HEADER HYDROLASE/HYDROLASE INHIBITOR 03-AUG-18 6EAU
TITLE CRYSTALLOGRAPHIC STRUCTURE OF THE OCTAPEPTIDE DERIVED FROM THE BTCI
TITLE 2 INHIBITOR BOUND TO BETA-TRYPSIN IN SPACE GROUP P 21 21 21.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATIONIC TRYPSIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BETA-TRYPSIN;
COMPND 5 EC: 3.4.21.4;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: CYS-THR-LYS-SER-ILE-PRO-PRO-CYS;
COMPND 8 CHAIN: I;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 MOL_ID: 2;
SOURCE 6 SYNTHETIC: YES;
SOURCE 7 ORGANISM_SCIENTIFIC: VIGNA UNGUICULATA;
SOURCE 8 ORGANISM_TAXID: 3917
KEYWDS INHIBITOR COMPLEX, BTCI, HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.C.FERNANDES,N.F.VALADARES,S.M.FREITAS,J.A.R.G.BARBOSA
REVDAT 3 11-OCT-23 6EAU 1 REMARK
REVDAT 2 08-JAN-20 6EAU 1 REMARK
REVDAT 1 07-AUG-19 6EAU 0
JRNL AUTH J.F.FENANDES,N.F.VALADARES,S.M.FREITAS,J.A.R.G.BARBOSA
JRNL TITL CRYSTALLOGRAPHIC STRUCTURE OF THE OCTAPEPTIDE DERIVED FROM
JRNL TITL 2 THE BTCI INHIBITOR BOUND TO BETA-TRYPSIN IN SPACE GROUP P 21
JRNL TITL 3 21 21.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.18 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.18
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.78
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 79855
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.143
REMARK 3 R VALUE (WORKING SET) : 0.142
REMARK 3 FREE R VALUE : 0.161
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.510
REMARK 3 FREE R VALUE TEST SET COUNT : 2008
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 30.7950 - 2.8439 1.00 5998 155 0.1368 0.1531
REMARK 3 2 2.8439 - 2.2575 1.00 5789 153 0.1387 0.1625
REMARK 3 3 2.2575 - 1.9722 1.00 5746 146 0.1287 0.1526
REMARK 3 4 1.9722 - 1.7919 1.00 5703 142 0.1321 0.1440
REMARK 3 5 1.7919 - 1.6635 1.00 5678 153 0.1340 0.1441
REMARK 3 6 1.6635 - 1.5654 1.00 5698 144 0.1374 0.1395
REMARK 3 7 1.5654 - 1.4870 1.00 5652 143 0.1397 0.1570
REMARK 3 8 1.4870 - 1.4223 1.00 5669 147 0.1450 0.1726
REMARK 3 9 1.4223 - 1.3675 1.00 5640 145 0.1547 0.1923
REMARK 3 10 1.3675 - 1.3203 0.99 5565 152 0.1627 0.1791
REMARK 3 11 1.3203 - 1.2790 0.97 5496 131 0.1667 0.1829
REMARK 3 12 1.2790 - 1.2425 0.94 5289 133 0.2008 0.2267
REMARK 3 13 1.2425 - 1.2098 0.91 5124 140 0.2098 0.2230
REMARK 3 14 1.2098 - 1.1803 0.85 4800 124 0.2524 0.2721
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) : 0.110
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.360
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.83
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 : 0.024 1821
REMARK 3 ANGLE : 1.427 2495
REMARK 3 CHIRALITY : 0.090 276
REMARK 3 PLANARITY : 0.008 316
REMARK 3 DIHEDRAL : 12.522 668
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 16 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.8174 -67.6648 81.0984
REMARK 3 T TENSOR
REMARK 3 T11: 0.0850 T22: 0.0888
REMARK 3 T33: 0.0972 T12: -0.0005
REMARK 3 T13: -0.0069 T23: 0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 0.9408 L22: 1.3336
REMARK 3 L33: 1.3903 L12: -0.2695
REMARK 3 L13: 0.3366 L23: -0.1490
REMARK 3 S TENSOR
REMARK 3 S11: 0.0048 S12: -0.0537 S13: -0.0520
REMARK 3 S21: 0.0502 S22: 0.0410 S23: -0.0426
REMARK 3 S31: 0.0172 S32: -0.0140 S33: -0.0492
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 91 THROUGH 123 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.7887 -59.7744 77.6769
REMARK 3 T TENSOR
REMARK 3 T11: 0.0439 T22: 0.0829
REMARK 3 T33: 0.0839 T12: -0.0330
REMARK 3 T13: 0.0102 T23: 0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 1.2592 L22: 4.5896
REMARK 3 L33: 2.0192 L12: -1.3185
REMARK 3 L13: 0.4982 L23: 0.0719
REMARK 3 S TENSOR
REMARK 3 S11: -0.0749 S12: -0.0056 S13: -0.0163
REMARK 3 S21: 0.0304 S22: 0.0485 S23: -0.0211
REMARK 3 S31: -0.1586 S32: 0.0582 S33: 0.0305
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 124 THROUGH 155 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.3814 -65.3418 71.8216
REMARK 3 T TENSOR
REMARK 3 T11: 0.0740 T22: 0.1020
REMARK 3 T33: 0.0992 T12: 0.0206
REMARK 3 T13: -0.0200 T23: 0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 2.3112 L22: 2.3331
REMARK 3 L33: 1.9054 L12: 0.6239
REMARK 3 L13: 0.3597 L23: -0.5364
REMARK 3 S TENSOR
REMARK 3 S11: 0.0288 S12: 0.0447 S13: -0.0067
REMARK 3 S21: -0.0063 S22: 0.0862 S23: 0.1979
REMARK 3 S31: -0.0908 S32: -0.2831 S33: -0.1012
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 156 THROUGH 215 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.9269 -57.6377 67.7942
REMARK 3 T TENSOR
REMARK 3 T11: 0.1274 T22: 0.1028
REMARK 3 T33: 0.0806 T12: 0.0291
REMARK 3 T13: -0.0180 T23: -0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 1.4823 L22: 1.2583
REMARK 3 L33: 1.8693 L12: -0.1896
REMARK 3 L13: 1.0473 L23: -0.2776
REMARK 3 S TENSOR
REMARK 3 S11: -0.1003 S12: -0.0194 S13: 0.0777
REMARK 3 S21: -0.0717 S22: 0.0367 S23: 0.0759
REMARK 3 S31: -0.2957 S32: -0.2090 S33: 0.0349
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 216 THROUGH 245 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0312 -54.7555 71.5109
REMARK 3 T TENSOR
REMARK 3 T11: 0.1546 T22: 0.0585
REMARK 3 T33: 0.0795 T12: 0.0071
REMARK 3 T13: 0.0047 T23: -0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 6.0275 L22: 1.1249
REMARK 3 L33: 2.0426 L12: 0.6837
REMARK 3 L13: 1.7132 L23: 0.4328
REMARK 3 S TENSOR
REMARK 3 S11: -0.1981 S12: 0.0434 S13: 0.1747
REMARK 3 S21: -0.1637 S22: 0.1308 S23: -0.0314
REMARK 3 S31: -0.3494 S32: -0.0193 S33: 0.0600
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 1 THROUGH 8 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.3007 -56.7065 82.4682
REMARK 3 T TENSOR
REMARK 3 T11: 0.3245 T22: 0.3055
REMARK 3 T33: 0.1768 T12: 0.0794
REMARK 3 T13: 0.0226 T23: -0.0304
REMARK 3 L TENSOR
REMARK 3 L11: 2.6031 L22: 7.7113
REMARK 3 L33: 3.6223 L12: -0.0175
REMARK 3 L13: -0.1769 L23: -5.1966
REMARK 3 S TENSOR
REMARK 3 S11: -0.1445 S12: -0.7525 S13: 0.2323
REMARK 3 S21: 1.2237 S22: -0.0847 S23: 0.3873
REMARK 3 S31: -0.7881 S32: -0.7606 S33: 0.1511
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 6EAU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-AUG-18.
REMARK 100 THE DEPOSITION ID IS D_1000235946.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-MAY-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : LNLS
REMARK 200 BEAMLINE : W01B-MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.20009
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE-CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79894
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.180
REMARK 200 RESOLUTION RANGE LOW (A) : 30.780
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 14.10
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 36.3800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.18
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.22
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.190
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: 3RU4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0,1M HEPES SODIUM 2 M LITHIUM SULFATE
REMARK 280 MONOHYDRATE, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 295K
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 29.90850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.48200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.78450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 33.48200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.90850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.78450
REMARK 290 SMTRY3 4 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: 2200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -109.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I
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 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 HG1 THR A 134 O2 SO4 A 307 1.46
REMARK 500 HG1 THR A 98 O2 SO4 A 304 1.55
REMARK 500 O LYS A 159 HH TYR A 184A 1.59
REMARK 500 O4 SO4 A 301 O HOH A 402 2.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 189 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
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 ASP A 71 -78.35 -124.04
REMARK 500 ASN A 79 -10.95 82.51
REMARK 500 SER A 214 -67.94 -126.33
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 777 DISTANCE = 6.36 ANGSTROMS
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 308 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 70 OE1
REMARK 620 2 ASN A 72 O 91.8
REMARK 620 3 VAL A 75 O 163.9 81.5
REMARK 620 4 GLU A 80 OE2 102.5 156.8 88.8
REMARK 620 5 HOH A 429 O 84.4 84.7 109.3 78.7
REMARK 620 6 HOH A 531 O 80.6 104.0 86.8 96.4 162.8
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 308
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3RU4 RELATED DB: PDB
REMARK 900 RELATED ID: 2G81 RELATED DB: PDB
REMARK 900 RELATED ID: 6EAT RELATED DB: PDB
REMARK 900 RELATED ID: 6EAU RELATED DB: PDB
REMARK 900 RELATED ID: 6EAW RELATED DB: PDB
REMARK 900 RELATED ID: 6E5M RELATED DB: PDB
REMARK 900 RELATED ID: 6EAX RELATED DB: PDB
DBREF 6EAU A 16 245 UNP P00760 TRY1_BOVIN 24 246
DBREF 6EAU I 1 8 PDB 6EAU 6EAU 1 8
SEQRES 1 A 223 ILE VAL GLY GLY TYR THR CYS GLY ALA ASN THR VAL PRO
SEQRES 2 A 223 TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY
SEQRES 3 A 223 GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA
SEQRES 4 A 223 HIS CYS TYR LYS SER GLY ILE GLN VAL ARG LEU GLY GLU
SEQRES 5 A 223 ASP ASN ILE ASN VAL VAL GLU GLY ASN GLU GLN PHE ILE
SEQRES 6 A 223 SER ALA SER LYS SER ILE VAL HIS PRO SER TYR ASN SER
SEQRES 7 A 223 ASN THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU LYS
SEQRES 8 A 223 SER ALA ALA SER LEU ASN SER ARG VAL ALA SER ILE SER
SEQRES 9 A 223 LEU PRO THR SER CYS ALA SER ALA GLY THR GLN CYS LEU
SEQRES 10 A 223 ILE SER GLY TRP GLY ASN THR LYS SER SER GLY THR SER
SEQRES 11 A 223 TYR PRO ASP VAL LEU LYS CYS LEU LYS ALA PRO ILE LEU
SEQRES 12 A 223 SER ASP SER SER CYS LYS SER ALA TYR PRO GLY GLN ILE
SEQRES 13 A 223 THR SER ASN MET PHE CYS ALA GLY TYR LEU GLU GLY GLY
SEQRES 14 A 223 LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL
SEQRES 15 A 223 CYS SER GLY LYS LEU GLN GLY ILE VAL SER TRP GLY SER
SEQRES 16 A 223 GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS
SEQRES 17 A 223 VAL CYS ASN TYR VAL SER TRP ILE LYS GLN THR ILE ALA
SEQRES 18 A 223 SER ASN
SEQRES 1 I 8 CYS THR LYS SER ILE PRO PRO CYS
HET SO4 A 301 5
HET SO4 A 302 5
HET SO4 A 303 5
HET SO4 A 304 5
HET SO4 A 305 5
HET SO4 A 306 5
HET SO4 A 307 5
HET CA A 308 1
HETNAM SO4 SULFATE ION
HETNAM CA CALCIUM ION
FORMUL 3 SO4 7(O4 S 2-)
FORMUL 10 CA CA 2+
FORMUL 11 HOH *387(H2 O)
HELIX 1 AA1 ALA A 55 TYR A 59 5 5
HELIX 2 AA2 SER A 164 TYR A 172 1 9
HELIX 3 AA3 TYR A 234 SER A 244 1 11
SHEET 1 AA1 7 TYR A 20 THR A 21 0
SHEET 2 AA1 7 LYS A 156 PRO A 161 -1 O CYS A 157 N TYR A 20
SHEET 3 AA1 7 GLN A 135 GLY A 140 -1 N ILE A 138 O LEU A 158
SHEET 4 AA1 7 PRO A 198 CYS A 201 -1 O VAL A 200 N LEU A 137
SHEET 5 AA1 7 LYS A 204 TRP A 215 -1 O LYS A 204 N CYS A 201
SHEET 6 AA1 7 GLY A 226 LYS A 230 -1 O VAL A 227 N TRP A 215
SHEET 7 AA1 7 MET A 180 ALA A 183 -1 N PHE A 181 O TYR A 228
SHEET 1 AA2 7 GLN A 30 ASN A 34 0
SHEET 2 AA2 7 HIS A 40 ASN A 48 -1 O CYS A 42 N LEU A 33
SHEET 3 AA2 7 TRP A 51 SER A 54 -1 O VAL A 53 N SER A 45
SHEET 4 AA2 7 MET A 104 LEU A 108 -1 O ILE A 106 N VAL A 52
SHEET 5 AA2 7 GLN A 81 VAL A 90 -1 N ILE A 89 O LEU A 105
SHEET 6 AA2 7 GLN A 64 LEU A 67 -1 N LEU A 67 O GLN A 81
SHEET 7 AA2 7 GLN A 30 ASN A 34 -1 N SER A 32 O ARG A 66
SSBOND 1 CYS A 22 CYS A 157 1555 1555 1.97
SSBOND 2 CYS A 42 CYS A 58 1555 1555 1.99
SSBOND 3 CYS A 128 CYS A 232 1555 1555 1.99
SSBOND 4 CYS A 136 CYS A 201 1555 1555 1.99
SSBOND 5 CYS A 168 CYS A 182 1555 1555 2.03
SSBOND 6 CYS A 191 CYS A 220 1555 1555 2.03
LINK OE1 GLU A 70 CA CA A 308 1555 1555 2.18
LINK O ASN A 72 CA CA A 308 1555 1555 2.19
LINK O VAL A 75 CA CA A 308 1555 1555 2.19
LINK OE2 GLU A 80 CA CA A 308 1555 1555 2.22
LINK CA CA A 308 O HOH A 429 1555 1555 2.34
LINK CA CA A 308 O HOH A 531 1555 1555 2.29
CISPEP 1 ILE I 5 PRO I 6 0 -2.92
SITE 1 AC1 8 PRO A 152 ASP A 153 VAL A 154 LYS A 156
SITE 2 AC1 8 HOH A 402 HOH A 520 HOH A 596 HOH A 652
SITE 1 AC2 7 ALA A 132 SER A 164 ASP A 165 HOH A 413
SITE 2 AC2 7 HOH A 444 HOH A 559 HOH A 631
SITE 1 AC3 8 LYS A 169 PRO A 173 GLY A 174 GLN A 240
SITE 2 AC3 8 HOH A 482 HOH A 552 HOH A 556 HOH A 604
SITE 1 AC4 6 ASN A 95 THR A 98 ASN A 100 HOH A 422
SITE 2 AC4 6 HOH A 511 HOH A 563
SITE 1 AC5 5 ILE A 47 ASN A 48 LYS A 239 ILE A 242
SITE 2 AC5 5 HOH A 430
SITE 1 AC6 5 ASN A 95 ASN A 97 SER A 110 HOH A 477
SITE 2 AC6 5 HOH A 601
SITE 1 AC7 9 CYS A 128 ALA A 129 SER A 130 THR A 134
SITE 2 AC7 9 SER A 202 HOH A 409 HOH A 411 HOH A 418
SITE 3 AC7 9 HOH A 435
SITE 1 AC8 6 GLU A 70 ASN A 72 VAL A 75 GLU A 80
SITE 2 AC8 6 HOH A 429 HOH A 531
CRYST1 59.817 61.569 66.964 90.00 90.00 90.00 P 21 21 21 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 0.016718 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016242 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014933 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
