HEADER HORMONE/GROWTH FACTOR 27-FEB-04 1SI5
TITLE PROTEASE-LIKE DOMAIN FROM 2-CHAIN HEPATOCYTE GROWTH FACTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEPATOCYTE GROWTH FACTOR;
COMPND 3 CHAIN: H;
COMPND 4 FRAGMENT: PROTEASE-LIKE DOMAIN;
COMPND 5 SYNONYM: SCATTER FACTOR; SF; HEPATOPOEITIN A; LUNG FIBROBLAST-DERIVED
COMPND 6 MITOGEN;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS CHYMOTRYPSIN HOMOLOGY, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.KIRCHHOFER,X.YAO,M.PEEK,C.EIGENBROT,M.T.LIPARI,K.L.BILLECI,
AUTHOR 2 H.R.MAUN,P.MORAN,L.SANTELL,R.A.LAZARUS
REVDAT 6 27-OCT-21 1SI5 1 REMARK SEQADV
REVDAT 5 14-AUG-19 1SI5 1 REMARK
REVDAT 4 24-JUL-19 1SI5 1 REMARK
REVDAT 3 11-OCT-17 1SI5 1 REMARK
REVDAT 2 24-FEB-09 1SI5 1 VERSN
REVDAT 1 28-DEC-04 1SI5 0
JRNL AUTH D.KIRCHHOFER,X.YAO,M.PEEK,C.EIGENBROT,M.T.LIPARI,
JRNL AUTH 2 K.L.BILLECI,H.R.MAUN,P.MORAN,L.SANTELL,C.WIESMANN,
JRNL AUTH 3 R.A.LAZARUS
JRNL TITL STRUCTURAL AND FUNCTIONAL BASIS OF THE SERINE PROTEASE-LIKE
JRNL TITL 2 HEPATOCYTE GROWTH FACTOR BETA-CHAIN IN MET BINDING AND
JRNL TITL 3 SIGNALING
JRNL REF J.BIOL.CHEM. V. 279 39915 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15218027
JRNL DOI 10.1074/JBC.M404795200
REMARK 2
REMARK 2 RESOLUTION. 2.53 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.53
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.64
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.020
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 10399
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.248
REMARK 3 R VALUE (WORKING SET) : 0.246
REMARK 3 FREE R VALUE : 0.301
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 531
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.53
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.62
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1341
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.3230
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : 0.3850
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1765
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 33
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 56.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.73000
REMARK 3 B22 (A**2) : 0.73000
REMARK 3 B33 (A**2) : -1.09000
REMARK 3 B12 (A**2) : 0.36000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.432
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.312
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.229
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.678
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.912
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.874
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1701 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2317 ; 1.480 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 219 ; 4.846 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 65 ;40.606 ;22.923
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 261 ;16.101 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;15.707 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 258 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1284 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 753 ; 0.244 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 86 ; 0.190 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 20 ; 0.227 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.083 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1089 ; 4.099 ; 2.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1737 ; 6.520 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 612 ; 4.110 ; 2.500
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 580 ; 5.692 ; 5.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1SI5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1000021728.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAY-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : FRONT END, VERTICALLY
REMARK 200 COLLIMATING PREMIRROR, DOUBLE-
REMARK 200 CRYSTAL SILICON (111)
REMARK 200 MONOCHROMATOR WITH A FIXED-
REMARK 200 HEIGHT EXIT BEAM, TOROIDAL
REMARK 200 FOCUSING MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : TRUNCATE, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : CCP4 (TRUNCATE)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10933
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.530
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.24600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.53
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.62
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.36800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NACL, CACL2, PEG 1500, PH 7.2, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 45.03333
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 90.06667
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 90.06667
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 45.03333
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: H
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 HIS H 645
REMARK 465 HIS H 646
REMARK 465 ARG H 647
REMARK 465 GLY H 648
REMARK 465 LYS H 649
REMARK 465 VAL H 650
REMARK 465 THR H 651
REMARK 465 HIS H 729
REMARK 465 HIS H 730
REMARK 465 HIS H 731
REMARK 465 HIS H 732
REMARK 465 HIS H 733
REMARK 465 HIS H 734
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 TYR H 723
REMARK 475 LYS H 724
REMARK 475 VAL H 725
REMARK 475 PRO H 726
REMARK 475 GLN H 727
REMARK 475 SER H 728
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU H 575 CG CD OE1 OE2
REMARK 480 THR H 605 OG1 CG2
REMARK 480 ILE H 606 CG1 CG2 CD1
REMARK 480 LYS H 609 CG CD CE NZ
REMARK 480 SER H 643 OG
REMARK 480 GLN H 644 CG CD OE1 NE2
REMARK 480 GLU H 662 CG CD OE1 OE2
REMARK 480 GLU H 680 CG CD OE1 OE2
REMARK 480 GLN H 681 CG CD OE1 NE2
REMARK 480 HIS H 682 CG ND1 CD2 CE1 NE2
REMARK 480 LYS H 683 CG CD CE NZ
REMARK 480 MET H 684 CG SD CE
REMARK 480 ARG H 685 CG CD NE CZ NH1 NH2
REMARK 480 LYS H 714 CG CD CE NZ
REMARK 480 LYS H 718 CG CD CE NZ
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 OH TYR H 602 ND1 HIS H 717 2.16
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 ILE H 518 -26.42 -142.57
REMARK 500 LEU H 523 98.50 -62.56
REMARK 500 GLN H 534 -1.54 -58.05
REMARK 500 GLU H 559 -29.55 -32.56
REMARK 500 PRO H 574 -154.95 -50.59
REMARK 500 GLU H 575 -110.29 -67.91
REMARK 500 ASP H 591 -151.34 -152.54
REMARK 500 TYR H 602 84.54 -29.06
REMARK 500 SER H 643 82.73 -14.67
REMARK 500 LYS H 663 -55.35 75.27
REMARK 500 GLN H 681 -87.54 -86.19
REMARK 500 HIS H 682 -104.35 -77.34
REMARK 500 MET H 684 -157.77 -140.97
REMARK 500 TYR H 723 172.16 -57.72
REMARK 500 VAL H 725 122.03 65.37
REMARK 500 PRO H 726 106.86 -51.43
REMARK 500 GLN H 727 -83.28 -78.19
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1SI5 H 495 728 UNP P14210 HGF_HUMAN 495 728
SEQADV 1SI5 SER H 604 UNP P14210 CYS 604 ENGINEERED MUTATION
SEQADV 1SI5 HIS H 729 UNP P14210 EXPRESSION TAG
SEQADV 1SI5 HIS H 730 UNP P14210 EXPRESSION TAG
SEQADV 1SI5 HIS H 731 UNP P14210 EXPRESSION TAG
SEQADV 1SI5 HIS H 732 UNP P14210 EXPRESSION TAG
SEQADV 1SI5 HIS H 733 UNP P14210 EXPRESSION TAG
SEQADV 1SI5 HIS H 734 UNP P14210 EXPRESSION TAG
SEQRES 1 H 240 VAL VAL ASN GLY ILE PRO THR ARG THR ASN ILE GLY TRP
SEQRES 2 H 240 MET VAL SER LEU ARG TYR ARG ASN LYS HIS ILE CYS GLY
SEQRES 3 H 240 GLY SER LEU ILE LYS GLU SER TRP VAL LEU THR ALA ARG
SEQRES 4 H 240 GLN CYS PHE PRO SER ARG ASP LEU LYS ASP TYR GLU ALA
SEQRES 5 H 240 TRP LEU GLY ILE HIS ASP VAL HIS GLY ARG GLY ASP GLU
SEQRES 6 H 240 LYS CYS LYS GLN VAL LEU ASN VAL SER GLN LEU VAL TYR
SEQRES 7 H 240 GLY PRO GLU GLY SER ASP LEU VAL LEU MET LYS LEU ALA
SEQRES 8 H 240 ARG PRO ALA VAL LEU ASP ASP PHE VAL SER THR ILE ASP
SEQRES 9 H 240 LEU PRO ASN TYR GLY SER THR ILE PRO GLU LYS THR SER
SEQRES 10 H 240 CYS SER VAL TYR GLY TRP GLY TYR THR GLY LEU ILE ASN
SEQRES 11 H 240 TYR ASP GLY LEU LEU ARG VAL ALA HIS LEU TYR ILE MET
SEQRES 12 H 240 GLY ASN GLU LYS CYS SER GLN HIS HIS ARG GLY LYS VAL
SEQRES 13 H 240 THR LEU ASN GLU SER GLU ILE CYS ALA GLY ALA GLU LYS
SEQRES 14 H 240 ILE GLY SER GLY PRO CYS GLU GLY ASP TYR GLY GLY PRO
SEQRES 15 H 240 LEU VAL CYS GLU GLN HIS LYS MET ARG MET VAL LEU GLY
SEQRES 16 H 240 VAL ILE VAL PRO GLY ARG GLY CYS ALA ILE PRO ASN ARG
SEQRES 17 H 240 PRO GLY ILE PHE VAL ARG VAL ALA TYR TYR ALA LYS TRP
SEQRES 18 H 240 ILE HIS LYS ILE ILE LEU THR TYR LYS VAL PRO GLN SER
SEQRES 19 H 240 HIS HIS HIS HIS HIS HIS
FORMUL 2 HOH *33(H2 O)
HELIX 1 1 ARG H 533 CYS H 535 5 3
HELIX 2 2 LEU H 541 ASP H 543 5 3
HELIX 3 3 ASN H 639 LYS H 641 5 3
HELIX 4 4 VAL H 709 ILE H 720 5 12
SHEET 1 A 7 GLN H 563 ASN H 566 0
SHEET 2 A 7 TYR H 544 LEU H 548 -1 N LEU H 548 O GLN H 563
SHEET 3 A 7 MET H 508 TYR H 513 -1 N ARG H 512 O GLU H 545
SHEET 4 A 7 HIS H 517 LYS H 525 -1 N GLY H 521 O VAL H 509
SHEET 5 A 7 TRP H 528 ALA H 532 -1 N LEU H 530 O SER H 522
SHEET 6 A 7 LEU H 579 LEU H 584 -1 N MET H 582 O VAL H 529
SHEET 7 A 7 VAL H 567 TYR H 572 -1 N VAL H 571 O LEU H 581
SHEET 1 B 6 ARG H 630 TYR H 635 0
SHEET 2 B 6 SER H 611 GLY H 616 -1 N GLY H 616 O ARG H 630
SHEET 3 B 6 PRO H 676 GLU H 680 -1 N VAL H 678 O SER H 613
SHEET 4 B 6 ARG H 685 ILE H 691 -1 N GLY H 689 O LEU H 677
SHEET 5 B 6 GLY H 704 ARG H 708 -1 N VAL H 707 O VAL H 690
SHEET 6 B 6 GLU H 656 ALA H 659 -1 N ALA H 659 O GLY H 704
SSBOND 1 CYS H 519 CYS H 535 1555 1555 2.02
SSBOND 2 CYS H 612 CYS H 679 1555 1555 2.05
SSBOND 3 CYS H 642 CYS H 658 1555 1555 2.04
SSBOND 4 CYS H 669 CYS H 697 1555 1555 2.03
CRYST1 63.700 63.700 135.100 90.00 90.00 120.00 P 31 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 0.015699 0.009064 0.000000 0.00000
SCALE2 0.000000 0.018127 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007402 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
