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HEADER HYDROLASE 27-JUL-23 8PZG
TITLE METAGENOMIC LIPASE ORF17
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ORF17;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METAGENOME;
SOURCE 3 ORGANISM_TAXID: 256318;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PHAT2
KEYWDS LIPASE, ESTERASE, METAGENOMIC, ENZYME, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.RANGEL PEREIRA,A.BALAN,M.HYVONEN
REVDAT 1 27-NOV-24 8PZG 0
JRNL AUTH M.RANGEL PEREIRA,A.BALAN,M.HYVONEN
JRNL TITL NOVEL LIPASES ISOLATED FROM METAGENOMIC LIBRARY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.40 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.51
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 3 NUMBER OF REFLECTIONS : 98406
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4919
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 38.5100 - 4.3500 0.99 3550 177 0.1643 0.2078
REMARK 3 2 4.3500 - 3.4500 1.00 3442 170 0.1525 0.1890
REMARK 3 3 3.4500 - 3.0200 1.00 3396 176 0.1641 0.1690
REMARK 3 4 3.0200 - 2.7400 0.98 3314 159 0.1710 0.1894
REMARK 3 5 2.7400 - 2.5400 0.93 3116 175 0.1598 0.1855
REMARK 3 6 2.5400 - 2.3900 0.89 3010 132 0.1490 0.1876
REMARK 3 7 2.3900 - 2.2700 0.88 2952 134 0.1421 0.1793
REMARK 3 8 2.2700 - 2.1800 0.90 2966 165 0.1387 0.1837
REMARK 3 9 2.1700 - 2.0900 0.90 2965 163 0.1425 0.1866
REMARK 3 10 2.0900 - 2.0200 0.91 2981 171 0.1460 0.2008
REMARK 3 11 2.0200 - 1.9600 0.91 3052 151 0.1489 0.1965
REMARK 3 12 1.9600 - 1.9000 0.92 3018 172 0.1557 0.2264
REMARK 3 13 1.9000 - 1.8500 0.92 3024 174 0.1533 0.2299
REMARK 3 14 1.8500 - 1.8000 0.92 3054 157 0.1522 0.2147
REMARK 3 15 1.8000 - 1.7600 0.93 3053 171 0.1627 0.2207
REMARK 3 16 1.7600 - 1.7300 0.93 3081 169 0.1721 0.2544
REMARK 3 17 1.7300 - 1.6900 0.93 3059 151 0.1738 0.2474
REMARK 3 18 1.6900 - 1.6600 0.94 3083 177 0.1717 0.2399
REMARK 3 19 1.6600 - 1.6300 0.94 3057 150 0.1665 0.1901
REMARK 3 20 1.6300 - 1.6000 0.94 3106 186 0.1755 0.2547
REMARK 3 21 1.6000 - 1.5800 0.94 3093 155 0.1763 0.2467
REMARK 3 22 1.5800 - 1.5500 0.95 3132 178 0.1862 0.2615
REMARK 3 23 1.5500 - 1.5300 0.95 3058 168 0.1968 0.2695
REMARK 3 24 1.5300 - 1.5100 0.95 3121 187 0.2044 0.2825
REMARK 3 25 1.5100 - 1.4900 0.95 3137 144 0.2045 0.2525
REMARK 3 26 1.4900 - 1.4700 0.95 3066 151 0.2177 0.3011
REMARK 3 27 1.4700 - 1.4500 0.96 3167 179 0.2315 0.3071
REMARK 3 28 1.4500 - 1.4300 0.95 3146 156 0.2368 0.2933
REMARK 3 29 1.4300 - 1.4200 0.96 3106 161 0.2464 0.3157
REMARK 3 30 1.4200 - 1.4000 0.96 3182 160 0.2645 0.3237
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) : 0.167
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.653
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.64
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.91
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 : 0.005 4702
REMARK 3 ANGLE : 0.717 6367
REMARK 3 CHIRALITY : 0.072 703
REMARK 3 PLANARITY : 0.007 843
REMARK 3 DIHEDRAL : 12.783 1804
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 8PZG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-NOV-24.
REMARK 100 THE DEPOSITION ID IS D_1292131976.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 98409
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 38.510
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.9
REMARK 200 DATA REDUNDANCY : 4.040
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.9600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
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) : 0.68300
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
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG6000. 0.1 M HEPES, PH 7.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 21.99000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 79.72000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.47500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 79.72000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.99000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.47500
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 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 MET A -8
REMARK 465 SER A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 ALA A 300
REMARK 465 GLU A 301
REMARK 465 MET B -8
REMARK 465 SER B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 ALA B 300
REMARK 465 GLU B 301
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 HOH A 500 O HOH A 522 1.89
REMARK 500 O HOH B 686 O HOH B 692 1.91
REMARK 500 O HOH B 449 O HOH B 540 1.98
REMARK 500 O HOH A 577 O HOH A 610 1.99
REMARK 500 O HOH B 481 O HOH B 550 1.99
REMARK 500 NH2 ARG B 296 O HOH B 401 2.02
REMARK 500 O HOH A 541 O HOH A 637 2.05
REMARK 500 O HOH A 420 O HOH A 605 2.05
REMARK 500 O HOH B 520 O HOH B 576 2.06
REMARK 500 N THR B 2 O HOH B 402 2.09
REMARK 500 O PRO A 261 O HOH A 401 2.11
REMARK 500 NH1 ARG A 50 O HOH A 402 2.11
REMARK 500 O HOH A 413 O HOH A 422 2.11
REMARK 500 O ALA B 153 O HOH B 403 2.12
REMARK 500 O HOH A 439 O HOH B 488 2.14
REMARK 500 O HOH B 507 O HOH B 535 2.17
REMARK 500 NE2 GLN A 5 O HOH A 403 2.18
REMARK 500 O HOH A 530 O HOH A 579 2.19
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 472 O HOH B 677 1455 1.95
REMARK 500 O HOH B 401 O HOH B 516 4455 2.05
REMARK 500 O HOH A 555 O HOH B 420 3554 2.09
REMARK 500 O HOH B 407 O HOH B 612 4455 2.13
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 THR A 33 -2.69 68.54
REMARK 500 THR A 33 -1.57 68.54
REMARK 500 PHE A 68 -167.29 -113.57
REMARK 500 SER A 118 -118.58 61.70
REMARK 500 MET A 207 130.34 -171.01
REMARK 500 THR B 33 -1.01 67.19
REMARK 500 SER B 118 -119.03 59.10
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8PZG A -8 301 PDB 8PZG 8PZG -8 301
DBREF 8PZG B -8 301 PDB 8PZG 8PZG -8 301
SEQRES 1 A 310 MET SER HIS HIS HIS HIS HIS HIS SER MET THR GLN GLN
SEQRES 2 A 310 GLN ALA LYS ALA ASN GLY ILE SER ILE ASN TYR GLU ASP
SEQRES 3 A 310 ARG GLY PRO ALA ASP GLY ILE PRO ILE LEU LEU VAL ASN
SEQRES 4 A 310 GLY TYR THR SER THR MET MET SER TRP PRO LEU GLU LEU
SEQRES 5 A 310 MET ASP GLY LEU LYS ALA ARG GLY PHE ARG VAL ILE ARG
SEQRES 6 A 310 TYR ASP ASN ARG ASP VAL GLY ARG THR GLU LYS PHE LYS
SEQRES 7 A 310 GLY VAL PRO ASP ILE GLY GLU VAL VAL LYS ALA LEU ARG
SEQRES 8 A 310 GLU GLY LYS THR PRO GLU THR PRO TYR THR LEU SER ASP
SEQRES 9 A 310 MET ALA ALA ASP GLY ILE GLY LEU MET ASP ALA LEU GLY
SEQRES 10 A 310 ILE GLU ARG ALA HIS VAL MET GLY ILE SER MET GLY GLY
SEQRES 11 A 310 MET ILE VAL GLN ALA MET ALA ILE ASN HIS PRO GLU ARG
SEQRES 12 A 310 LEU VAL SER VAL THR SER ILE MET SER THR THR GLY ASN
SEQRES 13 A 310 TYR ASP LEU PRO LYS ALA SER ASP GLU ALA MET ALA ALA
SEQRES 14 A 310 LEU GLN GLN GLN PRO ALA SER HIS ASP ARG GLU VAL VAL
SEQRES 15 A 310 ILE ARG HIS ARG MET LYS ALA ARG ARG VAL TYR GLN SER
SEQRES 16 A 310 PRO ALA PHE PRO ARG SER ASP GLU ALA LEU TYR ALA LEU
SEQRES 17 A 310 CYS ALA THR GLU PHE ASP HIS MET TYR TYR PRO GLU GLY
SEQRES 18 A 310 ALA SER ARG GLN TYR ALA ALA ILE VAL GLY ASP GLY SER
SEQRES 19 A 310 ARG VAL GLU ARG LEU LYS LYS VAL ARG VAL PRO PHE LEU
SEQRES 20 A 310 VAL ILE HIS GLY LYS ALA ASP PRO LEU VAL PRO VAL GLU
SEQRES 21 A 310 GLY GLY ILE ASP THR ALA LYS CYS VAL PRO GLY ALA LYS
SEQRES 22 A 310 LEU GLU LEU ILE GLU GLY MET GLY HIS ASP LEU PRO VAL
SEQRES 23 A 310 GLU LEU CYS PRO ARG TYR VAL ASP LEU ILE ALA GLU HIS
SEQRES 24 A 310 ALA LEU ALA ALA GLY ARG LYS ALA ALA ALA GLU
SEQRES 1 B 310 MET SER HIS HIS HIS HIS HIS HIS SER MET THR GLN GLN
SEQRES 2 B 310 GLN ALA LYS ALA ASN GLY ILE SER ILE ASN TYR GLU ASP
SEQRES 3 B 310 ARG GLY PRO ALA ASP GLY ILE PRO ILE LEU LEU VAL ASN
SEQRES 4 B 310 GLY TYR THR SER THR MET MET SER TRP PRO LEU GLU LEU
SEQRES 5 B 310 MET ASP GLY LEU LYS ALA ARG GLY PHE ARG VAL ILE ARG
SEQRES 6 B 310 TYR ASP ASN ARG ASP VAL GLY ARG THR GLU LYS PHE LYS
SEQRES 7 B 310 GLY VAL PRO ASP ILE GLY GLU VAL VAL LYS ALA LEU ARG
SEQRES 8 B 310 GLU GLY LYS THR PRO GLU THR PRO TYR THR LEU SER ASP
SEQRES 9 B 310 MET ALA ALA ASP GLY ILE GLY LEU MET ASP ALA LEU GLY
SEQRES 10 B 310 ILE GLU ARG ALA HIS VAL MET GLY ILE SER MET GLY GLY
SEQRES 11 B 310 MET ILE VAL GLN ALA MET ALA ILE ASN HIS PRO GLU ARG
SEQRES 12 B 310 LEU VAL SER VAL THR SER ILE MET SER THR THR GLY ASN
SEQRES 13 B 310 TYR ASP LEU PRO LYS ALA SER ASP GLU ALA MET ALA ALA
SEQRES 14 B 310 LEU GLN GLN GLN PRO ALA SER HIS ASP ARG GLU VAL VAL
SEQRES 15 B 310 ILE ARG HIS ARG MET LYS ALA ARG ARG VAL TYR GLN SER
SEQRES 16 B 310 PRO ALA PHE PRO ARG SER ASP GLU ALA LEU TYR ALA LEU
SEQRES 17 B 310 CYS ALA THR GLU PHE ASP HIS MET TYR TYR PRO GLU GLY
SEQRES 18 B 310 ALA SER ARG GLN TYR ALA ALA ILE VAL GLY ASP GLY SER
SEQRES 19 B 310 ARG VAL GLU ARG LEU LYS LYS VAL ARG VAL PRO PHE LEU
SEQRES 20 B 310 VAL ILE HIS GLY LYS ALA ASP PRO LEU VAL PRO VAL GLU
SEQRES 21 B 310 GLY GLY ILE ASP THR ALA LYS CYS VAL PRO GLY ALA LYS
SEQRES 22 B 310 LEU GLU LEU ILE GLU GLY MET GLY HIS ASP LEU PRO VAL
SEQRES 23 B 310 GLU LEU CYS PRO ARG TYR VAL ASP LEU ILE ALA GLU HIS
SEQRES 24 B 310 ALA LEU ALA ALA GLY ARG LYS ALA ALA ALA GLU
FORMUL 3 HOH *560(H2 O)
HELIX 1 AA1 THR A 35 TRP A 39 5 5
HELIX 2 AA2 PRO A 40 ARG A 50 1 11
HELIX 3 AA3 ASP A 73 GLU A 83 1 11
HELIX 4 AA4 THR A 92 GLY A 108 1 17
HELIX 5 AA5 SER A 118 HIS A 131 1 14
HELIX 6 AA6 SER A 154 GLN A 163 1 10
HELIX 7 AA7 ASP A 169 TYR A 184 1 16
HELIX 8 AA8 SER A 192 MET A 207 1 16
HELIX 9 AA9 TYR A 209 GLU A 211 5 3
HELIX 10 AB1 GLY A 212 ASP A 223 1 12
HELIX 11 AB2 ARG A 226 LYS A 231 1 6
HELIX 12 AB3 PRO A 249 VAL A 260 1 12
HELIX 13 AB4 PRO A 276 GLU A 278 5 3
HELIX 14 AB5 LEU A 279 ARG A 296 1 18
HELIX 15 AB6 THR B 35 TRP B 39 5 5
HELIX 16 AB7 PRO B 40 ARG B 50 1 11
HELIX 17 AB8 ASP B 73 GLU B 83 1 11
HELIX 18 AB9 THR B 92 LEU B 107 1 16
HELIX 19 AC1 SER B 118 HIS B 131 1 14
HELIX 20 AC2 SER B 154 GLN B 163 1 10
HELIX 21 AC3 ASP B 169 GLN B 185 1 17
HELIX 22 AC4 SER B 192 MET B 207 1 16
HELIX 23 AC5 GLU B 211 GLY B 223 1 14
HELIX 24 AC6 ARG B 226 LYS B 231 1 6
HELIX 25 AC7 VAL B 250 VAL B 260 1 11
HELIX 26 AC8 PRO B 276 GLU B 278 5 3
HELIX 27 AC9 LEU B 279 LYS B 297 1 19
SHEET 1 AA1 8 GLN A 4 ALA A 8 0
SHEET 2 AA1 8 ILE A 11 ASP A 17 -1 O ILE A 11 N ALA A 8
SHEET 3 AA1 8 PHE A 52 TYR A 57 -1 O ARG A 56 N GLU A 16
SHEET 4 AA1 8 ILE A 24 VAL A 29 1 N ILE A 26 O ILE A 55
SHEET 5 AA1 8 ALA A 112 ILE A 117 1 O MET A 115 N LEU A 27
SHEET 6 AA1 8 LEU A 135 ILE A 141 1 O ILE A 141 N GLY A 116
SHEET 7 AA1 8 PHE A 237 GLY A 242 1 O LEU A 238 N SER A 140
SHEET 8 AA1 8 LYS A 264 ILE A 268 1 O LYS A 264 N VAL A 239
SHEET 1 AA2 8 GLN B 4 ALA B 8 0
SHEET 2 AA2 8 ILE B 11 ASP B 17 -1 O ILE B 13 N ALA B 6
SHEET 3 AA2 8 PHE B 52 TYR B 57 -1 O ARG B 56 N GLU B 16
SHEET 4 AA2 8 ILE B 24 VAL B 29 1 N ILE B 24 O ARG B 53
SHEET 5 AA2 8 ALA B 112 ILE B 117 1 O HIS B 113 N LEU B 27
SHEET 6 AA2 8 LEU B 135 ILE B 141 1 O ILE B 141 N GLY B 116
SHEET 7 AA2 8 PHE B 237 GLY B 242 1 O LEU B 238 N SER B 140
SHEET 8 AA2 8 LYS B 264 ILE B 268 1 O GLU B 266 N VAL B 239
CISPEP 1 GLY A 19 PRO A 20 0 -2.27
CISPEP 2 GLY B 19 PRO B 20 0 -5.15
CRYST1 43.980 74.950 159.440 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 0.022738 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013342 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006272 0.00000
TER 2297 ALA A 299
TER 4601 ALA B 299
MASTER 327 0 0 27 16 0 0 6 5112 2 0 48
END |