| 7x0d-pdb | HEADER HYDROLASE 21-FEB-22 7X0D
TITLE CRYSTAL STRUCTURE OF PHOSPHOLIPASE A1, CAPLA1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOLIPASE A1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CAPSICUM ANNUUM;
SOURCE 3 ORGANISM_TAXID: 4072;
SOURCE 4 GENE: PLA1, T459_03599;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PHOSPHOLIPASE A1, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.HEO,I.LEE,S.MOON,W.LEE
REVDAT 1 13-APR-22 7X0D 0
JRNL AUTH Y.HEO,I.LEE,S.MOON,J.YUN,E.KIM,S.PARK,J.PARK,W.KIM,W.LEE
JRNL TITL CRYSTAL STRUCTURES OF THE PLANT PHOSPHOLIPASE A1 PROTEINS
JRNL TITL 2 REVEAL A UNIQUE DIMERIZATION DOMAIN
JRNL REF MOLECULES 2022
JRNL REFN ESSN 1420-3049
JRNL DOI 10.3390/MOLECULES27072317
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_2155
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.11
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.333
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 67351
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.062
REMARK 3 FREE R VALUE TEST SET COUNT : 3409
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 49.1061 - 6.9087 1.00 2943 136 0.1681 0.1891
REMARK 3 2 6.9087 - 5.4860 1.00 2806 176 0.1862 0.2339
REMARK 3 3 5.4860 - 4.7932 1.00 2832 140 0.1710 0.2120
REMARK 3 4 4.7932 - 4.3552 0.99 2755 150 0.1579 0.2004
REMARK 3 5 4.3552 - 4.0432 0.97 2710 143 0.1683 0.2178
REMARK 3 6 4.0432 - 3.8050 0.96 2675 135 0.1796 0.2394
REMARK 3 7 3.8050 - 3.6145 0.95 2630 157 0.1874 0.2670
REMARK 3 8 3.6145 - 3.4572 0.96 2650 141 0.1990 0.2628
REMARK 3 9 3.4572 - 3.3241 0.95 2599 150 0.2019 0.2364
REMARK 3 10 3.3241 - 3.2094 0.95 2660 124 0.2197 0.2554
REMARK 3 11 3.2094 - 3.1091 0.95 2634 152 0.2226 0.2501
REMARK 3 12 3.1091 - 3.0202 0.95 2657 133 0.2299 0.2686
REMARK 3 13 3.0202 - 2.9407 0.95 2601 143 0.2298 0.2769
REMARK 3 14 2.9407 - 2.8690 0.95 2635 143 0.2349 0.3173
REMARK 3 15 2.8690 - 2.8038 0.95 2613 145 0.2315 0.2915
REMARK 3 16 2.8038 - 2.7441 0.95 2639 135 0.2424 0.3304
REMARK 3 17 2.7441 - 2.6892 0.95 2574 156 0.2368 0.3378
REMARK 3 18 2.6892 - 2.6385 0.95 2636 152 0.2462 0.2986
REMARK 3 19 2.6385 - 2.5914 0.95 2615 147 0.2505 0.3170
REMARK 3 20 2.5914 - 2.5474 0.96 2691 133 0.2601 0.3341
REMARK 3 21 2.5474 - 2.5063 0.96 2632 142 0.2702 0.3492
REMARK 3 22 2.5063 - 2.4678 0.96 2624 128 0.2703 0.3610
REMARK 3 23 2.4678 - 2.4315 0.96 2702 128 0.2996 0.3449
REMARK 3 24 2.4315 - 2.3973 0.89 2429 120 0.2910 0.3613
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.337
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.704
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.56
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.58
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 : 0.002 12769
REMARK 3 ANGLE : 0.545 17315
REMARK 3 CHIRALITY : 0.042 1848
REMARK 3 PLANARITY : 0.004 2200
REMARK 3 DIHEDRAL : 13.668 7483
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 7X0D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-FEB-22.
REMARK 100 THE DEPOSITION ID IS D_1300027809.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0082
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67379
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.390
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 (%) : 96.1
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.11900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.9700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.58900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.790
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 2YIJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES (PH 7.5), 0.2M AMMONIUM
REMARK 280 SULFATE, 10% PEG 8000, 10% 2-PROPANOL, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
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 29.78400
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 2970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 101.95560
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 29.78400
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 147.31857
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 0
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 SER A 3
REMARK 465 ASP A 160
REMARK 465 GLY A 161
REMARK 465 GLY A 162
REMARK 465 LEU A 163
REMARK 465 LEU A 164
REMARK 465 PRO A 165
REMARK 465 LEU A 166
REMARK 465 PHE A 167
REMARK 465 GLY B 0
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 SER B 3
REMARK 465 PRO B 91
REMARK 465 ASP B 92
REMARK 465 ASP B 160
REMARK 465 GLY B 161
REMARK 465 GLY B 162
REMARK 465 LEU B 163
REMARK 465 LEU B 164
REMARK 465 PRO B 165
REMARK 465 LEU B 166
REMARK 465 PHE B 167
REMARK 465 GLY C 0
REMARK 465 MET C 1
REMARK 465 GLY C 2
REMARK 465 SER C 3
REMARK 465 LEU C 90
REMARK 465 PRO C 91
REMARK 465 ASP C 92
REMARK 465 ASP C 160
REMARK 465 GLY C 161
REMARK 465 GLY C 162
REMARK 465 LEU C 163
REMARK 465 LEU C 164
REMARK 465 PRO C 165
REMARK 465 LEU C 166
REMARK 465 PHE C 167
REMARK 465 GLY D 0
REMARK 465 MET D 1
REMARK 465 GLY D 2
REMARK 465 SER D 3
REMARK 465 PRO D 91
REMARK 465 ASP D 92
REMARK 465 ASP D 160
REMARK 465 GLY D 161
REMARK 465 GLY D 162
REMARK 465 LEU D 163
REMARK 465 LEU D 164
REMARK 465 PRO D 165
REMARK 465 LEU D 166
REMARK 465 PHE D 167
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 PHE B 110 NH1 ARG B 135 1.91
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 ALA A 93 -4.00 -156.86
REMARK 500 GLU A 102 30.82 -98.59
REMARK 500 TRP A 143 -34.73 -144.96
REMARK 500 SER A 221 -125.16 63.05
REMARK 500 ASP A 262 -156.16 -103.16
REMARK 500 ILE A 360 -41.35 -136.12
REMARK 500 VAL B 140 -66.65 -127.73
REMARK 500 TRP B 143 -30.83 -144.50
REMARK 500 ARG B 185 -23.87 120.38
REMARK 500 SER B 221 -127.27 61.99
REMARK 500 ASP B 262 -158.40 -92.65
REMARK 500 PRO B 288 -8.09 -59.90
REMARK 500 ILE B 360 -42.64 -136.11
REMARK 500 TRP C 143 -38.20 -141.54
REMARK 500 SER C 221 -127.48 58.76
REMARK 500 ASP C 262 -163.36 -77.95
REMARK 500 ILE C 360 -42.06 -136.73
REMARK 500 VAL C 380 109.36 57.09
REMARK 500 LEU C 389 103.02 -56.92
REMARK 500 GLU C 396 122.05 85.25
REMARK 500 VAL D 140 -65.25 -127.18
REMARK 500 TRP D 143 -31.63 -140.11
REMARK 500 ASN D 210 22.30 -77.00
REMARK 500 SER D 221 -126.13 60.02
REMARK 500 ASP D 262 -154.94 -97.76
REMARK 500 ILE D 360 -41.37 -137.33
REMARK 500 TYR D 395 -3.90 -140.30
REMARK 500 GLU D 396 126.05 66.41
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7X0D A 1 397 UNP A5YW95 A5YW95_CAPAN 1 397
DBREF 7X0D B 1 397 UNP A5YW95 A5YW95_CAPAN 1 397
DBREF 7X0D C 1 397 UNP A5YW95 A5YW95_CAPAN 1 397
DBREF 7X0D D 1 397 UNP A5YW95 A5YW95_CAPAN 1 397
SEQADV 7X0D GLY A 0 UNP A5YW95 EXPRESSION TAG
SEQADV 7X0D TRP A 113 UNP A5YW95 TYR 113 ENGINEERED MUTATION
SEQADV 7X0D GLY B 0 UNP A5YW95 EXPRESSION TAG
SEQADV 7X0D TRP B 113 UNP A5YW95 TYR 113 ENGINEERED MUTATION
SEQADV 7X0D GLY C 0 UNP A5YW95 EXPRESSION TAG
SEQADV 7X0D TRP C 113 UNP A5YW95 TYR 113 ENGINEERED MUTATION
SEQADV 7X0D GLY D 0 UNP A5YW95 EXPRESSION TAG
SEQADV 7X0D TRP D 113 UNP A5YW95 TYR 113 ENGINEERED MUTATION
SEQRES 1 A 398 GLY MET GLY SER MET ALA GLU LYS TRP GLU GLU LEU SER
SEQRES 2 A 398 GLY LYS ASN ASN TRP GLU GLY LEU LEU ASN PRO LEU ASP
SEQRES 3 A 398 LEU ASP LEU ARG LYS TYR ILE ILE GLN TYR GLY GLU LEU
SEQRES 4 A 398 ALA GLN ALA THR TYR ASP THR PHE ILE SER GLU ARG ALA
SEQRES 5 A 398 SER LYS TYR ALA GLY ALA SER ARG TYR SER MET GLU ASN
SEQRES 6 A 398 PHE PHE THR LYS VAL GLY LEU ASP PRO SER LYS TYR HIS
SEQRES 7 A 398 VAL THR LYS PHE PHE TYR GLY THR SER SER ILE PRO LEU
SEQRES 8 A 398 PRO ASP ALA PHE MET THR ARG SER LEU SER ARG GLU ALA
SEQRES 9 A 398 TRP SER LYS GLU SER ASN PHE MET GLY TRP ILE ALA VAL
SEQRES 10 A 398 ALA THR ASP GLU GLY LYS VAL ALA LEU GLY ARG ARG ASP
SEQRES 11 A 398 ILE VAL ILE ASN TRP ARG GLY THR LEU GLN VAL LEU GLU
SEQRES 12 A 398 TRP VAL ASN ASP LEU GLN PHE LEU LEU VAL PRO ALA PRO
SEQRES 13 A 398 LYS VAL PHE GLY ASP GLY GLY LEU LEU PRO LEU PHE HIS
SEQRES 14 A 398 PRO LEU VAL HIS HIS GLY PHE HIS ASN ILE TYR THR THR
SEQRES 15 A 398 GLU ASN PRO ARG SER GLN PHE ASN LYS THR CYS VAL ARG
SEQRES 16 A 398 ASP GLN VAL MET GLU GLU VAL LYS ARG LEU VAL GLU GLU
SEQRES 17 A 398 TYR LYS ASN GLU GLU VAL SER ILE THR VAL THR GLY HIS
SEQRES 18 A 398 SER LEU GLY ALA SER LEU ALA THR LEU ASN ALA VAL ASP
SEQRES 19 A 398 ILE ALA PHE ASN GLY ILE ASN LYS SER SER ASN GLY LYS
SEQRES 20 A 398 GLU PHE PRO VAL THR ALA PHE VAL PHE ALA SER PRO LYS
SEQRES 21 A 398 VAL GLY ASP LEU ASN PHE HIS LYS ALA PHE SER LYS LEU
SEQRES 22 A 398 LYS HIS LEU HIS ILE LEU ARG ILE HIS ASN LEU LEU ASP
SEQRES 23 A 398 ILE VAL PRO LYS TYR PRO PRO VAL GLY TYR PHE ASP VAL
SEQRES 24 A 398 GLY GLN GLU LEU MET ILE ASP THR THR LYS SER PRO TYR
SEQRES 25 A 398 VAL LYS PRO PRO GLY GLU VAL VAL SER TRP HIS LEU LEU
SEQRES 26 A 398 GLU PRO TYR LEU HIS GLY ILE ALA GLY THR GLN GLY ILE
SEQRES 27 A 398 GLY MET THR ALA GLY PHE LYS LEU GLU VAL ASN ARG ASP
SEQRES 28 A 398 ILE SER LEU VAL ASN LYS GLN TRP MET ILE LEU LYS ASP
SEQRES 29 A 398 GLU TYR CYS ILE PRO PRO LEU TRP TRP SER GLU LYS HIS
SEQRES 30 A 398 LYS GLY MET VAL GLN GLN GLN ASP GLY SER TRP LEU LEU
SEQRES 31 A 398 GLN ASP ARG ASP ASP TYR GLU PHE
SEQRES 1 B 398 GLY MET GLY SER MET ALA GLU LYS TRP GLU GLU LEU SER
SEQRES 2 B 398 GLY LYS ASN ASN TRP GLU GLY LEU LEU ASN PRO LEU ASP
SEQRES 3 B 398 LEU ASP LEU ARG LYS TYR ILE ILE GLN TYR GLY GLU LEU
SEQRES 4 B 398 ALA GLN ALA THR TYR ASP THR PHE ILE SER GLU ARG ALA
SEQRES 5 B 398 SER LYS TYR ALA GLY ALA SER ARG TYR SER MET GLU ASN
SEQRES 6 B 398 PHE PHE THR LYS VAL GLY LEU ASP PRO SER LYS TYR HIS
SEQRES 7 B 398 VAL THR LYS PHE PHE TYR GLY THR SER SER ILE PRO LEU
SEQRES 8 B 398 PRO ASP ALA PHE MET THR ARG SER LEU SER ARG GLU ALA
SEQRES 9 B 398 TRP SER LYS GLU SER ASN PHE MET GLY TRP ILE ALA VAL
SEQRES 10 B 398 ALA THR ASP GLU GLY LYS VAL ALA LEU GLY ARG ARG ASP
SEQRES 11 B 398 ILE VAL ILE ASN TRP ARG GLY THR LEU GLN VAL LEU GLU
SEQRES 12 B 398 TRP VAL ASN ASP LEU GLN PHE LEU LEU VAL PRO ALA PRO
SEQRES 13 B 398 LYS VAL PHE GLY ASP GLY GLY LEU LEU PRO LEU PHE HIS
SEQRES 14 B 398 PRO LEU VAL HIS HIS GLY PHE HIS ASN ILE TYR THR THR
SEQRES 15 B 398 GLU ASN PRO ARG SER GLN PHE ASN LYS THR CYS VAL ARG
SEQRES 16 B 398 ASP GLN VAL MET GLU GLU VAL LYS ARG LEU VAL GLU GLU
SEQRES 17 B 398 TYR LYS ASN GLU GLU VAL SER ILE THR VAL THR GLY HIS
SEQRES 18 B 398 SER LEU GLY ALA SER LEU ALA THR LEU ASN ALA VAL ASP
SEQRES 19 B 398 ILE ALA PHE ASN GLY ILE ASN LYS SER SER ASN GLY LYS
SEQRES 20 B 398 GLU PHE PRO VAL THR ALA PHE VAL PHE ALA SER PRO LYS
SEQRES 21 B 398 VAL GLY ASP LEU ASN PHE HIS LYS ALA PHE SER LYS LEU
SEQRES 22 B 398 LYS HIS LEU HIS ILE LEU ARG ILE HIS ASN LEU LEU ASP
SEQRES 23 B 398 ILE VAL PRO LYS TYR PRO PRO VAL GLY TYR PHE ASP VAL
SEQRES 24 B 398 GLY GLN GLU LEU MET ILE ASP THR THR LYS SER PRO TYR
SEQRES 25 B 398 VAL LYS PRO PRO GLY GLU VAL VAL SER TRP HIS LEU LEU
SEQRES 26 B 398 GLU PRO TYR LEU HIS GLY ILE ALA GLY THR GLN GLY ILE
SEQRES 27 B 398 GLY MET THR ALA GLY PHE LYS LEU GLU VAL ASN ARG ASP
SEQRES 28 B 398 ILE SER LEU VAL ASN LYS GLN TRP MET ILE LEU LYS ASP
SEQRES 29 B 398 GLU TYR CYS ILE PRO PRO LEU TRP TRP SER GLU LYS HIS
SEQRES 30 B 398 LYS GLY MET VAL GLN GLN GLN ASP GLY SER TRP LEU LEU
SEQRES 31 B 398 GLN ASP ARG ASP ASP TYR GLU PHE
SEQRES 1 C 398 GLY MET GLY SER MET ALA GLU LYS TRP GLU GLU LEU SER
SEQRES 2 C 398 GLY LYS ASN ASN TRP GLU GLY LEU LEU ASN PRO LEU ASP
SEQRES 3 C 398 LEU ASP LEU ARG LYS TYR ILE ILE GLN TYR GLY GLU LEU
SEQRES 4 C 398 ALA GLN ALA THR TYR ASP THR PHE ILE SER GLU ARG ALA
SEQRES 5 C 398 SER LYS TYR ALA GLY ALA SER ARG TYR SER MET GLU ASN
SEQRES 6 C 398 PHE PHE THR LYS VAL GLY LEU ASP PRO SER LYS TYR HIS
SEQRES 7 C 398 VAL THR LYS PHE PHE TYR GLY THR SER SER ILE PRO LEU
SEQRES 8 C 398 PRO ASP ALA PHE MET THR ARG SER LEU SER ARG GLU ALA
SEQRES 9 C 398 TRP SER LYS GLU SER ASN PHE MET GLY TRP ILE ALA VAL
SEQRES 10 C 398 ALA THR ASP GLU GLY LYS VAL ALA LEU GLY ARG ARG ASP
SEQRES 11 C 398 ILE VAL ILE ASN TRP ARG GLY THR LEU GLN VAL LEU GLU
SEQRES 12 C 398 TRP VAL ASN ASP LEU GLN PHE LEU LEU VAL PRO ALA PRO
SEQRES 13 C 398 LYS VAL PHE GLY ASP GLY GLY LEU LEU PRO LEU PHE HIS
SEQRES 14 C 398 PRO LEU VAL HIS HIS GLY PHE HIS ASN ILE TYR THR THR
SEQRES 15 C 398 GLU ASN PRO ARG SER GLN PHE ASN LYS THR CYS VAL ARG
SEQRES 16 C 398 ASP GLN VAL MET GLU GLU VAL LYS ARG LEU VAL GLU GLU
SEQRES 17 C 398 TYR LYS ASN GLU GLU VAL SER ILE THR VAL THR GLY HIS
SEQRES 18 C 398 SER LEU GLY ALA SER LEU ALA THR LEU ASN ALA VAL ASP
SEQRES 19 C 398 ILE ALA PHE ASN GLY ILE ASN LYS SER SER ASN GLY LYS
SEQRES 20 C 398 GLU PHE PRO VAL THR ALA PHE VAL PHE ALA SER PRO LYS
SEQRES 21 C 398 VAL GLY ASP LEU ASN PHE HIS LYS ALA PHE SER LYS LEU
SEQRES 22 C 398 LYS HIS LEU HIS ILE LEU ARG ILE HIS ASN LEU LEU ASP
SEQRES 23 C 398 ILE VAL PRO LYS TYR PRO PRO VAL GLY TYR PHE ASP VAL
SEQRES 24 C 398 GLY GLN GLU LEU MET ILE ASP THR THR LYS SER PRO TYR
SEQRES 25 C 398 VAL LYS PRO PRO GLY GLU VAL VAL SER TRP HIS LEU LEU
SEQRES 26 C 398 GLU PRO TYR LEU HIS GLY ILE ALA GLY THR GLN GLY ILE
SEQRES 27 C 398 GLY MET THR ALA GLY PHE LYS LEU GLU VAL ASN ARG ASP
SEQRES 28 C 398 ILE SER LEU VAL ASN LYS GLN TRP MET ILE LEU LYS ASP
SEQRES 29 C 398 GLU TYR CYS ILE PRO PRO LEU TRP TRP SER GLU LYS HIS
SEQRES 30 C 398 LYS GLY MET VAL GLN GLN GLN ASP GLY SER TRP LEU LEU
SEQRES 31 C 398 GLN ASP ARG ASP ASP TYR GLU PHE
SEQRES 1 D 398 GLY MET GLY SER MET ALA GLU LYS TRP GLU GLU LEU SER
SEQRES 2 D 398 GLY LYS ASN ASN TRP GLU GLY LEU LEU ASN PRO LEU ASP
SEQRES 3 D 398 LEU ASP LEU ARG LYS TYR ILE ILE GLN TYR GLY GLU LEU
SEQRES 4 D 398 ALA GLN ALA THR TYR ASP THR PHE ILE SER GLU ARG ALA
SEQRES 5 D 398 SER LYS TYR ALA GLY ALA SER ARG TYR SER MET GLU ASN
SEQRES 6 D 398 PHE PHE THR LYS VAL GLY LEU ASP PRO SER LYS TYR HIS
SEQRES 7 D 398 VAL THR LYS PHE PHE TYR GLY THR SER SER ILE PRO LEU
SEQRES 8 D 398 PRO ASP ALA PHE MET THR ARG SER LEU SER ARG GLU ALA
SEQRES 9 D 398 TRP SER LYS GLU SER ASN PHE MET GLY TRP ILE ALA VAL
SEQRES 10 D 398 ALA THR ASP GLU GLY LYS VAL ALA LEU GLY ARG ARG ASP
SEQRES 11 D 398 ILE VAL ILE ASN TRP ARG GLY THR LEU GLN VAL LEU GLU
SEQRES 12 D 398 TRP VAL ASN ASP LEU GLN PHE LEU LEU VAL PRO ALA PRO
SEQRES 13 D 398 LYS VAL PHE GLY ASP GLY GLY LEU LEU PRO LEU PHE HIS
SEQRES 14 D 398 PRO LEU VAL HIS HIS GLY PHE HIS ASN ILE TYR THR THR
SEQRES 15 D 398 GLU ASN PRO ARG SER GLN PHE ASN LYS THR CYS VAL ARG
SEQRES 16 D 398 ASP GLN VAL MET GLU GLU VAL LYS ARG LEU VAL GLU GLU
SEQRES 17 D 398 TYR LYS ASN GLU GLU VAL SER ILE THR VAL THR GLY HIS
SEQRES 18 D 398 SER LEU GLY ALA SER LEU ALA THR LEU ASN ALA VAL ASP
SEQRES 19 D 398 ILE ALA PHE ASN GLY ILE ASN LYS SER SER ASN GLY LYS
SEQRES 20 D 398 GLU PHE PRO VAL THR ALA PHE VAL PHE ALA SER PRO LYS
SEQRES 21 D 398 VAL GLY ASP LEU ASN PHE HIS LYS ALA PHE SER LYS LEU
SEQRES 22 D 398 LYS HIS LEU HIS ILE LEU ARG ILE HIS ASN LEU LEU ASP
SEQRES 23 D 398 ILE VAL PRO LYS TYR PRO PRO VAL GLY TYR PHE ASP VAL
SEQRES 24 D 398 GLY GLN GLU LEU MET ILE ASP THR THR LYS SER PRO TYR
SEQRES 25 D 398 VAL LYS PRO PRO GLY GLU VAL VAL SER TRP HIS LEU LEU
SEQRES 26 D 398 GLU PRO TYR LEU HIS GLY ILE ALA GLY THR GLN GLY ILE
SEQRES 27 D 398 GLY MET THR ALA GLY PHE LYS LEU GLU VAL ASN ARG ASP
SEQRES 28 D 398 ILE SER LEU VAL ASN LYS GLN TRP MET ILE LEU LYS ASP
SEQRES 29 D 398 GLU TYR CYS ILE PRO PRO LEU TRP TRP SER GLU LYS HIS
SEQRES 30 D 398 LYS GLY MET VAL GLN GLN GLN ASP GLY SER TRP LEU LEU
SEQRES 31 D 398 GLN ASP ARG ASP ASP TYR GLU PHE
HET SO4 A 401 5
HET SO4 B 401 5
HET SO4 C 401 5
HET SO4 D 401 5
HETNAM SO4 SULFATE ION
FORMUL 5 SO4 4(O4 S 2-)
FORMUL 9 HOH *508(H2 O)
HELIX 1 AA1 LYS A 7 SER A 12 1 6
HELIX 2 AA2 ASP A 25 PHE A 46 1 22
HELIX 3 AA3 ASN A 64 VAL A 69 1 6
HELIX 4 AA4 THR A 118 GLY A 126 1 9
HELIX 5 AA5 ALA A 154 GLY A 159 1 6
HELIX 6 AA6 HIS A 173 THR A 181 1 9
HELIX 7 AA7 CYS A 192 TYR A 208 1 17
HELIX 8 AA8 SER A 221 ASN A 237 1 17
HELIX 9 AA9 ASP A 262 LEU A 272 1 11
HELIX 10 AB1 ILE A 286 TYR A 290 5 5
HELIX 11 AB2 ASP A 305 SER A 309 5 5
HELIX 12 AB3 LEU A 323 THR A 334 1 12
HELIX 13 AB4 ASP A 350 LYS A 356 5 7
HELIX 14 AB5 LYS A 362 CYS A 366 5 5
HELIX 15 AB6 GLU A 374 LYS A 377 5 4
HELIX 16 AB7 LYS B 7 SER B 12 1 6
HELIX 17 AB8 ASP B 25 THR B 45 1 21
HELIX 18 AB9 ASN B 64 VAL B 69 1 6
HELIX 19 AC1 THR B 118 GLY B 126 1 9
HELIX 20 AC2 ALA B 154 GLY B 159 1 6
HELIX 21 AC3 HIS B 173 THR B 181 1 9
HELIX 22 AC4 CYS B 192 TYR B 208 1 17
HELIX 23 AC5 SER B 221 ASN B 237 1 17
HELIX 24 AC6 ASP B 262 LYS B 271 1 10
HELIX 25 AC7 ILE B 286 TYR B 290 5 5
HELIX 26 AC8 ASP B 305 SER B 309 5 5
HELIX 27 AC9 LEU B 323 THR B 334 1 12
HELIX 28 AD1 ASP B 350 LYS B 356 5 7
HELIX 29 AD2 LYS B 362 CYS B 366 5 5
HELIX 30 AD3 GLU B 374 LYS B 377 5 4
HELIX 31 AD4 LYS C 7 SER C 12 1 6
HELIX 32 AD5 ASP C 25 PHE C 46 1 22
HELIX 33 AD6 ASN C 64 VAL C 69 1 6
HELIX 34 AD7 THR C 118 GLY C 126 1 9
HELIX 35 AD8 VAL C 140 ASN C 145 1 6
HELIX 36 AD9 ALA C 154 GLY C 159 1 6
HELIX 37 AE1 HIS C 173 THR C 181 1 9
HELIX 38 AE2 CYS C 192 TYR C 208 1 17
HELIX 39 AE3 SER C 221 ASN C 237 1 17
HELIX 40 AE4 ASP C 262 LYS C 271 1 10
HELIX 41 AE5 ILE C 286 TYR C 290 5 5
HELIX 42 AE6 ASP C 305 SER C 309 5 5
HELIX 43 AE7 LEU C 323 THR C 334 1 12
HELIX 44 AE8 ASP C 350 LYS C 356 5 7
HELIX 45 AE9 LYS C 362 CYS C 366 5 5
HELIX 46 AF1 GLU C 374 MET C 379 5 6
HELIX 47 AF2 LYS D 7 SER D 12 1 6
HELIX 48 AF3 ASP D 25 THR D 45 1 21
HELIX 49 AF4 ASN D 64 VAL D 69 1 6
HELIX 50 AF5 THR D 118 GLY D 126 1 9
HELIX 51 AF6 HIS D 173 THR D 181 1 9
HELIX 52 AF7 CYS D 192 TYR D 208 1 17
HELIX 53 AF8 SER D 221 ASN D 237 1 17
HELIX 54 AF9 ASP D 262 LYS D 271 1 10
HELIX 55 AG1 ILE D 286 TYR D 290 5 5
HELIX 56 AG2 ASP D 305 SER D 309 5 5
HELIX 57 AG3 LEU D 323 THR D 334 1 12
HELIX 58 AG4 ASP D 350 LYS D 356 5 7
HELIX 59 AG5 LYS D 362 CYS D 366 5 5
HELIX 60 AG6 GLU D 374 LYS D 377 5 4
SHEET 1 AA1 7 TYR A 76 GLY A 84 0
SHEET 2 AA1 7 ASN A 109 ALA A 117 -1 O ILE A 114 N THR A 79
SHEET 3 AA1 7 ARG A 128 TRP A 134 -1 O VAL A 131 N ALA A 115
SHEET 4 AA1 7 VAL A 213 HIS A 220 1 O THR A 216 N ILE A 130
SHEET 5 AA1 7 VAL A 250 PHE A 255 1 O THR A 251 N VAL A 217
SHEET 6 AA1 7 LEU A 275 ASN A 282 1 O LEU A 278 N ALA A 252
SHEET 7 AA1 7 GLN A 300 ILE A 304 1 O GLN A 300 N ARG A 279
SHEET 1 AA2 2 LEU A 151 PRO A 153 0
SHEET 2 AA2 2 LEU A 170 HIS A 172 -1 O VAL A 171 N VAL A 152
SHEET 1 AA3 2 MET A 379 GLN A 381 0
SHEET 2 AA3 2 TRP A 387 LEU A 389 -1 O LEU A 388 N VAL A 380
SHEET 1 AA4 7 TYR B 76 GLY B 84 0
SHEET 2 AA4 7 ASN B 109 ALA B 117 -1 O ILE B 114 N THR B 79
SHEET 3 AA4 7 ARG B 128 TRP B 134 -1 O VAL B 131 N ALA B 115
SHEET 4 AA4 7 VAL B 213 HIS B 220 1 O SER B 214 N ILE B 130
SHEET 5 AA4 7 VAL B 250 PHE B 255 1 O THR B 251 N VAL B 217
SHEET 6 AA4 7 LEU B 275 ASN B 282 1 O LEU B 278 N ALA B 252
SHEET 7 AA4 7 GLN B 300 ILE B 304 1 O GLN B 300 N ARG B 279
SHEET 1 AA5 2 LEU B 151 PRO B 153 0
SHEET 2 AA5 2 LEU B 170 HIS B 172 -1 O VAL B 171 N VAL B 152
SHEET 1 AA6 2 MET B 379 GLN B 381 0
SHEET 2 AA6 2 TRP B 387 LEU B 389 -1 O LEU B 388 N VAL B 380
SHEET 1 AA7 7 TYR C 76 GLY C 84 0
SHEET 2 AA7 7 ASN C 109 ALA C 117 -1 O ILE C 114 N THR C 79
SHEET 3 AA7 7 ARG C 128 TRP C 134 -1 O VAL C 131 N ALA C 115
SHEET 4 AA7 7 VAL C 213 HIS C 220 1 O THR C 216 N ILE C 130
SHEET 5 AA7 7 VAL C 250 PHE C 255 1 O THR C 251 N ILE C 215
SHEET 6 AA7 7 LEU C 275 ASN C 282 1 O HIS C 276 N ALA C 252
SHEET 7 AA7 7 GLN C 300 ILE C 304 1 O GLN C 300 N ARG C 279
SHEET 1 AA8 2 LEU C 151 PRO C 153 0
SHEET 2 AA8 2 LEU C 170 HIS C 172 -1 O VAL C 171 N VAL C 152
SHEET 1 AA9 7 TYR D 76 GLY D 84 0
SHEET 2 AA9 7 ASN D 109 ALA D 117 -1 O ILE D 114 N THR D 79
SHEET 3 AA9 7 ARG D 128 TRP D 134 -1 O VAL D 131 N ALA D 115
SHEET 4 AA9 7 VAL D 213 HIS D 220 1 O THR D 216 N ILE D 130
SHEET 5 AA9 7 VAL D 250 PHE D 255 1 O THR D 251 N ILE D 215
SHEET 6 AA9 7 LEU D 275 ASN D 282 1 O LEU D 278 N ALA D 252
SHEET 7 AA9 7 GLN D 300 ILE D 304 1 O GLN D 300 N ARG D 279
SHEET 1 AB1 2 LEU D 151 PRO D 153 0
SHEET 2 AB1 2 LEU D 170 HIS D 172 -1 O VAL D 171 N VAL D 152
SHEET 1 AB2 2 MET D 379 GLN D 381 0
SHEET 2 AB2 2 TRP D 387 LEU D 389 -1 O LEU D 388 N VAL D 380
CISPEP 1 ASN A 22 PRO A 23 0 0.81
CISPEP 2 TYR A 290 PRO A 291 0 -5.44
CISPEP 3 PRO A 314 PRO A 315 0 -0.14
CISPEP 4 ASN B 22 PRO B 23 0 2.04
CISPEP 5 TYR B 290 PRO B 291 0 -5.46
CISPEP 6 PRO B 314 PRO B 315 0 -4.86
CISPEP 7 ASN C 22 PRO C 23 0 0.26
CISPEP 8 TYR C 290 PRO C 291 0 -5.20
CISPEP 9 PRO C 314 PRO C 315 0 -2.14
CISPEP 10 ASN D 22 PRO D 23 0 0.40
CISPEP 11 TYR D 290 PRO D 291 0 -3.67
CISPEP 12 PRO D 314 PRO D 315 0 -0.98
CRYST1 102.313 59.568 147.319 90.00 90.14 90.00 P 1 21 1 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 0.009774 0.000000 0.000024 0.00000
SCALE2 0.000000 0.016788 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006788 0.00000
TER 3117 PHE A 397
TER 6219 PHE B 397
TER 9313 PHE C 397
TER 12415 PHE D 397
MASTER 341 0 4 60 42 0 0 612939 4 20 124
END
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