILE LYS LEU LYS ILE VAL LYS
SEQRES 8 B 337 PRO GLU ASN ALA SER GLY THR LEU PRO ALA PHE MET PHE
SEQRES 9 B 337 PHE HIS GLY GLY GLY TRP VAL LEU GLY ASP PHE PRO THR
SEQRES 10 B 337 HIS GLU ARG LEU ILE ARG ASP LEU VAL ARG ALA SER GLY
SEQRES 11 B 337 ALA ALA ALA VAL TYR VAL ASP TYR THR PRO SER PRO GLU
SEQRES 12 B 337 ALA HIS PHE PRO VAL ALA ILE ASN GLN ALA TYR GLU ALA
SEQRES 13 B 337 THR LYS TRP VAL ALA GLU HIS GLY GLN GLU ILE GLY VAL
SEQRES 14 B 337 ASP GLY SER ARG LEU GLY LEU VAL GLY ASN SER VAL GLY
SEQRES 15 B 337 GLY ASN MET VAL ALA SER VAL ALA LEU GLN ALA LYS GLN
SEQRES 16 B 337 PHE ASN GLY PRO LYS ILE ARG TYR ASN VAL MET LEU TRP
SEQRES 17 B 337 PRO VAL THR ASP ALA ASN PHE ASP THR ALA SER TYR ASN
SEQRES 18 B 337 GLN PHE GLU ASN GLY TYR PHE LEU SER LYS ASN MET MET
SEQRES 19 B 337 LYS TRP PHE TRP ASP ASN TYR THR THR SER ALA ALA ASP
SEQRES 20 B 337 ARG ASN ASN ILE LEU ALA SER PRO LEU ARG ALA SER THR
SEQRES 21 B 337 ALA GLN LEU LYS GLY PHE PRO GLU THR LEU ILE GLN THR
SEQRES 22 B 337 ALA GLU LEU ASP VAL LEU ARG ASP GLU GLY GLU ALA PHE
SEQRES 23 B 337 GLY ARG LYS LEU ASP ALA ALA GLY VAL PRO VAL THR VAL
SEQRES 24 B 337 THR ARG TYR ASN GLY MET ILE HIS ASP TYR GLY LEU LEU
SEQRES 25 B 337 ASN PRO LEU SER GLN GLU PRO THR VAL LYS VAL ALA LEU
SEQRES 26 B 337 GLU GLN ALA GLY ALA ALA LEU HIS GLU HIS LEU LYS
FORMUL 3 HOH *911(H2 O)
HELIX 1 AA1 THR A 3 ILE A 9 1 7
HELIX 2 AA2 SER A 10 ALA A 14 5 5
HELIX 3 AA3 THR A 29 GLY A 42 1 14
HELIX 4 AA4 PRO A 46 MET A 50 5 5
HELIX 5 AA5 THR A 51 GLN A 64 1 14
HELIX 6 AA6 ASP A 114 GLY A 130 1 17
HELIX 7 AA7 PRO A 147 GLY A 164 1 18
HELIX 8 AA8 GLN A 165 ILE A 167 5 3
HELIX 9 AA9 SER A 180 PHE A 196 1 17
HELIX 10 AB1 THR A 217 PHE A 223 1 7
HELIX 11 AB2 SER A 230 THR A 242 1 13
HELIX 12 AB3 SER A 244 ASN A 249 1 6
HELIX 13 AB4 SER A 254 ALA A 258 5 5
HELIX 14 AB5 SER A 259 LYS A 264 1 6
HELIX 15 AB6 LEU A 279 ALA A 293 1 15
HELIX 16 AB7 LEU A 312 SER A 316 5 5
HELIX 17 AB8 GLU A 318 LEU A 336 1 19
HELIX 18 AB9 LEU B 4 ILE B 9 1 6
HELIX 19 AC1 SER B 10 ALA B 14 5 5
HELIX 20 AC2 THR B 29 GLY B 42 1 14
HELIX 21 AC3 PRO B 46 MET B 50 5 5
HELIX 22 AC4 THR B 51 GLN B 64 1 14
HELIX 23 AC5 ASP B 114 GLY B 130 1 17
HELIX 24 AC6 PRO B 147 GLY B 164 1 18
HELIX 25 AC7 GLN B 165 ILE B 167 5 3
HELIX 26 AC8 SER B 180 PHE B 196 1 17
HELIX 27 AC9 THR B 217 PHE B 223 1 7
HELIX 28 AD1 SER B 230 THR B 242 1 13
HELIX 29 AD2 SER B 244 ASN B 249 1 6
HELIX 30 AD3 SER B 254 ALA B 258 5 5
HELIX 31 AD4 SER B 259 LYS B 264 1 6
HELIX 32 AD5 LEU B 279 ALA B 293 1 15
HELIX 33 AD6 LEU B 312 SER B 316 5 5
HELIX 34 AD7 GLU B 318 LEU B 336 1 19
SHEET 1 AA116 ALA A 71 VAL A 80 0
SHEET 2 AA116 GLN A 83 PRO A 92 -1 O GLN A 83 N VAL A 80
SHEET 3 AA116 ALA A 132 VAL A 136 -1 O TYR A 135 N LYS A 88
SHEET 4 AA116 LEU A 99 PHE A 105 1 N PHE A 102 O ALA A 132
SHEET 5 AA116 VAL A 169 ASN A 179 1 O GLY A 175 N MET A 103
SHEET 6 AA116 TYR A 203 LEU A 207 1 O LEU A 207 N GLY A 178
SHEET 7 AA116 THR A 269 LEU A 276 1 O LEU A 270 N MET A 206
SHEET 8 AA116 VAL A 297 ILE A 306 1 O TYR A 302 N THR A 273
SHEET 9 AA116 VAL B 297 ILE B 306 -1 O ARG B 301 N ARG A 301
SHEET 10 AA116 THR B 269 LEU B 276 1 N THR B 273 O TYR B 302
SHEET 11 AA116 TYR B 203 LEU B 207 1 N MET B 206 O LEU B 270
SHEET 12 AA116 VAL B 169 ASN B 179 1 N LEU B 176 O VAL B 205
SHEET 13 AA116 LEU B 99 PHE B 105 1 N MET B 103 O GLY B 175
SHEET 14 AA116 ALA B 132 VAL B 136 1 O ALA B 132 N PHE B 102
SHEET 15 AA116 ALA B 84 PRO B 92 -1 N LYS B 88 O TYR B 135
SHEET 16 AA116 ALA B 71 GLN B 79 -1 N GLN B 72 O LYS B 91
CISPEP 1 SER A 141 PRO A 142 0 4.97
CISPEP 2 PHE A 146 PRO A 147 0 3.30
CISPEP 3 GLY A 198 PRO A 199 0 -2.08
CISPEP 4 SER B 141 PRO B 142 0 4.33
CISPEP 5 PHE B 146 PRO B 147 0 2.83
CISPEP 6 GLY B 198 PRO B 199 0 -2.91
SITE 1 AC1 3 PHE A 228 LEU A 229 HIS A 307
CRYST1 65.086 89.396 68.929 90.00 111.26 90.00 P 1 21 1 4
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 0.015364 0.000000 0.005977 0.00000
SCALE2 0.000000 0.011186 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015567 0.00000
TER 5149 LYS A 337
TER 10189 LYS B 337
MASTER 357 0 0 34 16 0 1 6 5919 2 0 52
END |